ID A0A5N6EKV0_9EURO Unreviewed; 1909 AA.
AC A0A5N6EKV0;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN ORFNames=BDV33DRAFT_205604 {ECO:0000313|EMBL:KAB8218246.1};
OS Aspergillus novoparasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8218246.1, ECO:0000313|Proteomes:UP000326799};
RN [1] {ECO:0000313|EMBL:KAB8218246.1, ECO:0000313|Proteomes:UP000326799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8218246.1,
RC ECO:0000313|Proteomes:UP000326799};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116}.
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DR EMBL; ML733452; KAB8218246.1; -; Genomic_DNA.
DR Proteomes; UP000326799; 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 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR031567; CRIM_dom.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR047854; RFC_lid.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF6; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF08519; RFC1; 1.
DR Pfam; PF16979; SIN1_PH; 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};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000326799}.
FT DOMAIN 339..418
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1015
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1909 AA; 209609 MW; FFE9A82FC2938D61 CRC64;
MPADIRSFFG GKPSSSQGSS ASPAKPPAKK EEPAGRKRRG RKVVDDSDDE DDVKATKAPP
PKPKELTKPK PEEPQGEVTT TSDYFASSKK RGRPAKTSAA TPIKESQPPN DTISEESKAS
KSPRANKQTE KKEAPKRPTR ESKRKATTVL DDEKLGGDDI FATEFGKPGK GDDDYVEDEH
SEKDSDLEEL AVKPATAASS RLGRKKPASK LASDDDDVFM EDAPKQPKRA TKSAASQPGR
KRKSEALGKE EEDEPQESPK KGTSHSKASS TARAPKKPKG SPSKKDQPES KEIQNIFDSI
PTVRPPSPPP ESGDKKKFNP FAARARSPAA AGTAEIPVGA ENCLAGLSFV FTGVLDTLGR
EEGQNLVKKY GGKVTGAPSS KTSYVVLGGD AGPKKLKTIR DHNLKTINEE GLFELIRRLP
ANGGDGKAAE KYEEKRKAED KKIRAMAAEI EQEEKRKAKA TSTAAARASA GTQAPSNSQG
PRPEDELWTT KYAPTSMNMI CGNKTAVEKL QSWLRDWHKN AKGNFSKPGK DGTGIYRAVM
IHGPPGIGKT TAAHLVAKLE GYDIVETNAS DTRSKKLVET GLLGVLDTTS LQGYFAADGQ
KVHREKKNMV LIMDEVDGMS AGDRGGVGAL AAIAKKTHIP LILICNERRL PKMKPFDHVT
YELPFRRPTA EQIRARLSTI CFREGLKIPP PVLDSLIEGT HADIRQIINM LSTVKLDQQN
LNFEKGREMS KAWEKHVILK PWDIVSKILS AQMFSPSSKA TLNDKIELYF NDHEFSYLML
QENYLRTRPA LSGNYQGKEQ KLKLLELADN AASSISDGDL VDKMIHGTQQ QWSLMPTHAV
FSFVRPASFA YGNMTERAGF TNWLGQNSKQ GKLWRCTKEI QGHMRLRASG DRDEIRQQYL
PLIWDKLVRR LMKDGKEGVE DVIDFMDSYF LTRDDWDALV ELGLGPMDQS MVKLDTQTKA
TFTRLYNQRS HPLPFMKASS VTAPKKMPKE KPDIEDAIDE SDDEVLEDDT KEDDESEELD
LKKDKYVRVP KKPAAKSAAK GGSGKGKKAK KAADDDFIDD DEKPKKGRGR KAKAYFTIWQ
LRTSYLSTIK DGIGDRLINV NNSVLNTPGF RAAGWSSAST NPSAQSVAAH IRRTYSPPIP
TTAAVTSEYY QLGVSRDANE AQRLGLGEDG EEDEGGMVTG KSSTEVIGRR PHGRAGKRTH
RKERQQNDSY KQRDAEEDDS SDLSDESDDD VDSQRASQQI KFPKLPIRTR AGSSPIRSTD
RQEGPQLMVT SPSHPTMGMH YRTGSLGTAV SVNERPRRDT TTTASSDMSS DNEMGSLASR
KQIQFSGQDQ VIELASNRRR GAGNRNLGGL DEHPEDSGAE SEDSALSSDF DATAGSASLL
VGVGITGSLD SSSPMMMHKL PNGTGSQTAS PRKAKTPAPE LQDLPPPRPI STVQPVSLLS
KALNARKRAP TNPVEKFAVL SGKGLTDALN IKLYLPFSSD PEEPIDLPIA RESKLAEQPA
PVTVVEAIGL ALWRYSEEGR QPAIERNKLT VNRWALRMVE DGEVEYDFPA LGRTSQITDF
TSNNNRATGA RGRGRGKQYD EFALVEASDS EFEENERQFP MESQAVLPED TNDAASALNV
PPAQPTSQNK APRPNPILGQ PFSSALNDNT LTPADRPAVP TSHATPRLGV SKTLKIRFIN
IEGSTQVTTL NTSTDSYIAE ILDSVCKRWG LDKGNYLLKV MGSNTIAPLD RTVEALGNLT
ELDLVRRRFG PQSLTGSPGS SSPNAPLQID SGTVPSSKKA KKGGPRMLHP LAQQQDLIGG
YYRRYHVFRK QSMSFTASNH KILTFDNDYM HIMPGDTAKT GSETKTRSIS FNDVVGCKVS
RRHPKNFRVV VLRGNDANEQ KRYDFEARNA LEAVEIVDEI KKNMAHYRI
//
