ID A0A3Q0FMM4_ALLSI Unreviewed; 612 AA.
AC A0A3Q0FMM4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000604};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000604};
GN Name=LOC102379235 {ECO:0000313|RefSeq:XP_025047430.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025047430.1};
RN [1] {ECO:0000313|RefSeq:XP_025047430.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149,
CC ECO:0000256|PIRNR:PIRNR000604};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000256|PIRNR:PIRNR000604}.
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DR RefSeq; XP_014381091.1; XM_014525605.1.
DR RefSeq; XP_025047430.1; XM_025191645.1.
DR AlphaFoldDB; A0A3Q0FMM4; -.
DR STRING; 38654.A0A3Q0FMM4; -.
DR KEGG; asn:102379235; -.
DR InParanoid; A0A3Q0FMM4; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05115; PTKc_Zap-70; 1.
DR CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035838; SYK/ZAP-70_N_SH2.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF369; TYROSINE-PROTEIN KINASE ZAP-70; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PIRSF; PIRSF000604; TyrPK_SYK; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000604};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000604};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000604};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000604};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000604}.
FT DOMAIN 10..102
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 163..267
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 331..590
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT BINDING 337..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT BINDING 362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 612 AA; 69413 MW; 2FC5B358DF70FD8C CRC64;
MPDAAAHLPF FFGSISRSEA EEHLKLAGMG DGLFLLRQCL RSLGGYVLSM VFNLQFYHYP
IERQMNGTYA IAGGKAHCGP EELCEFYSKD ADGLCCTLRK PCTRPSGVEP ESGIFDNMRD
NMVREYIRQT WKLEGDALEQ AIISQAPQVE KLIATTAHES MAWYHGNISR EEAERRLYSG
AQPDGKFLLR QRKENGTYAL SLVYGKTVYH YRIDQDKSGK YSIPEGTKFD TLWQLVEYLK
LKADGLIYNL KECCPNPSTP SGLVAPVLPA HPSMSVQRQF SSLNADGYTP EPIGAGKSRV
LPMDTSVYES PYSDPEDLKD KKLFLKRDHL MIDEVELGSG NFGCVKKGVY KMRKKQIDVA
IKVLKSNNEK AVKDEMMKEA EIMHQLDNPY IVRMIGVCEA ESLMLIMEMA SGGPLNKFLS
SKKDEIPMSN IVELMHQVAI GMKYLEEKNF VHRDLAARNV LLVNHHYAKI SDFGLSKALG
ADDSYYKART AGKWPLKWYA PECILYHKFS SKSDVWSYGV TMWEAFSYGQ KPYKKMKGPE
VMSFIEQGKR MESPAECPPE MYSLMQQCWT FKWEDRPGFV TVETLIRSYY YSIAAKTEKG
PNVEDKTSAA FP
//
