ID A0A091DY38_FUKDA Unreviewed; 1014 AA.
AC A0A091DY38;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=H920_10953 {ECO:0000313|EMBL:KFO27691.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27691.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27691.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27691.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KN122870; KFO27691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DY38; -.
DR eggNOG; KOG1609; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR14471:SF5; E3 UBIQUITIN-PROTEIN LIGASE MARCHF10-RELATED; 1.
DR PANTHER; PTHR14471; MARCH7/10 E3 UBIQUITIN PROTEIN LIGASE FAMILY MEMBER; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 867..937
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 35..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 113418 MW; C043CD2D067ADA28 CRC64;
MMHEARDRQK FFSDVQYLRD MQHKMDFEYQ ACLRRQENRR DEKKRDQFCG QETGSERSLF
SSKASSKQSS GGEESLTEPR PSSRKSEIKC DSKLPAIDQT PVKQKHKSTM SPRKPEQVGP
SKTSPEAPKI LSRKGRPYLG RLTVSPEMHS LRAAEDRSRQ KWQPPAKAPT RWGPDDPVVH
QEDSMWAIKT KLKRTTQEKR NFISSSQLMR TAENPAEGTK QVDQNALSLN EPYSALSQTF
QRMRNPQVLS GSLGPPLTST TMGGPRKTPF RFQDKEFYSM LSLNTEGENN NIGEETYTEE
EILLVGMQSP CSPSNYKPST FLGTSATYAK NKNFEENDEH CRGNSLRSKP NGGSLRISNT
MEPVTKQFSV GQRMLQDWPD GQSAEENNRR NSGNEKNTFD SCHTKSNSNP DNDLNDENVS
GDCISVHDGP GICDYERDCQ DYLSDSRNSP NYLISDRPTA PRSSMNSSYN ALGSLMHIAL
SDHVPTDLSA SSTLDKEFYS MLSLNTEGEN NNIGEETYTE EEILLVGMQS PCSPSNYKPS
TFLGTSATYA KNKNFEENDE HCRGNSLRSK PNGGSLRISN TMEPVTKQFS VGQRMLQDWP
DGQSAEENNR RNSGNEKNTF DSCHTKSNSN PDNDLNDENV SGDCISVHDG PGICDYERDC
QDYLSDSRNS PNYLISDRPT APRSSMNSSY NALGSLMHIA LSDHVPTDLS ASSTLGHPLD
PRFGVCQQLP PIRSRSPSAN TENHNYFPGN SAREFGVRRA EGITLPSQPQ GAPLYADLLL
NPQGSGSPVD SPPSSLPRGN LQGHWHVLGS LRENVPFTFL VISEFPNQND NTDCTSVSGF
TNGKGAPEKK ADPEKLKRLQ ESLLEEDSEE EGDLCRICQI AGGSPTNPLL EPCSCVGSLR
FVHQKCLKKW LKVKITSGAD LNAVQTCEMC KQVLLVNLDD FNLTDFYQKH QQSRAQSELM
NSGLYLMLLL RLYEQRFAEL MSLDYRRIVR ERTQGPDSET WKQHAELQAG PESD
//
