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Database: UniProt
Entry: D3Q1D7_STANL
LinkDB: D3Q1D7_STANL
Original site: D3Q1D7_STANL 
ID   D3Q1D7_STANL            Unreviewed;       505 AA.
AC   D3Q1D7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=TAP domain protein {ECO:0000313|EMBL:ADD45717.1};
GN   OrderedLocusNames=Snas_6093 {ECO:0000313|EMBL:ADD45717.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD45717.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD45717.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; CP001778; ADD45717.1; -; Genomic_DNA.
DR   RefSeq; WP_013021288.1; NC_013947.1.
DR   AlphaFoldDB; D3Q1D7; -.
DR   STRING; 446470.Snas_6093; -.
DR   KEGG; sna:Snas_6093; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_013364_3_3_11; -.
DR   OMA; INESPAW; -.
DR   OrthoDB; 4006962at2; -.
DR   Proteomes; UP000000844; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; TRIPEPTIDYL AMINOPEPTIDASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000844};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..505
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003048794"
FT   DOMAIN          90..450
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          474..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  54769 MW;  180701C5B37A755E CRC64;
     MRRKRRAVGF AVAAALTVAA AVTVTQTAMA DPAAEIDWKP CKDADGDVEC GTIEVPVDYA
     KPDGKKIKIG LAKRAATNPE ARVGSLMVDP GGPGGSGVDM VKGSKIGSKQ LQEKFDFIGF
     DPRGINTSTQ IKCDEEQLAA ARSVGVPTTK KKFAKLAKAN KKLADGCRKL TGPLFDHADN
     LHTVEDIESA RKALGDEKLN FLGYSYGTLM GQQYAEKYPK NIRSMVLDGN MDHSIESPWE
     FASTETAAVE RNFNSFAKWC DETKDCALYG EDTTKVYGEL RDAARAGKLK DPENGDPIDF
     YAFSERASLI NESPAWPEVA KDLKVLRDGK GQLKLDGKAK AEPVEYVFQS MFCSDWDVSI
     KNFGEWRDIT DRLAEEYPNT QWSSYVGTLT SCIGDPVKTT NPQAPLEIDG APPLVMIGNL
     NDYATVYEWS EVAAEQSGAT LITYEGYGHT IYGRGVECVD KPVESYLIDL EVPDSGLSCE
     SQETPGGGDS GRRSGAPGTG PWAGR
//
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