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Database: UniProt
Entry: A0A1T5K836_9MICO
LinkDB: A0A1T5K836_9MICO
Original site: A0A1T5K836_9MICO 
ID   A0A1T5K836_9MICO        Unreviewed;       642 AA.
AC   A0A1T5K836;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit {ECO:0000313|EMBL:SKC59629.1};
GN   ORFNames=SAMN06309945_1983 {ECO:0000313|EMBL:SKC59629.1};
OS   Okibacterium fritillariae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Okibacterium.
OX   NCBI_TaxID=123320 {ECO:0000313|EMBL:SKC59629.1, ECO:0000313|Proteomes:UP000190857};
RN   [1] {ECO:0000313|EMBL:SKC59629.1, ECO:0000313|Proteomes:UP000190857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2059 {ECO:0000313|EMBL:SKC59629.1,
RC   ECO:0000313|Proteomes:UP000190857};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FUZP01000002; SKC59629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5K836; -.
DR   STRING; 123320.SAMN06309945_1983; -.
DR   OrthoDB; 182039at2; -.
DR   Proteomes; UP000190857; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42678; AMIDASE; 1.
DR   PANTHER; PTHR42678:SF34; AMIDASE C869.01-RELATED; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190857};
KW   Transferase {ECO:0000313|EMBL:SKC59629.1}.
FT   DOMAIN          187..512
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  66379 MW;  ED3B6D41321B51FE CRC64;
     MRSFRSSPTA SGVDRPLVSQ RNRSVPTNSA FSRRSRLTVT AATGLASVLA LGTLAVVPTA
     TAATPVAEPA AAALLAPYYT DLDLTGDRQV TTADLELLAS HLGDTDASTG WSAVAAADTD
     GDKTITATDI AALSQRMIYD DGDFELIEAS TIDMQAAMNA GVLTSVELTQ DYIDRIAAYD
     KATPDASAVG RALNSIITVN KQALTAAAAA DAERASKGMT SMLLGIPIAV KDNYDTKDMP
     TTGGCGCWDD NQTTTDAAMV AGLRNAGAVI LAKASLDEFA FGFASEFSSY QLAGTSTLVA
     SPYNLSRTAG GSSGGTGASI AANLAGIGFG TDTGGSIRIP STYNQLVGIR PTVGLASRDG
     IIPLALSQDT GGPIARSVTD AAVALDAVTG VDAADPVTSE QTGKVPESYT SSLDPEALKG
     KRIGYVTTMI GTNPTNVRLW NQAKATLEAQ GATVVAVEQT PAFKRVLDEG SGSTNEFKHD
     LNEYIANHLA PNVAARSLQG IVDSGKYVPS RKSTYTGRDA ITEAQYQAWA GPTGTHTTQI
     ATGQALVTKM MDDLALDSLV YPSGTPYNTQ STNMRLSPNT GMPAISVPMG QAIAADNTIT
     GAGVNLEFLG RDYAEGTIIG LAYAFEQATH YRTTPALYGP LG
//
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