ID G0WEE7_NAUDC Unreviewed; 1393 AA.
AC G0WEE7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Restriction of telomere capping protein 1 {ECO:0000256|ARBA:ARBA00015098};
GN Name=NDAI0G03810 {ECO:0000313|EMBL:CCD26158.2};
GN OrderedLocusNames=NDAI_0G03810 {ECO:0000313|EMBL:CCD26158.2};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26158.2, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26158.2, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the WD repeat RTC1 family.
CC {ECO:0000256|ARBA:ARBA00008863}.
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DR EMBL; HE580273; CCD26158.2; -; Genomic_DNA.
DR RefSeq; XP_003671401.2; XM_003671353.2.
DR STRING; 1071378.G0WEE7; -.
DR GeneID; 11495657; -.
DR KEGG; ndi:NDAI_0G03810; -.
DR eggNOG; KOG0269; Eukaryota.
DR HOGENOM; CLU_008512_0_0_1; -.
DR OMA; GRDGKCC; -.
DR OrthoDB; 119005at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:InterPro.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR037590; WDR24.
DR InterPro; IPR049566; WDR59_RTC1-like_RING_Znf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR46200; GATOR COMPLEX PROTEIN WDR24; 1.
DR PANTHER; PTHR46200:SF1; GATOR COMPLEX PROTEIN WDR24; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF17120; zf-RING_16; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 242..284
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 345..376
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1346..1385
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 14..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1393 AA; 155855 MW; FA9113F2D5C15F40 CRC64;
MMNMPPRRDI AVSRNKMHST HHGSLPRSYS SIGSSMKNDS STITSINRSS LRTSLHLPSS
SERSSYYIQK HFHKNNISNN GNSKNTDSVG STDKTQGKIS NNNGNILRHA DPAESKQSSG
LLYSHRTNKE LSSISKINDP NNNGLMCAGK DHLGFYRFSP ENESITLVHD ILDSNSGSLR
HGVKATNNRI KRGKKIKLST IADIKTGFGE QKNLIAICTN STDISIFDII KILILKPLIN
HISEHTRSIN SFDFNMIQTH LIISGGQDAC VKIWDLRSNA TRNSTPCDIS FNTASDSIRD
IKWMPGHDFV HSINNGAGYK FASIHDSGYL LKYDIRKPGQ IEKKINAHTG PGLCLNWHPH
HNYIATGGRD GKCCLWYLGD KPSPNLENAM EQINEMSQHP PSSSHSMSAA SVLNHTWNPG
NLNSSNVSSF PEMTINTGSP ITKLKFRPSF DVNVFNSLLA LSSMGDEAQV SIYSLARKYI
PKNVLLTSAS SLGLAWWDDA LIFNVDKNSF INGWDISKEP TVLQNLPKNV TKWRDLDGNG
LLFIDQKAGS YEVANDVKPV ISKKALASNN RVNINQILSP IPSQSTADTV IPTTTKKIMQ
NIKMGLTGHS KRPSMHSLER PSLGQSFSTR SVLQNKNNNT VLPPKNVSSL SLSNVQNNHS
NIVDVTINGL IEKRTIDEPI IVTLDLPCIL NDIRMSQLPK DLVTEETMRI KESPVEVFKY
LAKELEFSYI KGRHYDIENG IDDDKIRDKD QYDNEKSKNE AHEMLGEKYG LLENTTWTNL
IANRRKEEHE ASNSDDATSI SKSSISSHIL DRSVTGAGES NEKSPSIKPP SSLRKTAKLR
KEREISKLTE SMHQSAAIQI QDKTDTLIDL VSICNHNSEV YFRIGDSPNF KTWILIRDAL
LWELKRLNDP LKREVIYDKE QLTHVMGKIQ EGHAKDTDDK TQKTLRNDKN RISKRIESID
SDSSKFITSD RGSFIEENSL TVEQSSPEIK EVSETSEEDE LRLAKQEECP QQQKSMLESI
TELRKLSKLG DGSSQDASAV EDENELSKRN VNNVQPKSAI FQSDKESVKT SSEDKTIESS
GDQGKNDDVV AVATKTKPTK IIPILRRKSE RPSFIDTFMT AIPPTDGAMG TKSPQLCNTP
SPFSNTSPRS HMSSLRSFAG SPSDLTLFRR KTTSYFQNEA LDTSGLDLTS LSSGENDEII
EPERKVHVIP PWNTKRIIQQ VYEQAVAEGN VFLVINILLL FQDMYHITSM DIVKSSVYHF
ISLLHRYELF GCAASLLKYC PWNDIMGAEG DQSTIQIYCE KCGALLMNEV SKRKLTMEAQ
QTHDKTVLGK FGYWYCDSCR KPNSLCVICE CPMKKLTLTA LRCGHEAHFQ CFKNWFLDEG
MNTCPAGCLG ELI
//
