ID A0A016SSV6_9BILA Unreviewed; 867 AA.
AC A0A016SSV6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Protein tyrosine kinase {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0181.g836 {ECO:0000313|EMBL:EYB93481.1};
GN Synonyms=Acey-kin-32 {ECO:0000313|EMBL:EYB93481.1};
GN ORFNames=Y032_0181g836 {ECO:0000313|EMBL:EYB93481.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB93481.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}.
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:EYB93481.1}.
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DR EMBL; JARK01001517; EYB93481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SSV6; -.
DR STRING; 53326.A0A016SSV6; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR CDD; cd13190; FERM_C_FAK1; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR041390; FADK_N.
DR InterPro; IPR049385; FAK1-like_FERM_C.
DR InterPro; IPR041784; FAK1/PYK2_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24418:SF367; INACTIVE TYROSINE-PROTEIN KINASE KIN-32; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF21477; FERM_C_FAK1; 1.
DR Pfam; PF18038; FERM_N_2; 1.
DR Pfam; PF03623; Focal_AT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF68993; FAT domain of focal adhesion kinase; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50057; FERM_3; 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|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 3..329
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 372..634
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 696..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..725
FT /note="Polar 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 867 AA; 97092 MW; 7CC6B0D48167A248 CRC64;
MDSIARVFTV GNGCKAVRYD EETTVERVLQ VVLQGIGIAA VAHAHFALRL LAGPSPRTAG
DHVWLHPCLL ISNLRHTYAR FLPSSACPQE LSFELRLRFI PQSAYELLLT ESNAFFYLNE
QVFEDFLGHV AWKVNLEAAL ELAALKVCRD CLEKQAKSCL DHKVDTDSID VDAAMQAFIP
KTVLCSANTK PSALKRQFVQ LLKKFAPLPA TESVLRSLSI LIDIVKFDVE VFKASMGVGW
ASPVDLLVGP EVGLSYRINE RCEISRLAEL RSVLEIIIRK MEQSSEKAIV QLKISGNAQP
MLITVATHDI AESLAHLIDG YQMMYNQGSS VYRMKGLERC ESADMRATTV IHRPHSSVPG
VSHDLRIRRE HVTLKELIGG GQFGNVYRGT LADPGAPPVT VAVKVCKMEN EPTDTQLILQ
ESHLMKNLQH DNIISLIGVC MDAPMWLVME LAPLGELRQY LQSNRASLSL TSLFLYSLQV
ARAICYLHGK SLVHRDIAAR NVLVSTPKCV KLTDFGLSRA LDYDAVYTAS RGKLPIKWLA
PESINYREFS MASDIWMYGV CVWEILSWGA KPWQGVANAD VITRVETGAR LPCPDGCPVA
LYNYLELMVW ALQPAKRPTA KEIVSVMESI HDQLKKHVPP EEIHLIRPAQ NVPVLLTNIS
TLPNLTLWRT LEEQKRQGEE DDKWLDEQED LTAYDPAEEH ERTHNGFAST SRTASNGSIN
GKPNGGISPN LVLVSRAVNA VTEAVDRLNN TFNVNMKHDD FVSSIRDITS KLREMFAEST
DVLGQMPEER RKEVEMTEAL IGNDMRQMGK VVQQVVDNTN NPSYHIYRRE VVRIAKEMAV
NCTNFLSLFE NRNRVKLPDF RAVLSDC
//
