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Database: UniProt
Entry: W6MX38_9ASCO
LinkDB: W6MX38_9ASCO
Original site: W6MX38_9ASCO 
ID   W6MX38_9ASCO            Unreviewed;      1185 AA.
AC   W6MX38;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Maintenance of telomere capping protein 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=KUCA_T00004197001 {ECO:0000313|EMBL:CDK28215.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28215.1};
RN   [1] {ECO:0000313|EMBL:CDK28215.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28215.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK28215.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28215.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the WD repeat WDR59 family.
CC       {ECO:0000256|ARBA:ARBA00038452}.
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DR   EMBL; HG793129; CDK28215.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MX38; -.
DR   STRING; 1382522.W6MX38; -.
DR   HOGENOM; CLU_001497_0_0_1; -.
DR   OrthoDB; 23438at2759; -.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR   CDD; cd16488; mRING-H2-C3H3C2_Mio-like; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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; IPR049567; WDR59-like.
DR   InterPro; IPR049566; WDR59_RTC1-like_RING_Znf.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR46170; GATOR COMPLEX PROTEIN WDR59; 1.
DR   PANTHER; PTHR46170:SF1; GATOR COMPLEX PROTEIN WDR59; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF00400; WD40; 2.
DR   Pfam; PF17120; zf-RING_16; 1.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50908; RWD; 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|PROSITE-ProRule:PRU00175};
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|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   REPEAT          109..151
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          196..229
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          437..548
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          1131..1170
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          664..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  132781 MW;  F217C38F5EAEFBB3 CRC64;
     METQKGSPYD SATFGNSLSL RVDGAIGAMS LSPCGRDAVL AGRRGLFVID LDDPFAQPRW
     LHHVTSWEVA DVQWSPHKSK PSWVVSTSNQ KALVWNLARS STDAIEHVLH AHDRAITDIN
     FHPDNPEVLA TCSVDTFSFA WDLRTPRRPV ARWADWRSAT SQVKWNYKNP NIIASAHDNY
     FYIWDMRKGA MPLEKIMAHN GRVNGLDFSR DHETEIISCS NDMTVKFWDY GESVTEPKFT
     INTDFPVSRA RHVPFGDKGC GIMPAHGGNN SVYIVNYKDQ TGESKLRPGY IFKGHTEPVK
     DFLWRSRHSD NTSVDDRDVQ LVTWSKDNDL RLWPVSEDIY DRFNYEKNKE LPEGTKLIDF
     DYRTYRSEPV TSSDDRLKRF KKDAFVSSRG SSSRDNQFNH LDWISGVRIG QSAQAPSDSP
     NAFSFGGDSL QPANLGEEVS SVGHKFPKLR FEKISVSTGQ LILSLNGPWS ATNKEDLVFL
     RMEINFPKDY PSKTGKPTFN IEENQDLDSE KEKEILQNLN EISERFCGAG RHCLEQCLRS
     LLGEKVSLEF DAFDENDLPL DPFDIPQAGD FNDVESMPTS LSDDSDDELV PITSTSVQTE
     TDGMPFTKPA FDSTPIPKGC GAVWTASGHL VCFFIPKHEE NKPTQLKFDQ QGFTLAGTLK
     KKKAGSSVGD ASSKGGRVAS SKLEDSSGES SDSDSYSSDD SFSNDLDILQ NDRPYRSAVT
     GLMRKNVGLR HYTLGEAKSA TLGNASVPTE RSLGTQTSRG HNSNIVTIHD FSDLIPSKME
     LAYEYRMLGD TPEKLSVHNA AVAEKYGYKD IADCWKILEV ILVKDVHLPD ILNNSDLSVV
     LQHELHQKFV TDLSKVDVET NYRFYWGAHP FGSRWLARAI MEYYEKLGNI QMLAMLACIM
     HEHKLHKTDP TIPIHTPYMR PPTLVNKQSV IGRFASAKGS NVGDNELEAV GNSACSSVSS
     YDASGSVSFH SGSPERFGSY FKRGIGNVPP LPGVSPTNSG SRKSVVTMTS RTSSFLIPQK
     SHILQGAPKV KIQMFNEVAL DLSDDVYSVP LLDPAFEEKY QMYRSQYASL LFYWGLPVNR
     IKVLKFNYED SIFKNSAAVD EYRGQVGLNG YSDTHIKDLS KAKVLKEQKL CNYCSMTIKK
     RLIVCTTCNH IMHADCAMQW WEGEQQTECP GGCGCICLSK KFYEH
//
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