YR826_MIMIV
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 03-AUG-2022, entry version 107.
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; 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; AAQ09588.2; -; Genomic_DNA.
DR RefSeq; YP_003987358.1; NC_014649.1.
DR SMR; Q7T6X2; -.
DR PRIDE; Q7T6X2; -.
DR GeneID; 9925489; -.
DR KEGG; vg:9925489; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1657
FT /note="Putative serine/threonine-protein kinase/receptor
FT R826"
FT /id="PRO_0000253997"
FT TRANSMEM 742..762
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 1134..1277
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1399..1651
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 909
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1522
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 1405..1413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
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"
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
