ID L5LYR5_MYODS Unreviewed; 561 AA.
AC L5LYR5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=MDA_GLEAN10025803 {ECO:0000313|EMBL:ELK31202.1};
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:ELK31202.1, 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; KB106364; ELK31202.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LYR5; -.
DR eggNOG; KOG0070; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd04158; ARD1; 1.
DR CDD; cd19773; Bbox2_TRIM23_C-IX_rpt1; 1.
DR CDD; cd19774; Bbox2_TRIM23_C-IX_rpt2; 1.
DR CDD; cd16645; mRING-HC-C3HC3D_TRIM23_C-IX; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR PANTHER; PTHR11711:SF163; E3 UBIQUITIN-PROTEIN LIGASE TRIM23; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00024}.
FT DOMAIN 4..49
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 109..155
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 132..159
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK31202.1"
SQ SEQUENCE 561 AA; 63217 MW; 2569C59248A2380C CRC64;
VLECGVCEDV FSLQGDKVPR LLLCGHTVCH DCLTRLPLHG RAIRCPFDRQ VTDLGDSGVW
GLKKNFALLE LLERLQNGHI GQYGAAEEAI GISGEREWKR EEKTEKNIDS IIRCDEDEAH
VASVYCTVCA THLCSECSQV THSTKTLAKH RRVPLADKPH EKTMCSQHQV HAIEFVCLEE
GCQTSPLMCC VCKEYGKHQG HKHSVLEPEA NQIRASILDM AHCIRTFTEE ISDYSRKLVG
IVQHIEGGEQ IVEDGIGMAH TEHVPGTAEN ARSCVRAYFS DLHETLCRQE EMALSVVDAH
VREKLIWLRQ QQEDMTILLS QVSTACLHCE KTLQQDDCRV VLAKQEITRL LETLQKQQQQ
FTEVADHIQL DASIPVTFTK DNRVHIGPKM EIRVVTLGLD GAGKTTILFK LKQDEFMQPI
PTIGFNVETV EYKNLKFTIW DVGGKHKLRP LWKHYYLNTQ AVVFVVDSSH RDRVNEAHSE
LAKLLTEKEL RDALLLIFAN KQDVAGALSV EEITELLSLH KLCCGRSWYI QGCDARSGMG
LYEGLDWLSR QLVAAGVLDV A
//
