ID A9V009_MONBE Unreviewed; 930 AA.
AC A9V009;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDQ88929.1};
GN ORFNames=MONBRDRAFT_25650 {ECO:0000313|EMBL:EDQ88929.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88929.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ88929.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH991552; EDQ88929.1; -; Genomic_DNA.
DR RefSeq; XP_001746034.1; XM_001745982.1.
DR AlphaFoldDB; A9V009; -.
DR STRING; 81824.A9V009; -.
DR EnsemblProtists; EDQ88929; EDQ88929; MONBRDRAFT_25650.
DR GeneID; 5891432; -.
DR KEGG; mbr:MONBRDRAFT_25650; -.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; A9V009; -.
DR OMA; WHESSTP; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR003903; UIM_dom.
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; PF00097; zf-C3HC4; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 24..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 682..782
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 805..914
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 152..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 99675 MW; FEAD145AC9B08D4C CRC64;
MAGSSLVTAE LKQHLQEFEK ALQCAICLGL LEDPLRTGCH HEFCRGCLHS MLASSRSTPC
PLCKTPVTKR YALIISCLLL SFCVLKSLNE CPSLSQVIQQ SKHVIVALNH DLKQQGLDDE
MADVFPASQL PGMQSQDSPL AANQNTPIAL HTTSSAQVTR PSIPVADRNN TKTAKRLHVF
ADTVEPVPEQ APPAKNQKTA SRASRQASTA RTGKSRSRGN AAADPAGTMA TKALATTSAR
QTKARQQRRK KRDTAQLSEE EQIALAIELS RKSARAERIH RRDSSPEASD VEMEEDVTCG
RAVPQSAQHN AQSWSPKTVR PSPETAAAQT SQDPLIKTSP KVTPSKNKDA ETEDEDDDEW
AGVRPSRHQT GAQAGRLGQE IANLEVRLAD SDSDSDFDLP SINLEINTSQ APPANANLPL
PLVTANTVAK PPSQPTLTSP ARGPVSDKGP IADVLVSKDS SRSSTASPLP KASASGSDDE
SVRSRPRGRA SLLARNGSEA LLSPRGTPPT ISDSRPRTHS SSIELARASP TPSLAPTPHE
TTLASEPMSF GSFTAAQRIP STIDMSASQS GTLMLFPDPP APRKQATLAT PAAASPSASS
RVAPPAAPPQ PEPAAVQKPT QPETMESWHE SSTPPEPILP RPAQRREAPM LDQISATMDE
SQALEPPSTA GAVMPAAEEE AAEPLFLSGI VLLASGSGTG QSNGLDIESL LTRARACGAQ
VCHEFAPSVT HVIGPAKEDG VAAQYTMKLM LGLLHQKWLV SWGWLDRSLA SGTRADEATY
ELRRMMAEVE RDGIPAAARL DPTHQAGRLF RGICFALSDK AVGEVGETWR DEVLAVIRAT
GATLKSEREV LDIARRQAPA DRDCFVIGSE STYKMHRTDP LWAEAAQLDC LVELYWITDS
IAHLELQAVE EYLLNDEIFE ADTQGTEAPI
//
