ID A0A3N4YLQ0_9MICO Unreviewed; 386 AA.
AC A0A3N4YLQ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Adenylyltransferase/sulfurtransferase {ECO:0000313|EMBL:RPF20244.1};
GN ORFNames=EDD34_0824 {ECO:0000313|EMBL:RPF20244.1};
OS Myceligenerans xiligouense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Myceligenerans.
OX NCBI_TaxID=253184 {ECO:0000313|EMBL:RPF20244.1, ECO:0000313|Proteomes:UP000280501};
RN [1] {ECO:0000313|EMBL:RPF20244.1, ECO:0000313|Proteomes:UP000280501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15700 {ECO:0000313|EMBL:RPF20244.1,
RC ECO:0000313|Proteomes:UP000280501};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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:RPF20244.1}.
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DR EMBL; RKQZ01000001; RPF20244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4YLQ0; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000280501; 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 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; 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:RPF20244.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RPF20244.1}.
FT DOMAIN 326..377
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 258..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 39187 MW; 9788BB7B4302DE55 CRC64;
MKPLPPLVPV RESLPSGERR RAARHLLLDG FGPDAQARLA GARVVVIGAG GLGSPVLQYL
AAAGVGTLGI VDDDVVAPSN LQRQVLHGPG DADRPKTTSA ADSLRVLRGP GLKVTEHRLR
LDATNARELL GGYDLVVDGS DTFATRYAVS DAAAALGMPV VWGTVLGWDG QVAVWWSAAP
GGRGITYPDV FGPQPPEGES CETVGVLGPA CGAVGSAMAV EAVKLLTGTG DVALGRILVY
DARTSGWDTI PLAAPEPYGG RRAAPPTAVV PDGYGADDDG ADDDGADDDG ADDDGADAGV
AAYLPDGVLV VDVGRLPARL PAGTAAVRAD LESLAGGDLP AALADHPADA PIVVVCERGL
RSRGAAALLA DLGWRDVTPA GHLLFT
//
