ID A0A2P6VL47_9CHLO Unreviewed; 990 AA.
AC A0A2P6VL47;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=C2E20_2093 {ECO:0000313|EMBL:PSC74787.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC74787.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC74787.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC74787.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Component of the replication protein A complex (RPA) required
CC for DNA recombination, repair and replication. The activity of RPA is
CC mediated by single-stranded DNA binding and protein interactions.
CC Probably involved in repair of double-strand DNA breaks (DSBs) induced
CC by genotoxic stresses. {ECO:0000256|RuleBase:RU364130}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000256|ARBA:ARBA00037883}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex). {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364130}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000256|ARBA:ARBA00038211}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|ARBA:ARBA00005690, ECO:0000256|RuleBase:RU364130}.
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:PSC74787.1}.
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DR EMBL; LHPF02000004; PSC74787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6VL47; -.
DR STRING; 554055.A0A2P6VL47; -.
DR Proteomes; UP000239649; 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; 3.90.1200.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR InterPro; IPR047192; Euk_RPA1_DBD_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1.
DR PANTHER; PTHR22603:SF66; ETHANOLAMINE KINASE; 1.
DR Pfam; PF01633; Choline_kinase; 2.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:UP000239649};
KW Zinc {ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 314..413
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 478..615
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 106204 MW; 78BE4F3737EC00DB CRC64;
MLATGAVSSL KASGALGEAV ALKVAGDLQR LDNGKIKCQL TDGKENIASV FTSQVASEFG
SALKSEAVVR VQEGNVSAVG GGHVLIVARA ELVPAGMSND TAAVEGLAPV KEEAQEGGAA
KPEPMATDGP CAAEAAAKTP AAALKKSDGL AKASPYATPA AHPTPPSAGW AQKLAGSAGG
SASKRPVQPI SALNPYNNNW AVKAKVVSKG PKRSFTRGSV FTAEIVDQQG TSIEATFWRD
AADAAHNLLE EGKVYIFARG NVKPADKRYS RVRNDYALHF DTASELEACS DDIDTSAMHA
KLEFVPIDQL AAYADKKMSV DLVGVVSEVR LLGSVKRKTD QVELSRRDLT ILDQSLKNVT
VTLWGSAAEG AGRELEDAAA SGGTLVMAIS SCRVSSYNGV SVSSLQRSAV LINPTDIPEA
VVLREWYDSE GRGAATTHVG EGLASAIKRT GSGGPAERES LEVFRASAPA STDNKPRYAT
VGATFASINA DQALYYMANP ENNRKVVEQG PGQYYCEYDG TTLPTMVRRY IFAAKVMDES
GEVLVQVFNE QAEQLLGMKA DELADIREAD PKRYNEVLQG ALWQDSVLRV KAQAQEYNGD
IRQRYSVADI RPVDLSICLG QTRSSGQQRV ATGMTSQFAP HLAGLSVDSH APEAHLHDAI
RAACLTLLPG WTGTPDSCLA ISLVGGGISN VLFKVTADAI VSPRAVVFRI YGDNTEQFID
RQRELQVMAL VHARGFGPRV LATFSNGRIE EWLEGMRALQ PEELLKWCLT LPARCAVFIT
RHHRFAWRVW ARPLAASVSG WTLPREVVQV EAAAARAASP HVFSHNDLLS GNVVVPVAGS
ATTADVAQVT IEAASLGDAS GICAFEVASK PRGLVTFIDF EYADWAPRGF DWGNHFCEYA
GFECDYSRYP GPQAAAAFIR SYLAAGGDPA DEAHVQRCVA EANVYALAAH QYWGTWSLLQ
ARWSFIDFDY TIRDRFSSRA CRRVRALFYA
//
