ID F5IT82_9BACT Unreviewed; 944 AA.
AC F5IT82;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=PA14 domain-containing protein {ECO:0000259|PROSITE:PS51820};
GN ORFNames=HMPREF9455_00299 {ECO:0000313|EMBL:EGJ99266.1};
OS Dysgonomonas gadei ATCC BAA-286.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGJ99266.1, ECO:0000313|Proteomes:UP000004913};
RN [1] {ECO:0000313|EMBL:EGJ99266.1, ECO:0000313|Proteomes:UP000004913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGJ99266.1,
RC ECO:0000313|Proteomes:UP000004913};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:EGJ99266.1}.
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DR EMBL; ADLV01000006; EGJ99266.1; -; Genomic_DNA.
DR RefSeq; WP_006797802.1; NZ_GL891979.1.
DR AlphaFoldDB; F5IT82; -.
DR STRING; 742766.HMPREF9455_00299; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_000631_7_3_10; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000004913; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06591; GH31_xylosidase_XylS; 1.
DR Gene3D; 2.60.120.380; -; 1.
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 InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
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; IPR037524; PA14/GLEYA.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51820; PA14; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000004913};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..944
FT /note="PA14 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003328341"
FT DOMAIN 227..368
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 944 AA; 108572 MW; F7B422E4A41E744B CRC64;
MKKIQLVLAS LLSVFLLTSC QSGPYKKTSD GVIVTLKTEN TNSTKHVRLQ IINDDIIRVS
ATPANNFPEN KSLITIYDKT KTEGWDVSEQ DGNVILKTAT TIASVSLATG EVSFSDINGN
LILSENKGGG KIFSGIEMEG KKAYTMQQIF ESPADEAFYG LGQHQADEYN YKGKNEVLFQ
YNTKVSVPFV LSSKNYGILW DNYSLTKFGD PRDYADLDQF KLYDKTGKEG GLTATYMVNG
DTKQVFTERS ESQIDYENLE TVKKFPQDFP FYNSRITWEG EIEAKEAGKY HFILYYAGYT
TIYMDDEVIV PERWRTAWNP NSYKFTVDMK AGEKRKLKLD WKPDGGISYI GLKALSPRPE
EEQSKLSLWS EMGDQIDYYF IRGNDADDVI KGYRTITGKS QVMPKWAMGF WQSRERYKTS
DELLTAINEY RKRNIPLDNI VLDWSYWPQD AWGSHDFDPE RFPDPKGMID SVHAMDARIM
ISVWPKFYYT TDNYKAFDEK GWMFNRAVKD SIRDWIGSGY IAGFYDAYSE GARKMFWDQM
NEKLYSKGID AWWMDASEPD ILSNASMQYR KDLMTPTALG SSTEYFNAYA LANAMAIYDG
QRSVKPNDRV FLLTRSGFAG TQRYSTATWS GDIGTRWEDM KAQISAGLNF AMSGIPYWTM
DIGGFCVEKR YEVAKEGSED LKEWRELNTR WFQFGAFCPL FRSHGQFPTR EIYNLAPESH
PAYKSMVYYT KLRYQMMPYI YSLAGMTYFN DYTIMRALVM DFGKDIKTHN ISDQYMFGPD
IMVCPVYTYK ATSRNAYFPA NTNWYDFESN KYIAGGQTLN VSAPYERIPL YIKEGAILPM
GKDIQTTKEI QKDLTLKVYT GANGEFTLYE DEGVNYNYEK DAYSTIKFTY DEASKTLSIG
DTKGEYEGMP KERIFRVEWI TKDGKKSVSE VKYTGKANEI KMAQ
//
