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Database: UniProt
Entry: Q7T6Y2
LinkDB: Q7T6Y2
Original site: Q7T6Y2 
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   16-JAN-2019, entry version 97.
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; dsDNA viruses, no RNA stage; 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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         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}.
DR   EMBL; AY653733; AAQ09578.2; -; Genomic_DNA.
DR   RefSeq; YP_003987364.1; NC_014649.1.
DR   ProteinModelPortal; Q7T6Y2; -.
DR   SMR; Q7T6Y2; -.
DR   PRIDE; Q7T6Y2; -.
DR   GeneID; 9925495; -.
DR   KEGG; vg:9925495; -.
DR   OrthoDB; 715at10239; -.
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:0016849; F:phosphorus-oxygen lyase activity; IEA:InterPro.
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   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; Pkinase_Tyr; 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; Complete proteome; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   1624       Putative serine/threonine-protein
FT                                kinase/receptor R831.
FT                                /FTId=PRO_0000041753.
FT   TRANSMEM    747    767       Helical. {ECO:0000255}.
FT   DOMAIN      786   1049       Protein kinase 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN     1109   1252       Guanylate cyclase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00099}.
FT   DOMAIN     1364   1615       Protein kinase 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     792    800       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND    1370   1378       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS    756    762       Poly-Leu.
FT   COMPBIAS   1052   1091       Ser-rich.
FT   ACT_SITE    908    908       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE   1487   1487       Proton acceptor. {ECO:0000250}.
FT   BINDING     813    813       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   BINDING    1391   1391       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    169    169       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    225    225       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    292    292       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    364    364       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    720    720       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    737    737       N-linked (GlcNAc...) asparagine; by host.
FT                                {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
//
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