ID A0A4Y9YXE7_9APHY Unreviewed; 994 AA.
AC A0A4Y9YXE7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=EVJ58_g1860 {ECO:0000313|EMBL:TFY67064.1};
OS Rhodofomes roseus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Rhodofomes.
OX NCBI_TaxID=34475 {ECO:0000313|EMBL:TFY67064.1, ECO:0000313|Proteomes:UP000298390};
RN [1] {ECO:0000313|EMBL:TFY67064.1, ECO:0000313|Proteomes:UP000298390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105464 {ECO:0000313|EMBL:TFY67064.1,
RC ECO:0000313|Proteomes:UP000298390};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Fomitopsis rosea.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
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:TFY67064.1}.
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; SEKV01000064; TFY67064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9YXE7; -.
DR STRING; 34475.A0A4Y9YXE7; -.
DR Proteomes; UP000298390; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 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; 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; IPR012178; RFC1.
DR InterPro; IPR047854; RFC_lid.
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; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 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, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000298390}.
FT DOMAIN 278..358
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 106937 MW; 0CBE80DE232E7731 CRC64;
MAGTKIKPSA KSQGKDIRGF FAGGGGGSKS AGSSMSTQRS NGSLKPSGST KPDVIEIMSD
EDHVESGSKH FHPKATPRST QPKSERVMDE DDTPSPAPTL KRKKTLIVSS DEEDEEAEKA
SPPKKKAAVA ASSSKAASSS TSASKPTPKA KEPAPRRTST PAKKRKQDDD FIASSSEEEV
HDDYQDNEDE DLPKKGKAKS KAAPQKAPSK KAVPAKKGAS AKAPAEKATG TKGKAAAKEE
TVDADEDKPK PKFNWAAAKA AKAAGPMAPG SKPLPTPAAP DCLAGLSFVF TGELTSLSRD
EAVELAKRNG GRITGQPSSK TSYVVVGSDA GPSKLAAIKK NNLKTLDEDG FLNLIATRVP
DMSSLDDKTK KKLEKDREAI RTAAAEMEKR EKKAAKASAA SGSTSKTAAE NKLWTDRYAP
QTLKEVCGNK GQVEKLQRWL HDWSSSLKSG FKKPGKDGMN VFRAVLITGS PGIGKTTSAH
LCAKLEGFTP IELNASDARS KKLVENSTNI ANTSLDGWMG GGQTTNAAGV TITEKSCLIM
DEVDGMSAGD RGGVGALAAL IRKAKIPIIC IANDRGAPKL KPLATVAYNL TFRKPEVASV
RSRILSIAFK EKMKIPANVI DQLIEGAQSD IRQVLNMLST WRLQADTMDF DEGKALVKMN
EKYAIMTPFN IIQKMLGPYM FSSTSRETLN DKMELYFHDH SFVPLFIQEN YLKTQPARVK
NLDGPEKALK QLELLDKAAA SISDGDLVDS LIHGPEQHWS LMPLHAVCST VRPASFLYGM
GVAYGGPNAM SFPQWLGQNS KQNKLTRQLT EVQARMRLHV SGDKAEIRQS YIPAMFPYIV
KPLVDEGASA VDEVIERMDD YFISREDWDT IVELGVDQNK DDFVLKKIST ATKTSFTRKY
NARDHPIPFH KAADMGKAPR QLAAAGPIPD LEEALDVDEV EDAADEVEDA SDHDVSKDKL
IKAPKKAAAK SATAKGTTKG TAKGTAKGKA KAKK
//
