ID A0A0L6UNG8_9BASI Unreviewed; 1171 AA.
AC A0A0L6UNG8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN ORFNames=VP01_460g4 {ECO:0000313|EMBL:KNZ50079.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ50079.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ50079.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ50079.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|ARBA:ARBA00009841}.
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:KNZ50079.1}.
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; LAVV01009735; KNZ50079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6UNG8; -.
DR STRING; 27349.A0A0L6UNG8; -.
DR VEuPathDB; FungiDB:VP01_460g4; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 1.
DR CDD; cd17752; BRCT_RFC1; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR CDD; cd18086; HsC9orf114-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003750; Put_MeTrfase.
DR InterPro; IPR047854; RFC_lid.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF37; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF02598; Methyltrn_RNA_3; 2.
DR Pfam; PF08519; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT DOMAIN 57..147
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..718
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 129723 MW; D829B1E32A54BBE6 CRC64;
MAKRTPPEKP DSSKAPAAKK AKTEPEAGTS APAKPRWFPG KERAGPSAPG SKEIPEGKEN
CLAGLTFVFT GELESLSRED AQALCKKYGG RVTTSPSSKT SFVVLGSDAG PKKLEMIKKH
KIKSITEDEF LNLIASKPSG ELDAKTLKKQ EEEVRKVEQV AKSLGPPKES KSGKKSTGHL
WTVKYAPKCL GDLCGNKTQI DKVQAWLHDW PKFRRSNFTK PGKDGLGMYR CVVLSGPPGV
GKTSAAHLVA KAEGYEVIEL NASDTRSKKL LEIGFKDIVG NSSIAGFLET STERSNKLVL
IMDEVDGMSA GDRGGVGALN ALIKKSQIPI IAIANDMSTP KMKPLKATAL SLVFRRPHVN
TIRSRMMSIA FREGMKIPPN AIDQLVAGSQ SDIRQIINML STWKIGNSKE GPSKTMDFDQ
ARQLTSENEK DVIVSPWILM SKIFGPQTWS QTSSMTFIDK CNLYFHDHDM LPLFVQDGYV
KHDYGQARNY VGPEKAAKKM ELLSLAADSI ADGDLVDRMI HGPQQHWSLM PLHGVFSVVR
PAYYCHGPST SGDFGGFSFP SWFGKNSTQG KLNRIMGEIH GRMRMKISGD KREALMNYLP
VLYPRLIDPL IQDGGADQVD GIIELMDDYY LTKEEWDNLV EVMAIGTSPD DLLKRIPSAT
KSALTRKYNK TSHPIPFQKE VVVAFKKIKS DAIPDVEELA EIDVEEEELD EEDDDGKSDE
DISKDKLIKA KKPAARASFG TGTRKAPASK AAPNQTSKTK KLLMTTNTPH EGKKRRRKSS
GRCRAEMKQR VRESTDRLLA QVTDSSDEDE QTKTEHNPTA EFQRIHKPHK PSANVTSTKG
RQYTVSVALP GSIVNNAQTW ELKTALVGQI ARACAIFSVN EIVIFDESIP EADTSSAKPS
TYGRAKYRTP ADQLDPDAPD DAQFQPSHFV ARILEYLECP QYLRKSLFPL HPDLRLAGLL
PPLDLPHHFR KDHETPWREG CILPADKIDN YIAGAHHHPK KKHHKKQADK KNLWADVGLA
QPVEVLLDQD VSLPDWTRVT VQMPTGEGKL EGIGEFKHML LVLGGLSGLE LSIAKDETLE
PRLTAADAPL LFDYWLNTLP FQGSRTVRTE EAFQDFPRQQ TGHFVAIRAQ LQPYIHRLKA
PSRTPKNPHH FSTRILSGND LIGQGTESSD G
//
