ID A0A0E9NJ39_SAICN Unreviewed; 412 AA.
AC A0A0E9NJ39;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DUF159 domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=G7K_3981-t1 {ECO:0000313|EMBL:GAO49843.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO49843.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO49843.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49843.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO49843.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO49843.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000256|ARBA:ARBA00008136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO49843.1}.
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DR EMBL; BACD03000026; GAO49843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NJ39; -.
DR STRING; 698492.A0A0E9NJ39; -.
DR OMA; THGIKRE; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; SOS response associated peptidase-like; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604:SF0; ABASIC SITE PROCESSING PROTEIN HMCES; 1.
DR PANTHER; PTHR13604; DC12-RELATED; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; BB1717-like; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46198 MW; E2233A377AE0CFDE CRC64;
MYSTPTHSRG KDVTAPTNHS HNLQEHVWSI RSGIGKGAEE LQEELRRMNL PPREFRRPET
VRRGYNLAPN TNQPILRQLS PQNGDTLSSD PSTSSTASSP PLVLEAAKWG LIPFWTKSPP
NYAQGLKTIN ARDDSITSDR SMWHAMRDRK RCVVFCRGYF EWLKKGEGKM GKVPYFMKRK
DGGLVAMAGL WDRVRYEGSE DYIHSFTIIT THSSPSLSFL HDRMPVILPP SEIESWLDPT
RAWDKELATL LRPNDEGLEW YPVRPDVGKV GNEGVELIKP VDEAKGSLMG FFGKGGEVGK
EVKGAPPSDK DQHMKREVVK QERDEEILVG EKSNNGLSEN NAPLPLPVTP AKKRRVSSTP
EPPSTSKKIK TEMTPVPSSA KMTPKRSSAK QKANEEKKAE GSMPITAFFR KK
//
