ID A0A3Q2ZMS4_KRYMA Unreviewed; 1964 AA.
AC A0A3Q2ZMS4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSKMAP00000004290.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000004290.1}
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000256|ARBA:ARBA00025760}.
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DR RefSeq; XP_017272669.1; XM_017417180.1.
DR STRING; 37003.ENSKMAP00000004290; -.
DR Ensembl; ENSKMAT00000004373.1; ENSKMAP00000004290.1; ENSKMAG00000003224.1.
DR GeneTree; ENSGT00940000158164; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR Gene3D; 1.20.5.1010; TRPM, tetramerisation domain; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF15; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 6; 1.
DR PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 861..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..950
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1063..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1699..1933
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 554..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1964 AA; 222918 MW; E3B6FF21C9560B31 CRC64;
MKSRDLSRTE PQSTDMSRKS WIEETFFKRE CVKFIPSSWD LHRCVPVCQV CQSLIRCCCG
RLMGEHSWQE SVPPISLYPG PGQGMKENWS MEVHTKASPT NAYGIIDFQD TATRVCRAKY
VRVAVDSKPD ALLQLMLREW QMERPKLLLS VHGGSENFTL PPKVKQAFSK GLITAALSTE
GWILTDGINT GVSKYVGEAV KIFGGHDLRK RNTIGITPWG MIDNNVDLIG RDVFRPYQLL
GNPLSKRACL NRFHSHFLLV DNGMLGKHGC QQGLRRKLEK HIHLQRIHPR LNQGVPVVCV
VVEGGPAIVS TVLDYVSSVP PVPVFVFEGS GKAADLLAFL HKQTANNREL DADIKEDFLV
RIGDVFGVER TEATRLYGLL QQCMDHRLSI TIFDSESEDQ TAPDAAILSS TLKGTKASPA
EQLSMALAWD RADIAQKDIL VYGQHWQVGS LEQAMLDSLV MDRVSFVKLL IDNGMTMSRF
LTVDRLEELY NTHQGQTQRF MHHLVEDAKQ TSLPIGYRVS LIDMGTVIEY LIGGAYRSTY
TRKNFRAAYN RLQNKAQQSS SGSFPKQRRG LSSKKNRSLQ DLHFFRTAQP YKPKEEQSAP
PVNSHKMALS PDFGGALLPC PFNFNDLFVW AVLQQRQQMA LFLWQHGEEA LARAVVACKL
YRSMAFEARQ SNMDDNMAER FKTFSLEFGQ LAVDVLDCSF RQNEQMAMKL LTSEMEAWSH
FTCLQLAVSS CHRPFVSHSC TQTLLTDLWT GPLNMRKNSF LKIILSLLLP PAILLLEFKS
KAEMCHVPQS HEAMPFGLES VKSLPAAEGS DHTDCRDAER GLSIQDKCGG PVSETVSSVS
AQWLSWIRRV YEFYTAPVVK FWFHTMSYLA FLMLFSYVVL VKMEEKPSVQ EWLVIVYIGS
TALEKTREVL MSEPRKLSQK LKIWFSEYWN ISDFIAIALF LFGFSMRWFG DRTTGRISYC
LDIIFWFVRV MDLLAVNQHA GPYLTMITKM TSNMFFIVVM MVIVLLSFGV SRKAILSPDE
EPSWCLAQDI VSQPYWMIFG EVYAGEMGGE SFLALFLQAV YMFFQYIIMV NILIAFFNNI
YFDMASTSNK LWRYNRYRYI MTYLERPWLP PPLILFSHVA LAVGGIFGRF RRDAEREEAG
SGLKLYLGHE DRKKLYEFEE KCVEVYFYEK NEDVHSSQLN RIRATAERAE EMCGMMGEVS
EKVNFIQHSL SELDSQLGQL QDLSALAVDT LTLLSASDNL YQEEARLAQC RLVTASHRAL
PHSWTLPHRS GTDSDGSNSR RTMVKACMST PPSLLKCSAL TGSALASQEC HKGVRGGKEE
KQEQSEPGPE IDEGSHCSAV EHPSENWLGG SRPASRTFFS QFYGGSVHNP AARNQMPSES
CESSRCGSPL SPRGFGLPHN RPWTCDPYLY PNQRKPFMEE GEEEEAEKEE NEKETSPKQL
SNVEDDIQPR HSSHWRRPAL SPRWAFMPRD RPYGFCRSLS SSMENMTFYG APLSPKKDSF
PSLDEPKNKD CLYGKSGFRD DTSLQCSRSQ EWAKSSDFTS AMDSRGKSHK RKMVKIKESP
PDMTVQSNPS GASWKKRQRF FGEATCWSAS TSLSQLHFDS SEMMQKQMSS HQDMWSPTHS
AWNSWAKSMS RRSSLQSCAA PEVKSSSFQS SDNLYPHFSA MERNNLMRLA HTIPFTPISM
FGGEEVSVYS LEDVPSDSEP ESRSVSWSSR GHSAMLQPLS SEEGSLDGGL RQGCRMICTW
AEQDVLKPGM VYVVKAFKTE VVRAWQRYFH GSTALQLCLR EIQQQRAAQK MMQVFNQIKP
DDMHHSPRFL DVSLVLWHSN GQWLTIERNL TGDFRKYNNN TGEEITPCCS LEDMLLAFSH
WTYEYSWREL LLLDIQGVGE ELTDPTVIMA DYQSGGRNEM LFGPDNLGDA AISGFLQKHT
CNFCCHRLGL KDSSNKSNQI IHAGCMDFLP GLFKEAFGQL REQQ
//
