ID E3M213_CAERE Unreviewed; 1287 AA.
AC E3M213;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=Cre-abl-1 {ECO:0000313|EMBL:EFO89953.1};
GN ORFNames=CRE_07410 {ECO:0000313|EMBL:EFO89953.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR EMBL; DS268422; EFO89953.1; -; Genomic_DNA.
DR RefSeq; XP_003109811.1; XM_003109763.1.
DR STRING; 31234.E3M213; -.
DR EnsemblMetazoa; CRE07410.1; CRE07410.1; WBGene00058433.
DR eggNOG; KOG4278; Eukaryota.
DR HOGENOM; CLU_006516_0_0_1; -.
DR InParanoid; E3M213; -.
DR OMA; TYGMAPY; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:EnsemblMetazoa.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:EnsemblMetazoa.
DR GO; GO:1901075; P:negative regulation of engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:EnsemblMetazoa.
DR GO; GO:0007283; P:spermatogenesis; IEA:EnsemblMetazoa.
DR CDD; cd05052; PTKc_Abl; 1.
DR CDD; cd09935; SH2_ABL; 1.
DR CDD; cd11850; SH3_Abl; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
DR InterPro; IPR011009; Kinase-like_dom_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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF162; TYROSINE-PROTEIN KINASE ABL; 1.
DR Pfam; PF08919; F_actin_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00808; FABD; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
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; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 166..239
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 245..348
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 375..626
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 641..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1287 AA; 145594 MW; 0774B82BCDD772D6 CRC64;
MREKRALLTF LHTNRLSFTF LLFTPGFLHS LPKTSLIFSF EVVIIKLRSQ LHNLPCRASR
KMGHSHSTEK EINDNELFTC EDTVFDRPVA SPKSEISSKL AEEIERSKSP LKLEMFRPTF
DTFRPPNSDS STFRGSQSRE DLVACSSMNS VNNVHDMNTV SSSSSSSAPL FVALYDFHGV
GEEQLSLRKG DQVRILGYNR NNEWCEARLY STRKNDASSQ RRLGEIGWVP SNFIAPYNSL
DKYTWYHGKI SRSDSEAILG SGITGSFLVR ESETSIGQYT ISVRHDGRVF HYRINVDNTE
KVSYMYVLDL TDHHMFITQE VKFRTLGELV HHHSVHADGL ICLLMYPASK KDKTRGLFSL
SPNAPDEWEL DRSEIIMHNK LGGGQYGDVY EGYWKRHDCT IAVKALKEDA MPLHEFLAEA
AIMKDLHHKN LVRLLGVCTH EAPFYIITEF MCNGNLLEYL RRTDKSILPP IILVQMASQI
ASGMSYLEAR HFIHRDLAAR NCLVSDHNVV KIADFGLARF MKEDTYTAHA GAKFPIKWTA
PEGLAFNTFS SKSDVWAFGV LLWEIATYGM APYPGVELSN VYGLLEKGFR MDGPQGCPAS
VYRLMLQCWN WSPSDRPRFR DIHYNLETLI SSNSLNDEVQ KQLKKGSEKK LESDKRRSHV
RERSDSKTRH SSHHDRDRDR ESLHSRNSNP ELANKNFLRN DDNGVTVFFN QPSSKVTSFR
SQVPYPAPPQ QSAKPKLLKS VLSSNARHAS EEFERNDQDD IVPLAEKNVR KAVTRLGGTM
PKGQRIDAYL DSMRRVDSWK ESTDADNEGA GSSSLSRTVS NDSLDTLPLP DSMNSSTYGK
MHPVTGENVF LRQIRSKLKK RSETPELDHI DSDTADEATK SDKSPFGSLN KSTIKYPVRN
GSEFGDHHTR ASPVPVPPSR NASVSVKAEP KAEDSSDETT KDGGMWGPKH AVTRKIEVVK
NDSYPNVEGE LKAKIRNLRH VTKEENNSSP DDSPLDATDT TNDSAIVMPR DEKAKVRQLV
TQKVSPLQHH RPFSLQCPNN STSSAISHSE HADSSETSSL SGIHDDKMKP EIPRKRSNGD
TKIVPVTWVI NGGDKETNGM SRTKSLRDIT TKFEKLGTPS MTESKIEETP YREHALEIKG
SSKRFSMMEG NNELKHVVPS RKNRNLEETG SIEEEPVGKD MIVSLLRVIQ KDFVNLSDLA
SSEITDEKLQ QFMIMADNVQ KLHSTCSVYA EQISPHSKFR FKELLSQLET YNRQIKFSHN
PRAKPVDGKL VMAFQDCFDQ IMRLVDR
//