ID A0A109FFG6_9BASI Unreviewed; 1168 AA.
AC A0A109FFG6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=RHOSPDRAFT_34853 {ECO:0000313|EMBL:KWU43543.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU43543.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU43543.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU43543.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954488; KWU43543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FFG6; -.
DR STRING; 1305733.A0A109FFG6; -.
DR OrthoDB; 67404at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; 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; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 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|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 95..134
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 126178 MW; BE8101B9DEB4FCED CRC64;
MSPPPAKRRR TSSPRPLLSP QTAGSPPPRP SRRPASPLVQ PRNGRRHPLD GFNDEGDSGE
EAEGVTGTGS TRTSSDMDHQ PQSHEEEEEE EEEHCAICLS PIENRAVVSP CHHGQFCWGC
IRAWTDQSRK CPLCLGPIEH LIHNIRSAKD YQNHYLLPLP TASSSSDFVA TFPPPPAARG
GSFARSRPGA ATMNPTLPRH ALYGRQSRTS RFSSSNRVDE RDEATWRERE QERALERRRY
IYREGLYAKH VASNRYTGFK PFSPHTFSRN EELKAKVIKF IRRELQVFPA VDVAFLTTYL
VTIASQLDLR SPSAIRLISD FLSEEDAQHL VHEISTFARS PFTSLEGYDR FVQYGRPQRR
LEEEEEAAEE GGSMSRGVSD RPRFEEHMSG SRGARGGEEE QEWERERRSS AGRPPFPSST
GRDSTSGNYR SGRSPSPPSA PLPRRYSSSG SAPNGRPPPP PASNPRHRQP YRPVEPNWRE
RDQRYTGSYY ATAASESRRG DGGNGGGRRG RRGGFVDGST ASHMRGRGGG GGPASSAVYE
EGGGGGRRRY ESRGRRKSPS LSLALPTRDS MSPPPPRRRR RRYSADDNDD DDDDGWPSRR
RFSPAPLPRS YKDERETSPL PTSETRVQGP SRSPPSPRSR SPARPRSRSR SRSKTPLQRP
EPLSPLPSPP PPPPLPAAGA AGGGPAIDSE LDDAISLVGP SFSIGPGSSK SNNSPLPSPL
TATPAGPPPP PTSSRERPMS SSSTFDTSAP PLPPPPRGKP TLTIFGAARR LLGNGRVVTL
ARDGRASLQA QSDVFRNAGA SASYGRRGAA GANSRPRQQE SCYNQATPNR PTASSSSSSS
SPAASAMLGP PRKPLLGRLG GIVPPPISTS STAPVPSASS RDAAASPTTP TSSKATSPAD
SLRARLHARL TAEYRQALAA SSRSTTLPPV FEDPDGAVPP ATTTTTTTTN KSDLRSLLQA
RLQAEKALAS EDLVRTRTAA SLASARDAHE RVNEPTVFSQ ETRDLLMARL DEERRFVDEE
AQAGRPASST SASAFDTYEY GHDLAYDDGY YDYNPSYRTS AVFMDDHAAA ELAPNEKDLV
ASSPSSSSAA LAPASVTPST SESSLKAALL AKRRAAIQDE LKKFSGQLKE KEMRQKLMMQ
KRRSGTTAGG GGGGGGDASA EAQARAGP
//
