ID Q8TPP5_METAC Unreviewed; 559 AA.
AC Q8TPP5;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN OrderedLocusNames=MA_1861 {ECO:0000313|EMBL:AAM05266.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM05266.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM05266.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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DR EMBL; AE010299; AAM05266.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TPP5; -.
DR DNASU; 1473750; -.
DR EnsemblBacteria; AAM05266; AAM05266; MA_1861.
DR KEGG; mac:MA_1861; -.
DR HOGENOM; CLU_006533_0_2_2; -.
DR InParanoid; Q8TPP5; -.
DR OrthoDB; 8087at2157; -.
DR PhylomeDB; Q8TPP5; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd05121; ABC1_ADCK3-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR Pfam; PF03109; ABC1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 527..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 129..461
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 559 AA; 63577 MW; 19F45306CA825052 CRC64;
MLHKRFRRYS MLKRYGQIIE VLQKYGFGYI VDQIGLGSFG DFTSRLKKQE KRDEHNLSGP
VRTRRILEEL GPTYIKLGQL LSMRRDLVPL EYAAEFSKLQ DDAPSFGFEE VELIIREELG
LPVEDLFESF EKKPLACASI GQVHRAKLKN GDDVVVKVQR PGIKEVIESD LDIMYSLSRL
LTEHIPEARL YRPVELVDEL SRSILAEIDY SQEGWNTDRF AENFKDSEQI HIPKVYWDYT
GTRVLTLEYI EGIKGGRVDL LEKQGFDRSA IALAVAGSFL KQVFEDGFFH ADLHPGNILI
MEDGIVAFLD FGMVGHLSSE TRDMFLNGMT AMVKGDSSLF VEVLRDMGGI DSHVDTKVLK
VDFDYFRSKY YGRALKNLDA SVIIEELIEV LRKNQVKVPY NITLLVRGTL AVEGFGLIID
PDLNLAELVE PYAKNAIKES FYPQNIARVL YDNISSWSRI FQRAPTKISH ILDNAENGYL
GIKLESEETK RLISEINTAS NRLSFSLIIS AIIVASSLIT QTNMKPLLWG VPLLGIFGFL
LASIFGMWLI FNIFRTGRI
//
