YR831_MIMIV
ID YR831_MIMIV Reviewed; 1624 AA.
AC Q7T6Y2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative serine/threonine-protein kinase/receptor R831;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=MIMI_R831;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; AY653733; AAQ09578.2; -; Genomic_DNA.
DR RefSeq; YP_003987364.1; NC_014649.1.
DR SMR; Q7T6Y2; -.
DR PRIDE; Q7T6Y2; -.
DR GeneID; 9925495; -.
DR KEGG; vg:9925495; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR024370; PBP_domain.
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 Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF12849; PBP_like_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1624
FT /note="Putative serine/threonine-protein kinase/receptor
FT R831"
FT /id="PRO_0000041753"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 786..1049
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1109..1252
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1364..1615
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1054..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 908
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1487
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 792..800
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1370..1378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1624 AA; 182517 MW; E02C29A6D1159E87 CRC64;
MHSVYTKYTI ILILLVIYQG LPTNTQVASR IFGVGSKSSG PLYRQLIDIY SYTYDNAVFI
FEDLPIDVIL TQVDYIDYVG LDRCISHEYE EIFNLVQFPL AGQAIVMTYN IPELANLDTR
IVIDRQTLGK IWTGEISKWN HPDIIALNPT LNGTLPDKEI KLGYNDDGNV SISGIVQAAL
SSFYGNFATE FNNAGQLFAN MSFANESRCV NIGPSSRERF DWVKNTTYSL TFVNYADVFN
NTNPNISVMN MYNKAGNLVE PSLESVQFAM ADFKDEYSNN NFALDVFDAP GNNSWPLSYV
NYIVMSKRFF QLDCSRADVV LKFIAWVYTN TAASKALTQN QFYPLDNTLK KVSIDNIYIV
KCNNVSVSEQ QYLISFGGST SIVPSWLTAF TSGSIVAKYY STLSSNSIEL LTTHGCDFAV
TINGVDQKFY QEIEDLAVMP LAAFSIVPAY NIPEIVGKTL VLDIDVIVKI YLGEITNWND
TKIRNLNPEI SNYLPNAIIN VVVQNIESDI NQIFTKFLSQ ESEIFSQEIG QTYNPDLSLF
NSSVIFVDDI DGLGDELIDN KYSFGFWTDF GVRLLSRVQT VQMASLKIND DIIEPNYDTL
KNAISSESNQ IARSTNSNVW PITSMISIVY PETTMKNKDK AVAIAEFMYW TQYDPLAINS
ANNKGYYLAS SDPQLRSVVL DLLKNFKFED ESVSSYANCI YQGSICSNFG TCIESACICN
SSRTGTYCEK IITDSENNTL IIILATVIPI ACIFGLLLLT LLIVIIFLLK HRNTTNNDWE
IDFSELEIGE TLGTGGYGEV YKSIWKGTEV AVKLISSKHV SKDMERSFFE EVKIMTSLRH
PNVVLFMAAS TKSPNMCIVM EFMSLGSLYD LLGNELIPEI PYALKIKMAY QASKGMHFLH
SSGIVHRDLK SLNLLLDSKW NVKVSDFGLT KVKSELDKKK TNDNIIGTIH WIAPEILNDS
TEVDYILADV YSFGIILWEL LTREQPYKGM TPAAIAVSVI RDGMRPPISD EAVTAHSIEY
IDLIKQCWHS DTIIRPTFLE IMTRLSNILG DSSNMTSGTS SSSLSSGGIG KSITDSKSSN
SRSSVESSNT SNTFRGIDRH NSHPTGEVTV AFIDIISASK LWEYDPDGMC ESTKMYNEII
RRVTKKYGGY ESFISKDRNS GEGSFCLVFS DAIQAINSCE EMQLQLLNAN WPKKILQHPA
AAEEFDRTDQ LIFRGLRVRM ALHCGSVKIS QDPMTRKYQY SGSTVNITGK ITTLTHGGQI
IVSENLYQKV NNDFTFITVG KIDIPDYPSK MTLYEIKFEI LKNRFFGGIT YVNYNDDTDS
GTADDSNYDS GKIIDIDYMA DIDKEDSFLT SANMCRWIIN YDEISIGKQI GLGSYGIVFN
GKWKGVDVAV KKFVKQKLSE TQLLEFRAEM AFLSELKHSN IVTFIGACIK KPNICIVTEY
MRMGNLRDVL KNPDIKITFA NKLKLLYGAA MGIDYLHSSN PMIVHRDIKP ANILVDEHFN
VKIADFGFAR IKEDNTTMTR CGTPCWTAPE VIRGEKYCEK ADVFSFGVVM WEVLTGKEPF
AECNFMKVSL DILEGGRPII PSDCPHEFAK LIKKCWHAKA HKRPTMTEVV QQLMLITEQF
DHKV
