ID A5KME8_9FIRM Unreviewed; 2210 AA.
AC A5KME8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=F5/8 type C domain protein {ECO:0000313|EMBL:EDK24364.1};
GN ORFNames=RUMTOR_01419 {ECO:0000313|EMBL:EDK24364.1};
OS [Ruminococcus] torques ATCC 27756.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=411460 {ECO:0000313|EMBL:EDK24364.1, ECO:0000313|Proteomes:UP000003577};
RN [1] {ECO:0000313|EMBL:EDK24364.1, ECO:0000313|Proteomes:UP000003577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24364.1,
RC ECO:0000313|Proteomes:UP000003577};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDK24364.1, ECO:0000313|Proteomes:UP000003577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24364.1,
RC ECO:0000313|Proteomes:UP000003577};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus torques (ATCC 27756).";
RL Submitted (APR-2007) 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:EDK24364.1}.
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DR EMBL; AAVP02000005; EDK24364.1; -; Genomic_DNA.
DR RefSeq; WP_004845999.1; NZ_DS264346.1.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR PaxDb; 411460-RUMTOR_01419; -.
DR HOGENOM; CLU_001692_0_0_9; -.
DR Proteomes; UP000003577; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF07554; FIVAR; 6.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS50022; FA58C_3; 2.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW 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..2210
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002685579"
FT TRANSMEM 2188..2205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..266
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1186..1355
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 2157..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2210 AA; 242222 MW; 967FA5684665D527 CRC64;
MKKKFFSAAL AAAMVVTSVF STTSVAGAAE NETAVPYGKV TVEQKDNTVT IGNDAIKRTF
STADKKLFTT EIVNKRTGGE GTTFTPQEGS EEFVVKTTKE QKGSITLEAI NRDGWTATAD
SYQNASGDSD GPASNLLDGR TESIWHSNYG GTGQGDQDYP HNVVITFGKD VTFQSFSYTP
RKEGENTNGN IKGYKLYAST AENKLDYESE DWGEPIAEGE FEYNGTNPIY VNLKEACTAK
QIKFVATSSN NGERFAGGAE FNLHADKAPV DTDDRAFETS DLELKDGNEA VKVEDTTATI
NGKEKTGKKV TFSFKPYTHK NVEYSIDEVI VMYEGDHFMR KFLEIDVPDD KMADAEIDYI
DLESLKVAES DAQWTIPRGQ GGVVQMEEFK ANLGQPIYIQ GMFFGCEFPA ADTEIVNGTG
FMRYYSGKTF SRLKEDNQLT TDDKYVTWQT VAGAARSTEQ EVIQADFFEY IKSIATPSEF
RTQYNSWFDN MMKISDENIL ASFIEIDREL NKAEVRPLDS YVVDDGWNAY NDGSIGAGSH
AQSGAIENTE GFWTFNEKFP EGLTPSSELV KKFGSNFGVW VGPRGGYNFY TTLANIIERA
QKGSKAGHSI DVADRVYVEN FKKMAIKWQQ DWDVNYWKWD GFADTAQYNH FNNLGGADGV
PVYSESNHHM TGGYHQMYHV TDLWEAWIDL MEAVRQSEKE DGINKLWISL TCYVNPSPWY
LQWANSVWIQ CVHDQKDASF GTTKMNKQIT YRDACYYDFL KNHQFQFPLQ NLYNHDPIYG
KEGTGMTVNT ATDEDFQNYL YMLSTRGTAF WELYYSDSIM TDGKYEITGE FLEWAEENYH
MLKNSKMIGG KPDITKLSNG DLSDQTQAEA YGFSCFDGTD GIISLRNPSA NADKTIKFTF
DRTMGVAEGA GTLNYYLEHS YLLSDKSAQT GTLKYGQEYT VNLKPNEVRI LRVSAEKDTT
APKIDRIMTD GAKELTVKFD EKVSGNLFKV ENAKVSSIKK SADDTTYHIV LAEAPANEAT
VKVIPQDIKD MSGNKATEAA SVVYHKDSVI VEKEAIAEAG EIAAADRSLN SNNGFTVYAA
VNTTATDKSL VSQNGQYELK VTAEGKASFT LNGATAVSGK SINDGAEHKV VGVKENNGML
KLYVDGTLEG SAYNEKNRFH EVKKAAITAG EGVTAAAVYD IAYGYNEVAN LGEQEGLPKL
KLTNDMITVS ETSEGSKDKV LDGDNTTYWT SQKVEEGTVS SDNAWLQVDL GATYKLDQVD
YTPRYYNDAK NYWHCTGNIK NLIVEIRKDG EDTWTSVTGE NGLDLSDKIV NKNDQTLFPA
EVTFEAQEAR YVRISGTSSY HWQATDENKY ITVGDLAIYG EKVEAKNIAK DANVTAKWTA
DDTDAAKGGD RPMSMAVDGN KTDFGSNYAE FGADNRRESS YMQVDLGAVC DVNSLSLYRY
WGDGRTYGDT VVAVAEKETD FAEGKATIVY NADDQNVHKL YTQAPEKFDE DYAETAQGKS
WTLPEGTKAQ FVRVYMYGRA NNDTTTNHVV ELEVYGTKPE EGETPGVDIT ALIERLSVLS
AVDTSNATTD SAAAFNALLK EGYDLVATGA QTQEEVAAMI KKLEGAEAKL VDASALKKAI
ADAEKKVETS TVTSAEPVKA KIAEAKQLLV NGTKDAIDAM VAELTEAVKG LVARGDVTDL
KALIDQYAKE NLKAEDHTTS TWSAYETALN AANAIVTDNS NSDQAAVDAA KKVLEDAHAA
LAKRGNTDAL KALIEEYKEL KEADYTHETW VKYEEALEAA NGIVADNSNK TQAEVDAAKD
ALKAAKEALV KAPVDPQLDK SKLQAAVDAA KAKDENAYTT ASYNAMEKVL AEAEELLTNG
KDQAAIDAKA KDLNDAVAAL VERGNTDALK ALIAEYKAEG LKEADYTTDS WKAYTDALTA
AEKVVKDNSN LDQAAVDAAK KALEDAHTAL VKVEQINKEA LKAAIDAAKA ADANLYTTDS
YKAMKTVLSD AEKVLKDSKD QTEIDAAAKA LNDAVTALVQ RGNTDALKAL IEEYKDLKEA
DYTADSWKEY ADALKAAKAI VEDNSNSDQA AVDAALNALR DARVALKLSG KPSVDKSELQ
AAYDKYKDKK NDGYTAESWA KFENALKSAK AILDNEAATA DQVKAALAQL NSAAEGLTKT
QTPPKNDPQT PSTPSQGGSV QTGDTAHVAL WLVLAGMSVI AYVAVRRKRA
//
