ID A0A2T0XYY7_9MICO Unreviewed; 375 AA.
AC A0A2T0XYY7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Adenylyltransferase/sulfurtransferase {ECO:0000313|EMBL:PRZ05303.1};
GN ORFNames=BCE75_10950 {ECO:0000313|EMBL:PRZ05303.1};
OS Isoptericola sp. CG 20/1183.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1881052 {ECO:0000313|EMBL:PRZ05303.1, ECO:0000313|Proteomes:UP000239858};
RN [1] {ECO:0000313|EMBL:PRZ05303.1, ECO:0000313|Proteomes:UP000239858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG 20 {ECO:0000313|EMBL:PRZ05303.1,
RC ECO:0000313|Proteomes:UP000239858};
RA Rubin E.;
RT "Comparative analysis of microorganisms from saline springs in Andes
RT Mountain Range, Colombia.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PRZ05303.1}.
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DR EMBL; PVTW01000009; PRZ05303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0XYY7; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000239858; Unassembled WGS sequence.
DR GO; GO:0016779; F:nucleotidyltransferase 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 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; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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 Nucleotidyltransferase {ECO:0000313|EMBL:PRZ05303.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239858};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PRZ05303.1}.
FT DOMAIN 288..352
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 256..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 38379 MW; 615C94C24D7A050E CRC64;
MPLDPVVPQD RSAGPLPPEE RRRAARHLLL EGFGRAAQER LAAARVLVVG AGGLGSPALQ
YLAAAGVGTM GVVDDDVVEL SNLQRQVLHG EDTVGTPKTA SAARALRRLA PEVEVVEHRE
RLDASNARRV LAGYDVVVDG CDTFATRYAV SDAAAALGLP VVWGTVLGWD GQVAVWWSAA
PDGRSITYPD VFGPQPAAEG ESCATVGVLS PACGVVGATL AVEAVKLLTG TGEPALGRLL
SYDARTSTWD EVPLAPAAGA SVEESDAAAS RSSSRSRARG ASGGAGEGAE GALVVDVSLV
AGDGPEGSVW VRLEDLAGGE YPPELAAHPK DAPVVVVCPY GLRSRGAATL LAGDGWTAVE
SRPLRPGVAD RSPDA
//
