ID E6XC22_CELAD Unreviewed; 356 AA.
AC E6XC22;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=UBA/THIF-type NAD/FAD binding protein {ECO:0000313|EMBL:ADV50027.1};
GN OrderedLocusNames=Celal_2745 {ECO:0000313|EMBL:ADV50027.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV50027.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV50027.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
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DR EMBL; CP002453; ADV50027.1; -; Genomic_DNA.
DR RefSeq; WP_013551498.1; NC_014934.1.
DR AlphaFoldDB; E6XC22; -.
DR STRING; 688270.Celal_2745; -.
DR KEGG; cao:Celal_2745; -.
DR eggNOG; COG0476; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_013325_1_0_10; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000008634; 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 PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 270..355
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 356 AA; 39305 MW; D0E44BF4D97F144B CRC64;
MNLERYSRQT QLKEFGLEAQ EKLSVAKILV IGAGGLGVPA LTYLNAMGVG TLGIVDNDVV
SLSNLHRQVS YYESEVGEPK VTSLIKKLKV QNSDTKLVAH HTFLTTENAL ELIAQYDLVL
DASDNFPTRY LVNDACVILK RPFVYGALHS FEGQVSVFNY QNGPTYRCIF PTMPNPAEIP
NCDENGVLGV VPGIIGSLQA LEAVKVITGI GEVLSGKFLL FDGLSQNYQK INFKKVAGNI
TITALKDSYE FNCAVPQASV SAQQFAELLQ SEKIQLLDVR TTEEYHHYHI ADSIHIPLSD
LESNLEKIDY SKTIYVICQS GIRSQKAIHL ITAIKPEVRL VNIEGGINKL KSYALR
//
