UniProt: A0A178A7I5

Database: UniProt
Entry: A0A178A7I5_9PLEO

LinkDB:  A0A178A7I5_9PLEO 
Original site:  A0A178A7I5_9PLEO

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Ontology (8)   
   GO (8)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
All databases (24)   

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ID   A0A178A7I5_9PLEO        Unreviewed;      1088 AA.
AC   A0A178A7I5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN   ORFNames=IQ06DRAFT_261925 {ECO:0000313|EMBL:OAK93656.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK93656.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK93656.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK93656.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441730; OAK93656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178A7I5; -.
DR   STRING; 765868.A0A178A7I5; -.
DR   InParanoid; A0A178A7I5; -.
DR   OrthoDB; 6297at2759; -.
DR   Proteomes; UP000077206; 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; 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   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:SF6; 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:UP000077206}.
FT   DOMAIN          344..423
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          457..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          989..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1027
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1054
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  119545 MW;  6D260E199C0CB7DA CRC64;
     MPADIRSFFG GGGAKASQGS QDTQKDEKPT TKKAAPKKTG RASRVIDDSD DDEEEVKPMK
     ATPKKPPPKK AKREPTPELE ETTTSDFFGS SNKPKRSEPV KKKAAETPKG TPKKATGRVS
     KTATPASNGR ASGRAKKPVR SYAERDGDDE YADDDLDGAD DIFGDEIKGK KGDDYMEDPV
     SDDDLAVKLP HRGTPKAPAK QQQKIKDEDD FDPEDGDVDM KDLDADDDFV EPDEDEQASK
     SRPKKTTASR KRKTPELDDD DEEEEDEKPK KKRTAPAKSP AKKKAKKEDD AESADIQAIY
     DSIPTVRAPT PPARDPDAKF DWRANAGRAE PAPLGGSSGD MPSGSETCLA GLTFVFTGVL
     QKWGRTEAQE LVKRHGGKVT GAPSKKTNYV VLGTDAGPSK LEKIRTMEIK TIDEDGLTQL
     IEKLTAAGNK GDSKAQAAYK EKQRKEEEAI KKQAAELERE EKQRLKDKKA ADAAAGRTTA
     SAVTSAAQSA GPEVDSRLWT TKYAPTTLNQ ICGNKATVEK IQRWLQRFPK NVKTGFKLAG
     PDGSGVFRAV MLHGPPGIGK TTAAHLVAKL EGYDIVERNA SDTRSKKLIE EGLRGVLSTN
     SLHGYFAGDG QKVDSAKKKL VLIMDEVDGM SAGDRGGVGA LAAVCKKTEV PMILICNDRR
     LPKMKPFDFV TYDLPFRRPT TDQIRSRIMT IAFREGLKMP APVVNALIEG SHADIRQVVN
     MISTAKLDQE AMDFDGGKRM SKNWEKHVIL KPWDITQKIL GGGMFAASSK ATLNEKIELY
     FNDHEFSPLM LQENYLGTHP MQALNYSGKE KNLKTLELAS QAADSISDGD LVDRMIHGSQ
     QQWSLMPTHA VFSFVRPASF VAGSTAGNQT RFTSWLGKNS NQNKLIRLVK EIQAHMRLRS
     SGDRHEVRQQ YIPVLWTEMV QKLQREGKEA VPAVIELMDS YFLTKDDFDA IMELGVGPMD
     QEKIKIDTQA KATFTRLYNQ QSHPLPFMKA SSVVAPKKQT KEKPDLEEAI EESDDGEVVE
     EIKEDDEDVD LSKDKYVKQP KKKAAAKKGS AAAKKGKKAK AEDSEDEDED VKPKGKGKAK
     AAPKGKKK
//

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