ID R6M7V4_9FIRM Unreviewed; 1804 AA.
AC R6M7V4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Coagulation factor 5/8 type domain protein {ECO:0000313|EMBL:CDB95713.1};
GN ORFNames=BN647_01463 {ECO:0000313|EMBL:CDB95713.1};
OS Firmicutes bacterium CAG:41.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263021 {ECO:0000313|EMBL:CDB95713.1, ECO:0000313|Proteomes:UP000018139};
RN [1] {ECO:0000313|EMBL:CDB95713.1, ECO:0000313|Proteomes:UP000018139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:41 {ECO:0000313|Proteomes:UP000018139};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902}.
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:CDB95713.1}.
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DR EMBL; CBEM010000074; CDB95713.1; -; Genomic_DNA.
DR Proteomes; UP000018139; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR039514; 6GAL-like.
DR InterPro; IPR039743; 6GAL/EXGAL.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42767; ENDO-BETA-1,6-GALACTANASE; 1.
DR PANTHER; PTHR42767:SF1; GLYCO_HYDR_30_2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF20578; aBig_2; 1.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF14587; Glyco_hydr_30_2; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000018139};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1804
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004425879"
FT DOMAIN 736..890
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1804 AA; 195938 MW; 67314D18D93F6A46 CRC64;
MNKKKIISTI LACAMLPFGG LISASAQDTK PTYVQLNPAD ASPFNNGEFQ GWGTALCWWA
NRLGYSEKLT NAAAEAFFSD EGLGLDIARY NLGGGDDPTH NHINRSDSKV PGVYSDYKLS
SDGKDVESIT YDITKDQNQL NIAKAALKAN PDLYFEGFSN SAPYFMTKTG CTSGGGTVNS
DGTVTSNGNL NNLNDDMYDD FAKFIADATK LFKDNGIEFK SYSPMNEPDT DYWGYGSLKQ
EGCHFDPGTS QSKMITETRK ALDNAGFADV LVAGMDETIL KKTANNLGSL TDEAKTALGR
VDTHTYPAPD RGYHAQVKAK ALELGKNLWQ SEVDGNWDGA DLASMIIEDV NGMQPSAWVM
WDIIDRHKDS EFVDPTTQKK TEENNSANYT NALWGVGMAD HDKEELVLTN KYYVYGQFTK
YINPGDTIIA SSANTLAAYN KNTGDIKIVA NNASNSSDVD YEFDLSGFST IGTNVRKIRT
DMQGNEKWAE IKDGALLDGK TLTTTLKANT VTTYLIETGA KVTSFEPTST GLKYSYTPSE
TLNGYNQYFA VYDKNGLLKA VTVNQPTGEL TGDFTDCTFK FMVWDGVTPK ANVISTVSKG
GIDYAAIIGG GNEIRCGEEL QLTLGTNMEG DVTWSIDDES AKNGIAEISQ TGLIKAKKPG
KVNVIAKVGD YTTSKTYYIT TYATISGAAS IGVGKTSQYT LDTNAEGTPV WSISDEKVAT
ISQDGTVTGV SAGTVTITVT IGDVKATKDI NVTMYTLSGT ASWGNATTAP KDADDYRKAA
DGDFNTYFDG LQNGYVMYDF GNTVKVNNVK LAARSGNGMP EKTVGGKVQA SNDGITWTDL
YTISTAIPSG QYTTISSTDL ADQNAYRYFR YTNDTNMTNI AEFLIDATPS EEMADEAPSV
TDIDEMSDDF ENATNIFNAS AGDLSADGNQ VYATGLERFG NVFVPVKATA KAELSQAQTL
TSKDKFRLTF DMFAGWEQNG KENTFSVKDA DGNEVVGFTI TGGGYNLNQM RIGGTDVLAD
VSEKPVIQCK STDIRNGAFR GANGWQTSSQ KYANNTGFNK KVEIIIDGTG SASVSFTGGE
TDVSYTGTIS TPISVKSLEL TGSYNGARGR VVSYDNFDAD VISYSSELAA PTPTPEPTAA
PTVPESGELI NMNFDNGDLT STSSYGKATG TPKFVTVDNK KCIQFDGTSG TVVTLTDANG
NSLLTGQKNI TISFKVKPTT TTTSWWFFAA PNGSAQTYQK EQYLGAMTNN GTLTSERYNN
SGTRSQSATG AYNTNEWNDV IISIADGVTD VYVNGTRTSS VDSTVNISDM LGKNSVAYIG
KANWGTGEFA TGYIDDFVIY NYAYENPLNS LDLGDLTAVT EDITIPTQEG VTWSTSDAAV
VTTAGKITRS DETKTATLTA KMTKDGVEFT RNFDVTVLGY TAVIDSFKAY ADGNKIVYAS
DYDSAKDKYA VKVSLADSDG TAVGTEQTNA TGSFDNLEVG KYKITATLSD GTTEKKKVEK
TINIKNLDDM SAYLFVHFVD TQEDATREQI YFSVSKDGKT WTTLNNKQPY LTSNVGTQGV
RDPYILRGED GKFFIIATDL SVYNLKNNWT AAAQQGSKSI VVWESSDLVN WSEASLVKIN
NDNASCTWAP EACYDPEKDE YMVFWASVVS DDSYQKYRIY RSYTKDFKTF SAPELYIEEP
NAVIDTTIID HEGTYYRFTK NEAKSSITMQ ECTSLSGDWK DVASYNLGSM TGYEGPTIYK
LNGKNEWCLL LDYFSKSKGY KPFVTTDITK GEFTADSDFS FDGTYRHGTV MPITQAEYES
LTAE
//
