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Database: UniProt
Entry: A1UCS1_MYCSK
LinkDB: A1UCS1_MYCSK
Original site: A1UCS1_MYCSK 
ID   A1UCS1_MYCSK            Unreviewed;       400 AA.
AC   A1UCS1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:ABL90629.1};
GN   OrderedLocusNames=Mkms_1417 {ECO:0000313|EMBL:ABL90629.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90629.1};
RN   [1] {ECO:0000313|EMBL:ABL90629.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL90629.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000518; ABL90629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UCS1; -.
DR   STRING; 189918.Mkms_1417; -.
DR   KEGG; mkm:Mkms_1417; -.
DR   HOGENOM; CLU_013325_1_1_11; -.
DR   OrthoDB; 9804286at2; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00158; RHOD; 1.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          308..398
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   400 AA;  43150 MW;  605F29765D40E371 CRC64;
     MSGNVGTLPQ QSLPPLVEPV GELTREEVAR YSRHLIIPDL GLDGQKRLKN AKVLVIGAGG
     LGSPTLLYLA AAGVGTIGIV EFDVVDESNL QRQVIHGQSD IGRPKAQSAR DSILEINPLV
     NVRLHEERLE PENAVGLFEQ YDLILDGTDN FATRYLVNDA AVLAHKPYVW GSIYRFEGQV
     SVFWEDAPNG LGLNYRDLYP EPPPPGMVPS CAEGGVLGIL CASIASVMGT EAIKLITGIG
     EPLLGRLMVY DALDMTYRTI KIRKDPATPK ITELIDYEAF CGVVSDAAAA AAADSTVTPR
     ELRELIDAGK PVALIDVREQ VEWDINRIEG AELIPKSAIE AGDGLAKLPH DRIPVLYCKT
     GVRSAEALAA VKKAGFSDAL HLQGGIVAWA KQLEPDMVMY
//
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