ID G8EBS4_9VIRU Unreviewed; 1651 AA.
AC G8EBS4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:AEQ61033.1};
GN Name=MAMA_R949 {ECO:0000313|EMBL:AEQ61033.1};
OS Acanthamoeba castellanii mamavirus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus.
OX NCBI_TaxID=554168 {ECO:0000313|EMBL:AEQ61033.1, ECO:0000313|Proteomes:UP000240353};
RN [1] {ECO:0000313|EMBL:AEQ61033.1, ECO:0000313|Proteomes:UP000240353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hal-V {ECO:0000313|EMBL:AEQ61033.1,
RC ECO:0000313|Proteomes:UP000240353};
RX PubMed=21705471;
RA Colson P., Yutin N., Shabalina S.A., Robert C., Fournous G., La Scola B.,
RA Raoult D., Koonin E.V.;
RT "Viruses with more than 1,000 genes: Mamavirus, a new Acanthamoeba
RT polyphaga mimivirus strain, and reannotation of Mimivirus genes.";
RL Genome Biol. Evol. 3:737-742(2011).
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DR EMBL; JF801956; AEQ61033.1; -; Genomic_DNA.
DR SMR; G8EBS4; -.
DR Proteomes; UP000240353; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13999; STKc_MAP3K-like; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
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 PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
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; Nucleotide cyclase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEQ61033.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 747..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 793..1057
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1135..1278
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1394..1645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1089..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
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
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