ID A0A1V9XR43_9ACAR Unreviewed; 852 AA.
AC A0A1V9XR43;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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_08124 {ECO:0000313|EMBL:OQR75903.1};
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:OQR75903.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR75903.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR75903.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OQR75903.1}.
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DR EMBL; MNPL01005616; OQR75903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XR43; -.
DR STRING; 418985.A0A1V9XR43; -.
DR InParanoid; A0A1V9XR43; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
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; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..62
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 95289 MW; 33F68B52C8A3DB09 CRC64;
MEDTGQEICR VCRTEAAADR PLYHPCICTG SIKFIHQECL VQWLRYSKKD YCELCNHHFS
FMPIYSADMP KRLPTRDIVH GLLASIGAAL KCWLHYTLRR AAAADGAVEH ATDGGPAENL
AAADAVVERV APGDGQVPAG AAVVADDVLE NNRGAGIGAA GIREGAADGA VGGHAGENWR
ALDLQAVARQ AGLVNNPDDD DQGQWNAEWE RGGEDITWQR LLGLDGSLVF LEHMFWVLSL
NTLFMFLFAL VPFYFGEWLA ALVDITQHVE QFEFRGPLVT FIGYIVAAFI LMMLYMLCQG
ARFRRARRIV GLCYLIIKVS LLAVAEVGLL PMVCGAWLNI CSMELFGNSL PLLQTHLKAA
PATNAFLHWL IGMIYIYYFA FFVLLLREVV RPGVLWFLQN INDPDFHPIQ EMIQMSVMLH
VRRLVVSLVI FGSAILLMVW LPLRIMKRLT PSLIPYNVSM QTADMPSTEI SMELMILQVV
LPALLEQGHT KQFVKWCVKL WCRGVSSVLG IGSYLLGEQN DGEGRDGAAA DGDAQDNERE
ENVQQQPREL AAVHQALVNA HMPSPNVPYV RSTYFAFRIA GLLLCVCVTL TLVSMTILTV
PVSVGRWVMS IAIPNTRLHE FYTVGAGLYV CWLAIRAVSL ARSWLPRGWS SIYQSLLSSA
LVGLKALTVC VLLLGLVPLL IGIHFDLIIV IPLRVPLHAS PVLYLFHDWA LGVLHTKIIG
ALTLVGPNWW LKAALDQVYQ DGVRNMNVTR IVRDIVLPCV AILGLSLSLP YIFVHSVLAH
FVSDATLHLS LRRIYPTLLL GILLSWYAVF QWRQFRRLYE HIKNDKYLVG RRLVNYERQQ
QQQQQQQQLQ VA
//
