ID A0A1G4K2C7_9SACH Unreviewed; 1291 AA.
AC A0A1G4K2C7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=LADA_0H08064G {ECO:0000313|EMBL:SCU97753.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU97753.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|EMBL:SCU97753.1, ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU97753.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LT598461; SCU97753.1; -; Genomic_DNA.
DR STRING; 1266660.A0A1G4K2C7; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000190274; Chromosome H.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..84
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 261..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 146782 MW; FBDB85C88C9BEA13 CRC64;
MDQSGPGVSS LNENMGVPNG ASCRICRGDH TEETPLFHPC KCRGSIKYIH EGCLMEWVAS
KNVDLSRPGS EIKCDICHYP IQLSTVYDAN TPDRVPISLV IRTTIAVLLR KVQHTLCITL
AAVLLVVGVP LTWNFLGKLT AMVLFGGKLP ISGQFFKSVL FGFESDVPDK VSDLDIVIQL
LKNYRFSVAQ IIFVAIIHIA LYFQYDMVVR EAIFNKMVFH KIGPRFSKEE LMTEKLKQQF
PGMDENTIHH IVQLMRARER PADPNQEEHF DENPVEGVRE NDNNANEGEN GEGLGVEINR
DNRVATADYQ EPESSTGQSV QEARNAEGEN FGHVDDEDDD EDDGDYVPSD ALSSRSSSSS
IISSDHEPND EERGQLLEDA DPVRVFQQRR AVNELEELLG AQQPNLPEGQ PHNIAFMEVP
NEPVADAAEI NEALNQQDGP AVLGLHLRFR NIPFYFLATT IFLALYLYLA YAIPTFVGNL
LQGAYWFACS WGLRGIIQLA KLARVPALYA EATRRYPPID TWMSWSLSRI FDSFTYLHST
YVDYENKSST VAQSIPALTT YCTFLGLICG STNVICRGCG ATNGMKNPTW RFIFQLFFAI
RCSLKVFLLF AIELVGFPVL AGLMIDLSLI SPCLQEHSKF LFVGTLNIWV PSIWALYWSI
GTSYMFWFAK YVGMVRNYII RPGVLFFIRS SDDPNIRILH DSLIQPMRIQ ISRLTLSMGI
YAMFIIIGFG FHTRVLFPVV LHSNVLPFAD QESLTLSLIG LSVLNSNLIM DFNKTFKLFI
RQYWTKVFGI CCGKLRLSSF ILDKDISTER GYVMYRNVAY KLFFSERAKW SNPELYLDPK
TPSQARELFK TQNNIHAYFI PNGVLMRVPA NDIISRNYVQ TLFVPVTKDN KLLKPLDIEA
IKERNKEVIG EFSHLDDQST EFDAYSRVYT PPNFRLRYSS LIFLIWLFAS LLFIGLGLLF
NLIGRITLLG LLYPFVRFQF VRGLCVMYKN LFAVGLVPVV VGASVFMIGL ELYQELRISR
FLRDQHAVEE EQQEQAREEA REDQEGLRHP VEHAGEDEGI PLWNRLAGQQ KNIMSCLIGF
VGAAKFVFVL DYNFSTIVLF VKLLLRGNSP TETRQRFFMT MTFTDAPFDL AEWKSIEVVL
FACWLLSSLL VEHKAFFSAL MRERDDETCH LLRKQLRTLL TECLTTAGLI IPLQLTVCAM
EYASNGDYYS SILSTFDFLL NSRGLTPASE MPWTMLQMTF YLISPVICAR YYLTGLLRSA
NNFLHKSISI TKEEVYGRGR TLTNLPEDIE L
//
