ID W9WJU0_9EURO Unreviewed; 742 AA.
AC W9WJU0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=A1O7_01195 {ECO:0000313|EMBL:EXJ64856.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ64856.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ64856.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ64856.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC essential during biosynthesis of the molybdenum cofactor. Acts by
CC mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and
CC mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-
CC adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-
CC COSH) of their C-terminus. The reaction probably involves hydrogen
CC sulfide that is generated from the persulfide intermediate and that
CC acts as a nucleophile towards urm1 and mocs2a. Subsequently, a
CC transient disulfide bond is formed. Does not use thiosulfate as sulfur
CC donor; nfs1 probably acting as a sulfur donor for thiocarboxylation
CC reactions. {ECO:0000256|ARBA:ARBA00043893}.
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:EXJ64856.1}.
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DR EMBL; AMGW01000001; EXJ64856.1; -; Genomic_DNA.
DR RefSeq; XP_007753423.1; XM_007755233.1.
DR AlphaFoldDB; W9WJU0; -.
DR STRING; 1182544.W9WJU0; -.
DR GeneID; 19175808; -.
DR VEuPathDB; FungiDB:A1O7_01195; -.
DR eggNOG; KOG2017; Eukaryota.
DR HOGENOM; CLU_013325_1_2_1; -.
DR OrthoDB; 53913at2759; -.
DR Proteomes; UP000019473; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019473};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 401..479
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 464..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 79349 MW; 6DEAACABF8214E2B CRC64;
MNYFHPRLTE KHDEPPPPFP PLIPAPLLAS SRYNRQLLLP QLRLRGQERL LSSKVLIIGL
GGLGSPAALY LAGAGIGTLG LMDSDCVEVS NLHRQIAHTE DAARAGLSKV RSAAATCRAL
NSEIQYVCHD EQASGANILA TVAQYDVVLD CTDNPATRYL ISDACVILGK VLISGAAQRG
EGMLIVLNSP PAAPPTPDVG AAAAASAASA TQDKGPCYRC VFPRPPAPET VRSCSEIGIL
GPVVGTIGTL MAGEAIKLIS AGRHLPPPPA VTPTAQRVNG IANTDAVVDP PSKHKHTMLL
YNTFATDPRS VFRTITLRGR RGDCLACGDD ETLAQKNLTR ITPEMVSQGR LDYRAFCGVA
DDVKLLGEEN RVNASEFLEQ HARQRRDGKA RDEERTRVKE RKRQTIVVDV REEHEFELGS
KVSGSVNIPL SRILRHGDAA FDQLGLECGS SAGDGANHPE RVVDQESKSH VPTAGQEVVN
GPEYETGPQG GQINREPDNP VTNGTNVNFP TAGDGDRNSG SLAALTESSA IGPDGRKVNR
ESHIRARAKD EYSYRGSQHK PDRGMLNREA HVPVAAATRI ASDTNSAGAG LDGGMLDDES
PIPIPSHTAT QSTFLSADFP TRPAESVTSA HENVDYSNRP GDDDHDHDRG NVSDDDELPA
VYFVCQRGND SQIAAQQLMT RIQTVRDARG TDRATSTATP TATAVAETKA RRQKLPWIGD
IKGGFLALER HTNSYAGGGS RS
//
