ID A0A087QL93_APTFO Unreviewed; 1434 AA.
AC A0A087QL93;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Coagulation factor V {ECO:0000313|EMBL:KFM01997.1};
DE Flags: Fragment;
GN ORFNames=AS27_13045 {ECO:0000313|EMBL:KFM01997.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM01997.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM01997.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM01997.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KL225737; KFM01997.1; -; Genomic_DNA.
DR STRING; 9233.A0A087QL93; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd14450; CuRO_3_FV_like; 1.
DR CDD; cd14454; CuRO_4_FV_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR46806:SF9; COAGULATION FACTOR V; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000354-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 848..987
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1107..1258
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1263..1417
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DISULFID 157..183
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 238..321
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 492..518
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 595..676
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 925..951
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1107..1258
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM01997.1"
FT NON_TER 1434
FT /evidence="ECO:0000313|EMBL:KFM01997.1"
SQ SEQUENCE 1434 AA; 163849 MW; 1FCAA887D58BE612 CRC64;
LLLGSWWPDS EKHVVGAMKV REHYIAAQIT SWTYKPESEE KSRLEHSDPV FKKISYREYE
VDFKKEKPAN IFAGLLGPTL RAEVGDTLVV HLKNMADEPV NIHPQGIVYN KNAEGSLYDD
RTSSAEKRDD AVFPGQVYTY VWDITEEVGP READLPCLTY AYYSHKNISR DFNSGLIGAL
LICKKGSLNE DGSQKLFDKE YVLMFGVFDE NKSWQRSASL KYTINGYTDG TLPDLEACAY
DNISWHLIGM SSKPEIFSIH INGQSMEQRH HRVSAVNLVG GASTTVNMTV SEEGRWLISS
LVQKHLQGKA GMHGYLTVRD CGDKEVKKSR LSFKERLMVK SWEYFIAAEE VTWDYAPSIP
DSLDRHYKAQ HLDNFSNLIG KKYKKAIFRQ YTDASFTKRL ENPRPKETGI LGPIIRAQLN
DKVKVVFKNK ATRPYSIYFH GVTLSKNAEG ADYPLGPTNN GTQSRGIDPG KTYTYEWKIA
KTDQPTAQDA QCITRLYHSA VDTERDIASG LIGPLLICKS EALTQRGMQK KADGEQQAMF
AVFDENKSWY IEDNIKDYCS NPASVKRDDP KFYNSNIMHT INGYVSDSSE ILGFCQDSVV
QWHFSSVGTH DEIVSVRLSG HAFLYQGKYE DVLNLFPMSG ESVTVEMDNV GTWLLASWGT
PEMSYGMRLR FRDARCDYEE DYTFDVVDFT YAKTDKKAVS ALVEEDVQEG DREDLDYQDY
LASSYSIRSS RKATGDEEKQ NLTALAWEHF DDPYMTDPKV NINEQRNPDN IAEHYLRSKG
NERRYYIAAE EVCWNYAGYK KSTMMNDKTC KDGTIYKVIF QSYTDSTFTT LQDEDEYKEH
LGILGPVIRA EVDDVILVHF KNLASRPYSL HAHGLLYEKS SEGSVYDDES TAWFKEDDEV
QPNNSYIYVW YANRRSGPVQ AGAACQSWIY YSDLNLEKDI HSGLIGPILI CQKGTFSKSR
NSRTSTRDFF LLFMVFDEEK SWYFDKRSRR PCTEKTQEMQ QCHKFYAING ITYNLQGLSM
YEGELVRWHL LNMGGPKDIH VVHFHGQTFI EQGEPKHQLG TYTLLPGSFR TIEMKPQRPG
WWLLDTEVGE YQQAGMQASY LVIEKECRTP MGLASGVILD SQINASHHID YWEPKLARLN
NSGTYNAWST TMKKEQPPWI QVDFQRQVLL TGIQTQGAKQ FLKSLYIQKF LIFYSKDKRK
WSTFKGDSSP AQKIFEGNSD AYGVKENIID PPIIARYIRV YPTEAYNRPT LRMELLGCEV
DGCSLPLGME NGEIKNTQIT ASSVKTFWFN TWDPSLARLN QKGKMNAWRA KLNNDQQWLQ
IDLLTIQKIT AIATQGVTSL STENFVKTYV ILYSDQGSEW KSYTDDSSSV AKVFLGNENS
NGHVKHFFNP PILSRFIRIV PRTWYHGIAL RVELYGCDFG GGLAVKRTDE SGSS
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