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Database: UniProt
Entry: A0A318XH95_9FIRM
LinkDB: A0A318XH95_9FIRM
Original site: A0A318XH95_9FIRM 
ID   A0A318XH95_9FIRM        Unreviewed;      1577 AA.
AC   A0A318XH95;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cohesin domain-containing protein {ECO:0000313|EMBL:PYG86545.1};
DE   Flags: Fragment;
GN   ORFNames=LY28_02973 {ECO:0000313|EMBL:PYG86545.1};
OS   Ruminiclostridium sufflavum DSM 19573.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=1121337 {ECO:0000313|EMBL:PYG86545.1, ECO:0000313|Proteomes:UP000248132};
RN   [1] {ECO:0000313|EMBL:PYG86545.1, ECO:0000313|Proteomes:UP000248132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19573 {ECO:0000313|EMBL:PYG86545.1,
RC   ECO:0000313|Proteomes:UP000248132};
RA   Kyrpides N.;
RT   "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT   genomes (KMG-I) project.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PYG86545.1}.
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DR   EMBL; QKMR01000020; PYG86545.1; -; Genomic_DNA.
DR   Proteomes; UP000248132; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08548; Type_I_cohesin_like; 5.
DR   Gene3D; 2.60.40.680; -; 6.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR002102; Cohesin_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF03442; CBM_X2; 7.
DR   Pfam; PF00963; Cohesin; 5.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 6.
DR   SUPFAM; SSF81296; E set domains; 7.
DR   PROSITE; PS51172; CBM3; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248132};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          378..537
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PYG86545.1"
SQ   SEQUENCE   1577 AA;  162069 MW;  809768CB6830EFBE CRC64;
     GILANITFEI TGTQKVTTPV KFNEGGAFGD GDMAKITKIK LTDGSVAIDG DGGQASATIA
     PTTVTVDLTA LSDVNVTLTP NGNTFAGITG LTKGTDYTVS GNTVTISKSY LSTLAVGTKT
     LTFDFGTANN PVLTIKVIKT EIGSDLNVKI GTAAGKKGDV VTVPITFANV AKVGNVGTFN
     FYVGYDSKLL KATKVTAGDI VVNAAVNFST QIKDGTISFV FLDGTIGDEL ITADGVLADI
     TFEILGQYDQ TTPVVFNQGG AFGDGNMSKI TNIKFTEGSV DIDGDVLVLP ATITPTTATF
     DKYAPADIKV TMTPNGNTFA GITGLTKGTD YTVSGNTVTI LKSYLSTLTV GSKSLTFDFG
     TASNPVLKVT VTDSTPQVTS DIQVQYHNNN SSATGNTITG NYKVINKGSS ALNLADLKLR
     YYFTADSSAA FSLYCDHAAA TDANGGNYTA LTSAVKGSFV KMSPATSTAD TYLEISFSSG
     SIPAGGSLTI QTRVAKTDWS NFDMSNDYSY KAAGSYQDWE TITAYLNGKL VSGKEPVSGP
     VVTPATITPT TATFDKYAPK DVVVTMTPNG NTFAGITGLK SGIDYTVSDN TVAIKSSYLG
     TLAKDTTKTF TFDFGTTSNP TLKVTIKDST PVEGLDVTIG TATGTAGDTV IIPVTFANVA
     KAGNVGTFNF YVGYDKTLLK AQSVTAGDIV VNSAVNFTTQ INAEAGTISF VFLDNTIGDE
     LITKDGVLAN IKFTVLGTKK VTTAVKFNEG GAFGNGDMAK ISAVNFKDGS VSITEGPVVE
     LGVALGTATG TAGDTVTVPV TFADVAKVGN VGTFNFYVGY DAAQLEALSV EAGDIVVNPA
     VNFSTKIDAS KGTISFVFLD NTIGDELIAA DGVLANIKFK VLGTKETTTT VKFNDGGAFG
     DGDMAKISSV KFTNGSVAIK TGTVVQDPAI SPVLATFDKY VPADIKVTLT ANGNTFKGIT
     GLVSGTDYTV SGSTVTISKT YLSTLSLGMN SLTFDFGTAT SPVLKLTVTD STPVPAGKLS
     VEIGTASGKA GDTITVPVTM ANVAKVGNVG TFNFYVGYDS AQLKATKVTA GDIVVNAPVN
     FSTKIDATKG TVSFVFLDNT IGDELIAADG VLANITFEVL GTAKTTTTVK FNEGGAFGDG
     NMAKITSVEL KDGSVSIEEG TTVVVPATLS ATTATFDKYA PADISVTYTA NGNTFAGITG
     LTKGTDYTVS GSTVTISKSY LSTLAVGTKA LTFDFGTASN PVLTVTVKDS TPVVVPATLS
     ATTATFDKYA PADISVTYTA NGNTFAGITG LTKGTDYTVS GSTVTISKSY LSTLAVGTKA
     LTFDFGTASN PVLTVTVKDS TPVVVPATLS ATTATFDKYT PADVAVTYTA NGNTFAGITG
     LTKGTDYTVS GSTVTISKSY LSTLAVGTKA LTFDFGTASN PVLTVIIKDS TPVVTGLAVA
     IGTAAGNTGD TTVTIPITLK NVSKVGDVGT FNFYMNYDPT LLKATKVTAG DIVVNAPVNF
     SSKINATAGT ISFVFLDNTI GDELITTDGV LANITFTVLG TSTQTAAVSF TEGGAFGDGN
     MSKIKDVTFT NGSVKLN
//
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