ID A0A395SUU6_FUSSP Unreviewed; 252 AA.
AC A0A395SUU6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA replication complex GINS protein PSF2 {ECO:0000256|ARBA:ARBA00015139, ECO:0000256|PIRNR:PIRNR028998};
GN ORFNames=FSPOR_257 {ECO:0000313|EMBL:RGP76268.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP76268.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP76268.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP76268.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- FUNCTION: The GINS complex plays an essential role in the initiation of
CC DNA replication. Has a role in chromosome segregation.
CC {ECO:0000256|ARBA:ARBA00025163}.
CC -!- SUBUNIT: Component of the GINS complex.
CC {ECO:0000256|PIRNR:PIRNR028998}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR028998}.
CC -!- SIMILARITY: Belongs to the GINS2/PSF2 family.
CC {ECO:0000256|ARBA:ARBA00010565, ECO:0000256|PIRNR:PIRNR028998}.
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:RGP76268.1}.
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DR EMBL; PXOF01000006; RGP76268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SUU6; -.
DR STRING; 5514.A0A395SUU6; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0000228; C:nuclear chromosome; IEA:UniProt.
DR GO; GO:0032993; C:protein-DNA complex; IEA:UniProt.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProt.
DR CDD; cd11712; GINS_A_psf2; 1.
DR CDD; cd21694; GINS_B_Psf2; 1.
DR Gene3D; 1.20.58.1020; -; 1.
DR Gene3D; 3.40.5.50; -; 1.
DR InterPro; IPR021151; GINS_A.
DR InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR InterPro; IPR007257; GINS_Psf2.
DR PANTHER; PTHR12772; DNA REPLICATION COMPLEX GINS PROTEIN PSF2; 1.
DR PANTHER; PTHR12772:SF0; DNA REPLICATION COMPLEX GINS PROTEIN PSF2; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF028998; GINS_Psf2_subgr; 1.
DR SUPFAM; SSF158573; GINS helical bundle-like; 1.
DR SUPFAM; SSF160059; PriA/YqbF domain; 1.
PE 3: Inferred from homology;
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR028998};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR028998};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 51..204
FT /note="GINS subunit"
FT /evidence="ECO:0000259|Pfam:PF05916"
FT REGION 88..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 27469 MW; E249B238A728E3C8 CRC64;
MALPLPSGLT PSEVAFLCEM ELVTVVPRQR LESIELLTGT TPALRPPHRS NLPLWLAILL
KKQRRANIVP PPWLHPDSLR DIVHHETKVD PKGWAPPPPP PARADSRGNA RRLNPFLDDE
TVLSPPFLPS CTSDAPAGAL PYHWFEVAEM LLAHASDDIA SSSEVRSLLR DLQEVRAAKM
RSSTAQLEGG VDGVMSLRGV GAMELAESRG FVIGVVEGVR KLGASTETTR REEEEEGGGQ
ESDEQSDEDM GL
//
