GenomeNet

Database: UniProt
Entry: A0A093HCK5_STRCA
LinkDB: A0A093HCK5_STRCA
Original site: A0A093HCK5_STRCA 
ID   A0A093HCK5_STRCA        Unreviewed;       388 AA.
AC   A0A093HCK5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Urokinase-type plasminogen activator {ECO:0000256|ARBA:ARBA00019414};
DE            EC=3.4.21.73 {ECO:0000256|ARBA:ARBA00013183};
DE   Flags: Fragment;
GN   ORFNames=N308_00250 {ECO:0000313|EMBL:KFV79406.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV79406.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV79406.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV79406.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC       active enzyme plasmin. {ECO:0000256|ARBA:ARBA00004018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC         plasmin.; EC=3.4.21.73; Evidence={ECO:0000256|ARBA:ARBA00000942};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL206163; KFV79406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093HCK5; -.
DR   STRING; 441894.ENSSCUP00000008270; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24264:SF38; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_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:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Kinase {ECO:0000313|EMBL:KFV79406.1};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Transferase {ECO:0000313|EMBL:KFV79406.1}.
FT   DOMAIN          1..34
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          40..119
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          148..388
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        24..33
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV79406.1"
FT   NON_TER         388
FT                   /evidence="ECO:0000313|EMBL:KFV79406.1"
SQ   SEQUENCE   388 AA;  43767 MW;  507F67D11C98128C CRC64;
     DCNCLNGGTC ITYYLFSRIN RCLCPEGYSG IHCEIDTDNK CYMENGEDYR GIATEKECLP
     WDLPSVIRRG SYHTDLKNAL QLGLGKHNYC RNPNGRSRPW CYTKKGFSIQ ETPCNIQKCH
     TQTAHLNKIL SFTEPTCGQR SFSKYFKIVS GSRAEVESQP WIAGIFQNIK GIDHFLCGGS
     LIDPCWVLTA AHCFHSQSKD KSAYKVFLGK SILNATDNKE QVFMVDNIIS HPDFTDETGG
     NENDIALIRI KTTSGQCAVE TKYVRMVCLP EKNLYLPDNT QCEISGYGKQ DFYDIYYAQR
     LMSANVNLIS QTKCTHEYYD NIRVTDNMVC AGDSTWKTDA CKGDSGGPMV CEHNGRMTLY
     GIVSWGDGCA KKNKPGVYTR VTQYLSWI
//
DBGET integrated database retrieval system