ID B8GFQ1_METPE Unreviewed; 1387 AA.
AC B8GFQ1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=PKD domain containing protein {ECO:0000313|EMBL:ACL17934.1};
DE Flags: Precursor;
GN OrderedLocusNames=Mpal_2670 {ECO:0000313|EMBL:ACL17934.1};
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL17934.1, ECO:0000313|Proteomes:UP000002457};
RN [1] {ECO:0000313|EMBL:ACL17934.1, ECO:0000313|Proteomes:UP000002457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c
RC {ECO:0000313|Proteomes:UP000002457};
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:e01280-15(2015).
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DR EMBL; CP001338; ACL17934.1; -; Genomic_DNA.
DR STRING; 521011.Mpal_2670; -.
DR CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR KEGG; mpl:Mpal_2670; -.
DR eggNOG; arCOG02508; Archaea.
DR eggNOG; arCOG03991; Archaea.
DR HOGENOM; CLU_255164_0_0_2; -.
DR OrthoDB; 103676at2157; -.
DR Proteomes; UP000002457; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR CDD; cd00146; PKD; 10.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 13.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR041342; CMB_fam35.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR36842; PROTEIN TOLB HOMOLOG; 1.
DR PANTHER; PTHR36842:SF1; TOL-PAL SYSTEM PROTEIN TOLB; 1.
DR Pfam; PF18099; CBM_35_2; 1.
DR Pfam; PF18911; PKD_4; 12.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00089; PKD; 14.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 13.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 12.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002457}.
FT DOMAIN 49..125
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 160..238
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 344..432
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 441..509
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 527..604
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 635..687
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 704..772
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 788..871
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 870..955
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 985..1039
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1041..1124
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1143..1281
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1305..1387
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 1290..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 143142 MW; E247184F13ADFDA8 CRC64;
MRLPKSNPSG RLFLVSLMVI MACLLIPGAF AASATADHTN DKGYGGIGPI VNFTVDHSSI
TAGDSVKFTD TSYDNITSQA WDFGDGSISL DANPTHTYTA AGTYVVALNV QNATGYASNT
SGMTVNGYTL PSITVASVQD VAPQFNIGLN GNTYGVFGAT GSASTFSNAT VNVGDALTFT
DASTGVPTTW SWNFGDASDL ITTQNATHTF TQAGTYVVYL TAGNVNGQKT SNSLTIVVNG
GIAPVSAFTA SNNGVENSSV AGTPDYANAA YLNGTAPMTV SFTDKSTKVP SSWSWTKNGT
VFSTEQNPSL TLNQGQYQII LNATNAQGSN LSSIWINVAG PSTPIAHFVA TPSTGTAPLS
VQFNDTSDGG LAAPTSWLWN FGDGTQGSTV QNATHTFTAA GTYTVTLQTR NGAGVSTPFT
GTITVNSPTT PSANFKINGS TADNYAQNPV TILVGQPVYF NDTSSGSPSS YNWIFSDGQP
VPTQANVSRS FSVPGTFWVY HTVTNAAGSD SKLNLFTVTV APVTAAPVAS FTKNATDGEA
PLTVLFTNTS TGAPTTFQWL INGVQQGTDA NLTYTFATPG TYSVVLIASN AGGSSAAAAQ
TVTVSGVSGI PNANFTFTSP SFAAPSQVQF TYAGGNATQF LWTFDDGTTS TEMNPVHTYQ
NAGTYSVRLT TTNAKGTNYK INDVTITPLG NPVASFNANT TAVTKASAAS AQVSGQSPFT
VVFNDTSSER PTAWYWNLGD GTTSTSQNIT HTYTTPGKYA VYLVVANSLG ASDYVYAPTL
INVSAPSPVT DFSATPSTGA APLNVQFTDL SGNNPFAWAW NFGDGSISGA QNPSHTYTTA
GNYTVTLTTQ NSVGTSTKSK VVSVISLSKP VSNFTFAPAA GQAPLTVQFA DTSSNSPSSW
SWTFTDDFST SNVQNPSHTF ATAGTYGVLL TASNAAGAGD MKLQTITVSA APVITPVADF
TATPTTGVAP LSVQFADKST NADVWVWTFG DGATSTLQNP PAHTYTTAGT YTVQLQAVNS
TSSRSNTASK TITVTAAPQT LQAAFNVNAQ TVQLGTAVTG TDASTGYPAA WSWDFGDGFT
ASSQNINHIY SAVGTYTLSL TVTNGTQTST ASKTINVSAA PTTTVTTTAT QGQPYNGPHN
VPGTVQAEDY DLGGQNVAYY DTTSGNAGGA YRTDDVDIEA GASGYAVAYV IGGEYLTYSV
EAAADGDYPV TLRAANPDGT TKTVTVSAGS SSTPVSVAST GSFDTYNSFT SAGTLHLEQG
RNVVKVAFSA SRMNLDYITI GSGVTPTTTV TTQPTTTVTT QPTTGAASFT VSPTSGKHSL
SVALTDTTTG GNPVSWKWNC GNGQTFSGQN IGLNRIWYNN AGTYTITLTV TDANGSTRTA
THTVTVS
//