ID K7G7K1_PELSI Unreviewed; 3068 AA.
AC K7G7K1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000016262.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000016262.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; AGCU01046027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01046036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006117141.1; XM_006117079.2.
DR Ensembl; ENSPSIT00000016338.1; ENSPSIP00000016262.1; ENSPSIG00000014147.1.
DR GeneID; 102457610; -.
DR KEGG; pss:102457610; -.
DR CTD; 7204; -.
DR GeneTree; ENSGT00940000154766; -.
DR HOGENOM; CLU_000373_2_0_1; -.
DR OrthoDB; 2906033at2759; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 6.
DR CDD; cd14113; STKc_Trio_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF104; TRIPLE FUNCTIONAL DOMAIN PROTEIN; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 49..194
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1276..1451
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1463..1575
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1640..1705
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1953..2129
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2141..2255
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2522..2587
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2656..2746
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2767..3021
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2271..2523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2611..2631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 741..768
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 862..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1820..1839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2336..2351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2360..2377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2427..2442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2448..2479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2480..2494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2495..2523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3068 AA; 347042 MW; 2B666C429288236B CRC64;
MSSSTTTTST TSSSNAGEGA DEAAKDSADI AAFFRAGFRK NDEMKAMDVL PILKEKVAYL
SGGRDKRGGP ILTFPARSNH DRIRQEDLRR LISYLACIPS EEVCKRGFTV IVDMRGSKWD
SIKPLLKILQ ESFPCCIHVA LIIKPDNFWQ KQRTNFGSSK FEFETNMVSL EGLTKVVDPS
QLTPEFDGCL EYNHEEWIEI RVAFEDYISS ATHMLSRLEE LQDILSKKEL PQDLEGARNM
IEEHSQLKKK VIKAPIEDLD LEGQKLLQRI QSSESFPKKN SGSGNADLQN LLPKVSTMLD
RLHSTRQHLH QMWHVRKLKL DQCFQLRLFE QDAEKMFDWI THNKGLFLNS YTEIGTSHPH
AMELQTQHNH FAMNCMNVYV NINRIMSVAN RLVESGHYAS QQIKQIASQL EQEWKAFAAA
LDERSTLLDM SSIFHQKAEQ YMNNVDSWCK ACGEVELPSE LQDLEDAIHH HQGIYEHISL
AYSEVSQDGK SLLDKLQRPL TPGSSDSLTA SANYSKAVHH VLDVIHEVLH HQRQLENIWQ
HRKVRLHQRL QLCVFQQDVQ QVLDWIENHG EAFLSKHTGV GKSLHRARAL QKRHEDFEEV
AQNTYTNADK LLEAAEQLAQ TGECDPEEIY QAAHQLEDRI QDFVRRVEQR KILLDMSVSF
HTHVKELWTW LEELQKELLD DVYAESVEAV QELIKRFGQQ QQTTLQVTVN VIKEGEDLIQ
QLRDSAISSN KTPHNSSINH IETVLQQLDE AQSQMEELFQ ERKIKLELFL QLRIFERDAI
DIISDLESWN DELSQQMNDF DTEDLTIAEQ RLQHHADKAL TMNNLTFDVI HQGQDLLQYV
NEVQASGVEL LCDRDVDMAT RVQDLLEFLH EKQQELDSAA EQHRKHLEQC VQLRHLQAEV
KQVLGWIRNG ESMLNAGLIT ASSLQEAEQL QREHEQFQHA IEKTHQSALQ VQQKAEAMLQ
ANHYDMDMIR DCAEKVASHW QQLMLKMEDR LKLVNASVAF YKTSEQVCSV LESLEQEYKR
EEDWCGGADK LGPNSETDHV TPMISKHLEQ KEAFLKACTL ARRNADVFLK YLHRNSVNMP
GMVTHIKAPE QQVKNILNEL FQRENRVLHY WTMRKRRLDQ CQQYVVFERS AKQALEWIHD
NGEFYLSTHT STGSSIHHTQ ELLKEHEEFQ ITAKQTKERV KLLIQLADGF CEKGHAHAAE
IKKCVTAVDK RYRDFSLRME KYRTSLEKAL GISSDSNKSS KSLQLDIIPA SVPGSEVKLR
DAAHELNEEK RKSARRKEFI MAELIQTEKA YVRDLRECMD TYLWEMTSGV EEIPPGIVNK
EHIIFGNMQE IYEFHNNIFL KELEKYEQLP EDVGHCFVTW ADKFQMYVTY CKNKPDSTQL
ILEHAGAYFD EIQQRHGLAN SISSYLIKPV QRITKYQLLL KELLTCCEEG KGEIKDGLEV
MLSVPKRAND AMHLSMLEGF DENIESQGEL ILQESFQVWD PKTLIRKGRE RHLFLFEMSL
VFSKEVKDSS GRSKYIYKSK LFTSELGVTE HVEGDPCKFA LWVGRTPTSD NKIVLKASSI
ENKQDWIKHI REVIQERTIH LKGALKEPIH IPKTAPTTKQ KGRRDGEDLD SQGDGSSQPD
TISIASRTSQ NTLDSDKLSG GCELTVVIHD FTACNSNELT IRRGQTVEVL ERPHDKPDWC
LVRTTDRSPA AEGLVPCGSL CIAHSRSSME MEGIFNHKDS LSVSSNDASP PASVTSLQPH
MIGAQSSPGP KRPGNTLRKW LTSPVRRLSS GKADGHVKKL AHKHKKSREV RKSADTGSQK
DSDDSAATPQ DETIEERGRN EGLSSGTLSK SSSSGMQSCG EEEGEEGADA VPLPPPMAIQ
QHSLLQPDSQ DDKTSSRLLV RPTSSETPSA AELVSAIEEL VKSKMALEDR PSSLLVDQGD
SSSPSFNPSD NSLLSSSSPI DEMEERKSSS LKRRHYVLQE LVETERDYVR DLGYVVEGYM
ALMKEDGVPD DMKGKDKIVF GNIHQIYDWH RDFFLGELEK CLEDPEKLGS LFVKHERRLH
MYIVYCQNKP KSEHIVSEYI DTFFEDLKQR LGHRLQLTDL LIKPVQRIMK YQLLLKDFLK
YSKKANLDTT ELEKAVEVMC IVPKRCNDMM NVGRLQGFDG KIVAQGKLLL QDTFLVTDQD
TGLLPRCKER RVFLFEQIVI FSEPLDKKKG FSMPGFLFKN SIKVSCLCLE ENVDNDPCKF
ALTSRMGDVT ETFVLHSANP GMRQLWIHEI NQILENQRNF LNALTSPIEY QKNHSSGGGG
SSNSSGPSSC SGITSSSRSR PSRIPQPVRH HSPVLVSSAA SAQAEADKMS GMSIHNPSLP
PHSTSLETGL SQPGRHPPIA ETDGPERKAE QIPKMKVIES PRKTAGNVSG SADGAQKELR
GSLEDNRSRS NIGSLTLGKP RPGAISPMNS PLSTTFPSPL GKETFPPSSP LQKGSFWSSI
PASPASRPGS FTFPGDNDSL QRQVHRHSSH SKDTDRMSTC SSTSEQSVHS TQSNGSESSS
SSNISTMLVT HDYTAVKEDE INVYQGEVVQ ILASNQQNMF LVFRAATDQC PAAEGWIPGY
VLGHTSAVII DNHDGTMKKS TSWHTALRLR KKSEKKDKDG KREGKLENGY RKSREGLANK
VSVKLLNPNY IYDVPPEFII PLSEVTCETG ETIVFRCKVC GRPKASVTWK GPDHNTLSND
SHYSISYSDL GEASLKIIGV TTEDDGIYTC IAANDMGSVS SSASLRVLGP GSDGIMVIWK
DNFDSLYSEV VELGRGRFSV VKKCDQKGTK RAVATKFVNK KLMKRDQVTH ELGIMQNLQH
PQLIGLLDTF ETSTSYILVL EMADQGRFLD CVVQWGNLTE GKIRLYLGEI LEAVQYLHNC
RIAHLDLKPE NILVDQSSAK PTIKLADFGD AVQLNTTYYI HQLLGNPEFA APEIILGNPV
SLTSDVWSIG VLTYVLLSGV SPFLDESVEE TCLNICRLDF SFPDDYFKGV SQKAKDFVCF
LLQDDPAKRP SAALVLQEQW LQLGNSKNVD SIDISRLTSF IERRKHQNDV RPIRSIKNFL
QSRLLPRV
//
