ID E7G6G8_9FIRM Unreviewed; 1836 AA.
AC E7G6G8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:EFW06356.1};
GN ORFNames=HMPREF9488_00356 {ECO:0000313|EMBL:EFW06356.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW06356.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW06356.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW06356.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000256|ARBA:ARBA00006699}.
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:EFW06356.1}.
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DR EMBL; ADKX01000005; EFW06356.1; -; Genomic_DNA.
DR RefSeq; WP_008787484.1; NZ_GL636577.1.
DR STRING; 100884.GCA_000269565_01352; -.
DR GeneID; 78229234; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG3250; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR eggNOG; COG5498; Bacteria.
DR HOGENOM; CLU_237222_0_0_9; -.
DR OrthoDB; 6636047at2; -.
DR Proteomes; UP000003157; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 5.
DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR038970; Lyase_8.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR012970; Lyase_8_alpha_N.
DR InterPro; IPR004103; Lyase_8_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 5.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 5.
DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR PROSITE; PS50022; FA58C_3; 5.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EFW06356.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003157};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1836
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003218279"
FT TRANSMEM 1810..1828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 728..826
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 848..976
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 986..1141
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1151..1301
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1307..1456
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT COILED 1609..1657
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1836 AA; 206729 MW; B20E7504BB5DF863 CRC64;
MTKKLSKIIL AMTLFLSLIF GQGNTVQAAS QTVLTGQEAI ATIKTRLKDY FLELDTIDDG
SKVETCYVSK AEDYLKLIQE DGSFADVDYD AHNNAANGAA WSPYLALDRL QAIAIAYHKE
GNSLYHSDAA KNGLDKAIKN WVTHGKRNGK PDGPYSSNWW ENEVGVQLRF SRIGLFMEDI
MSDEAFNIIL TKLVEKTPVK YGTGQNNLWF DQNHVYHALL TKNETRLKEM VDDYLNYCLS
TQLDDKTAEA VQIDNSFYMH GKQFYSNGYG MSMFRDMSFW IYILRETQFS IGQEVVTRMG
NYMLNGTSWT IRGDIIELYL GYRPYKFDVG YQNYAEEYIE PLKRMITADP SRANEYQKVL
NNIQNPTESN GKNGNYYMWR SGYGAHMKDG YGVNIKMDSK SVIGGEWRGS WSGQPDGGNL
IYWSSSASST VTVDGDEYTS VYPTFDWAHT PGTTTPNRIP PDYTNSGRLT NGSTHMIGAS
NGQYGSISYV MNKKETQATK SYFFFDDEFV ALGAGINSKE STAIHTTLNQ SKANQVTVDG
QTVPTGTKAG SYTGKWIHND KIGYIFPKET AFKVSNRLQK DNPSLWKEAE KEATPETFTA
WVDHGVKPVD ESYEYIVLPN KTTGEVDTYS KNIPIDILAN TKDIQAVRHK DLNITQINFY
KAGSLEYKDG YTVSVDKACN IIIDESNGTR KITVAVNDTE DSKVVNVDFF YEGQETTTKF
VSKGLPYAGQ PITLTEGQDD RYLASSSTTG HPVKNVIDGN ESTYWESQGS SDEWISIFAG
SGKYINSIDV VWGDNYATQY DVYGSSDGIN YKKIKSITDG QGNTENITIG GLYKYIKVAM
KNSHGSHYQV KEVKFHDSQL LSLNKTVEVS STSTNDPGNV KENAVDGNTN TRWSSLRKES
GFDKQEEWIS VDLGRKARID AIEVLWESAC SNDFTIEVSN DNETWTTVQQ NLKPDSSLNN
QIVLDKSVEG RYVRIHSYSS ASKYGISIFE LSIYGQNISR NIALNKTADS SSDYKSDTVV
AKAVDGNTQS KWSSGRKDPG YDTQEEWMSV DLGQISYIDG VKIDWESGCS ENYSIEISDD
NENWTTVKEH LKSNTVAASD KHYIDNVMFD ETLEARYIKI HSYSSRTKYG INIWELDVLG
EVKDIQEPDV EEEINIALNK TSKASSEYLD TKDGNKVYYS SLAFDGNYDK VGSKQSRWAS
NRKTNDEWIY VDLTDTYNIS KIVLDWEEAC GKDYDLQVSL DGETWTTITK VRDNSAPKGS
KHNVREYLYE EDIYARYVRM QGIAPAGEYG YSLWEFEVYG DLVKLEDVNI ALNKPSTASS
ERKNPVTGFV LESKYAFDGS TENRGDNFQS RWVSTTRKDN PGVNVDSQYI QVDLEDVYNI
SKVVLNWEGA CGKEYKIQVS DDGQTWTDIS HVTDGKAGIK EFTYENSAVG RYVRMLGIVP
VGQYGYSLWE FEVYGLTLKS ELKEYYDENK NIDVSNYTPK SVAAYRDALD HVVEVYKNKD
ATSSQIIDAK QQLKDAIDGL TLKADKKALE NIIKKANDIS TDVYTEKTVK VLNEALKDAK
NVYADENATQ KQVTTAVSGL QKAIDGLVKK ANKDALIKEI KKAEAIDKNQ YTKETVKELE
AALKKANDIN KNVNVSQSEV DKAVKSLQAA IKGLEKKDDP VINVPDEDKV ITVHNNNKDV
TVKGQLPRDI QLIAEVLDDK QIEELMKKIE KQNSEFLQTA QIERLYDMKF LLNEEVYRFQ
KEVEVSLTID ESLKDKQLGI IYIDEQGNIT KIPSRVEGNR IIFTAEHFST YGIVSYGEEK
KPETGDTTST GIYVAIMLGM LGLGYVLLKK KKENDI
//
