ID A0A0D2B3R2_9EURO Unreviewed; 245 AA.
AC A0A0D2B3R2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DNA replication complex GINS protein PSF1 {ECO:0000256|ARBA:ARBA00015143, ECO:0000256|RuleBase:RU368085};
GN ORFNames=PV06_02495 {ECO:0000313|EMBL:KIW46871.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW46871.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW46871.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW46871.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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; KN847333; KIW46871.1; -; Genomic_DNA.
DR RefSeq; XP_016267087.1; XM_016403190.1.
DR AlphaFoldDB; A0A0D2B3R2; -.
DR STRING; 215243.A0A0D2B3R2; -.
DR GeneID; 27354569; -.
DR VEuPathDB; FungiDB:PV06_02495; -.
DR HOGENOM; CLU_079191_0_0_1; -.
DR OrthoDB; 166901at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0000811; C:GINS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:InterPro.
DR CDD; cd11710; GINS_A_psf1; 1.
DR CDD; cd21696; GINS_B_Psf1; 1.
DR Gene3D; 1.20.58.1030; -; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
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.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 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:UP000053342}.
FT DOMAIN 29..164
FT /note="GINS subunit"
FT /evidence="ECO:0000259|Pfam:PF05916"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 27467 MW; F6DCE6EB71EBF5CD CRC64;
MASRDLQNLQ IEQAGGKVAQ HAKRTLTLPT LPPYQTELVR GCVRETRDLD RDVTRLLEPY
TTTVSTVDED GNPTSTQQST FNPVDHPETA CALLVDHLSM RRNKRCLLAY HRVRAEKLES
LAWEGRDIDE HQQQQDPMRA GGAGDQGGGG GGSSSQQNAL SPEEESYFRK YTDLLAQYKG
QWTDVDLTGT LDPPRDLFID VRVLKDAGEI QTEYGAINLT KNSQFYVRQA DVERLIAMGF
LQRLS
//
