ID A0A0P7UQN6_SCLFO Unreviewed; 767 AA.
AC A0A0P7UQN6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Z043_120053 {ECO:0000313|EMBL:KPP61807.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP61807.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP61807.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP61807.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPP61807.1}.
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DR EMBL; JARO02009288; KPP61807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7UQN6; -.
DR STRING; 113540.ENSSFOP00015018797; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000034805};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..63
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 183..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 85985 MW; 7DFAE3B0E3FAF705 CRC64;
MDTAEEADIC RVCRSEGTPD KPLYHPCVCT GSIKFIHQEC LVQWLKHSRK EYCELCKHRF
AFTPIYSPDM PSRLPIQDIF AGLVTSIGTA IRYWFHYTLV AFAWLGVVPL TACRIYKCLF
TGSVSSLLTL PLDMLSTENL LADCLQGCFV VTCTLCAFIS LVWLREQIVH GGAPQWLEQN
FEQGANAGGQ PNEAPDADNA PAENEPPADI PPAENEGAAG NPDDHLEGAE DLDGDDEEEE
EEEDDDVAGE EDAADANNGA QDDMNWNALE WDRAAEELTW ERMLGLDGSL VFLEHVFWVV
SLNTLFILVF AFCPYHIGHF SVVGLGFERQ EMFDASLKDR ETSFDSAPGT TMFLHWLVGM
VYVFYFASFI LLLREVGHHD APVSELSLEL LLLQVVLPAL LEQGHTRQWL KGLVRAWTVT
AGYLLDLHSY LLGDQEESDN NGNQPANNNH QQIRNNAIPA VGEGLHAAHQ AILQHGGPVG
FQPYHRPMRF PFRIVLLIAF MCVTLLAASL VCLTLPGRWL MSFWTGSTKI HELYTAACGL
YVCWLSIRGV TVLLAWMPQG RTVILHKVQE WSLMILKSLI VALLVAGVIP LLLGLLFELV
IVAPLRVPLD QTPLFYPWQD WALGVLHAKI IAAITLMGPQ WWLKTVIEQV YANGIRNIDL
HFIIRRLAAP VITVLLLSLC VPYVIAAGIV PIIGVTMDMQ NLVQRRIYPF LLMVVILMGI
LSFQIRQFKR LYEHIKNDKY LVGQRLVNYE RKAGKTSMVP PPSSPQH
//