ID K2MRH6_TRYCR Unreviewed; 615 AA.
AC K2MRH6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=MOQ_006564 {ECO:0000313|EMBL:EKF29640.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF29640.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF29640.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF29640.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF29640.1}.
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DR EMBL; AHKC01012824; EKF29640.1; -; Genomic_DNA.
DR AlphaFoldDB; K2MRH6; -.
DR EnsemblProtists; EKF29640; EKF29640; MOQ_006564.
DR OrthoDB; 118643at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF65; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 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:UP000007350};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 567..609
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 328..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 67476 MW; CEA811A8A5867789 CRC64;
MVMPLGDNTA GDARYAFSHV HSLLAPGYGA PAGRAASTEQ NEVMREGNAG MHAATMSTTS
TQRASMPRLG SALMTNGLTV NAQFSAYQEG LFTQMQGRDG LAAAGGSPTR GERFHARWDS
SLDSNNNIGG SRPTTLDTGS SDVAQLRGYV VTPISIGSLT EATPFAIPSS YVTSPVVARE
RVPAATTTTT TTTGSMMMSS SANSFQHHVK FDSPLTSRFE STRGGPIRPS GLVVPPYSLD
NVSQAHNEEK IGVTNNETYS SLMSYGGTTP PSYHVDPCMH AIFPYCRQMP QNAIYSTTPR
NTVNTTIPVS NVLHTGSFSA GRGLSAPYHN TGMAPPPLSY HEQTQHQPRP YPRETAAEAS
DHASNPPMRR TRRRQESTFW ELFERLAYRP SGQNRRSATN TGTQRRTGQG YEGGNHPFGG
WLRHSRRVAE YTQPIVPSFS PVRPRPGTPP PPQTLSREAQ GSRITLRFSS NHRPSRLSEM
YLFEAAFAPD VDNMSYEELL ELAERIGRVE CGVSRERLQQ LRVVLQPIHF GVTSPRQEKM
GTARGSVPSP QDVQRSLHAH EEESLTCCVC LDSFSVGNVA TQLPCCRHFL HEDCSSRWFE
SQFRCPICTR DVRET
//