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
//