ID S2VFW7_9ACTO Unreviewed; 417 AA.
AC S2VFW7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF00561};
GN ORFNames=HMPREF9237_01587 {ECO:0000313|EMBL:EPD26308.1};
OS Actinotignum schaalii FB123-CNA-2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=883067 {ECO:0000313|EMBL:EPD26308.1, ECO:0000313|Proteomes:UP000014393};
RN [1] {ECO:0000313|EMBL:EPD26308.1, ECO:0000313|Proteomes:UP000014393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB123-CNA-2 {ECO:0000313|EMBL:EPD26308.1,
RC ECO:0000313|Proteomes:UP000014393};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum schaalii FB123-CNA2.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:EPD26308.1}.
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DR EMBL; AGWM01000012; EPD26308.1; -; Genomic_DNA.
DR RefSeq; WP_016443192.1; NZ_KE150263.1.
DR AlphaFoldDB; S2VFW7; -.
DR STRING; 59505.FB03_04415; -.
DR PATRIC; fig|883067.3.peg.1558; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_024518_2_0_11; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000014393; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000014393}.
FT DOMAIN 50..205
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 417 AA; 46892 MW; C425141D485E886D CRC64;
MTTTTHYLGQ LRLDELSLTV PLTADREDTR TIDVFARIAT RPGGESLPYL FYLQGGPGYE
AWRPSLSPLE PSWLNVALER YRVVFVDERG TGRSTPVGED ILRTGSTAQV AEYLSHLRAD
GIVRDCEALR RELGVEKINL LGQSFGGFTT VHYLSVAPEH IDQAFLTGGL TAVRRSADDV
YSLTWEKMRE HSEEYYRRFP AHRDRVRELV DLAGSGSIEL PSGEIVSPSR LRSLGHLLGS
DNGWRELYYL LEKDPASTAF RYDLAAAMPF DGRNPLYYVL HESSYADGVV TNWSAERTQP
EDFRTDTSLL YGEHVWAEWA DTVPAFQPWK DVVEKLATWP WPQLYFPEAL RESGARGAAA
VYVNDAYVPV EFSLETGALL PGIHRYVTST HEHSGLRSSN GAVLRTLFEL ADGTRLR
//
