ID V5E398_KALBG Unreviewed; 581 AA.
AC V5E398;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PSEUBRA_SCAF9g01417 {ECO:0000313|EMBL:EST04631.1};
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:EST04631.1, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; KI545895; EST04631.1; -; Genomic_DNA.
DR RefSeq; XP_016289620.1; XM_016439721.1.
DR AlphaFoldDB; V5E398; -.
DR STRING; 1365824.V5E398; -.
DR GeneID; 27422438; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_469384_0_0_1; -.
DR OMA; CNGQFVE; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF4; E3 UBIQUITIN-PROTEIN LIGASE IRUKA; 1.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 337..394
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 20..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 62356 MW; 4B7EC7C2A89221B1 CRC64;
MTPDPTCPRC NGQFVEIIDE TAPVNDNDAD DDDGVEANYP FGALPSSRSQ PFTFHTGQAT
AGSLPQFLGQ MLSAVAAPSN APNTSRQDAS WNSQSDYQRR WAEQGPGHSQ SSSTTRSGNT
SFGPFGMQWN VQYGSGGGDP YQRAAQNQAE HNQRQQQQQT MGSPPTLSNF LRYAFGGADS
TDNNARQEDT YFHDDGMGGA GGVADGRHFN HDNRGTYHQP PQSPNNNNAG RPHNDLPPEL
GALRNLFTGL FGESATQGGS LLDILAAGAQ GGAGGPRGQW GDYVIGQQGL DDIISQLMEQ
TQGSNAPPPA EEDVIKKLER FTRKDKERIE KARNQDCPTC KDEFLPSPEA KADDDPQADD
DQQEELIAMP CRHIFHVDCL VPWLRLNGTC PVCRISIAKP REDQTSATNS GRNATASQQA
QLSINANASS TSTDQSVPGG WPSPPNPFTS LFGAFSNRHP NEGVHIPRES PGDSTTTYHP
SPPTSTTVTS TVYPATARTG GTPGIGGGEV VNSIISSPPL VDDRAEFFEP DEPTQEHSGG
REDMRETLRR AAEARARNSS NAEGAAARRG GQPTLEPDEL D
//
