GenomeNet

Database: UniProt
Entry: G3AKI5_SPAPN
LinkDB: G3AKI5_SPAPN
Original site: G3AKI5_SPAPN 
ID   G3AKI5_SPAPN            Unreviewed;       626 AA.
AC   G3AKI5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN   ORFNames=SPAPADRAFT_135958 {ECO:0000313|EMBL:EGW33590.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW33590.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC       stranded DNA-binding heterotrimeric complex, may play an essential role
CC       in DNA replication, recombination and repair. Binds and stabilizes
CC       single-stranded DNA intermediates, preventing complementary DNA
CC       reannealing and recruiting different proteins involved in DNA
CC       metabolism. {ECO:0000256|RuleBase:RU364130}.
CC   -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC       A complex (RPA). {ECO:0000256|RuleBase:RU364130}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364130}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC       {ECO:0000256|ARBA:ARBA00005690, ECO:0000256|RuleBase:RU364130}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL996501; EGW33590.1; -; Genomic_DNA.
DR   RefSeq; XP_007375105.1; XM_007375043.1.
DR   AlphaFoldDB; G3AKI5; -.
DR   STRING; 619300.G3AKI5; -.
DR   GeneID; 18869930; -.
DR   KEGG; spaa:SPAPADRAFT_135958; -.
DR   eggNOG; KOG0851; Eukaryota.
DR   HOGENOM; CLU_012393_2_0_1; -.
DR   InParanoid; G3AKI5; -.
DR   OMA; FNDQCDA; -.
DR   OrthoDB; 1122034at2759; -.
DR   Proteomes; UP000000709; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04474; RPA1_DBD_A; 1.
DR   CDD; cd04475; RPA1_DBD_B; 1.
DR   CDD; cd04476; RPA1_DBD_C; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR   InterPro; IPR047192; Euk_RPA1_DBD_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013955; Rep_factor-A_C.
DR   InterPro; IPR007199; Rep_factor-A_N.
DR   InterPro; IPR031657; REPA_OB_2.
DR   InterPro; IPR004591; Rfa1.
DR   NCBIfam; TIGR00617; rpa1; 1.
DR   PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR   PANTHER; PTHR23273:SF4; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT; 1.
DR   Pfam; PF04057; Rep-A_N; 1.
DR   Pfam; PF08646; Rep_fac-A_C; 1.
DR   Pfam; PF16900; REPA_OB_2; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU364130};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364130};
KW   Metal-binding {ECO:0000256|RuleBase:RU364130};
KW   Nucleus {ECO:0000256|RuleBase:RU364130};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Zinc {ECO:0000256|RuleBase:RU364130};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT   DOMAIN          6..102
FT                   /note="Replication factor-A protein 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04057"
FT   DOMAIN          301..396
FT                   /note="Replication protein A OB"
FT                   /evidence="ECO:0000259|Pfam:PF16900"
FT   DOMAIN          457..617
FT                   /note="Replication factor A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08646"
FT   REGION          138..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..172
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  70642 MW;  3FB007BF1F077A82 CRC64;
     MTLPPLTTNA LKDIFSTTAK DTVKTPLILQ VTNIKHVEGG SRSFRVLLFD GVFSGQGLVE
     ESCGTYLKNN GFARYQYIQV NDFSTVITQR HIIILKNVEI LGQGEKTENQ AKQIEAYYKE
     HPEEDFLALQ KAKGETYPNA DVAKTRSESP FTPQTTTSTP APPAPKPAPP VSASGAPIRI
     TPIETISPYQ NNWTIKARVS YKGDLRTWSN AKGTGQLFSV NFLDESDEIK ATAFNETAER
     AYNLLEEGKV YYISKARVAA AKKKFNHLTH PYEITMEKDT EITECFDNTN VPKLHFNFVK
     LNKIQDLESN AIVDVIGALK IVNEPFKITA KSTGKEFDRR NITIVDETGF AIEMGLWNNT
     AVEFNIEQGS IIAFKGCKVQ DYNGRSLTLT QQGSVIPNPE SPEAYQLKGW YDNQGINESF
     KSLKVESSGA SSNQIENRKS IAQAQDENLG KGEKPDYFTV KATISYTKPD TFAYPACPNV
     VASNAGSQQA RPSQPCNRKL VEQPTDGTWR CERCDINYPE PTYRYIYNCS ILDETGQIWV
     TLFDNEARKL FGIDAGELTK IKEEDQDEFT RRIEDISFKE YQFRLRARQD TYNDQLRVRY
     QAVGIDFIDY STEAEYLCKQ LDNLLN
//
DBGET integrated database retrieval system