ID A0A1V9X7Z3_9ACAR Unreviewed; 900 AA.
AC A0A1V9X7Z3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BIW11_01835 {ECO:0000313|EMBL:OQR69526.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR69526.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR69526.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR69526.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR69526.1}.
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DR EMBL; MNPL01020593; OQR69526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9X7Z3; -.
DR STRING; 418985.A0A1V9X7Z3; -.
DR InParanoid; A0A1V9X7Z3; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000192247; 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: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; cd11787; SH3_SH3RF_2; 1.
DR CDD; cd11783; SH3_SH3RF_3; 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; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF13445; zf-RING_UBOX; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW 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 125..184
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 205..269
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 432..493
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 769..830
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 284..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 93757 MW; DE4ABB31C89ACB33 CRC64;
MDAAFLNELL ECSVCLEQLD SSSRVLPCQH TFCKRCLQEI VQSKGELRCP ECRTLVETKV
DELPVNIFLV RLLEGIKNKT PRKCQSAGQA AFAEQFLLGT GLCQGGPSSH PLGGPQAFYA
QPAHSAICCA KAIYPYESSN VSDLSFQKGD LINLIKRIDV NWYQGELKGK VGYVPASYIT
VVTLGPLATA LSSQGGPLGH SGQAMGQALA KALYDFQITD KSSEEKECLT FSRGEIIAVL
RRVDENWAEG RVGDRQGIFP ISFVEMNVAA KQLIKMITCS GPSRVAPAPP PPLSSSLSDQ
GGGAKTPSQT PDGLVTDFSM ATENKRHSLS ALNLTTALGT SLAAPASSST PANAEHRHSM
EILSDRELQS PQTPLAAPLV PAGPKLCPAP GSGPAAVTHS APPPPLGQNK LLEINATVRR
HPRPKDELGA PPTSLFYVAL YNYKPQKDDE LELKKGEVYM VSEKCQDGWF KGSALKSGAQ
GVFPGNYVQH TSKGGQQQQQ QGLQATPTFY ASTGPQTANP GLVQGFSNLC VSSPMRPRSN
PQLPLNALYG GTQRSSEWPL STNTAFSGQF GDVIVGGSAL PNAALMLGGG GGGAGSSGGM
LKCGQVQGGI QQGQYRSVVA PLKQGWTAAD HGSSPPLPSG QTQQPSQATV IAQHLSLVKR
LTRHKSKSPP PALGLGLVGG VSLDDSPPVH IRSGSCPSSH SSHSSPAGPS GGSAPTPGPL
HKKTASLDDA LASPSQSPLT PLTPVGVAGV TAPSQSGPTL TSGVGQTPAA AEPYRCIVPY
PANSDYELEL KVGDVVYVHK KRDDGWCKGT LQRTGQTGLF PASFVKQTTT TTEPPAYAAA
DYGLAQGHAP GVGAVGQLGG GGGLANLNSL PPAPAMFQCG PASAAMSYAP PTTHILNPPQ
//
