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Database: UniProt
Entry: S7Z3S3_PENO1
LinkDB: S7Z3S3_PENO1
Original site: S7Z3S3_PENO1 
ID   S7Z3S3_PENO1            Unreviewed;       208 AA.
AC   S7Z3S3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=CENP-S associating centromere protein X-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PDE_00101 {ECO:0000313|EMBL:EPS25170.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25170.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS25170.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CENP-X/MHF2 family.
CC       {ECO:0000256|ARBA:ARBA00009359}.
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DR   EMBL; KB644408; EPS25170.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7Z3S3; -.
DR   eggNOG; ENOG502S98G; Eukaryota.
DR   HOGENOM; CLU_071333_0_0_1; -.
DR   OrthoDB; 2716993at2759; -.
DR   PhylomeDB; S7Z3S3; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR018552; CENP-X.
DR   InterPro; IPR009072; Histone-fold.
DR   PANTHER; PTHR28680; CENTROMERE PROTEIN X; 1.
DR   PANTHER; PTHR28680:SF1; CENTROMERE PROTEIN X; 1.
DR   Pfam; PF09415; CENP-X; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   208 AA;  22418 MW;  FAAECAD84DD497F0 CRC64;
     MVDAPAQKKR QRPFKPPSRA SSSAGPSASA PKPKPKPKQT NSKAATNKAT SLATASNSNS
     HKAPTPAKRK RDDPPPSASE SADGSDADSD ASAHSRERSL SQEPDFILAE IITHHEKNED
     VNSSDPQIPS KLLTRLLHHH FQNEKTKIAK DANTVVAKYV DVFVREAIAR AAYERAGADN
     AATGSRIGDG FLEVEDLEKM APQLTMDF
//
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