ID M4AEP1_XIPMA Unreviewed; 1190 AA.
AC M4AEP1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 65.
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:ENSXMAP00000012935.2, 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:ENSXMAP00000012935.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000012935.2};
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 AlphaFoldDB; M4AEP1; -.
DR STRING; 8083.ENSXMAP00000012935; -.
DR Ensembl; ENSXMAT00000012951.2; ENSXMAP00000012935.2; ENSXMAG00000012897.2.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156184; -.
DR HOGENOM; CLU_001965_3_0_1; -.
DR InParanoid; M4AEP1; -.
DR OMA; ESRMEHG; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 312..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 780..848
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 894..952
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 988..1022
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 367..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1190 AA; 136765 MW; 918EB81091687D72 CRC64;
MSFFNFRKIF KLGPDKKKKQ YEHVHRDVNP EEIWEIIGEL GDGAFGKVYK AQNKQNGTLA
AAKVIDTKTE DELEDYMVEI DILASCNHHH IVKLLDAFYF EGKLWILIEF CAGGAVDAIM
LELERPLTEP QIRVVCKQTL DALTYLHEAK VIHRDLKAGN ILLSLDGEVK LADFGVSAKN
TNTLQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADIWS LGVTLIELAQ IEPPNHEMNP
MRVLLKIAKS EPPTLMHPSR WSPEFNDFLR RALDKNVDNR WNSTQLLQHP FVTSVTDSRP
LRELIAEAKA EVTEEIEDGK EEEEEEEPDT PAAVPGHKRA PSDVSMASSE EEKVPPTPSN
LESVTEKIEA EPVEDRSSDK LSDEGLGTSE VDKMEDEKLN EVSASNEDLT PAPTETSRDL
TSQDSAKVQL DVDQTEEISG EAAVSKPDEA VDSQKPPSEV EEAEEPKETS EKMDIEEDTT
QDKMKLDEDK QQAGEGGAAN SVESQEITEG TTADEVAVGE EESKDLKKEI AEHMTVTEDR
IKNITDETVE NVDTNNSQSN LIDTKINGDI DSKSSVEESS TEAVLENRST ENQSEETKDE
VPKESELPKQ KNESKVEEEL EERAPSESNQ ISDDVKVTSE VSEHGVISQD VSVKEDGEKG
TQADEVTSQD GVSVQESETD SESRIEHGSP AVAKSDVEKD SDSGSSSAAD SNSLDLNLSI
SSFLSKSKEG GSISMQESKR QKKTLKKTRK FMVDGVEVSV TTSKIVTDND AKSEEMRFLR
RQELRELRLL QKEEQRAQQE LSNKLQQQRE QIYRRFEQET TAKKRQYDQE VENLEKKQKQ
TIERLEQDHT SRLRDEAKRI KADQDKELSK FQNMLKNRKK EAVQEVGQSP KHMRKELMKR
LKEDLALLQT AEEQEFLQKQ QQELDGALKK IIQQHKLEIA TIERDCLNHK QQLLRAREAA
MWELEERHLQ EKHQLLKQQL KDQYFMQRHQ LLKRHEKEME QMQRYNQRLI EELKNKQNQE
RVRLPKIQRS DAKTRMAMFK KSLRITVAAA MTPDQERERI KQFAAQEEKR QKSERLNQHQ
KHENQMRDLQ LQCDSNIREL QQLQNEKCHL LIEHETQKLK ELDEEHSQEI KDWREKLRPR
KKALEEEFTR KLQEQEVFFK MSGESECLNP TTQSRVSKFY PIPNLQNSGL
//
