ID B4HH60_DROSE Unreviewed; 2358 AA.
AC B4HH60;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=Dsec\GM26621 {ECO:0000313|EMBL:EDW43536.1};
GN ORFNames=Dsec_GM26621 {ECO:0000313|EMBL:EDW43536.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW43536.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CH480815; EDW43536.1; -; Genomic_DNA.
DR RefSeq; XP_002032550.1; XM_002032514.1.
DR SMR; B4HH60; -.
DR STRING; 7238.B4HH60; -.
DR MEROPS; M12.011; -.
DR EnsemblMetazoa; FBtr0209606; FBpp0208098; FBgn0181474.
DR HOGENOM; CLU_229617_0_0_1; -.
DR OMA; SYPSNQN; -.
DR PhylomeDB; B4HH60; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 10.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 10.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF34; CUB AND SUSHI DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF01400; Astacin; 2.
DR Pfam; PF00431; CUB; 10.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 3.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 10.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00235; ZnMc; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 10.
DR PROSITE; PS51864; ASTACIN; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01180; CUB; 10.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 34..2358
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005123119"
FT DOMAIN 519..721
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 723..839
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 840..954
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 954..994
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 997..1114
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1114..1154
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1158..1270
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1271..1360
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1427..1629
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 1631..1768
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1769..1882
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1882..1922
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1925..2044
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 2044..2084
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2088..2200
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 2201..2317
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 39..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..469
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1391
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT ACT_SITE 1523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 1532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 584..606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 586..587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 1492..1514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 1494..1495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 1769..1796
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 2358 AA; 267419 MW; 27747623F36CE627 CRC64;
MRRRRGTPLG VSWTNCVLLL ATGLLVVLIS VHAKNPRPHR GLPAPAPAPV PESVDQVATE
NGHRREPTVD GSVLQRLSGS DRAVDEDEDV DEDGDEGLKH QHLEHRQQFD AYLGTIRRLR
RPYRSKYTIE QLMRLHVTPK VSEDIDMDPC KAGGFMDDIA LPEGDSGPVI AHTPINDEEH
ERQEVEQLLA DSPSPVHDPA SVSGAANSGP TKFNATFQLE LEKLKQEVYH EGLQVEEEGL
TDIIRKKTKL PSSGPVNLKA GQSQSQSQSA NEPVKPGSES PSDYAQASSY KNEVLPPSEQ
RIHTDKPARL TLAEIGPKSS NKTQSLHRNV DTRKIQSDNK DIEDDSGNNF VAKRRPSQIV
PTSLPEQRST PAHVYSNAGG NGMQLDDEVD FLHSRGVVRR RHRRGPKQRR SNQHLEHEAK
LQRLKEELSR PVIKGHHRQS HHQKQAQHRQ HHQSHHRKKH RRQQQHHRRR GQSTTQYVNH
SPPGFNQSQQ AQQQSVPEMD LLKAETPKNK EPLRHRVARA VTAKKERIWD YGVIPYEIDG
NFSGIHKALF KLAMRHWENS TCIKFVERDP EIHPNYIVFT VRSCGCCSFV GKRGNGPQAI
SIGRNCDKFG IVVHELGHVV GFWHEHTRPD REKHVVIEHN NIMKGQDYNF NMLSPDEVDS
LGMAYDYDSI MHYARNTFSK GTYLDTILPI EMKGRKRPEI GQRLRLSQGD IAQANLLYKC
PKCGRTFQES SGIFASPSHY TAGALSNETE HCEWRITATY GERVELKLEN MNIFKSNNCE
TDYLEIRDGY FEKSPLIGRF CGKVDKEVIR TESSRMLLTY VNTHRIEGFR GFKAEFDVVC
GGELFVDDAV GRLESPNYPL DYLPNKECVW KITVPDSYQV ALKFQSFEVE NHDNCVYDYV
VVRDGPGQDA PLIGVFCGYK PPPNMKSSGN SMYVKFVSDT SVQKAGFSAV FMKEVDECET
QNHGCEHECI NTLGGYECSC RIGFELHSDK KHCEDACGGV IEYPNGTITS PSFPETYPLL
KECIWEIVAP PKHRISLNFT HFDLEGTAHQ QSDCGYDSVT VYSKLGENRL KRIGTFCGSS
IPPTATSESN ALRLEFHSDK SIQRSGFAAV FFTDIDECAV NNGGCQHECR NTIGSYICMC
HNGYSMHENG HDCKEGECKY EISAPFGSIF SPNYPDSYPP NADCVWHFIT TPGHRIKLIF
NEFDVESHQE CTYDNVSVYD GESESSSVLG RFCGDKIPFP ISSTSNQMYM VLKTDKNKQK
NGFRASHSTA CGGYLRATSQ VQQFYSHARF GNQDYDDGMD CEWTIAAPDN SYVQLIFLTF
DIESSENCTF DYVQVFSDID DVYGQYEPMY GQYCGNVVPP KRPKDGIHQL KTARQYSGRR
RKQPHKSRNK AARRLPPPFL WTDDAVDVLQ HSHSPTLNGQ PMQRKRRAVT VRKERTWDYG
VIPYEIDTIF SGAHKALFKQ AMRHWENFTC IKFVERDANL HANYIYFTVK NCGCCSFLGK
NGNGRQPISI GRNCEKFGII IHELGHTIGF HHEHARGDRD KHIVINKGNI MRGQEYNFDV
LSPEEVDLPL LPYDLNSIMH YAQNSFSKSP YLDTITPIGI PPGTHLELGQ RRRLSRGDIV
QANLLYKCAS CGRTYQQNSG HIVSPHFVSS GNGVLSEFEG SGDAGEDPSA ESEFDASLTN
CEWRITATNG EKVILHLQQL HLMTSDDCTQ DYLEIRDGYW HKSPLVRRIC GNVSGEVITT
QTSRMLLNYV NRNAAKGYRG FKARFEVVCG GDLKLTRDQS IDSPNYPLDY MPDKECVWRI
TAPDNHQVAL KFQSFELEKH DGCAYDFVEI RDGNHSDSRL IGRFCGDKLP PNIKTRSNQM
YIRFVSDSSV QKLGFSAALM LDVDECKFTD HGCQHLCINT LGSYQCGCRA GYELQANGKT
CEDACGGVVD ATKSNGSLYS PSYPDVYPNS KQCVWEVVAP PNHAVFLNFT HFDLEGTRFH
YTKCNYDYLI IYSKMRDNRL KKIGIYCGHE LPPVVNSEQS VLRLEFYSDR TVQRSGFVAK
FVIDVDECSM NNGGCQHRCR NTFGSYQCSC RNGYTLAENG HNCTETRCKF EITTSYGVLQ
SPNYPEDYPR NIYCYWHFQT VLGHRIQLTF HDFEVESHQE CIYDYVAIYD GRSENSSTLG
IYCGGREPYA VIASTNEMFM VLATDAGLQR KGFKATFVSE CGGYLRATNH SQTFYSHPRY
GSRPYKRNMY CDWRIQADPE SSVKIRFLYF EIEYSERCDY DYLEITEEGY SMNTIHGRFC
GKHKPPIIIS NSDTLLLRFQ TDESNSLRGF AISFMAVDPP EDSVGEDFYA VTPFPGYLKS
MHSSETGSDH LLPPSRLI
//
