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Database: UniProt
Entry: A0A444WWS0_ARAHY
LinkDB: A0A444WWS0_ARAHY
Original site: A0A444WWS0_ARAHY 
ID   A0A444WWS0_ARAHY        Unreviewed;      1593 AA.
AC   A0A444WWS0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ahy_B10g100490 {ECO:0000313|EMBL:RYQ81898.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ81898.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ81898.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYQ81898.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily.
CC       {ECO:0000256|ARBA:ARBA00006643}.
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:RYQ81898.1}.
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DR   EMBL; SDMP01000020; RYQ81898.1; -; Genomic_DNA.
DR   Proteomes; UP000289738; Chromosome b10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd17734; BRCT_Bard1_rpt1; 1.
DR   CDD; cd15571; ePHD; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR031099; BRCA1-associated.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR032867; DYW_dom.
DR   InterPro; IPR046848; E_motif.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR046849; Eplus_motif.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   NCBIfam; TIGR00756; PPR; 5.
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; 1.
DR   Pfam; PF14432; DYW_deaminase; 1.
DR   Pfam; PF20431; E_motif; 1.
DR   Pfam; PF20430; Eplus_motif; 1.
DR   Pfam; PF13041; PPR_2; 3.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00249; PHD; 1.
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; PS51805; EPHD; 1.
DR   PROSITE; PS51375; PPR; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          110..144
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          211..245
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          281..311
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          312..346
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          623..661
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1205..1324
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          1395..1456
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          1477..1593
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          719..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..799
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1593 AA;  178968 MW;  E2F65C96D535F79E CRC64;
     MRLYSKFSSL VHTSQPLNPK IHLCSSTFLS SSSTTATQNP VPHIVTKCIA LLQFWASSIS
     KLRQIHAFSI RHGVPLNNPD MGKHLIFTIV SLSAPMSYAY HVFAVLHDPN VFTWNTMIRG
     YAESDDPSPA LHFYRKMSVS CVEPDTHTYP FLLKAVAKSL NVREGEAIHS VTVRKGFESL
     VFVQNGLLHM YAVCGDTESA HKVFESMVER DLVAWNSVIN GFALNGRPSE ALTLFREMNM
     EGLEPDGFTV VSLLSACAEL GALELGRRVH VFLLKVGLTE NMHVNNSLLD FYAKCGSIRE
     AKQVFGEMRK RNVVSFTSLI VGLAVNGFGE EALEFFKEME EQRVKPSEIT FVGVLYACSH
     CGMLNEGFNY FRRMKDEYGI MPRIEHYGCM VDLLSRAGLV KQAYEYIQNM PMQPNSVIWR
     TLLGACTIHG HLGLGEIARS HLLKLEPKHS GDYVLLSNIY AAERRWSDVQ TVRRSMLEDG
     VRKTPGYSMV ELGNRVYEFT MGDRSHPQSK DVYALLEKIT ELLKLEGYVP HTANVLADIE
     EEEKEQALSY HSEKVAIAFM ILNTPPGTPI RVMKNLRVCA DCHMAIKLIS KNQNRFRPYL
     ICQSSITMAN RTDLEEMGRE LQCPICLSLL NSPASLPCSH VFCNFCIVKS MKSSSDCPVC
     KIPFFPREVR PSPRSLNLVN IYKRMERSSG MNLFLTQNPH HSKFSDEETQ CQTDADCVRE
     DATRSHRNPA QKRKTLKNSV SGKENVPDTA KPSLPAKKRV QVPQDPLSET PFKNLSSGDS
     LYGTRKEGKE KDTDTANENP LQSERDVPVL SPFFWLREEE GVENLSQQTF GDKLIDESPT
     PSPPSFSDLK DSDDENPTKL TSDEVQNKTS FDLFDSELFE WTQRPCSPEL FSSPVKLQPL
     SAGVISENQE DLLDASKELE RNKSSDYAEN TKLQNSENET RLSDVLQPSV TSPFRSSGDI
     NGAKKYKKRS RKMREKAAQE QVVEQQDSIE GINVDSNRSL EITEDQSREK QQASNLGKTN
     LKCKRVCFDT RTDSNISVVF RNGEVNMAKD SYISHSQKET NKLACQMIPG KCQSKRSGKQ
     KLNYVQDQAE ELSCMQNQTD DELAGSASSM LSQQTDKNGK MSNKRQIKGK VFRKSISCGS
     ELRSTKKLKL SSDFISQTKV GEQIQPNEST QRCPGVKVLD DTSKEKCSTW MHVPVLPNCE
     SQAEKYQCVF CHSSEESEVS GPMMHYYGTK PVDANYEGGS KVIHSHRNCT EWAPNVYFDD
     NAINLEAEIS RSRRIKCGFC GLKGAALGCY EKSCRRSFHV PCAKWTTHCR WDMENFVMLC
     PLHTSCILPC ESSGSKGKSN KCRTRDSKSL AFKHGPTNQK GTALGSYKKI VLCCSALSIQ
     ERDIVSEFQR VTKVTVLKKW DSSVTHVIAS TDENKACKRT LKVLMGILEG KWILNIEWIK
     ACMKEMKPVD EESYEINLDI HGIHDGPHLG RLRVLNKQPK LFDGFKFYFV GDFMPSYKGY
     LQDLVTAAGG VILNRKPVSG DANSTSPGMH PPQTLIIYNL ELPDKCSPSK RDTISTQRRH
     DAEVLASSTG SKIASNTWIL NSIAACKLQI LAE
//
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