ID G1VL42_9FIRM Unreviewed; 2306 AA.
AC G1VL42;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9022_00723 {ECO:0000313|EMBL:EGX66947.1};
OS Erysipelotrichaceae bacterium 2_2_44A.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=457422 {ECO:0000313|EMBL:EGX66947.1, ECO:0000313|Proteomes:UP000003043};
RN [1] {ECO:0000313|EMBL:EGX66947.1, ECO:0000313|Proteomes:UP000003043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_2_44A {ECO:0000313|EMBL:EGX66947.1,
RC ECO:0000313|Proteomes:UP000003043};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C.E., 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., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium 2_2_44A.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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:EGX66947.1}.
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DR EMBL; ADCZ01000009; EGX66947.1; -; Genomic_DNA.
DR RefSeq; WP_008727432.1; NZ_CP048838.1.
DR GeneID; 61925201; -.
DR PATRIC; fig|457422.3.peg.748; -.
DR HOGENOM; CLU_001337_1_1_9; -.
DR OrthoDB; 176168at2; -.
DR BioCyc; EBAC457422-HMP:GMFD-735-MONOMER; -.
DR Proteomes; UP000003043; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM00635; BID_2; 2.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2306
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039283978"
FT DOMAIN 927..1010
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1717..1875
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 103..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2222..2279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1652..1697
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2136..2163
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2306 AA; 254083 MW; 0F2D6AF3F06F3602 CRC64;
MKRKTVNKAI VLSTAAAMAA GSTTIGVLAD SVTATSVKKD TIKDQTAVNI LKPKSGYTYL
SSVASAAKQD NIVTVAYENG EKAQITFLEN NLFRFDMEPD GKSDSFKDYA TPNNSEETGR
IIQQKDDSSE YNKPSPTVEE TDGYITISTD SVRLEIDKAT SMMKLLNAKT KEVIWEESAP
IQYKSGSTIQ TLKKQGNENF YGGGTQNGRF VHTGQAINIV NENGWTDGKV SSPNPFYWST
NGYGVVRNTF KPGKYDFGNT TEGKVTTTHN ENRFDAYFFV GDKPTDILNS YFKLTGDPAL
MPMKSFYLGH LNCYNRDEWK AASGNSGSLL EDGKRYQEKN NAGVAEPGWT LETLNGKSDK
NDSAYKFSAR AVIDGHVSND MPFGWFIPND GYGCGYGQSD TSLDDNIANL KNFTQYAAQY
GIGTGLWTQS DLTPNPKEPI HLQRDFEKEV KEGGIRTLKT DVAWVGQGYS FGLNGISHAY
DIVAETKDRP TIVTLDGWAG TQRYGGIWTG DQTGGNWEYI RFHIPTYIGQ SLSGNPNVSS
DVDGIFGGSS LIQTRDIQWK SFTTMMLDMD GWGSFPKKPY IFGEDTTSIN RMYLKLRAEL
MPYIYSTAYT SANLGEGSEK GKPQVRAMFL EYPDDPNTYG TNVQYQFMMG QNLLVAPIYQ
DTAMKDNGDD IRNGIYLPDE DQVWIDYFTG KQYRGNQTLN NFDAPIWKLP LFVKNGAILP
MFTENNNAEP ISDTNTKGLD KSKRIVEFYP DATKKSTNYT LYEDDGKSID NTNKDQPTYG
DVVTTHFTSK VDNGTATLTA EKSTGSYGGY NANRETTFVV NVSKEPSDIT AKVGDQTLNK
ADFTVVTSQE EFDKAKGNTY FYNAKPNLNK YATADSDFAS KEITTTPKLY VKFAKMNVNN
KAVQLQVKDF VNDGKLNKYE LNKNLGVPQN LTVDEDNVTP TSIPLTWSAV SGATGYEVET
DGVIQGGITS TSYTHEDLEY HSKHTYRIRA INEDGFSAWS APLEAQSALD PYRNVPKDIE
LKWPYGDQWG AVKNALDFDY GNMFHSTDNA INKDFIMDMK KVYDMDRFEY TPRQDNKGNG
AVQQMDIYAS IDGTDYSLVH EGVQDEWTYS NDMSVRDTKT VDLKGVRARY LKLVPRKSKG
GFFSAAEMQP YKIDGTEGIL PGDTNKDGVV DDNDLTQIDN YVGLEKGDAA WGQVKDMDWN
NNGYIDALDV AYTTTQLNGG IAKPAGIPEG NIQFVADKAD VKKGEKLSIK AYGINMKNVY
ALGFQLPFNS SDLNYITTKP SLATINMKQF AFSRKKVEKE ADSVNDFNLN VVFSDIGNQT
MISGTQDLCT FEFIAMKDMN ITDAFYSEAK VTYVSSGLKE INPLKTPQDP SLPNTERILT
ENEVPSVTFS NDVNNNVPAT NLWQQDDWKK ILFDGNLSNN AEFKYYYGSA SDLTPDVKLP
TDMKFTFDKA RGITSFKVYN RESGNGRMTS IKAVAHTEAG QKVDLGTISE AKNIYEFNIP
KDAGKITSIT ITPLTSNGQA IANNDPNTVP EGGKENRMLT LHEIQFIEDS TQNVKDIVLD
KNNPTQINVN RIVDFKASVT PGNASNPFYE VTSSDPSVIS IIKTITPDGY AFALKGNKAG
KADITVSSQG VNDAGKKVMK RVSITVVDGV YLDDLQKMLQ DAKDTIAEEQ LYTKESLTKL
QDAIANAEKA MADKRSQSAV DNAVIDLHNA MVKLEYKGSD ELQPDSQALI PHTTIKPTAT
SSAGESPVTN LIDGQQNTFW HSDYSGANRL PQAVTLDLGG NYAIEQLDYL PRQDGSKNGD
ITEYRIEISE DGQNYKPVVQ GSFAHNDTEL LQKDSFNKVK FQRTMGRYVK FIALSALGDI
PNAYASAAEI QVYGIEVSDL KPATGIQLDV TELKDMETGM SQQIHAALTP ADSTDLLTWT
SSNEKVAIVD GSGLVTAVGS GTATVTVQAN ENVKAEISVS VRAEDKDLLT SLIQEAKTQA
EGYDNADIEK YLQDAITEAE THLNGDKDEI KAAYQALAAA MSEADLINQD VTAIKAFAAV
DLSKYEAGAA AETYKSLVQD SLALAKDPVQ NKDALAAAKK QLDEVYGNLV ALHLDRLQEA
VVYAEKLNMD NYVDNAERKV FIDALHEAKT LQPKTNQQIM ETIDRLSNAM KALTRRASKE
QIATIKKQFD VLSKLDKSQY SKADQKKIAD VLAAAKTAME NKNLSEADAE KVIEQLNSLL
TLKPIAPQKP DDGTEKPDGQ TKPDQPAVPG GTPQKPVGQD KEPVIANPST PVDTSDSTNN
AGWLAIIGLG GAAAWFTNKK RTKLKK
//
