ID L5M6N0_MYODS Unreviewed; 1078 AA.
AC L5M6N0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=MDA_GLEAN10021664 {ECO:0000313|EMBL:ELK34299.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34299.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB103229; ELK34299.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M6N0; -.
DR eggNOG; KOG4430; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF2; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 139..178
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 27..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..681
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..935
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 123332 MW; C9CEE5890BFC0DCF CRC64;
MRHAGGCFVL TRGGPWGGRG SCRRLPATIG DERFTSQGSQ QPPGSPLSRE EGEAPPHAPT
PEGPRRSRRV RLRGSCRHRP GFLGRRELAT SAPARHSPTF SEVMASAAKE YKMDNFSPKA
GTSKLQQTVP ADASPDSKCP ICLDRFDNVS YLDRCLHKFC FRCVQEWSKN KAECPLCKQP
FDSIFHSVRA EDDFKEYVLR PSSCNGSFAT PDGRRFRYRT TMTRERSAFY SPSRTMNRRT
TTPPDSGVLF EGLGISTRPR DGEISQFMRQ IPRRPTTTDE RSLRKIQEQD IINFRRTLYR
AGARVRNIED GGRYRDISAE FFRRNPACLH RLVPWLKREL TVLFGAHGSL VNIVQHIIMS
NVTRYDLESQ AFVSDLRPFL LNRTEHFIHE FISFARSPFN MAAFDQHANY DCPAPSYEEG
SHSDSSVITI SPDEAETREM DVNVATVSRA PWDDETPGPS YSSSEQVHAV MSSLLNSSDS
SDEELVTERA TSQIPEVQTN ADLNNDSDSS SDNCVIVGFV KPLAERTPEL VELSSDSEEL
GSYEKVETVK TQEQEQSYSS GDSDVSRCSS PRYVLGKDEQ INKGHCDSST RIKSKKEEKQ
CTSLSSPRDL SSSVRGDSVY SPYNHRHRRR GRSRSSDSRS QSRSGHDQKN HRRHHGKKRM
KRKRSRSRES SKPRSRRDKK RSRTRDSSWS RKSQTLSLSS ESTSRSRSRS SDHSKRRSQS
RTRDHYYLKN NYGRRYKWEY TYYSRNKDRD GYESSYRRRT LSRAHYSRQS SSPEFRIQSF
SERTNARKKN NHSERKYYYY ERRRSRSLSS NRSKTASTGP DRVRNEKPGG KRKYKTRHLE
GTNEVAQPSR EFTSKVKEGH CQKSSSKLGG NYKNESDSFS DSRSSDRETK HKKRKRRTRS
LSVEIIYEGK ATDTNRHHKK KKKKHKKKHK KHHGDNASHS PVVITIDSDS DKDSEVKEDI
ECDNSGPQDP LQSEFLAPLE TFETEDIVTI EDEVSVLDKE CDITTLNDLN NANRTVDNIP
LQPASLEQTL NVREESTFAA DLENQPRNVS IHSESSRQLS SPQKSLMPVC LGGDYDIS
//
