GenomeNet

Database: UniProt
Entry: F7RUH2_9GAMM
LinkDB: F7RUH2_9GAMM
Original site: F7RUH2_9GAMM 
ID   F7RUH2_9GAMM            Unreviewed;       499 AA.
AC   F7RUH2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Hydrolase, alpha/beta hydrolase fold family {ECO:0000313|EMBL:EGM68152.1};
GN   ORFNames=SOHN41_04056 {ECO:0000313|EMBL:EGM68152.1};
OS   Shewanella sp. HN-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM68152.1, ECO:0000313|Proteomes:UP000002956};
RN   [1] {ECO:0000313|EMBL:EGM68152.1, ECO:0000313|Proteomes:UP000002956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HN-41 {ECO:0000313|EMBL:EGM68152.1,
RC   ECO:0000313|Proteomes:UP000002956};
RX   PubMed=21868804; DOI=10.1128/JB.05578-11;
RA   Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA   Hur H.G.;
RT   "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT   Arsenic-Sulfide Nanotubes.";
RL   J. Bacteriol. 193:5039-5040(2011).
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:EGM68152.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFOZ01000046; EGM68152.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7RUH2; -.
DR   STRING; 327275.SOHN41_04056; -.
DR   Proteomes; UP000002956; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43798:SF27; HYDROLASE ALPHA_BETA HYDROLASE FOLD FAMILY; 1.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EGM68152.1}.
FT   DOMAIN          79..241
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          363..462
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   499 AA;  53890 MW;  5A2B0BAC1959B701 CRC64;
     MSALLLAMAS TATWASDVKK QDIKATDKAG ACYVEGVSDR LDCGFVTVPE NPNKPDGKQI
     QVHYAVLPAV KNTNHEEALL AIAGGPGQSA IDNAAGFNAM LSKVRQQRDI LLIDQRGTGR
     SNLLQCDQGE QSALSFDDDN VDSLAEAQKC LAKIDADVSQ YGSLNAIKDF EAVRAHLDYK
     KLHVYGISYG TRMAQLYMRL YPEHLATVTL DGIVPMQQSV LEIGASIDRG FELLFKDCQE
     TAACHAQFPE LKAEFEQVAA SLANAPITEN ISDPVTGEKT ILTMTRGKFY GAIRMALYQT
     NVRALVPHAI HQAAKNNFQP LLGLYALTID NAGMAMGMHA SVVCGEDMHR ITPAMREQAK
     HSFMGKTMLE GLEATCTAWK VPAVDASFSE PIGSDIPTLL LSGEIDPATP PSWGELAMEK
     LTNAKHFIAP YATHGVAYQS CANNLIADLV RSGSVKDLDG ECLKKDVRRS FYLNASSVEP
     LAVTSTKTTD NNASTGAKE
//
DBGET integrated database retrieval system