ID U7PLB0_SPOS1 Unreviewed; 868 AA.
AC U7PLB0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=HMPREF1624_07308 {ECO:0000313|EMBL:ERS96398.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96398.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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; KI440850; ERS96398.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PLB0; -.
DR STRING; 1391915.U7PLB0; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_330426_0_0_1; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000018087; 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; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF228; FINGER DOMAIN PROTEIN, PUTATIVE-RELATED; 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:UP000018087};
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 455..496
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 87..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 92866 MW; E2AEA22098F50515 CRC64;
MASAFSPSRQ RLATREGYDV AFCHNCFHEW YLNVGAASPP PPCPRCGAEV VEIVEDSDND
PRGYQQPGGL PMFAEVLMGL SGLGSLARNG NRSDGQTSDA GHDSHDGRDR NAPYDPFSNP
GGPGPGHDNG HRHDAMDAAN DPLDDDMYSD PDEADIDVEE YHGPNNVYMY RSTQRFGPGD
PDDPHDDPAL LGIGIHTYNP QAAGPPPHLR SPVPGQQARE VPPQEPPLAP QREPQEPPRR
VPAADPADPR AMIDTFMQFM HGLGDGNRAG RSGPETLFSG GTNNNQGGAN EPGHPGRQNM
PGAIPQHRTT TINTNFGTTS FTIATGPLQR DAAGNFSTVF ANIMGNVGPP NVDRQNPNQN
QRGPGGANGG NGTLPPFSDA LQNLLAMIVG QGAATATFNG DAVHSDEALD RIITMLMENN
RGPTGAPPAS QSALDALERK KVDAKMLEPD GHAECTICIT EVQLNEEILY LPCKHWFHEE
CVVTWLRQHN TCPVCRHAIA GNTNAAPNTV PNNSNTTPGA APPAGQGAQQ QQQQQQQQQQ
QPQQPQQRPI GDFMRNHRIN ASTHLADHLQ FHQQQVNRAR LNAIRATANR PPESGPVPVR
GAGPNLNLNV NLNPNPFGAF GGGAFGSPAG SPFTGSPFNG SPFQQPSPSP TPSSTTPPPS
SSHNASHYRS SRVPEREAAA ERERRRRDSH SPGAGPNASN RRFNLASQTD RLREQREQQQ
QQREQQEQQR DQQARMGAWM DYDEFPSAAS AFSTHGHQRP SQTSSQTPGQ TPTQSGSGSG
SNGATHYFWY SSMGPTHTGM PNASGGGHRA APGQGNSGYS MEPSSGGNES DVHNANNNDA
NNGGGGGGFF STLFRGFGSG NSSNTRRR
//
