ID A0A3Q1F5M1_9TELE Unreviewed; 816 AA.
AC A0A3Q1F5M1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=BRCA1-associated RING domain protein 1-like {ECO:0000313|Ensembl:ENSAPOP00000011589.1};
GN Name=BARD1 {ECO:0000313|Ensembl:ENSAPOP00000011589.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000011589.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000011589.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q1F5M1; -.
DR STRING; 80966.ENSAPOP00000011589; -.
DR Ensembl; ENSAPOT00000019198.1; ENSAPOP00000011589.1; ENSAPOG00000014164.1.
DR GeneTree; ENSGT00940000156532; -.
DR InParanoid; A0A3Q1F5M1; -.
DR OrthoDB; 2478587at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd17734; BRCT_Bard1_rpt1; 1.
DR CDD; cd17720; BRCT_Bard1_rpt2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039503; BARD1_Znf-RING.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF14835; zf-RING_6; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 28..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 453..485
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 486..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 519..551
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 605..687
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 701..814
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 172..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 88510 MW; 92CC1447D29B5E70 CRC64;
MDDNFGVQTK DWENTKEAVA NFRRLLLCSK CSSLMKEPVC LGMCEHMLCR SCAGPQAGDG
CVVCRSPAWV KDIQINRQLS SIVQLFCDLE SLLDPVKQPD SAVGEIQTQP ESSVFKNKKH
FKIWFSPRSR KVRCTVEKPS DATVPDSRSP GETAAAQLST LTAQRGDLSV FNFTSSSQDS
GSSSSQRCHS ESRNVKKRSN KKNDISRRVV VQGAGRATRK QTKQNMKKKM LEAINQKWGI
TEEVQASSEN EQPSADGARR SSKRVSFLSP PVTSDEPQPE VAQGSANELS AARSTMRESL
SGGSITVLNY QTQPGQSMSN SGVQDDKLSA NDPNPDDCPD KQDTLSPTEL SSKRSRVAEK
NCTLESTPKR PRASPGRRRK SVGQMSPAVL NPSSLTGPRC DKKTKTSRGE VGSSPSALLP
AISERHRKSP RSPSASVGRP SSGSPAVMKR NHKGETPLHL AAIKGDVEAV KELLDQGADP
NLKDNAGWTP LHEACNLGHL AVVEVLITRG ALLNTPGYEN DSPLHDAVRN GHPAIVKLLL
QFGASQNVLN LYGKRPADYA ASLEMLEIFQ EASEGTQYAN AHASSSPSAS LTVVKECVRR
DQSAVFLATK LSRPEQRKLA KLGPLLGGRT ADAFSGSVSH VVVPEGQMPT TYSTLLGVLA
GCWVVRYSWV EACVQAGKWM PEAEHEAGEG PQRSRINRCS LLPPLFDGCF FFLLGSFKAP
TKDELTRLIR EGGGQLLSRQ PKPDSDVTQT LSAAAYHALP GSDQALCTQY IIFDPQGPHK
PAVVRRGKVW SAPSTWIINC IAAFRLLPVA DPQMLV
//
