ID V5GTH9_KALBG Unreviewed; 834 AA.
AC V5GTH9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PSEUBRA_SCAF12g01802 {ECO:0000313|EMBL:EST09222.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09222.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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DR EMBL; KI545854; EST09222.1; -; Genomic_DNA.
DR RefSeq; XP_016294211.1; XM_016434458.1.
DR AlphaFoldDB; V5GTH9; -.
DR STRING; 1365824.V5GTH9; -.
DR GeneID; 27417062; -.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4159; Eukaryota.
DR HOGENOM; CLU_340428_0_0_1; -.
DR OrthoDB; 203654at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR23327:SF42; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN C14F5.10C; 1.
DR PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SMART; SM00464; LON; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 253..291
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 401..722
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 90746 MW; A7E9BFB0C39D196E CRC64;
MGIFGQNESE LESGTVGGVR AAASDSDDNS TTGSNQDSST ETAHESSAYR GLPRSLAAYV
DDEAAGWTMQ GGADFEGSEE ENSDRFWPDR VGGAYSRPLV SSNAGRRRGK AHLKRRRGRP
SDESTSGANS SSKDSRSHGD IKVARAELAE PSDQATLRHL DSGWSTEDST ASTTLQRANG
REALVDAVRR RRAAQAHSAA STASDADTDI DSQRRAIEAK HSLALSSRTG VNGEPLIQSV
ATLHSELVEV LECQLCYLLL YDPLTTPCGH TFCKSCFARS LDHGDRCPLC RADMPNFSFF
QDHRPNTALL KILTSDTATF SDDDGIDSDS TQEAKMTATS TYAGISIALG SDEGADASMG
GGRRAGLIVD DDPESAPHHY GFKRLYEQRK TAIEQEEREA RLSTPIFVCT LAFPGMPTIL
HIFEPRYRLM VRRCLESGNP RFGMVLPSRN NGGTEEYGTM LEIKSVQMLA DGRSMLETVG
SYRFRLLEKG SLDGYTVGRV ERVDDISLEE EAELERAVLV RRTELERKKA AEAVERPRAC
PMAPSSSAPV RTQPSSEEGQ PASDAVSARP DMPRAESDAL SIYRNSSSAD TRSEQQSEAQ
PMQASGTTAS RSSAERVEHD NDDDNADEAG LLPFKPVPAE PSIEELTDIC TTFIETLRSG
SAPWLLSRLN HTYGPMPSAD EVERLGYWMA LVMPIDEHEK AKLLPIRSSA LSIASSVLGS
KPAWTQLDDS RKMAAKQAAE KLISEHLVAV FSKSYCPYCS QAKSVIDKLG LDKSKVGILE
LDTMGSEGSD IQAYLQEKTS QRTVPNIFIN QKHLGGCSDL LDAQKSGKLQ QLVK
//
