ID Q5KIQ4_CRYNJ Unreviewed; 660 AA.
AC Q5KIQ4; Q55TN1;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN OrderedLocusNames=CND02140 {ECO:0000313|EMBL:AAW42905.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW42905.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW42905.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AE017344; AAW42905.1; -; Genomic_DNA.
DR RefSeq; XP_570212.1; XM_570212.1.
DR AlphaFoldDB; Q5KIQ4; -.
DR STRING; 214684.Q5KIQ4; -.
DR PaxDb; 214684-Q5KIQ4; -.
DR EnsemblFungi; AAW42905; AAW42905; CND02140.
DR GeneID; 3257283; -.
DR KEGG; cne:CND02140; -.
DR VEuPathDB; FungiDB:CND02140; -.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_015598_0_0_1; -.
DR InParanoid; Q5KIQ4; -.
DR OMA; VACRECA; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT DOMAIN 427..524
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 71745 MW; 617D2A693B4712EF CRC64;
MSQMGSVSGW YTNAYAGTFR SSRLRAPSLL PNRQIPAPIQ QTLVIDAAHN VHTGADVQGE
NGKSKVKRRE TVFGPDVGED DEPGWTDGAK EEISVDVVKK WVEKTKADEG LHPTTTLQAL
VNLKRPTLLL QQVEQSEPVE ETNKHDGITP IAYEHQKGER EETNFAPPLH TLKFSYDATT
PSVRISLLLY PTPQPPIEGK ESILEDHEPR LLYDGLHPGG FGQVFELPKK FAIDLRSAIQ
VPTEEKEEEG DDGKKDTLVA DGNPAEQVHQ LDVGTQGQQE NQGRRRFGLL RSNRADSGGL
EESQIEMTNQ GEGQKEGEAK EEKKPIEQGM RVLIRIDGVG PQGESLKRRN AQLTHILITG
TWVNDPNGSE NPQGGKRVWV VKVARREAVI GTHTFLLKEI FGLSQASSSP AYPPTSDDPY
ASTPNECIVC LTSPRDVVLL PCRHLVVCRE CAVGMVEFGA GNRVARREEM DSAETGQNGD
ASGENGTGGG ASSGGNVPQV AGGTTATGRE RRKKKVKGWY CPVCRQPYTS LLRLALPEAS
NVPARPSSRA SVRTTRTTKS LAPTLPDGAE RMLERLRPEG AGDSDEDADA ANEAQIDEPE
RPRFVLGEDK EEIEHHENLE KSPDPAMVST AVPVSTPASV SDGEHSVGEG GPKGWREVAA
//
