ID A0A1V4JDR1_PATFA Unreviewed; 1002 AA.
AC A0A1V4JDR1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-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 Name=RNF111 {ECO:0000313|EMBL:OPJ70194.1};
GN ORFNames=AV530_019396 {ECO:0000313|EMBL:OPJ70194.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ70194.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ70194.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ70194.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ70194.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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: 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}.
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:OPJ70194.1}.
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DR EMBL; LSYS01007908; OPJ70194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JDR1; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:UP000190648};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 950..991
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 132..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 108815 MW; 0FB6DAFD082EE70B CRC64;
MSRYNPQLEK VSQGLIDSVS VVAATRGLCA ARRGRFLPSG PGQAPAAATF SPWPRCLRPF
LKLPMSKWTP ECNIVYTLEA DMKSEVPSDA PKRQESLKGI LLNPEPIGAA KSFTAEVEMI
ASKVGNEFSH LCGDSQKQKD MNGNHTDQDK TIVVRKKRKS QQAGPSYSQN CPDKESQGVL
GLRQHLETQS EDNDSSFSDC ISSPSSSLHF GDSDTVTSDE EKDAPVRHSQ AVLNTTSRTH
SARSQKWPRT EADSVPGLLM KRPCFHSSSL RRLPYRKRFV KTSSSQRTQN QKERILMQRK
KREVLARRKY ALLPSSSSSS ENDLSSESSS SSSTEGEEDL FVSPGENHQN STAVPSGSID
EDVVVIEASS TPQVTANEEI NVTSTDSEVE IVTVGENYRS RSTLGHTRSH WGQSSSSHAA
RPQEQRSRSR ISTVIQPLRQ NAAEVVDLTV DEDEPTVVPT TSARVEPQVV SSAASSSAGA
STSAQASEVA PSSSSSQPSA ATDTATSLPS GGSAGTSAGD EIRRTASNTT LETGPPAMPS
DSSCPVERPP PVPAPCGASS SSGTSYHDQQ ALPVDLSSSG IRSHGSGAFH GTSAFDPCCP
GSSSRTAIYG HQAGAGPSQS ITMDGYGSSM VAQPQPQPPP QASLSSCRHY MHSPYASLTR
PLHHQASACP HSHGNPPPQP QPPPQVDYVI PHPVHPFHPS ISSHASSHPV PPPPPPPTHP
LASAAAPIPQ HLPATHQPIS HHIPATAPPA QRLHPHEVIQ RMEVQRRRMM QHPTRAHERP
PPHPHRMHPN YGHGHHIHVP QTMSSHPRQA PERSAWELGI EAGVTAATYP PGPLHPHLAH
YHAPPRLHHL QIGALPLMVP DMAGYPHIRY ISSGLDGTSF RGPFRGNFEE LIHLEERLGN
VNRGATQGTI ERCTYPHKYK KVTTDWFSQR KLHCKQDGEE GTEEDTEEKC TICLSILEEG
EDVRRLPCMH LFHQVCVDQW LITNKKCPIC RVDIEAQLPS ES
//
