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Database: UniProt
Entry: F4H5C3_CELFA
LinkDB: F4H5C3_CELFA
Original site: F4H5C3_CELFA 
ID   F4H5C3_CELFA            Unreviewed;       407 AA.
AC   F4H5C3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:AEE47846.1};
GN   OrderedLocusNames=Celf_3740 {ECO:0000313|EMBL:AEE47846.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE47846.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE47846.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002666; AEE47846.1; -; Genomic_DNA.
DR   RefSeq; WP_013772869.1; NC_015514.1.
DR   AlphaFoldDB; F4H5C3; -.
DR   STRING; 590998.Celf_3740; -.
DR   KEGG; cfi:Celf_3740; -.
DR   eggNOG; COG0476; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_013325_1_0_11; -.
DR   Proteomes; UP000008460; Chromosome.
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:UP000008460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          322..406
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          255..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  41787 MW;  16136AD0BA76189C CRC64;
     MPLPPLVDPG PPLTPAQVTR GSRHLLLPGL GVDGQRRLRN ARVLVVGAGG LGAPVLQYLA
     AAGVGTIGVV DDDVVDVTNL QRQVIHGTAD VGRLKVDSAR DAIAELDPDV RVVVHALRLD
     EGNVDDVLRR YDVVVDGTDN FPTRYLVNDA CVRLGLPEVW GSVLRFDAQT TVFWGRPPAG
     VPAVQLRDLF PAPPPPDTVP SCAEAGVLGA LCGQVGSVMA TEAVKLVTGL GEPLLGRVLV
     VDALRGRWSE VPLVGTARPG ADDGVAERSA APVSPRSAAA PAAPAAPTAA RAGASSATSP
     SRPLDDVVPT VTATELVARL DADPTTVLVD VREAAELAVV SVPGATHVPL ARVLDGSAVP
     DLPRDRPVLV ICQVGARSAL AARTLRAAGV DAANVEGGVL AWLAARA
//
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