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Database: UniProt
Entry: R4YVR7_9ACTN
LinkDB: R4YVR7_9ACTN
Original site: R4YVR7_9ACTN 
ID   R4YVR7_9ACTN            Unreviewed;       392 AA.
AC   R4YVR7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:CCM61878.1};
GN   ORFNames=BN381_10109 {ECO:0000313|EMBL:CCM61878.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM61878.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM61878.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM61878.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
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:CCM61878.1}.
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DR   EMBL; CANL01000001; CCM61878.1; -; Genomic_DNA.
DR   RefSeq; WP_012222739.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4YVR7; -.
DR   STRING; 1229780.BN381_10109; -.
DR   GeneID; 78311488; -.
DR   eggNOG; COG0476; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_013325_2_0_11; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000018291; Unassembled WGS sequence.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000018291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          27..117
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   392 AA;  42864 MW;  F520610EEFDFBF08 CRC64;
     MANFRELLTA TKQEIREVDT ETADRLRNEG SLILDVREAD EFETGAVPGA LFIPRGHLES
     QIEMKLPNKD TPVIVQCAGG VRSAFAAKTL EQLGYTDVTS MAGGFGKWKD EGRDWKVPQS
     LQPDQKNRYK RHLLLPEVGE EGQMKLLDAK VLLLGAGGLG SPSGLYLAAA GVGTIGIVDM
     DVVDESNLQR QILHTLDRVG MRKVDSARVA IESLNPDVKV ITHDVRLDAN NIADIISGYD
     LVVDGADNFP VRYMLNDASV KLGIPVIHGS IFRFEGNVTV FDPRRGPTYR DLLPEPPPPE
     MAPSCAEAGV LGVLPGIVGC IQAIETIKYL LDLGDPLIGR YLAFDALDMT FREFKIRPDP
     ANQITWENRD QIQVVELTDQ CMPAPLEAPA AA
//
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