ID A0A2G5UDV2_9PELO Unreviewed; 1095 AA.
AC A0A2G5UDV2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Cni-ark-1 {ECO:0000313|EMBL:PIC37728.1};
GN Synonyms=Cnig_chr_IV.g16257 {ECO:0000313|EMBL:PIC37728.1};
GN ORFNames=B9Z55_016257 {ECO:0000313|EMBL:PIC37728.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC37728.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC37728.1}.
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DR EMBL; PDUG01000004; PIC37728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UDV2; -.
DR Proteomes; UP000230233; Chromosome iv.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
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; 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:SF444; ACTIVATED CDC42 KINASE-LIKE; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 177..441
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 546..560
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 507..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1095 AA; 121246 MW; 2FB2284C807A6828 CRC64;
METFQHSASL LVSCSLAGRL EFVSSSRCPF QSYFSFIFFF FSPFLQLKLT SSAKLTEGSS
AKEAMRDEPA AANADATLNK LLQAADLTGY ESDLRRKLKL RNAADLQYVE EVDLLSIGMS
RPEQKRLRKE YTRMFPSGIF GKVKKAFKRS ESLDRKNSNS TGSREDDDHH VIPIEKITLC
KELGQGEFGS VWQAAWKNGN DVTQVAVKCV GSDKLLATSS SFLQEAAIMT RMRHEHVVRL
YGVVLDTKKI MLVSELATCG SLLECLHKPA LRDSFPVHVL CDYAEQIAMG MSYLESQRLI
HRDLAARNVL VFSPKLVKIS DFGLSRSLGV GEDYYRSEFT PNLKLPIAWC APECINFLKF
TSKSDVWAYG VTIWEMFSYG AMPWKGKSGG QILELVDRKK ELLPRPEACP EDIYDMLKEA
WTHQVTDRPN FSDIVSQFPE RRAQSVRAVV DCRDSAADHL HFKKDDLIVV ISRSPAQYPD
GYYWFGSLRN GKLGLFRPTD TVAHLGSEPP CSNVENGFNG EKSTEKGKKN KKVDKGEERE
RKKLLISEPV GDVRHTCHVG IDGTAFGLLQ LDKKAMCPTS SSPSTSRGST TTSQASPAPS
HTSSSTSSSV QLRENVARHG VSLKETMSLR DVGPLSRDAI NLRETVSPPI TRAPSQPPSY
SQPRPPPRSV SSVNNHHHSL PNGDQFSSLD RTRGSVTPTA PPLTSSAASS LKEPMNGISL
SIPNNHMSYM DDEEWVRSPG GVSASTTMTT LSYRKDPIPA PRGPVAAVYA RGKDIPTPAS
RSDVAICEEI EHLNRDLTNY SIGTICDYSE DRPLLDSFNK ACSNSTSHTP SSRLRFMTEE
EARKMNEKSL REHRKTEDLL KEERQREKKV DVVSPPDEAP IESLYSGQQR QQEGWSSAAQ
EAYKLLVECG TNLKQASVSP PPMSPASSRF TTLDRPTSTT TDRSSVSPAP PRPVTPPMAV
RSETISMRKV SEESMEQVTV EENSPKRVHI IETKLIDGPA RGMSPIQDRH VPAFTTPMSN
TFRKPPAPAP NGTNSSSDQK PPPCRPPKKF PLIIDERNLA YDNLNGFGAG ARVAPPVPPK
PKVSFADDSK KEIVN
//
