ID M3ZMS4_XIPMA Unreviewed; 2109 AA.
AC M3ZMS4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000003517.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000003517.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000003517.2};
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};
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DR Ensembl; ENSXMAT00000003522.2; ENSXMAP00000003517.2; ENSXMAG00000003487.2.
DR eggNOG; KOG0584; Eukaryota.
DR GeneTree; ENSGT00940000155474; -.
DR HOGENOM; CLU_000550_0_1_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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 CDD; cd14030; STKc_WNK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF46; SERINE_THREONINE-PROTEIN KINASE WNK1; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 281..539
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1797..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2067..2109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..945
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2086..2109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2109 AA; 224421 MW; D1AC3A2C8333D99B CRC64;
MSESSNKAVK FLSPHPPASS DSPCPSPQTP HKNVNGSASS DSHVVEKIGE QPEVRRRRHT
MERDSKTAEH RFFRRSVICD SNATALDLPS KATVLLTSPP DCEGTTLFFT PQIYRSEEQE
PEGEKNARGS YLQGTGFQPY SDRGGLVSQG HAHHAEEDLK VITVVVPTTS SADYGAKGPT
KEPTPTVLDV TDRVAGKQPD VKLCARGMQE TQCLSKDDKV DKPALEGNIS SPIEEKDQET
EEERGQAKAR AEQREAEKRV QEDIEEAETK AVGTSPDGRF LKFDIEIGRG SFKTVYKGLD
TETTVEVAWC ELQDRKLSKS ERQRFKEEAG MLKGLQHPNI VRFYDSWEGL CKGKKCIVLV
TELMTSGTLK TYLKRFKVMK IKVLRSWCRQ ILKGLHFLHT RAPPIIHRDL KCDNIFITGP
TGSVKIGDLG LATLKRASFA KSVIGTPEFM APEMYEEKYD ESVDVYAFGM CMLEMATSEY
PYSECQNAAQ IYRRVTSGVK PASFDKVAIP EVKEIIEGCI RTNKDERYAI KTLLNHAFFQ
EETGVRVELA EEDDGEMIAI KLWLRIEDVK KLKGKYKENE AIEFSFDLNR DVPEDVAQEM
VESGYVAEGD HKTMAKAIKD RVSLIRKKRE QRQLVREEQE KRKLEAEKRQ QEAFKAPHTQ
SKTEETEAEQ LHHQQTGLSH TSEGGLDSGQ GSSVFSSDSP HLGQLTMSYS CPPTSQPPSQ
PQTPYPQTPT VASHQHPGYS QPPQPMQVQT PTPKPSSGTP LVPAATQPDP TGTSLQAVLS
GQSSVSLQSP THTTLQQTSA QPSLPPPTST VPMATLPSPS ALPTPVVPSL PSPLPIPVGV
VPTLVLSPLP PVPTPVPQPL ATVVPVISVV TVPPDSPMEA PPKSASQASE GQLQPPQVLS
SIESHSETSG LSDGNEGGAG RHEGRSTKRH QRRSVRSRSR HEKTSKAKLH VLSISNRGDR
VAECQLETHN RKMVTFRFDL DGDNPEEIAQ IMVESEFILE SERESFIEQV REVIENADQK
GDTGGQMIGD KEEQIPARSG PMPDIPPSAT SQVVHSAGRR FIVSPVPEGR LKDQTLPPSP
TPAPPTPSEA AQSDTPGQML VLSQSAGAVT LQQAFSELRQ SKNQYDAGPN TAPASVHSTH
PPLQPAAVAA SPHSSVVTPS VDSSLNQVKE QLTEAPPLSL SSTSAPPVSF SPPFSSSPPP
TAVNQIILQS QPVMQAASRP QAQSQTQTQP PAYIQPQTVS TASQPTSVPT ASISSIPPTV
LTSSLLGQTV PFVSSPPSSA LKLSSDNPSV SPTSASAIPT TTIPGPQISP PSSAPPVPAA
GLSTSVGLQP VTTTVPPVQP TLVHSQPQTA VLPGQTHTHC GECDTRTEAS SESVGKPDDI
QALDMKLRSL FMDLGGGVPS TQGDILPAEA ASGAAAAGTS SPISAGPTST TSVTAPVSTQ
SVNPPLPPSS LALGPLGSAA PMQGPGTPVA TPASSIIPAS SMGQTTPSKT PLSRVPATSP
SAELLTPFPG PCLIQSQQPL EDLDAQLRRA LSPETVPVSH SSVPSIGQPI PFSLEEGKAA
SPAPLPTGGI KLGRFQVSLA AEEPAVQRPS CTESSSTTSS TSSSSSSSSL SSPENTLHKD
SPSRLRGKGV KGGDVVDGLP QKTPAGSHLI SPLGSPCLSP KPTTTIGRFQ VTTNSETRVG
RFSVSCAQEQ NQEPKQSPPP AARVAANGPS NPGQVLSPDS PHKASLPSLN NNSFNNSYMS
SDNDSEFEDE DFKQEVRGLR EKHIREIQAL HSRQKEEIEC LFTRLGKVPP AAVIPPLIAF
TGRRRRPTKS KSSKSSRSSS THGSKSPLQP GSTLSAQSVP AVYPGQLPLL APGVLADTVL
QPLKQSASSG NLCSAYTSEA ALSVPSLCAP TPGTNSTNAV SGSEGLGQSQ GGSQCLAPNM
PAPHQRKGTF TDDLHKLVDN WARDAMNLSQ GKRSAKQQQL QQAPAQGHSY EVTQSASLGR
KYSAPSQLCP CSIGGSAHLP ANPTSATSLA ARKGSLCNPP ASSALPQLQP PQFIPYAPSA
AYTTQWCGPA HSMTNPQQAP PQPLLVSASQ PLGPYAPPQG HLPGQGPYLL TTTLQKSVSS
PGGPNMRTT
//
