SHU2_ASHGO
ID SHU2_ASHGO Reviewed; 201 AA.
AC Q74ZQ8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Suppressor of hydroxyurea sensitivity protein 2;
GN Name=SHU2; OrderedLocusNames=AGR140C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous
CC recombination repair (HRR) pathway to repair MMS-induced lesions during
CC S-phase. Required for error-free repair of spontaneous and induced DNA
CC lesions to protect the genome from mutation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SHU2 family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54630.1; -; Genomic_DNA.
DR RefSeq; NP_986806.1; NM_211868.1.
DR PDB; 6DEX; X-ray; 2.10 A; B=1-201.
DR PDBsum; 6DEX; -.
DR AlphaFoldDB; Q74ZQ8; -.
DR SMR; Q74ZQ8; -.
DR STRING; 33169.AAS54630; -.
DR EnsemblFungi; AAS54630; AAS54630; AGOS_AGR140C.
DR GeneID; 4623108; -.
DR KEGG; ago:AGOS_AGR140C; -.
DR eggNOG; ENOG502S0XB; Eukaryota.
DR HOGENOM; CLU_1115918_0_0_1; -.
DR InParanoid; Q74ZQ8; -.
DR OMA; WLKLHLN; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..201
FT /note="Suppressor of hydroxyurea sensitivity protein 2"
FT /id="PRO_0000409731"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:6DEX"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6DEX"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:6DEX"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6DEX"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:6DEX"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:6DEX"
SQ SEQUENCE 201 AA; 22893 MW; 397D1465255D3CA5 CRC64;
MAETNFNYSK LLRNLVTEDN VLNEVVVSFL YQLFPRDLFV RAFSLLESAD MFIYVWMPTP
KEADELLESL YNGTPLYRPI VRPRGPDDRP VCVDLDHWFC SCTEFAATCR PHLVGDTPLS
DALFRPTEAA DPDDCFGMLA GLQHLRADPE KLMCEHLFAF AILLQTDLRV LRHFSTGPGA
QVFVLGITSI DEWLKLHLNV V