ID A0A0E9NRK3_SAICN Unreviewed; 972 AA.
AC A0A0E9NRK3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=G7K_6142-t1 {ECO:0000313|EMBL:GAO52055.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO52055.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO52055.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52055.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO52055.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO52055.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GAO52055.1}.
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DR EMBL; BACD03000058; GAO52055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NRK3; -.
DR STRING; 698492.A0A0E9NRK3; -.
DR OMA; PMKRHNI; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18433; BRCT_Rad4_rpt3; 1.
DR CDD; cd17723; BRCT_Rad4_rpt4; 1.
DR CDD; cd17731; BRCT_TopBP1_rpt2_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 5.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PTHR13561; DNA REPLICATION REGULATOR DPB11-RELATED; 1.
DR PANTHER; PTHR13561:SF20; DNA TOPOISOMERASE 2-BINDING PROTEIN 1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 3.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00292; BRCT; 5.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; BRCT domain; 5.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50172; BRCT; 5.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..85
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 107..195
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 331..426
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 438..521
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 586..680
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 912..954
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 218..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 107241 MW; FAF8B7C26D01474C CRC64;
MRDRAAEYDL TRSARPLARV VLCCTSVPSD IRSLVVQQAT KMGASYKADL TSDVTHLIAG
DIMTPKYKFS TKHRLDVKLM KVEWIGAMYE RWLEGEDINV EEYSEKFLLP PFLNLRICVT
SLPPSDRQKL HSLITSNGGH YSPDLSKTCT HLIAASKEGK KYEYAVKWGI RIVGQEWVRD
SLVRGAALSE ELYSLDLPEE ERGRGAWDKA IEKAEGLAPA KKRKQVSRVD EDEDDKPVLK
KKRSQLSQSF LGSAPTSNKT TPAGAAPVDD LWKDIFHMKP LAASTPIKPQ ADAAWHSDDE
EELDLSKVHP PPAYDESGTP ALDEPEEEKQ KEKGIWSGVY FYPWGFSEEK ANILYIYLTS
HGGHCVDTLS ALPHDKPERS FVVVSHSVPI VDCPNVPSER ATLVTEQWLE RCVHFGRRVE
IDDWVVSRPL VRTHIPGMKG LTIAMTGFTG VDLLHMSKLI NILGASYSET LRRDTSALIA
LKAEGRKWKM AGEWGVRILS REWVEDVARK GEVLGVGRYA MDGLGGGELP KREVQPMGPP
LMTREKQKER GSERRLEEGH SSRRLSMRMS DEDDEVIDKK KVRNATRARV LEGCTVCVSS
KLSDMTSEYL AIAVSLGANT VQTFSAGAGI THLVHESSRH ADAHPDFRAA KEAGCKIISP
SWLFECRKKA TKVDEAIFPH THAFETDAKE RVLADVGAKR AYSAPSAPVQ DPRVASGIGN
LAKLLQRNVT AGVLFDTAPK RVRGKLQGRA TASITTHRST SDPAPFDAAP NPLADEDARP
SQDGVKYDDP DAQREKRRIL MKLNGGVVDL TEHDDAGERG RSTREMSPET SSTRTDVPNI
YTSMTARREG TVIPENAAVV DLTESPGLAA LLQAANDVAH IDLSNESTEA SPQLLRHPPP
EPPSNKLSHI KCVICLESPT DLAATPCGHL FCDLCIRSAI QTTAGSGGKC PVCRRKLTVK
QIIPLEIKLG RT
//
