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Database: UniProt
Entry: A0A1E3NNW0_9ASCO
LinkDB: A0A1E3NNW0_9ASCO
Original site: A0A1E3NNW0_9ASCO 
ID   A0A1E3NNW0_9ASCO        Unreviewed;       398 AA.
AC   A0A1E3NNW0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=SGF29 C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51518};
GN   ORFNames=PICMEDRAFT_71807 {ECO:0000313|EMBL:ODQ47775.1};
OS   Pichia membranifaciens NRRL Y-2026.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ47775.1, ECO:0000313|Proteomes:UP000094455};
RN   [1] {ECO:0000313|EMBL:ODQ47775.1, ECO:0000313|Proteomes:UP000094455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ47775.1,
RC   ECO:0000313|Proteomes:UP000094455};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV454002; ODQ47775.1; -; Genomic_DNA.
DR   RefSeq; XP_019018888.1; XM_019164013.1.
DR   AlphaFoldDB; A0A1E3NNW0; -.
DR   STRING; 763406.A0A1E3NNW0; -.
DR   GeneID; 30180700; -.
DR   OrthoDB; 979810at2759; -.
DR   Proteomes; UP000094455; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR   CDD; cd20393; Tudor_SGF29_rpt1; 1.
DR   CDD; cd20394; Tudor_SGF29_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   InterPro; IPR037802; SGF29.
DR   InterPro; IPR010750; SGF29_tudor-like_dom.
DR   InterPro; IPR047288; Tudor_SGF29_rpt1.
DR   InterPro; IPR047287; Tudor_SGF29_rpt2.
DR   PANTHER; PTHR21539:SF0; SAGA-ASSOCIATED FACTOR 29; 1.
DR   PANTHER; PTHR21539; UNCHARACTERIZED; 1.
DR   Pfam; PF07039; SGF29_Tudor; 1.
DR   PROSITE; PS51518; SGF29_C; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094455};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          256..398
FT                   /note="SGF29 C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51518"
FT   REGION          124..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43002 MW;  361BC16DE351D9D7 CRC64;
     MSWDNIVLSL QETSNTLLAE NTKAISTKAK PKAKNKVKSK NIDDDSTNGL NQISLDVLLK
     VSKQLTTTLE DVEMFLKEKD VSFNTTSLAT DESIHDLIPS NEADDIDNEN LAFEGDLTAG
     RTAISSKEMS ANSTSTNTTM TYQSGLNAKG RGRGRPQGST NSRLQGSGVS ASAVSSKSFS
     AHSNNTASTN AEADEGSDNT AVNSTNSVGN SSSATGAAVS DKLITIGARY GYPPPPPLSS
     YNGKIGRSFY TSAYNPSTPI LPNSQVAYCP SNGRDGANNF ATMHSEWILC RVLRVISETR
     FEIQDPEPDE MHPQGQVFRA NYKEIILVPL HLVSSSISKL KEYKSGTRVL AKYPETTTFY
     PAEVMASKHG NCMLRFEGEE EVGKLTPVDR VFVLPCPK
//
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