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Database: UniProt
Entry: F8QH69_SERL3
LinkDB: F8QH69_SERL3
Original site: F8QH69_SERL3 
ID   F8QH69_SERL3            Unreviewed;       978 AA.
AC   F8QH69;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN   ORFNames=SERLA73DRAFT_79676 {ECO:0000313|EMBL:EGN92318.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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}.
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DR   EMBL; GL945507; EGN92318.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QH69; -.
DR   STRING; 936435.F8QH69; -.
DR   eggNOG; KOG1968; Eukaryota.
DR   HOGENOM; CLU_003574_1_0_1; -.
DR   InParanoid; F8QH69; -.
DR   OMA; LICNERN; -.
DR   OrthoDB; 6297at2759; -.
DR   Proteomes; UP000008063; 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:UP000008063}.
FT   DOMAIN          269..353
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..187
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   978 AA;  106702 MW;  8FA3748A6DF5137B CRC64;
     MPPAKKSPVV KKTSGKDIRT FFGGGGNSSQ TPSGPSQQNT QSQKQESNPT KPKPIEISDD
     DSEPAKPVAP KPKSERVMVV DSDEDEAPRQ PSRISHLKRK KAAIQSSSDE DEEPVMKVGP
     PKKKTAVTTK ASSKPSPSTP ISNGKKKTAV SNKGSSRTTR KKVVMDEDFA MTSSESEDDD
     PYVEGDEDEV VVVAKKGKSK AKEKNATSER TRTKPENTKK ERDVEPVKSE AEPKKDANAP
     TKSFNWAAAK AAKLAGPVAH GSKEVPEPKS MDCLAGLSFV FTGELSSFSR DEAVDLAKRF
     GGQVSRVTGQ PSSKTSFVIL GDNAGPSKLS AIKKHGLKSL SEDEFLNLIA TREGPGGPNG
     VGYDEKTKKK MEKEQDVIRK AAKELENREK QAMKNDSKHS GGSKPVDVSS QLWTTKYAPQ
     SLKEICGNKG QVEKLQLWLH DWSNNLKSGF KKPGKNGMNI FRAVMVTGSP GIGKTTSAHL
     CAKLEGFTPI ELNASDARSK KLVESGMNIN NTSLDGWMGG NSSINAVGVA ITDKTCLIMD
     EVDGMSAGDR GGVGALNALI KKSKIPIICI ANDRNAQKLK PLLATTFNLP FRKPEATAVR
     SRMLTIAFKE KMKLPANVID QLITGAQSDI RQVLNMLSTW KLSSDTMSFD EGKDLAKTNE
     KYTILTPFDV TYKMLGPYMF SSTSRETLGD KMELYFHDHS FVPLFIQENY LKTQPARLRS
     LEGPQKVLKQ LELMDKAASS ISDADLVDAL IHGPEQHWSL MPLHAVCSTV RPASFLYGAG
     GGYGGPNAMS FPQWLGQNSK QNKLNRQLGD VQIRMRLKVS GDKAEIRQSY LPALFPHIVK
     PLVDEGTSAV DEVIERMDEY YLSKEDWDTV VELGVDQNKD DAVLKKISAA TKTSFTRKYN
     AGEHPIPFHK AQDLGKVPKK LAGGPAPDLE EAFDLADDVP EEASDDEKKV KDVGDFKGDK
     LIKEAKAKKK GKAYTKAK
//
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