ID A0A165D782_9BASI Unreviewed; 279 AA.
AC A0A165D782;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Replication protein A, subunit RPA32 {ECO:0000313|EMBL:KZT52209.1};
GN ORFNames=CALCODRAFT_520857 {ECO:0000313|EMBL:KZT52209.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT52209.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT52209.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT52209.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000256|ARBA:ARBA00007815}.
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DR EMBL; KV424074; KZT52209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D782; -.
DR STRING; 1353952.A0A165D782; -.
DR InParanoid; A0A165D782; -.
DR OrthoDB; 5473935at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:InterPro.
DR CDD; cd04478; RPA2_DBD_D; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014646; Rfa2/RPA32.
DR InterPro; IPR014892; RPA_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989:SF16; REPLICATION PROTEIN A 32 KDA SUBUNIT; 1.
DR PANTHER; PTHR13989; REPLICATION PROTEIN A-RELATED; 1.
DR Pfam; PF08784; RPA_C; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF036949; RPA32; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 70..145
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 162..271
FT /note="Replication protein A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08784"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 29394 MW; 4D25F8A99DAFCC40 CRC64;
MSSPFYNNAG GGGGGGFNKS PYGSQESPAA GRSRTGTHSL RPVTIKQVME SSQAFVEAEW
QIDGHDCPSV TFVAQVRNKA QQATNTAFSL EDGTGHIDAR LWADSSDPDS AAGSEIENDM
WVRAQGTIKS FNGKKHVAAQ RVRPLTDKLE VYYHYCEALS VHLELTKGPA KGANGAAVNG
HAQANGTTNV HADYTMGGGG GGGGNDYSSM QPLDRAIMQF IESSGSSDGC HITAISRAVG
RTVPGATAEQ ISLALERLSD DGHVYNTVDD NHYQSVNAS
//
