ID A0A3Q1HDH7_ANATE Unreviewed; 1029 AA.
AC A0A3Q1HDH7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RNF111 {ECO:0000313|Ensembl:ENSATEP00000005395.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000005395.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000005395.1}
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 AlphaFoldDB; A0A3Q1HDH7; -.
DR STRING; 64144.ENSATEP00000005395; -.
DR Ensembl; ENSATET00000005486.2; ENSATEP00000005395.1; ENSATEG00000003774.2.
DR GeneTree; ENSGT00940000157691; -.
DR InParanoid; A0A3Q1HDH7; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000265040; 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 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:UP000265040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 977..1018
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
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 392..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 111969 MW; 8290194B34D99941 CRC64;
MKSEVPSEAP SRQEHLKESL VNPEPVEEAK NFANNMEVIG KAGSEYETLC ESRHRPLRDT
GTHRDSERSL PGRRKRKGQQ AGPSDCSLKE GHISESSLAP QRPRVELLQH PSEDEHNHES
SFSDCASSPS SSLRFGDSDT LSSEDEGEAG ATGGQHKAPA LTTGGATGVA PRPVLGRTRG
TRSHKWVRSE TEPVLLKRPC LNSRRSLHRK RFLKTAPGGG QRTQKQKERR LLQRKKREVI
ARRKYALLHS TSSSSEELSS DSSSPSSTEA EDELYVDVSS TSSQPNSATV ATGGLDEDVV
VIEATPAPAP AVPASEEINV TSTDSEVEIV TVGDGFRSRS VGGLGRIWAN SCSQSRLQEP
RGRHRLSTVI QPLRQNAGEV VDLTVDEDDL SVVPTTSGSI HPQTVRSSSS SSSHHASTSE
INDAPGPSTS CPGPISESMH TQRPSGSTRT ATEDDSRPGL SGTTGENTGT AMPRLPSCCQ
QHSPCGGPSP SHLSLSHSHS SCLQASSSQQ TSGSQHIHGH SHSSTHHFHH VHHPAPQPIG
SLPFQEPSCP VERPNALPAS CAGVSSSNSG SSSNTAHYHD QQTLPVDLSN SSVRSGGNSG
TSFHGSTSAF DPCCPGSTSR PPAYVSQATP GPSQPAVVDS FSSSMVAQPQ PQTQPQPCRH
YMHPPYGSLA RSLHHQPSTA CPHSHGNPQL TPQPPPQGDY VIPHTVTFHP PLPSHPSGHT
VPPAPPPPLA THHLSSSSAP LAQHLSTDHQ TLPHHMPALG ASVQRLHQHE ILQRMEVQRR
RMMQHPTRAH ERPPPHPHRM HPNYGHGHHI HVPQTMSSHP RQPEQRTAWE LGIEAGVTMP
PYPSGHLHSH LPHYHPPPRL HHFPIPFMHA GISEVTYPHI RYISSRMGGF GRTYEDLLHL
EERLGTVNRG ASQGTIERCT YPHKYKKKVL ERDIDQQLTP EAWASIGKNM HATPESRKLH
GKQDEDEGAD EDTEEKCTIC LSILEEGEDV RRLPCMHLFH QLCVDQWLLT NKKCPICRVD
IEAQLSAES
//
