ID A0A3Q2ZB27_KRYMA Unreviewed; 3066 AA.
AC A0A3Q2ZB27;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000000668.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000000668.1}
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 STRING; 37003.ENSKMAP00000000668; -.
DR Ensembl; ENSKMAT00000000698.1; ENSKMAP00000000668.1; ENSKMAG00000000255.1.
DR GeneTree; ENSGT00940000154766; -.
DR OMA; IGFRRNE; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.
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 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; IPR017441; Protein_kinase_ATP_BS.
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:SF210; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 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; 7.
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; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 56..202
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1283..1458
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1470..1582
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1647..1712
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1963..2044
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2513..2578
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2647..2737
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2760..3015
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1597..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2280..2514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 744..774
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1619..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1832..1849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2429..2448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2457..2476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2486..2514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2789
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3066 AA; 344898 MW; 724C05AEB2975780 CRC64;
AAFSRRFARA PCTPSQCCLT ARPQRCRGSF QEKKKQTPRA LNQIAASRNE EMRAMEVLPI
LKEKVAFLSG GRDRRGGPVL TFPSRSNHDR IRADDLRRLI AYLASIPSEE VCKHGFTVIV
DMRGSKWDSI KPLLKILQES FPSCIHVALI IKPDNFWQKQ RTNFGSSKFE FETTMVSLEG
LTKVVDPSQL TSDFDGSLDY NHEEWIEVRV AFEEFSGHAT QMLTRLEEMQ ETVSRKDFPQ
DLEGARRMIE EHAALKKKII KAPIEELDTE GQRLLQRIQS SDSSSSGGVC NSDTQGLVPR
ITQLLDKLHS TRQRLHQAWH VRKLQLDQCF QLRLFEQDAE KMFDWIMHNK GLFLASYTEI
GNNHPHAVEL QTQHNHFAMN CMNVYVNINR IVSVGSRLLE SGHYASQQIK QISGQLEQEW
KAFAAALDER STLLEMSASF HQKCDQYMSN VDSWCKACGE VDLPSELQDL EDAIHHHQGL
YEHITAAYSE VSQDGKALLD KLQRPLTPGS TDSLTASANY SKAGHHVLDI IHEVLHHQRQ
LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH
EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV RRVEQRKVLL
DMSVAFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT LQVTVNVIKE
GEDLIQQLRD SAISSNKTPH NSSINHIESV LQQLDEAQAQ MEELFQERKI KLELFLQLRI
FERDAIDIIT DLESWNEELT GQMNDFDTED LTLAEQKLQH HADKALTMNN LTFDVIHQGQ
ELLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQR ELDLAAEQHR RHLEQCVQLR
HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT HQSALQVQQK
AEALLQANHY DMDLIRDCAE NVASHWQQLM LKMEDRLKLV NASVAFYKTS EQVCSVLESL
EQEYKREEDW CGGADKLGPN CETDHVTPMI SKHLEQKEAF LKACTLARRN ADVFLKYMHR
NSVNMPGMLS HVKAPEQQVK NILNELLQRE NRVLHFWTMR KRRLDQCQQY VVFERSAKQA
LEWIHDTGEF YLSTHTSTGS SIHHTQELLK EHEDFHITAR QTKERVKLLI QLADGFCEKG
HSHAADIKKW VTAVDKRYRD FSLRMDKYRC SLEKALGIPS DSNKASKDLQ LDIIPATAPG
SEVKLRDAAA HELNEEKRKS ARRKDFIMTE LIQTEKAYVR DLRECMDTYL WEMTSGVEEI
PPGIVNKEHI IFGNMQDLYE FHHNLFLKEL EKYEQLPEDV GHCFVTWAEK FQMYVNYCKN
KPDSTQLILE HAGNYFDEIQ QRHRLANSIS SYLIKPVQRI TKYQLLLKEL LTCCEEGKGE
IKDGLEVMLS VPKKANDAMH LSMLEGFDEN IESQGELILQ DSFQVWDPKT LIRKGRERHL
FLFEMSLVFS KEVKDSNGRS KYIYKSKLFT SELGVTEHVE GDPCKFALWV GRTPTNDNKI
VLKAFNIENK QDWIKHVREV IQERTIHLRG ALKEPIHIPK ATTAKHHKGR RDGEDLDSQG
EGSSQPDTIS LASRTSQNTL DSDKLSGGCE LTVVIHDFMA SNSNELTVRR GQTVEVLERC
HDKPDWCLVR TTDRSPAQEG LVPCSMLCIA HSRSSMEMEG IFNHKDTLSV CSNDSIMPGS
SATLQPGHGI GSHSSPGPKR PGNTLRKWLT SPVRRLSSGK ADGHVKKLAQ KHKKSREVRK
SGEMTMGSQK DSDDSAATPQ DEILEERVRN EGLSSGTLSK SSSSGMQSCG EEEGEEGADS
VPLPPPMAIQ QHSLLQPDSQ DDKTSSRLSV RPSSSETPSA AELVSAIEEL VKSKMALEDR
PSSLSVEQGD SSSPSFNPSD NSLLSSSSPI EEMDERRASI LKRRHHVLSE LVDTEREYVR
DLSLVVEGYM SRMKEEGVPD DMKGKDKIVF GNIHQIYDWH KDFFLRELEK CLEDPDRLGP
LFLKQVCPPN SSIKAPLLRL TCYFLFPSQF LIHKPSHHLY IKNKLKRKAL TFFNLSLFQK
AVEVMCIVPK RCNDMMNAGR LQGFDGKIVA QGRLLLQDTF LVSDPEGGLL GRMKERRVFL
FEQLVIFSEP LDKKKGFSLP GFLYKNSIKV SCLGLEESVE GDPCKFILTS RSTSSTMESF
VLHSSHPGVC EVWTLQISQI LESQRNFLNA SISPAEYQRN HVGAGDGPCL TAIEAAGGGG
SVTSVSPVVG SGNNQSSTVP SGPQTGSRRP SRIPQPSRLP QPLRHQPGAD AEGPNKMLGS
SPRAVPPPLL PPGGSPQGKR PSQTPEDHTQ TPTPASAVNP IPRAKVGPLP STPTSKARPG
AVSPVASPLA TPAFGKDALP PPPPSPGQKS GSGFWSSMPG SPASRPSSFT FPGEAGETPV
RQNSNQISAG SGSQTHRHST HSKEADRMST CSSASEQSIQ STQSNGSESS SSSSVSTMLV
TQDYMAVKED EISVVQGEVV QILASNQQNM FLVFRAATEQ GPAAEGWIPG FVLGHTSAHV
PDCSEGPIKK SSSWHTSLRI RKKSEKKEKE PKKEIKLENG YRKSRDGLAN KVSVKLLNPN
YIYDAPPDFL VPLSDVTCDN GESVTLRCKV CGRPRATVAW RGPNQSNLTN NGHFSLAYSD
AGEATLRIIG TASEDDGVYT CIATNELGNA TTSASLRVLG KGVSTDGRRV SWKDNFESHY
TEVAELGRGR FSVVKRCDHR GTKRTVAVKH VNKKLMKRDR VTQELNLLQR LQHPHIVSLL
DTFETSGSYA LVLEMADQGR LLDYIVSWGN LTEEKVAGYL RNVLEALHYL HNCRIVHLDV
KPENLLVFHS SSGQPTVKLT DFGDAVQLNS AHYIHPVLGS PEFAPPELVL GDPVSLTSDL
WSLGVVTYVL LSGASPFLDE SAEETCLNIC RLDFSFPRDY FQGVSQVARD FVCLLLRSEP
SRRPPAGLCL QEPWLQAGPG DGRGRAEGCL DTARLISFVD RRKHQTDARP IGGIRSFIQS
RLQSRV
//
