ID A0A3Q2X1A0_HAPBU Unreviewed; 1006 AA.
AC A0A3Q2X1A0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000028614.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000028614.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Arkadia family.
CC {ECO:0000256|ARBA:ARBA00007622}.
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DR RefSeq; XP_005929641.1; XM_005929579.2.
DR RefSeq; XP_005929642.1; XM_005929580.2.
DR RefSeq; XP_005929643.1; XM_005929581.2.
DR AlphaFoldDB; A0A3Q2X1A0; -.
DR STRING; 8153.ENSHBUP00000028614; -.
DR Ensembl; ENSHBUT00000017931.1; ENSHBUP00000028614.1; ENSHBUG00000012547.1.
DR GeneID; 102294581; -.
DR CTD; 54778; -.
DR GeneTree; ENSGT00940000157691; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0021501; P:prechordal plate formation; IEA:Ensembl.
DR CDD; cd16681; RING-H2_RNF111; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 954..995
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 109408 MW; D4393DF1B39A8AA1 CRC64;
MKSEVPSEAA NRQEHMKEQL VNPEPMEASK SFPNNMEVIG KAGSDFETLC ESRHRPLRDT
GTHRDSERSF PGRRKRKGQQ AGPSDCSLKD GHISESSLAP QRPRVELLQQ PSEDEHNHES
SFSDCASSPS SSLRFGDSDT LSSEDEGEAG ATGGQHKAPA LTGGGATGVG LRPAMGRTRG
SRTHNWVRSD AEPVLLKRAC LSSRRPLHRK RFVKTAPGGG QRTQKQKERL LQQRKNREMF
ARKKYALHHS TSSSSEELSG DLSSESSTEA EDEMYVDVSS TSSQTNSAAV ASGALDEDVV
VIEASPAPAP AVPASEEINV TSTDSEVEIV TVGDGFRSRS VGGLGRMWGN SCSQNRLQEP
RGRHRLSTVI QPLRQNAGEV VDLTVDEDDL SVVPTTSGGI QPQTVRSSSS SSSSHQASTS
ELNDAPGPST SCPGSTPESM HTQRPSGSAR TGPEDDNRPG LSGTTGENAG VAMPRLPSCC
QQHSPCGGPS PGHLPLSHSH PSCLQASSPQ QTSSSQHSHS NTQHFLHHAH HPAPQPPGTM
LFPEPICPVV RPSALPAPCA GVSSSSNSSS SSNAAHYHDQ QTLPVDLSNS SVRSSGNSGA
SFHGSTSAFD PCCPGSTSRP PAYVSQPTPG PSQPSVVDSF NSPMVAQPQP QTQPQPCRHY
MHPTYGPLTR SLHHQSSSAC PHSHGNPQLT PQTPAQGEFL IPHTFHAPLS SHPPGHAVPP
APPPSLSTHH LTNSSAQLAQ HLPADHQTLP HMYRMEVQRR RMMQHPTRAH ERPPPHPHRM
HPNYGHGHHI HVPQTMSSHP RQPEQRTAWE LGIEAVAPFP SGHLHSHLPH YHPPPRLHHF
PIPFMHTGIS EVTYPHIRYI SSRITGFGRN YEDLLHLEER LGTVNRGASQ GTIERCTYPH
KYKKKVLERD IDQQLTPEAW ASIGKNMHAD PESRKLHGKQ DEDEGADEDT EEKCTICLSI
LEEGEDVRRL PCMHLFHQLC VDQWLLTNKK CPICRVDIEA QLSAES
//
