ID   A0A183BMQ8_GLOPA        Unreviewed;       793 AA.
AC   A0A183BMQ8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=RING-type domain-containing protein {ECO:0000313|WBParaSite:GPLIN_000189300};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000189300};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_000189300}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A183BMQ8; -.
DR   WBParaSite; GPLIN_000189300; GPLIN_000189300; GPLIN_000189300.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16457; RING-H2_BRAP2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR011422; BRAP2/ETP1_RRM.
DR   InterPro; IPR047243; RING-H2_BRAP2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR24007; BRCA1-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR24007:SF7; BRCA1-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF07576; BRAP2; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF02148; zf-UBP; 2.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00290; ZnF_UBP; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50271; ZF_UBP; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          45..83
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          80..170
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          502..592
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   COILED          192..303
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          616..727
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   793 AA;  90391 MW;  FD6B0B9ACD604182 CRC64;
     MTSNSTSIEP EKCQLRFVDI LETEEEAANI VGLLADPTYG ETPICSVCLD RMEENNVLTI
     LCNHSFHAEC IGQWADTTCP ICRYAQTPEL IPDQKCFDCG RTSDLWMCLI CGNVGCGRYA
     AAHAHQYKTS HIFTLQVGGK LVWDYAGDNY VHRLIESATD GKMIEYDGGG DGFEKGEEKI
     SAVQLEYTCL LTSQLENQRI HFEEKLREAE QRFNEHGRQA QQKLNALESE LSTVRAEREA
     TREELASTSA AKQLLDRKFQ QTHQRAQHLQ RELEEEKHLS SLLSKDKELL SKQKEELERL
     RRQEIVGLEE QLRDLMAHFD TQAKIQQQMD AGAVSKEELE TSTMDGDSRP FFYGNPFVEK
     HKGVLRFSKN CSPPNDCAML CMVDVPAFFT CRELVNFVRP VAPEIALMKV IRDDAANKYM
     VAIKFKSAAA ALSFHKQYND IEFNSIEPEK CQLRFVDILE TEEEAANIVG LLADPTYGET
     PICSVCLDRM EENNVLTILC CPICRYAQTP ELIPDQKCFD CGRTSDLWMC LICGNVGCGR
     YAAAHAHQYK TSHIFTLQVG GKLVWDYAGD NYVHRLIESA TDGKMIEYDG GGAGDGFEKG
     EEKISAVQLE YTCLLTSQLE NQRIHFEEKL REAEQRFNEH GRQAQQKLNA LESELCTVRA
     EREATREELA STSAAKQLLD RKFQQTHQRA QHLQRELEEE RHLSSLLSKD KELLSKQKEE
     LERLRRQEIV GLEEQLRDLM AHFDTQAKIQ QQMDAGAVSK EELETSTMAY TLNVEKLNRQ
     NINDLITMIF VFD
//