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Database: UniProt
Entry: A0A091P3G4_HALAL
LinkDB: A0A091P3G4_HALAL
Original site: A0A091P3G4_HALAL 
ID   A0A091P3G4_HALAL        Unreviewed;       554 AA.
AC   A0A091P3G4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Complement factor I {ECO:0000313|EMBL:KFQ02532.1};
DE   Flags: Fragment;
GN   ORFNames=N329_05610 {ECO:0000313|EMBL:KFQ02532.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ02532.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ02532.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ02532.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; KK652329; KFQ02532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P3G4; -.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR048722; CFAI_FIMAC_N.
DR   InterPro; IPR048719; CFAI_KAZAL.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF7; HYALIN; 1.
DR   Pfam; PF21286; CFAI_FIMAC_N; 1.
DR   Pfam; PF21287; CFAI_KAZAL; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00530; SRCR; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00057; FIMAC; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          29..77
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          81..196
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          312..545
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        153..163
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        188..200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        195..213
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        207..222
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        225..237
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        232..250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ02532.1"
FT   NON_TER         554
FT                   /evidence="ECO:0000313|EMBL:KFQ02532.1"
SQ   SEQUENCE   554 AA;  62473 MW;  F0016D8893C28C82 CRC64;
     ECLINQYTHK SCEKVFCHPW ERCVEGKCLC KLPYQCPKNG SSVCSTNGRY FPTYCHLKSY
     ECQQPKAKFL HKGKCMSEET FSISVGHGDS NLLRVKPMNQ KNYIFVCDGE WTMNEANVAC
     KHLGFESGAE YYQTNSSITE SASNSLHCVQ ITCRGLETSL AECHIEMKSR DSNEGFVSLQ
     CHENLRACSD GEFRCVNKKC ISLNKTCDGI NDCGDLSDEL CCRECRDNSF HCRSNICIPN
     KNVCNKEVDC LTGEDEARIL CAGKGTDKGA EKHSMDEDTF FLFVKERKMI KTLLRQVHCG
     LTNHTLTRRK RIVGGEIARK GEFPWQVAIK ETGSEGATVY CGGVYIGGCW VLTAAHCVRA
     NRVHLYRVWV GLLHTILYDQ ETDTFSLNRL IIHENYNAST YENDIALLEL KGFGKGECSL
     QQITPACIPW SEYMFKAGDR CKVSGWGLEK GYTKQYILKW GNVNLFQNCS EMYPGRFFKQ
     MACTYDGSID SCKGDSGGPL VCFDAENVAY VWGIVSWGEN CGEAGHPGVY TKVASYYDWI
     SHHVTRSLIA RYNI
//
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