ID A0A3B4DNZ1_PYGNA Unreviewed; 1583 AA.
AC A0A3B4DNZ1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000256|ARBA:ARBA00031556};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000026092.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000026092.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_017560037.1; XM_017704548.1.
DR RefSeq; XP_017560039.1; XM_017704550.1.
DR STRING; 42514.ENSPNAP00000026092; -.
DR Ensembl; ENSPNAT00000005973.1; ENSPNAP00000026092.1; ENSPNAG00000011360.1.
DR GeneID; 108431423; -.
DR GeneTree; ENSGT00440000034289; -.
DR OMA; QCNSELN; -.
DR OrthoDB; 5405431at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd17721; BRCT_BRCA1_rpt2; 1.
DR CDD; cd16498; RING-HC_BRCA1; 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; IPR011364; BRCA1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763:SF0; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN; 1.
DR PANTHER; PTHR13763; BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN BRCA1; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PIRSF; PIRSF001734; BRCA1; 4.
DR PRINTS; PR00493; BRSTCANCERI.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 22..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1382..1466
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1487..1583
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 108..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1583 AA; 172772 MW; E319B0295747126F CRC64;
MTAPKAEDVK RGIAVIWENL QCPICLDLMN APVSTRCDHQ FCKFCMMQLL EKSKRKEANC
PVCKMKVTKR SLQESPGFQR LVEGLQNLVQ SYEFDTCTSY FNGVPQKRKE TSVETQSSDQ
QRSEENAFSE SDMVEKSASR SSTAAAKDAF AKLMDLPASC PVSSEQDCSD SGVGDLPQVF
EKKPGELEDV PSTLEVRQNN SLTRNDGSED AETNVSQKRS SRRAKRIGLE PNRIVDKRQK
KSVEKVAEWL LKISPSSDTQ AKDNSEDLPT SNSCDSDRES ICSSSSTVVN VKVDDQDDAS
PPRDVPGRGL EEQVFGAVYK RERKGAKSKV NRSFSAERHI VTDPDHINLV VEEGGIKRNI
PKRKRSCALT PADFIKKSSD DKGERLVCDQ TEDPKESVVP NVEENKQDHI DESNTDGPLK
CVEEHEKLVD NCLDEKRDDN AENIEASPVF EVPLKRPGRR SKIKMQDAWK DLGCELKKDS
ICDDKTGRKR RISRNNCEST KDGHLEESKI AKCAKSLTLV STAGDEDVSL MKQLKSKPNL
VEAEINIESY PSTAEPQSPD ARKTRRSLRL QAFVAEVQGA RKRRRSTQTP LKPAHGSENN
PSQSTCSNQP KADNTNVNED NANVNQGNAS AGQVQSEQTE TSVRKNGCVC TSSFEKIETM
ETVEEAATFT CIPEANVPDQ SSLVSVVPDT ADQGGQNVPC SSVAVSSPGP LVADAPDSTL
PLKRQDSPST GVVAPSVVQT LTDGVLMSAG ENGSMNVEGD ANDSELDTEL LMKSFKGTKR
KSFLLGSPEP LHAETQQDAL EKIVEEEKQL LTEIPVISQD RDIRAGLANV CESEQPLNPC
VLAFYEKQPQ RSPSSFGNTG VASISILQAK SPALAKENQE NAFLKSTTNS PSSGLSPNKV
ARSSQDSRLS TNSCQLFFVG TTQDVVQICS SRGLGNQQSS KLTIHPPRTS DVQKETQGIH
WQTKVSLDPI KSSDIPVGGL PNSGVHSNNF ESSITPDGLL PEGAGSHALQ IIEPLTSQSL
DKVKEMEAEI LSQPCVQKKR KAQRLESSES DLSAEEDDLP TMAQIFKSHC SPSPSGQEEP
LSDLANQDGH QLQEPNPGLQ SPSQHSRPHS EPAPGTQSSQ LSQCVSPSQN REHLENVNAT
TVAAAVQDVN LPEPPCREEW ITSSQGSVDL FGTPEESEAV DGVCGNVALS RDSSQYSSEI
INTQQKEEMQ QELRRLERMM ALVSEALQRK ELDSGATAQT EEPDPSHSDQ HTAADLGEAG
RRVPGNPSDR QSGPDSGRDH VCVPPSPRAP DGLEAPQSHA PLTRGQAKTA GQQTGRGSQK
SWNSRRRSLR KLEAGPEVKD HSVVSEDSPT GSMKGREAKE PQREASVSGR LGISSTAGKM
ELVSSGLSAS ELAMVKKFAR KMHGSLSREM TPNTSHVIIK TDANLVCERT LKYFQGIAGR
KWVVSSLWIS ECFKQGKVLD EAQFEVRGDV INGSNHNGPL KSRTTAYDNL LMKGYEICFQ
GSFTGMTTDQ MEAMVEMCGA TVMKDPLMFS KHGACQLVVV QPGSDDSQSY YSALQKKATV
VTRAWLLDTI ATYTLQNPED YKP
//
