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Database: UniProt
Entry: Q8THC9_METAC
LinkDB: Q8THC9_METAC
Original site: Q8THC9_METAC 
ID   Q8THC9_METAC            Unreviewed;      2951 AA.
AC   Q8THC9;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Cell surface protein {ECO:0000313|EMBL:AAM07927.1};
GN   OrderedLocusNames=MA_4588 {ECO:0000313|EMBL:AAM07927.1};
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:AAM07927.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM07927.1, 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).
RN   [2] {ECO:0007829|PDB:2L0D}
RP   STRUCTURE BY NMR OF 272-376.
RA   Cort J., Lee D., Ciccosanti C., Janjua H., Acton T.B., Xiao R.,
RA   Everett J.K., Montelione G.T., Kennedy M.A.;
RT   "Solution NMR Structure of putative cell surface protein MA_4588 (272-376
RT   domain) from Methanosarcina acetivorans, Northeast StructuralGenomics
RT   Consortium Target MvR254A.";
RL   Submitted (JUN-2010) to the PDB data bank.
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DR   EMBL; AE010299; AAM07927.1; -; Genomic_DNA.
DR   PDB; 2L0D; NMR; -; A=272-376.
DR   PDBsum; 2L0D; -.
DR   SMR; Q8THC9; -.
DR   STRING; 188937.MA_4588; -.
DR   DNASU; 1476482; -.
DR   EnsemblBacteria; AAM07927; AAM07927; MA_4588.
DR   KEGG; mac:MA_4588; -.
DR   HOGENOM; CLU_225877_0_0_2; -.
DR   InParanoid; Q8THC9; -.
DR   PhylomeDB; Q8THC9; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   CDD; cd00146; PKD; 12.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 14.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR011635; CARDB.
DR   InterPro; IPR018765; DUF2341.
DR   InterPro; IPR021779; DUF3344.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF07705; CARDB; 2.
DR   Pfam; PF10102; DUF2341; 2.
DR   Pfam; PF11824; DUF3344; 3.
DR   Pfam; PF18911; PKD_4; 12.
DR   SMART; SM00635; BID_2; 1.
DR   SMART; SM00089; PKD; 12.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF49299; PKD domain; 12.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50093; PKD; 12.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2L0D};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT   DOMAIN          382..451
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          467..545
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          550..617
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          942..1020
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1025..1094
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1108..1179
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1507..1590
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2040..2118
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2125..2195
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2210..2293
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2573..2656
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2660..2727
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2931..2951
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          2144..2170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2951 AA;  319560 MW;  A6301655D2222D25 CRC64;
     MTKPKVMNIS SKYAIYILPL LLILLLACTA SALPTVAHDK VQGEMYVSST ANWESKYSTN
     NFDVPNGTVV FARYYVGVWA SSATTTSIST IFNGNAFATN PSCYSSGMGV TWIPYDVTDY
     VVPGEINTAT INSASWGDGR QYGTTLVVVL KNENKSQIEY WIADGLDWLH YGDYVGDEVD
     NSFTYFNGTV DLADVQSANL YSTHLTGYNY EDFNGYSLSD PADSVSGDYF NYIRWDNVKA
     SLVAENQTVN VGRGGDAYCS PVFHALSIAY KIPDLVPVSL TPVTVVPNTV NTMTATIENQ
     GNKDSTSFNV SLLVDGIVVD TQTVTSLESE NSTNVDFHWT LDGTANSYTL TVNVDPENAV
     NEGNESNNTL TALVGTTTAP IPVADFTATP TAGEVPLTVN FTDQSANSPL SWTWDFNNDG
     TMDSIMQNPT YTYDTPGNYT VKLTVSNGGG NDEEVKTDYI FVNYKRPIVN FTANLTKGNA
     PLTVQFNDTS LNSPTVWYWD FGDNTISTEQ NPVHTYTAAG NYTVNLTVTN AGGSNSSIKT
     EYITVGSGVP IANFTANTVS GYTPLEIRFF DTSTINPTSW AWDFGDNTTS TEQNPVHTYI
     SPGLYTVNFT VSNDYGSDIK TKANYIYAGK CKFSQNISFS AGGQAIYQQD IMIHRTSGTA
     YEENAGGLKI WHVYLGDSCR EDYGDLRFTD ATGTQLTYYL WPDYTSEEAR FCVRLERADQ
     PGRLTICYGD PGATTTSNGN ATYFLFDQFD GTALDTTKWE PVQDNGISVS SGGLHISSGT
     GNFAEIFSRT AVPSGIILQF RIQSKTYSTS LGFGNRDYTD NGSSIGLESF SSSYNSAIYS
     GEAYSNLRWA PPRTWTSKST DGDIIPDTPG GYYTEELVIS PDEPLKERRD GEAWTNSTRY
     VGVSGTKPIQ IEHYRKYGKM DLDYILARAY SSTPPSALGL GPIANFTVNM TNGNAPFTVH
     FTDSSKNSPA TWIWDFGDNT TSTEQNPVHT YVVAGNYTVN LTVTNSYGSD TGVKTDYISV
     GSGVPVANFT TNKTGGNAPL TVKFTDTSTI NPATWIWDFG DNTTSTEQNP VHTYVVAGNY
     TVNLTATNSY GSNTCVKIGY ITVGSGVPVA NFTANVTGGY APLTVQFNDT STVNPASWSW
     DFGDGNTSTE QHPVHTYMSA GTYTISLTVT NTYGSGTETK VDHIYAGMYE YNQQISYSAS
     DRAVYQQDIV VHRSNGTAYE ENADGLKVWH VYLGDNCRDD YGDVRFTDVT GAKLAYYLWP
     DYTSEQARFC VRIENTDQPG TLTICYGNPG ITTTSNGNAT YFLFDQFDGT VLDTTKWELV
     QNNGISVSSG GLHISSGTGN FAEIFSRTTV PSGIILQFRI QSKTYSTSVG FGNRDYTDNG
     SSIGLENYDS SYNSAIYSGE AYSNLRWAPP RTWSSKSTDG DIIPDTPDGY YTEELVISPD
     EPLKERRDGG TWTNSTRYVG VSGTKPIQIA HYRKYGKMDL DYILARAYST TPLFASAFSG
     EQQTAAPPVA SFTATPIYGF PHTIQFTDKS FNFPTEWTWD FGDGTTSPEQ NPVHTYAADG
     NYTITLTATN EYGTDTETKD YEVVTLFAAS LTVSPSSVQL NQSETQYFTA VAVDQLGNVI
     SNTSINWSSS NETIGTIDSN GLFTANVPGK VNITASAEGV TGLAEVTVMK ASPDFIVSVV
     TSPMYPISHN TVTATIENHG SEDASEVTAN VTIAGNTTTI TVPALAIGSS TTISVKDTAR
     WHVGDLVPIT VVVDPGNEID EANETNNVYT KNATISATSQ RYNGGRFSDG YDKVNNLFYA
     EGNVGVAVAI SGNYGSQYGV SGVTLTRKFS ADDLDIPAGA TIKSARLYQG STWYGDPGFN
     LQFNGHETQE ADAKYGDCIN GQYAFDVTTY LNTTGDNIAV LTSTNSLNKY AYYATVLIVV
     YEADSEPYRQ IWVNEGSDCL LADYGADLAW GYTMFDNVST DSLFSARTIT VLESDDGDVN
     SINFNGESLP TIKTGGSDPT IKYFSVTDAL QGGENELGVT GPSYFNFANA VLEVTQVTAS
     EANFTANVTS GNAPLNVEFT DTSTGTPTSW TWDFGDGKNS TEQNPTHTYT AEGTYTVKLT
     VSNSFGSDSE EKTGYITAGS VVLAPVANFS VDQTTGTAPL SVQFTDESTN TPTSWTWEFG
     DGKTSTEQNP THTYETIGTY TVKLTATNYG GSNFTIKTDY ITVTSNVSAP VASFTFDENS
     GRVPFTVQFT DTTTGSVSSW NWDFGDGGTS NEQNPTHTYV TEGSYNVTLT ATGPGGSNTI
     TSTEPVVVSA PLTSDSYNGG IPLTNVQNGT VSGDLWYDSY YAMETSAQKA FTLPSYTDIK
     WARLYVDVYD GHMENNYRGN VEISIDADGD STYELQKNET FNTTYSFPGE GGTGPVWLSD
     HLNRVTSDYQ MWYDLTGEIS GQTVNVQAIT SKIDSNFDGR VKAMTLVVAY DDGDSDEVYY
     WVNQGHDTVN PLDTEYTGST SFGTSTLASG WSSANLTAIY LASVDGIYSF QGTTLTSGTP
     QGSYYGDNTW DVSSMLTAGE YSIFTYNKQE EKYYKIPLAL MSVKYAGSGP TAPTAGFSAN
     VTEGEVPLTV LFSDESTGSP TAWVWDFGDN ETSSEQSPVH TYSAAGNYTV TLTVTNAAGS
     DSEVKTDYII VSESSMPEEP VAAFNANVTE GEVPLTVQFS DESTGSPTSW FWDFGDGANS
     TEQNPSHTYP SAGNYTVNLT VENAAGSDFE LKSDYIEVSD ASGSTVTLYF DPTSSSVAEN
     ESTEISIVAS NFPAGLSGYN LTVAIDDPAV AEIIDIEYPT WALITENSTL PGTSIYMKTI
     DLEDSVKEGA ADVMLATLTV SGKESGSANL SIGVKRLEDD SGDSIEPALL AGTIEVTLLS
     PLPDQEYAPK DLDGDGLYED LTGNGEFSFV DIVAYFHNMD WIEENMPVEY FDFNGNGRID
     FDDVVDMFGM I
//
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