YR818_MIMIV
ID YR818_MIMIV Reviewed; 1651 AA.
AC Q5UQG7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative serine/threonine-protein kinase/receptor R818;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=MIMI_R818;
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; AAV51078.1; -; Genomic_DNA.
DR RefSeq; YP_003987350.1; NC_014649.1.
DR SMR; Q5UQG7; -.
DR GeneID; 9925481; -.
DR KEGG; vg:9925481; -.
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 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1651
FT /note="Putative serine/threonine-protein kinase/receptor
FT R818"
FT /id="PRO_0000253996"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 793..1057
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1135..1278
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1394..1645
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1089..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 915
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1515
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 799..807
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 820
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1400..1408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1651 AA; 184362 MW; ACD50969F68DA309 CRC64;
MKSIGIFVVA LWLTHFCDGG QLGARIYSSG SESSVLLFDQ YINKYAFTNG DVKIIYEGKS
IFEILSETYV TDFNIFDRAI SQDNLDMFQI VQFPLAGQAI VMTYNLPELV NSSYRLVIDR
ETLGKIWYGA ISKWNDTAIQ NLNPTVGHLL PDTDIILGYS DDYIMTISGL IKMALSSFSP
EFDTELKYAN NTFNGMNPTK NGRGHNIGET STVRLEWLKK TSYGLTYINY ADVYNNGTDS
TVPMNMYNKA GYFVEPNLVS VQAAMSDFKI FYANNNSTID IYDAPGNKSW PLAYVNYLGC
SSAFGPMADC TRTIQMTNFI AWIYTNDAAS ESAIELQFYP LDKTLQKVAI DNLYNIKCNN
IAVLSQQYLI GFGAPISVMS LWPNSWTTVA STARYYSAPS SQALELQETY GADFGITVTG
VPNTYFNKMP DLGVMPLAAF TIVPAYNIPA INGTNGTLIL DYEIITDIYL GIINNWNDSR
IRALNGIEIN RKLPNVSITV IYQAVSSDYN FMFTDFMSKK SPKFAKKIGS TYFPILTLPN
NSMIITTDIY DVGNQLISNS NSFAFWPYFG ITMLSRQPTV QAASIRTEKG NIISSNSTTL
EKAINNFISK GGSIEDAPYI MGENDESWPL SALMTMIYRQ STIHYAAKAA AVADFAYWTQ
SNPTAINIAT IQGMYVASNN PTLKSRNLNL LKNFVVDGEP ISSIANCIYQ GTICSDMGTC
NNNSCLCNSY RKGIYCENIV SSSGESIGII LAIVIPVSFV ICCIIIVLVI ALIVSIRLHQ
RVEDEWEVDF HELDFMESLG SGGSGEVFKA MWKGTEVAVK KLVNSNITKD AERNFKQEIH
RMTSLRHPNV VLFMAASTRP PNMCIVMEFM SLGSLYDLLG NELVTEIPPV LRIRIAYQAA
KGMHFLHSSD IVHRDLKSLN LLLDSKWNVK VSDFGLTKIK DNNKGKSSTK EDSVCSIQWT
APEVLSEKQD IDYILADVYS FGIIMWELMT RLRPYIGLSP AAIAVAVIRD NLRPEIQEED
INLMSSDYVE LVNICWHKDT MIRPSFLEIM TKLSTLIGGS GITTGTSTSS SNQSSDYIGP
NIITRTKNIH NNDETKNSFG STTYGSNTIS SSSNTESDKI LSKLNKKKIP TGEVIIVFTD
IISAEQLWHH NPLAMKNATV LYNAVIRETL DKIGGYESFI YKDHNSGEGS FCLVFQEAID
AIDFCSISQK KLLEIDWPEE LLDHPAAASE KDINGTMIFA GPRVRMGLHA GTVKIMQDPV
TRRYEYSGVT VNIAAKITMM THGGQVIMSE QVTDKISNND CSNIKSLGQI EITDTNNYKV
NIFELRIEGL IGRFFGGVAF YNYDSVTEST DLDDTYPDSL NFSTNGILYG GIKQENEYLS
SAGLCRWIIN YDDIQIGKQI GVGSYGIVNM GKWKNINVAV KKFVKQKIDE KQMLEFRAEI
AFLSQLRHPH IILMIGACLK RPNICIVTEF MGNGSLRNVI KTTKPEWKLK IKMLYQTALG
IGYLHNSDPI IIHRDIKPSN ILVDDSMNVK IADFGFARIK EENSVMTRCG TPCWTAPEII
RGEKYTEKVD VFSFGIVMWE VLTCKEPFSG CNFMKVSMDI LEGARPQIPS DCPIDFTKLM
KQCWHAKPDK RPSMEDVIMG LNDMLGPEKS L
