ID ACDA1_METBF Reviewed; 806 AA.
AC Q46G04;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE EC=1.2.7.4 {ECO:0000255|HAMAP-Rule:MF_01137};
DE AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS CODH subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN Name=cdhA1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN OrderedLocusNames=Mbar_A0204 {ECO:0000312|EMBL:AAZ69188.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
RP INDUCTION, AND PATHWAY.
RC STRAIN=MS;
RX PubMed=6425262; DOI=10.1128/jb.158.1.231-237.1984;
RA Krzycki J.A., Zeikus J.G.;
RT "Characterization and purification of carbon monoxide dehydrogenase from
RT Methanosarcina barkeri.";
RL J. Bacteriol. 158:231-237(1984).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS EPSILON
RP SUBUNIT; IRON-SULFUR (4FE-4S); NICKEL-IRON-SULFUR (NI-4FE-4S) AND CARBON
RP MONOXIDE, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=18621675; DOI=10.1073/pnas.0800415105;
RA Gong W., Hao B., Wei Z., Ferguson D.J., Tallant T., Krzycki J.A.,
RA Chan M.K.;
RT "Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of
RT the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9558-9563(2008).
CC -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC cleavage of acetyl-CoA, allowing growth on acetate as sole source of
CC carbon and energy. The alpha-epsilon subcomponent functions as a carbon
CC monoxide dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137,
CC ECO:0000269|PubMed:6425262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2
CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC ECO:0000269|PubMed:18621675};
CC Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC -!- COFACTOR:
CC Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC ECO:0000269|PubMed:18621675};
CC Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC -!- ACTIVITY REGULATION: Carbon monoxide dehydrogenase activity is
CC inhibited by KCN and is rapidly inactivated by O(2).
CC {ECO:0000269|PubMed:6425262}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mM for CO (at 37 degrees Celsius) {ECO:0000269|PubMed:6425262};
CC Vmax=1300 umol/min/mg enzyme for CO dehydrogenase activity using
CC methyl viologen as electron acceptor (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:6425262};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:6425262}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits
CC (PubMed:6425262). The ACDS complex is made up of alpha, epsilon, beta,
CC gamma and delta subunits with a probable stoichiometry of
CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:6425262,
CC ECO:0000305|PubMed:18621675}.
CC -!- INDUCTION: Up-regulated during growth on acetate.
CC {ECO:0000269|PubMed:6425262}.
CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster
CC C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation.
CC Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges
CC the two subunits of the CODH dimer. Contains two additional 4Fe-4S
CC clusters, dubbed E and F, that probably transport electrons from
CC ferredoxin to the B cluster. {ECO:0000255|HAMAP-Rule:MF_01137,
CC ECO:0000305|PubMed:18621675}.
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_01137}.
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DR EMBL; CP000099; AAZ69188.1; -; Genomic_DNA.
DR PDB; 3CF4; X-ray; 2.00 A; A=1-806.
DR PDBsum; 3CF4; -.
DR AlphaFoldDB; Q46G04; -.
DR SMR; Q46G04; -.
DR STRING; 269797.Mbar_A0204; -.
DR PaxDb; 269797-Mbar_A0204; -.
DR KEGG; mba:Mbar_A0204; -.
DR eggNOG; arCOG02428; Archaea.
DR HOGENOM; CLU_361186_0_0_2; -.
DR OrthoDB; 35334at2157; -.
DR UniPathway; UPA00642; -.
DR EvolutionaryTrace; Q46G04; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR CDD; cd01916; ACS_1; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.2030; -; 2.
DR Gene3D; 1.10.8.190; Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1; 1.
DR HAMAP; MF_01137; CdhA; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004460; CdhA.
DR InterPro; IPR004137; HCP/CODH.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR NCBIfam; TIGR00314; cdhA; 1.
DR PANTHER; PTHR30109:SF6; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF03063; Prismane; 2.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW Nickel; Oxidoreductase; Repeat.
FT CHAIN 1..806
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha 1"
FT /id="PRO_0000436851"
FT DOMAIN 407..436
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 446..475
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 117
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000269|PubMed:18621675"
FT BINDING 250
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:18621675"
FT BINDING 278
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:18621675"
FT BINDING 323
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT BINDING 417
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 420
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 423
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 427
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 455
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 458
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 461
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 465
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT BINDING 523
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT BINDING 552
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT BINDING 587
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT ECO:0000269|PubMed:18621675"
FT TURN 50..57
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 98..132
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 190..218
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 378..398
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 551..557
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 591..603
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 613..623
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 636..647
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 656..661
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 675..679
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 692..698
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 702..712
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 720..737
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 745..748
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 760..771
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 777..780
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:3CF4"
SQ SEQUENCE 806 AA; 88775 MW; 25620ACDA618E9CA CRC64;
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELV NAGPTLFAGL ESYRDDWNFK
LLDRYEPVIT PMCDQCCYCT YGPCDLSGNK RGACGIDMLG HNGREFFLRV ITGTACHAAH
GRHLLDHLIE TFGEDLPLNL GQSNVLTPNI TISTGLSPKT LGEVKPAMEY VEEQLTQLLA
TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDIVQVTAYD FPRADPEAPL IEIGMGTIDK
SKPFLCVIGH NVAGVTYMMD YMEDHDLTDK MEIAGLCCTA IDLTRYKEAD RRPPYAKVIG
SMSKELKVIR SGMPDVIVVD EQCVRGDIVP EAQKLMIPVI ASNPKIMYGL PNRTDADVDE
TIEELRSGKI PGCVMLDYDK LGEICIRLTM EMAPIRDASG ITAIPTDEEF TNWVMKCADC
GACMIACPEE LDIPEAMGFA KEGDYSYLDI LHDQCIGCRR CEQVCKKEIP ILNIIEKAAQ
KQISEEKGLM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYPEGT KDVYYIAEEF
LKRNFIVVTT GCGAMDIGMF KDEDGKTLYE RFPGGFECGG LANIGSCVSN AHITGAAEKV
AAIFAQRTLE GNLAEIGDYV LNRVGACGLA WGAFSQKASS IGTGCNILGI PAVLGPHSSK
YRRALIAKNY EEDKWKVYDA RNGQEMAIPP APEFLLTTAE TWQEAIPMMA KACIRPSDNN
MGRSIKLTHW MELHKKYLGS KPEDWWKFVR NEADLPLATR EALLKELEKE HGWEIDWKRK
KVISGPKIKF DVSAQPTNLK RLCKEA
//
