ID A0A142CJL8_9VIRU Unreviewed; 1473 AA.
AC A0A142CJL8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AMQ10630.1};
OS Brazilian marseillevirus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Marseilleviridae; Marseillevirus.
OX NCBI_TaxID=1813599 {ECO:0000313|EMBL:AMQ10630.1, ECO:0000313|Proteomes:UP000203790};
RN [1] {ECO:0000313|EMBL:AMQ10630.1, ECO:0000313|Proteomes:UP000203790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH2014 {ECO:0000313|EMBL:AMQ10630.1,
RC ECO:0000313|Proteomes:UP000203790};
RX PubMed=26978387; DOI=10.3390/v8030076;
RA Dornas F.P., Assis F.L., Aherfi S., Arantes T., Abrahao J.S., Colson P.,
RA La Scola B.;
RT "A Brazilian Marseillevirus Is the Founding Member of a Lineage in Family
RT Marseilleviridae.";
RL Viruses 8:76-76(2016).
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DR EMBL; KT752522; AMQ10630.1; -; Genomic_DNA.
DR RefSeq; YP_009238627.1; NC_029692.1.
DR GeneID; 27112035; -.
DR KEGG; vg:27112035; -.
DR Proteomes; UP000203790; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13999; STKc_MAP3K-like; 2.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028081; Leu-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF13458; Peripla_BP_6; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AMQ10630.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000203790};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AMQ10630.1}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 755..1009
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1220..1467
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1013..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 782
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1473 AA; 162912 MW; B8086349FA110D76 CRC64;
MLRGSFFALL FLLSFAQMSQ TQVVISTTAA RSGPAVGIGG LIEGLQTAMF AANNKTTDDR
NGVLKTRNLE FLVLDDQQDY LQAVNNLQHL FSFPEDELLA ITCLAPMQTA IVQSFPPQVS
PPPLFGSFSG DVKLYTPFSR NYLNLRPSFD TEFYVMAQFL TSNLRVSRIA FVAGAGLDGT
SLNFTRSIEP FGLRVVAGHV IPDYTVISGP MMDEAVQIIT SANPQAIVIL LFGPQSAEFI
RRCKQILPNL VFIIETLVMN DTPNELWLTG DSANVYSLSP FPLLADNNSQ LQNEFYRDQE
AYFPQWTPAA EQAIEGYVNG RWIISILEKM TGNVTRKNFL ETVFSNPIIK IGEVFFGPLG
DDCESIIGCC NSATRQMYVF KYPNGYGEYA TEKPISWSSC NPTTLDFQVP TKLGQTLNVS
EASLRLGIPQ SSGFILLSYD DRGEQQLVKS NIDELERLDN VPLFISLPLE KALLVEKPVF
GVTPLPQEFK ENFFSVTLSP KEELWAVLQK GIGSSFADPF NSFADFLVAL ESFGKTQGEE
VVLVVGEKTS VFSKYPGSKF VFLSCLHPEV VVQEATSSGV SMNNILFASS IPFFQVQNIS
LTQEFTGNSQ AEFWSFVNFK FVQKVASGEF SSSRIETNVW SLLSTDLGGF VIGGYSNVCP
EGSELECCNK GSRTVFFANG DFGDEGSMNV PFCNAKFSAS STSSSSDNTG AIIGGVIGGV
AAVLLLCCLF AALVVFLVLS KRERKQEWDI DFAELECSKL IGEGYSGQVF EGTWKGQEVA
IKVLKSQTPT KKAVEEFKLE ASVLANLRHP NIILFMAACT KPPNMCIITE HMPLGSLFDI
LHNELIPAFP EGLAIKVATQ AAKGMHFLHS SGIAHRDFKS LNLLVNEKWD VKVSDFGMAS
FLKDGQVGIG TVFWTAPEIL NEEQNCDLQK ADVYSFGVVL WEMLTRKAPF EGKTPAMVAV
SVIRDDERPE IPKSSPFDQG YLELMINCWE KDPDARPTFL EVLSRISGLS PIGSSTNKSN
LSSTSSMDSE RTTRNTGKYP EPDEYVSLAL IDIVDAFSFW EEEPENAREV FTKFNSVCRA
SAEKYGAYES FVQGMEKGEG CILFVFSSEK SAMFCCEEIF ETLNETSWPG KCRAGIASGC
VLAKKGIPPV LFGETTEKLK KLCESALPGQ IQVDRVSSCR DFKRIQDSQR IFEEDEGSSV
KVSGLLSINT SRFVLNFKDI SIGKQIGLGS FGACFAGTWR GVDVCVKRVV DQNMNEDAKL
RFREEASLLA KFDEHKNIVT FVGACYQKPN ICLVTVLETP GDLGKVLASD ARIDMQTKKK
ILYGVCSGLG FLHSKNILHR DIKSSNVLVD EQWNAKISDF GFARLKESCA TQTSCGSPCY
TAPEILRGEK YDEKADIFSL GVLIWEVITR KIPYEGDSPI RVAEKVRDGK RLTVPFDCPK
RIRKIIQKCW DEFPDQRPSA LEVSLVFAEE EQV
//