ID A0A091R8H2_9GRUI Unreviewed; 1607 AA.
AC A0A091R8H2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Coagulation factor VIII {ECO:0000313|EMBL:KFQ35771.1};
DE Flags: Fragment;
GN ORFNames=N332_14430 {ECO:0000313|EMBL:KFQ35771.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ35771.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ35771.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ35771.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK811378; KFQ35771.1; -; Genomic_DNA.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd04228; CuRO_5_FVIII_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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:SF7; COAGULATION FACTOR VIII; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 4.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000354-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369}.
FT DOMAIN 1296..1444
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1449..1601
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 483..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 34..60
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 136..217
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1107..1133
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1174..1178
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1296..1444
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ35771.1"
FT NON_TER 1607
FT /evidence="ECO:0000313|EMBL:KFQ35771.1"
SQ SEQUENCE 1607 AA; 181052 MW; 002AA753919E593D CRC64;
DKDVKDIPVP PGQSFTYSWR ITTEDGPTQA DPRCLTRFYY SSINPVRDTA SGLIGPLLIC
FKKSMDQRGN QIMSDNTRLV LFSVFDENCS WYLEENIRRF CTDAAHVDTQ DPQFYTSNVM
HTINGFVFDN LQPKLCLHEV VYWYVLSVGA QTDFLSIFFS GNTFKRNMVF EDVLTLFPFS
GETVFMSLEK PGVWTLGCLN PNFRDRGMHA KFTVSQCHHE QYSDGEDYDF EDEEGAFDFQ
PRGFSKRKRR LRPCVNEQLD NITSTRNETE KPRLCVTEPS HVALLSNGTN PPSNGTSTHL
GTIPHPPDIS MSSLPETSYD PVSYESFLKD EQELSKTISQ NEGFGALPPR ERLVSVSEGV
HGAVTSGEYQ QWLHQATQAP EDALAGQKVT KASEVQEPVK RTMVQSGGTS EILEGEPQKT
SLWDSITYSS KAPLQENRNS FYENDLESNL GLQDVFSQGA EDNLLGATNE ISLNLYEPKE
TITTEPALST DPNSSSTLDN LSASSDETAD NRTSHAVVHR KSNYTSNELN ARLEKRLHKG
VSQGSYEPFE GKNVSSSNLG LSKAVQQILT DESNSLPAKS GSEQEASELA KDTRNNLLET
TFAHTNDLEP SNYIMTEERD ELILEAVFQD GTAAKELPEM DSFAFPESNV VANAFLNSPE
QFLRHRAPAP NVSSPDHGPR QDRSLESRGL VHGLGLPNTS WPGSREPLSE SNRAEQDLAS
QTPETAVNKK APKANKIMAT SSSETQAAVV PADLASNWDP VSLGERSPAL AELQSDRGAV
RGTSGSEPAE GRSQMEEETN SVEQLGQFSP QHPQVRANAT EKYVPENISG QSPEEILVKP
ASKENYTLSP SSPLLNNSTA KKRDEYVQAS PDGWQVLSGE DVLRENGKRE GHGLGELKED
GESNSTAGKR NHAPEHRERQ ALNNRTHSSP SRADKLDYDE YSDAEQTMED FDIYEEEEHD
PRSFQGEIRQ YFIAAVEVIW EYGNQRPQHF LKATHPWSGR RKPFQQYRKV VFREYMDSSF
TQPLQRGELD EHLGILGPYI RAEVEDVIMV TFKNLASRPF SFHSTLQAYE ETQGATQGGE
VVHPGEVRKY SWKVLPQMAP TTQEFDCKAW AYFSNVDLEK DLHSGLIGPL IICRRGVLSF
VFGRQLVVQE FSLLFTIFDE TKSWYFLENM KRNCRPPCHI QQDNPDFKRN HSFHAINGYV
RDTLPGLVMS QQQRVRWHLL NMGSTEDIHS VHFHGQLFSV RTNQEYHMGV YNLYPGVFGT
VEMRPSRAGI WRVECKVGEH QQAGMSALFL VYNPNCRNAL GLASGHIADS QITASGQYGQ
WAPHLARLHN TGSINAWSTG RSNASIQVDL LRLMIIHGIK TQGARQKFSS LYISQFVVFY
SLDGQRWKKY KGNATSTEML FFGNVDATTV KENSFNFPII ARYIRINVTH YSIRPTLRME
LIGCDLNSCS MPLGMENRGI PDQRISASSY STNVFFSWSP SHARLNLQGR TNAWRPKSNS
PSEWLQVDFE ETKKVTAIIT QGAKAVFTHM FVKEFAVSSS QDGVHWSPIL QDSKEKIFKA
NQDHTNTVMN TLEPPLFARY VRIHPRWWHN HIALRIEFLG CDTQQEY
//
