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Database: UniProt
Entry: E3M213_CAERE
LinkDB: E3M213_CAERE
Original site: E3M213_CAERE 
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
//
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