ID CARB_SCHPO Reviewed; 1160 AA.
AC O94313;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial {ECO:0000305};
DE Short=CPS;
DE Short=CPSase;
DE EC=6.3.4.16 {ECO:0000250|UniProtKB:P03965};
DE EC=6.3.5.5 {ECO:0000250|UniProtKB:Q7SH52};
DE AltName: Full=Ammonium-dependent carbamoyl phosphate synthetase;
DE AltName: Full=Arginine-specific carbamoyl phosphate synthetase, ammonia chain;
DE AltName: Full=Glutamine-dependent carbamoyl phosphate synthetase;
GN Name=arg4; ORFNames=SPBC215.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=200419; DOI=10.1111/j.1432-1033.1977.tb11830.x;
RA Urrestarazu L.A., Vissers S., Wiame J.M.;
RT "Change in location of ornithine carbamoyltransferase and
RT carbamoylphosphate synthetase among yeasts in relation to the
RT arginase/ornithine carbamoyltransferase regulatory complex and the energy
RT status of the cells.";
RL Eur. J. Biochem. 79:473-481(1977).
RN [3]
RP FUNCTION, AND PATHWAY.
RX DOI=10.1007/BF00381168;
RA Vissers S., Thuriaux P.;
RT "Genetical evidence of carbamoylphosphate compartmentation in
RT Schizosaccharomyces pombe and Schizosaccharomyces japonicus.";
RL Curr. Genet. 9:561-565(1985).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate
CC synthase (CPSase). CPSase catalyzes the formation of carbamoyl
CC phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and
CC phosphate donated by ATP, the first step of the arginine biosynthetic
CC pathway (Ref.3). The large subunit (synthetase) binds the substrates
CC ammonia (free or transferred from glutamine from the small subunit),
CC hydrogencarbonate and ATP and carries out an ATP-coupled ligase
CC reaction, activating hydrogencarbonate by forming carboxy phosphate
CC which reacts with ammonia to form carbamoyl phosphate (By similarity).
CC {ECO:0000250|UniProtKB:Q7SH52, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000250|UniProtKB:Q7SH52};
CC -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial]:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000250|UniProtKB:Q7SH52};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00409};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000305|Ref.3}.
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250|UniProtKB:Q7SH52}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:200419}.
CC -!- MISCELLANEOUS: In S.pombe, this enzyme is synthesized by two pathway-
CC specific (arginine and pyrimidine) genes under separate control. One is
CC linked to the arginine pathway and is designated CPSase A (arg5-arg4),
CC it is localized to mitochondria and repressed by arginine. A second
CC one, CPSase P, is part of a multifunctional protein (ura1) encoding 3
CC enzymatic activities of the pyrimidine pathway (GATase, CPSase, and
CC ATCase); it is localized to the cytoplasm and feedback inhibited and
CC repressed by pyrimidines. The carbamoyl phosphate synthesized by each
CC synthase is channeled to its respective pathway, in contrast to
CC Saccharomyces cerevisiae, in which the 2 synthases are localized to the
CC cytoplasm and appear to contribute to the formation of a single
CC cellular pool of carbamoyl phosphate. {ECO:0000305|PubMed:200419,
CC ECO:0000305|Ref.3}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA22122.1; -; Genomic_DNA.
DR PIR; T39898; T39898.
DR RefSeq; NP_596685.1; NM_001022608.2.
DR AlphaFoldDB; O94313; -.
DR SMR; O94313; -.
DR BioGRID; 277252; 7.
DR DIP; DIP-59124N; -.
DR IntAct; O94313; 1.
DR STRING; 284812.O94313; -.
DR iPTMnet; O94313; -.
DR MaxQB; O94313; -.
DR PaxDb; 4896-SPBC215-08c-1; -.
DR EnsemblFungi; SPBC215.08c.1; SPBC215.08c.1:pep; SPBC215.08c.
DR GeneID; 2540729; -.
DR KEGG; spo:SPBC215.08c; -.
DR PomBase; SPBC215.08c; arg4.
DR VEuPathDB; FungiDB:SPBC215.08c; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR InParanoid; O94313; -.
DR OMA; FPFNKFP; -.
DR PhylomeDB; O94313; -.
DR UniPathway; UPA00068; UER00171.
DR PRO; PR:O94313; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IEA:RHEA.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; EXP:PomBase.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IC:PomBase.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF57; CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Manganese; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1160
FT /note="Carbamoyl phosphate synthase arginine-specific large
FT chain, mitochondrial"
FT /id="PRO_0000145089"
FT DOMAIN 212..404
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 748..946
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1014..1160
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 81..478
FT /note="Carboxyphosphate synthetic domain"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT REGION 479..623
FT /note="Oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT REGION 624..1012
FT /note="Carbamoyl phosphate synthetic domain"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT REGION 1013..1144
FT /note="Allosteric domain"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 361
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 825
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 858
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 898
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 898
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 917
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00968"
FT BINDING 917
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 917
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 917
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 917
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 919
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 919
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 1160 AA; 127480 MW; 883FBAC4A8E79BC7 CRC64;
MALWATSMRR AIPGISKAFL GSNRVLETAG VSQLSKHLLP QWSGVPHRKI SASATNFNDK
VKESNTPDAN AYIRSGHIKA AEHEKVKKVV VVGSGGLSIG QAGEFDYSGA QAIKALRESS
VHTILINPNI ATIQSSHSLA DEIYFLPVTA EYLTHLIERE NPDGILLTFG GQTALNVGIQ
LDDMGVFARN HVKVLGTPIS TLKTSEDRDL FAKALNEINI PIAESVAVST VDEALQAAEK
VSYPVIIRSA YSLGGLGSGF ANNKEELQSM AAKSLSLTPQ ILVEKSLKGW KEVEYEVVRD
AANNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEEYHM LRTAAIKIIR HLGVVGECNV
QYALSPNSLE YRVIEVNARL SRSSALASKA TGYPLAYTAA KIALGHTLPE LPNAVTKTTT
ANFEPSLDYV VTKIPRWDLS KFQYVNREIG SSMKSVGEVM AVGRTFEESL QKALRQVDPS
FLGFMAMPFK DLDNALSVPT DRRFFAVVEA MLNQGYSIDK IHDLTKIDKW FLSKLANMAK
VYKELEEIGS LYGLNKEIML RAKKTGFSDL QISKLVGASE LDVRARRKRL DVHPWVKKID
TLAAEFPAHT NYLYTSYNAS SHDIDFNEHG TMVLGSGVYR IGSSVEFDWC GVSCARTLRK
LGHSTIMVNY NPETVSTDFD ECERLYFEEL SYERVMDIYE METASGIVVS VGGQLPQNIA
LKLQETGAKV LGTDPLMIDS AEDRHKFSQI LDKIGVDQPA WKELTSVAEA SKFANAVGYP
VLVRPSYVLS GAAMSVIRDE SSLKDKLENA SAVSPDHPVV ITKFIEGARE LDVDAVASKG
KLLVHAVSEH VENAGVHSGD ATIALPPYSL SEDILSRCKE IAEKVCKAFQ ITGPYNMQII
LAQNPDKPDT PDLKVIECNL RASRSFPFVS KTLGVNFIDV ATRSIIDQEV PAARDLMAVH
RDYVCVKVPQ FSWTRLAGAD PYLGVEMSST GEVACFGKDV KEAYWAALQS TQNFKIPLPG
QGILLGGDRP ELAGIAADLS KLGYKLYVAN KDAAKLLQPT SAEVVEFPVK DKRALRAIFE
KYNIRSVFNL ASARGKNVLD QDYVMRRNAV DFNVTLINDV NCAKLFVESL KEKLPSVLSE
KKEMPSEVKR WSEWIGSHDL
//
