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Database: UniProt
Entry: S9XHL5_SCHCR
LinkDB: S9XHL5_SCHCR
Original site: S9XHL5_SCHCR 
ID   S9XHL5_SCHCR            Unreviewed;       265 AA.
AC   S9XHL5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Alkyl transferase {ECO:0000256|RuleBase:RU363018};
DE            EC=2.5.1.- {ECO:0000256|RuleBase:RU363018};
GN   ORFNames=SPOG_03709 {ECO:0000313|EMBL:EPY53171.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY53171.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY53171.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SIMILARITY: Belongs to the UPP synthase family.
CC       {ECO:0000256|RuleBase:RU363018}.
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DR   EMBL; KE546988; EPY53171.1; -; Genomic_DNA.
DR   RefSeq; XP_013021427.1; XM_013165973.1.
DR   AlphaFoldDB; S9XHL5; -.
DR   STRING; 653667.S9XHL5; -.
DR   EnsemblFungi; EPY53171; EPY53171; SPOG_03709.
DR   GeneID; 25038026; -.
DR   eggNOG; KOG1602; Eukaryota.
DR   HOGENOM; CLU_038505_0_3_1; -.
DR   OMA; FDRRDLW; -.
DR   OrthoDB; 521455at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IEA:EnsemblFungi.
DR   GO; GO:0019408; P:dolichol biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   NCBIfam; TIGR00055; uppS; 1.
DR   PANTHER; PTHR10291:SF43; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT DHDDS; 1.
DR   PANTHER; PTHR10291; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363018}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..265
FT                   /note="Alkyl transferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004560737"
SQ   SEQUENCE   265 AA;  30650 MW;  985088A4FD7FC3AF CRC64;
     MGSLLDWLIH FPPLLWGLEQ VEEVAIRALK HGKIPQHVAF VMDGNRRWAR EHRVETIEGH
     SLGFETLKNL LRVCLKMGVK EVSTFAFSIE NFKRSKHEVD ALMDIAKNSL NQITAHGDMV
     DQYGIRIRIV GDLALLKPDV YETVVNVVES TKNNTRATLN VCFPYTSRHE ISNSVQSIVH
     LAEDGKLVPE DIDESLFEKH LLLNDSHPLD WLIRTSGVER LSDFLLWQVH EDSQISFIDS
     YWPDFSIWRF FPMLIRYQLQ SQQGE
//
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