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Database: UniProt
Entry: Q7T6X2
LinkDB: Q7T6X2
Original site: Q7T6X2 
ID   YR826_MIMIV             Reviewed;        1657 AA.
AC   Q7T6X2;
DT   17-OCT-2006, 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 R826;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=MIMI_R826;
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; AAQ09588.2; -; Genomic_DNA.
DR   RefSeq; YP_003987358.1; NC_014649.1.
DR   ProteinModelPortal; Q7T6X2; -.
DR   SMR; Q7T6X2; -.
DR   PRIDE; Q7T6X2; -.
DR   GeneID; 9925489; -.
DR   KEGG; vg:9925489; -.
DR   OrthoDB; 147at10239; -.
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     23       {ECO:0000255}.
FT   CHAIN        24   1657       Putative serine/threonine-protein
FT                                kinase/receptor R826.
FT                                /FTId=PRO_0000253997.
FT   TRANSMEM    742    762       Helical. {ECO:0000255}.
FT   DOMAIN      786   1049       Protein kinase 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN     1134   1277       Guanylate cyclase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00099}.
FT   DOMAIN     1399   1651       Protein kinase 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     792    800       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND    1405   1413       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS   1058   1065       Poly-Ser.
FT   ACT_SITE    909    909       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE   1522   1522       Proton acceptor. {ECO:0000250}.
FT   BINDING     813    813       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   BINDING    1426   1426       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    238    238       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    255    255       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    454    454       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    476    476       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    494    494       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    596    596       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
SQ   SEQUENCE   1657 AA;  186740 MW;  C43B8AA183A18312 CRC64;
     MRLNSQIVFC IVVVISCLSM IECKMGSRIY CSGSLSSVEL FSQYISNYAL RNDDVTIIYA
     GMSVDEINAD VYIADCSAYD RAIPQIYMIS YGLIQFPIVG QAIVIIYNVP GLSSHNMIID
     RETLGRIWTG NIRKWNDIQI QNLNPDIASQ LPNETITLGY NDAYYLSISE IMQLALRNFS
     EEFANAHTIA GGKFGNMIPA KQGYAIDAGE ASESRIDWVK NTPFSLSFAD FATVYPRNVS
     YMHMYNKAGK LVEPNITTVQ SAMADFKEIY TTNDFTIDIF DASGENSWPI SWVNYISMTS
     TFQQADCIRT KELLDFIAWF YMNNEIAEII KEYQYYPLDN TIKKIAIDNM YNVTCNGKVS
     QEHQYLIAFG SPLSIMASWP NTWASSMTTV KYYASLSDQA IELQKTFSGD FGITIKDFDK
     NKYLSSTMED IGVSHLAAFN IVPAYNIPEF IGLNETLVLN YETIVDIYLG LVTNWNDSSI
     RNSNNPYINS LLPNKTITVV VQKVESDVNE LFTNFLSCKS DKFNNAIGPT NLPEFDFVSN
     NVVYTEDVYG VGNTLVSTDY SFAFWPEPGI RLLSHMAIVQ AASIQTSTGT IIKPTNETLS
     KAVDNKINSI NRRDIEDGSW PFIAMMSLVY HQKTMQSFSK ASALADFIYW TQFDDTAASI
     ADTQGYYVAS IHPTILRENL ELLQSFTFED RTVSKVANCI FEGTICYNKG TCNNNVCLCN
     IDREGQFCEL EKTQSDTNIV TIILAVVIPI AFIIVCIICI LVVALIFSLR FRKGISDDWE
     IDFHELELGE QLGTGAFGEV HKGTWRGTEV AVKMISPDKT ITKDIERNFK DEVRVMTTLR
     HPNVVLFMAA STKPPKMCIV MEFMALGSLH DLLKNELIPD IPFALKVKIA YQASKGMHFL
     HSSGITHRDL KSLNLLLDIK WNVKVSDFGL TKFKSDVKSI NPEKFAGTIQ WTAPEILSED
     REVDYILSDV YSFGIIMWEL ITRDQPYFGM SPAAIAVSVI RDNYRPVISD QLRSEVAPEY
     IELLTSCWHF DPTIRPTFLE IMTRLSNLMG DSGMTGMSSS SSNSSKFDYN SFGKVQQFAI
     NRTDPDGIVQ NSYNRTDSYD LGSNNSHSSI TSDTNKSNKY LRQTNIQHPT GEVVVVFTDI
     ISAAQLWEFD ASEMKNATIL YNKLVRSICN ECGGYESLIS KERNSGEGSF CLIFSDVQNA
     ITFCEELQKQ LVGVNWSPKL LEHPITAIEK DINGTIIYAG LRVRIGLHFG STKINYDPIS
     RKYEYIGPTV TTAAAVTTIT HGGQIIMTED VANKLSTENS NKPVCLGRVD IDGIPDSLVL
     YEYVISALIG RFFGGVTRKN ASFVSNETST DYDDMDTDNS TFSARVPHQA YQYHAAIENN
     ERYLTSAGLC SWVINYDEIK MGEQIGLGSY GVVYRGKWKN VDVAIKKFIK QKIDENHLLG
     IREEIAFLKK LHHPNIITMV GASLKKPNIC IVTEYMAKGN LRDAMRTCTP KLEWHQKIKI
     LVNIAKGISY LHSFDPPIIH RDIKPSNILI DENWNVKIAD FGFARIKEEN AIMTRCGTPC
     WTAPEIIRND IYDEKVDVFS FGIVMWEVLT CKEPFIGANF MKITMDILED VRPKIPQDCP
     EEFAKLMRKC WHAKSTKRPT MDDVIIVLAK FCPDISV
//
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