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Database: UniProt
Entry: A0A178AQ83_9PLEO
LinkDB: A0A178AQ83_9PLEO
Original site: A0A178AQ83_9PLEO 
ID   A0A178AQ83_9PLEO        Unreviewed;       210 AA.
AC   A0A178AQ83;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 26.
DE   RecName: Full=DNA replication complex GINS protein PSF1 {ECO:0000256|ARBA:ARBA00015143, ECO:0000256|RuleBase:RU368085};
GN   ORFNames=IQ06DRAFT_327464 {ECO:0000313|EMBL:OAK98999.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98999.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK98999.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98999.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for correct functioning of the GINS complex, a
CC       complex that plays an essential role in the initiation of DNA
CC       replication, and progression of DNA replication forks. GINS complex
CC       seems to bind preferentially to single-stranded DNA.
CC       {ECO:0000256|RuleBase:RU368085}.
CC   -!- FUNCTION: The GINS complex plays an essential role in the initiation of
CC       DNA replication. {ECO:0000256|ARBA:ARBA00002340}.
CC   -!- SUBUNIT: Component of the GINS complex.
CC       {ECO:0000256|RuleBase:RU368085}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368085}.
CC   -!- SIMILARITY: Belongs to the GINS1/PSF1 family.
CC       {ECO:0000256|ARBA:ARBA00006677, ECO:0000256|RuleBase:RU368085}.
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DR   EMBL; KV441715; OAK98999.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AQ83; -.
DR   STRING; 765868.A0A178AQ83; -.
DR   InParanoid; A0A178AQ83; -.
DR   OrthoDB; 166901at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0000811; C:GINS complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd11710; GINS_A_psf1; 1.
DR   CDD; cd21696; GINS_B_Psf1; 1.
DR   Gene3D; 1.20.58.1030; -; 1.
DR   InterPro; IPR021151; GINS_A.
DR   InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR   InterPro; IPR005339; GINS_Psf1.
DR   PANTHER; PTHR12914:SF2; DNA REPLICATION COMPLEX GINS PROTEIN PSF1; 1.
DR   PANTHER; PTHR12914; PARTNER OF SLD5; 1.
DR   Pfam; PF05916; Sld5; 1.
DR   SUPFAM; SSF158573; GINS helical bundle-like; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU368085};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT   DOMAIN          20..129
FT                   /note="GINS subunit"
FT                   /evidence="ECO:0000259|Pfam:PF05916"
FT   REGION          107..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  23475 MW;  FA659E35C3F84326 CRC64;
     MYGEAANKLV QNAKRTQALP HLPPYASDLS RTIIREVRDL DRDVSSILAP YGSSFNPSAD
     PSTACALLVN HLCMRRNKRC LLAYHRVRAE KLEGYCWEGV DVLEQSGGGK EGDGGMGGKK
     DESSLSPEEE EYVRQYSDLL AAYKGQWTDI DLTGSLEPPR DLFIDVRVLK DAGEIQTEYG
     SITLTKNSQF YVRHGDVERL ISQGYLQRLS
//
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