ID   A0A3B3RTV1_9TELE        Unreviewed;       911 AA.
AC   A0A3B3RTV1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021156.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000021156.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; A0A3B3RTV1; -.
DR   STRING; 1676925.ENSPKIP00000021156; -.
DR   Ensembl; ENSPKIT00000001785.1; ENSPKIP00000021156.1; ENSPKIG00000005643.1.
DR   GeneTree; ENSGT00940000155171; -.
DR   Proteomes; UP000261540; Unplaced.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        370..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        524..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        677..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        722..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        765..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        807..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        850..869
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          182..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   911 AA;  102748 MW;  1ACEAE7250C7A291 CRC64;
     MDTAEEADIC RVCRSEGTPD KPLYHPCVCT GSIKFIHQEC LVQWLKHSRK EYCELCKHRF
     AFTPIYSPDM PSRLPVQDIL AGLVTSIGTA IRYWFHYTLV AFAWLGVVPL TACRMYKCLF
     TGSVSSLLTL PIDMLSMENL LADCLQGCFV VTCTLCAFIG LVWLREQIVH GGAPQWLEQN
     LEQPPNEAGQ PNEVPGEENG PAENQPVVPN GHAEEEEAVN DPEAQLDAEE DEDGDDEDED
     EEDDAAEDGE EANNGAQDDM NWNALDWDRA AEELTWERML GLDGSLVFLE HVFWVISLNT
     LFILVFAFCP YHIGHFSVVG LGFEDYIEAS HFDGLITTIV GYVLLAVTLI VCHGLAALVR
     FQRSRRLLGV CYIVVKVSLL VVVEIGIFPL ICGWWLDICS LEMFDASLKD RELSFDSAPG
     TTMFLHWLVG MVYVFYFASF ILLLREVLRP GVLWFLRNLN DPDFNPVQEM IHLPIYRHLR
     RFILSVVVFG SIVLLMLWLP IRIIKLVVPN FLPYNVMLYS DAPVSELSLE LLLLQVVLPA
     LLEQGHTRQW LKGLVRAWTV TAGYLLDLHS YLLGDQEESD DDGQQQANNN QQVRNEEAAP
     AVGEGLHAAH QAILQQGGPV GFQPYRRPVR FPFRIVLLIA FMCVTLLATS LICLTLPVFA
     GRWLMSFWTG SAKVHELYTA ACGLYVCWLS VRAVTVLLAW MPQGRTVLIL KVQEWSVMIL
     KSLVVAFLVT GVIPLLLGLL FEQVIVAPLR VPLDQTPLFY PWQDWALGVL HAKIIAAVTL
     MGPQWWLKAV IEQVYANGIR NMDLHFIIQK LAVPVISVLL LSLCVPYVIA AGIVPVMGVT
     VEMQNLVQRR IYPFLLMVVM LIGILFFQIR QFKRLYEHIK NDKYLVGQRL VNYERKAGKA
     NVAPPPSSTQ E
//