ID A0A423SJJ2_PENVA Unreviewed; 1248 AA.
AC A0A423SJJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN ORFNames=C7M84_017706 {ECO:0000313|EMBL:ROT64362.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT64362.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT64362.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT64362.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT64362.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT64362.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:ROT64362.1}.
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DR EMBL; QCYY01003260; ROT64362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423SJJ2; -.
DR STRING; 6689.A0A423SJJ2; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 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; IPR001452; SH3_domain.
DR InterPro; IPR049587; TNK-like_SAM.
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; PF00786; PBD; 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; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 838..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1060..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..382
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 382..452
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 482..496
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 454..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1248 AA; 137444 MW; 2DF33CC88EBC0AE8 CRC64;
MTTVPRGPGL YEFLTEAELQ HYYNNFKNDL KVQNVGQLKF VADEDLQAMG MSRPEVRRLK
KYFHKYCPQT YLSKFKKILL ARKDGQDSHE VVVPDEAGDR PSVRVPSKHI IPADAIVINK
ELGVGEFGVV QQGVWTNEEG ERIQVAIKCL SKERMQTQPM EFLKEAAIMH TIDSEHIVRL
YGVVLDTNAL MLVTELAPLR SLLECIKEPS LRVSFPVTSL CHFSIQICDG MSYLEGKRLI
HRDLAARNIL VFSKNKIKIS DFGLSRALGV GKDYYQTNFN VNLKLPIAWC APECINYLRF
TSASDVWAFG VTLWEMFSYG FQPWAALTGQ QILEAIDEPN FQRLEQPEAC PKEYYTIMLK
CWQHDPAKRP KFADLMDILP DCKPEQVQVV RDCEDPPTTP GGKRERLQYS VGDVITVLDK
RPVTDNPGVW KGVLNTGKTG HFNPANTVTY LGTNIPSNKS SFQRGDGKNP YSSRRRLRPE
MISGPQGDFK HTGHVGLDGA YFGDVSFLGD KYHQLPKQIV TPYKPSDDHD QSTSLTRASS
DVSDRAPLLK KVGDKGKSGP AAEHNWSDTA SEDQPDSPAR TRQSDHEYHE ISDEDEPLPK
VEPFRSSSFD LGPSLMDEVF KALGGSASSG PSSLDAPGSL PPLTPTQQSQ ALLEDNESHN
VKNEIKEMTN KFSNKECSKK KQAMVKPISA ADQRTLDSAI AMANALASKS ILELDRNLES
SADSDGVPDS PITPSSPSKQ GGSRFSFKFH CKGSPKPERR HFSAEAASIP DIQFRFALSL
FLSRLRGLLS ACSPLPAPSV PLRPIRPPGL SPGSLYLSYS LNCLSSAFSP SLLSLCRLVL
SAPAFPISAA SLSSCLLFRL HHLSFFSRVP ESMRCRWPAR RISLFCSRIC STLSLLFFRA
SSLLALSFSS VFLPAVASSL SPQSPSLFSV VVSLSHASFS HLLFLSLVSL SSVSSSISLS
SRSLRLSLSL SPLSSSLFPL PWTRPSLNSS SSFRPRASLS LFHVLLLSIS FPPLCIYLVL
IPSFLLFLHR SLPPSLSSTS LFLPPRSSSS FTPLSTVSRF LFDIPTLGPA HSFFFFFIFL
LLPRPHALYS VSFPCIYLPH YHSSSPPPRL TSLPQTLYSS LVSLSCSLPL SSSLVLLLLS
PLPLSYSRSS HSSSVSSPSP SLSLHLSLSL PLLSKPTILG GSKNPVSHTY PLYNQLVIII
IPSLTLSARA NTFTLSPLST PVPNPVSIFI IPSPWVTGGS GEVSLSVR
//
