ID N6TU36_DENPD Unreviewed; 714 AA.
AC N6TU36;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=YQE_11443 {ECO:0000313|EMBL:ENN71906.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN71906.1};
RN [1] {ECO:0000313|EMBL:ENN71906.1, ECO:0000313|Proteomes:UP000019118}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [2] {ECO:0000313|EnsemblMetazoa:ENN71906}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) to UniProtKB.
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 -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; APGK01054573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB741250; ENN71906.1; -; Genomic_DNA.
DR AlphaFoldDB; N6TU36; -.
DR EnsemblMetazoa; ENN71906; ENN71906; YQE_11443.
DR HOGENOM; CLU_015769_1_0_1; -.
DR OMA; PSHIPQC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019118; 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 GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd16750; RING-HC_SH3RF3; 1.
DR CDD; cd11786; SH3_SH3RF_1; 1.
DR CDD; cd11787; SH3_SH3RF_2; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR028502; SH3RF3_RING-HC_Zfn.
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; PTHR14167:SF30; ENDOPHILIN-A; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50002; SH3; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 128..187
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 190..252
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 429..490
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 655..714
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 80..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ENN71906.1"
SQ SEQUENCE 714 AA; 78485 MW; D17B10B1F3F788D6 CRC64;
MDEGTLNDLL ECSVCFERLD TSSKVLPCQH TFCRKCLQEI YQKHKELRCP ECRVLVTIKI
ENLPPNVLLM RILEGMKNSG VLAPPKRSQR PTKGASQHQP GVVSHSAHIQ QQNVDRSNNK
HSASHAVPHQ PYAKALYDYV PKEPGDLQFK KGDIIILKRK IDSHWYEGEC GGKQGVFPVT
YVQIITPVSS HIPQCKALYD FRMTNDEEEG CLVFNKGDVI NVIRRVDENW AEGKLDGRIG
IFPLSFVEMN SLARSLMKLS TNVQPGPSKV APPTPTTEES IPLIPTDHST SVTSVAQNIS
HQGPISASDS SSNNITSSSS STTPNVSSSN TSSSSSTAPS SPASPPARSS VVNSPHTRTI
EGRLTHHHHH HHGKEKRHSL TNMTVPHHTS AHRYSAEIAE STTGSHVSSS GASERSKRTV
PAVPAADPQL PATFMALYPY KPQKSDELEL KKGSFYLVTE ICQDGWYKGT SNRTQKCGVF
PGNYVTVLRG SAGEFSTGFP EGRMPVSFTK GTKGARNRPA DSAPPELPPR SSTPPTNVWH
VDSPRTNNAT NSQPKSDKNK ERKEKSTVSL MRRLASIKRS KSPPTSSYSM DNPVFEDATL
SAAGLTTPVH PVHVRSTETP QGGSSGSSPD VHRHRKSHSL DATGLKTSRT GSTQTVRERF
RCITPYPPNS DYELELQLND IIYVHKKRED GWFKGTQQRT GKTGLFPASF VESF
//
