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
//