ID C5X671_SORBI Unreviewed; 987 AA.
AC C5X671;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=SORBI_3002G275600 {ECO:0000313|EMBL:EER99237.2};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER99237.2, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER99237.2, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|EMBL:EER99237.2}
RP NUCLEOTIDE SEQUENCE.
RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F.,
RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A.,
RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N.,
RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S.,
RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K.,
RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.;
RT "WGS assembly of Sorghum bicolor.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- FUNCTION: May be involved in DNA replication and thus regulate cell
CC proliferation. {ECO:0000256|ARBA:ARBA00002386}.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex with RFC1. {ECO:0000256|ARBA:ARBA00011480}.
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; CM000761; EER99237.2; -; Genomic_DNA.
DR EMBL; CM000761; OQU89819.1; -; Genomic_DNA.
DR AlphaFoldDB; C5X671; -.
DR EnsemblPlants; EER99237; EER99237; SORBI_3002G275600.
DR EnsemblPlants; OQU89819; OQU89819; SORBI_3002G275600.
DR Gramene; EER99237; EER99237; SORBI_3002G275600.
DR Gramene; OQU89819; OQU89819; SORBI_3002G275600.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_1534651_0_0_1; -.
DR OMA; VKFPTWL; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; C5X671; baseline and differential.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:UP000000768}.
FT DOMAIN 223..304
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..922
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 106926 MW; B0DDE464B498393B CRC64;
MSSDIRKWFM KAHGKNAAPS GAAATKPSGA AAAEKKKPVL SIPEKKSAPP ALASCDHDPP
ARRKTSKYFG SKAEKDSDVE MADASAGNSA DKSAAKRKLQ KCNNELKEDN KPLPAKKISK
DEEDDDDDFV APPKKKTPVK PPPSKKAKVE SNAQVDDAED EDRMDEDAKT PSKGAGRGRG
RGGRGGAGAA PGGRGRGGGG RGFMNFGERK DPPHKGEKEV PEGAPDCLSG LTFVISGTLD
SLEREEAADL IKRYGGRVTG SISKKTSYLL ADEDLGGVKS NKAKDLGVPF LTEDGLFDLI
RKSKPAKAPV DKQQSNNSFE KLQKSQTKSS PAKVEKRAEA SAVGKSIASN SNAASASADK
QKPKNVDRGS MQWTEKYRPK VPNDIVGNQS MVKQLHDWLK SWDALFLHSG QKGKGKKQAD
SAAKKAVLLS GPPGIGKTTT AKVVSQMLGL QAIEVNASDS RGKADSKIEK GVGGSTSNSI
KELISNATLN YGDNRSKHPK AVLIMDEVDG MSAGDRGGVA DLIASIKISK IPIICICNDR
YSQKLKSLVN YCLMLNFRKP TKQQMGKRLM EIAKKEGIQA QENAMEELAE RVHGDIRMAL
NHLQYMSLSQ SVVKYDDIRE RLNSSSKDED ISPFTAVDKL FGFNGGRLRM DERIDFGMSD
PDLVPLIIQE NYINYRPNTL GKDESGVKRM NALARAAESI ADGDLVNVQI RRYRQWQLSQ
AACFASSIVP AAWMHGNREV LEAGERNFNR FGGWLGKYST TNKNRRLLED VHSHILASQQ
ANLDREALRL DYLTLILREL TDPLKKMPKD EAVQKVVEFM DTYSLSQEDF DTIVEVSKFK
GHPSPMDGIQ PAVKSALTKA YKQGSSSRVV RAADLINIPG MKKPLKKRVA AILEPLEESV
PEENGLASAE DDEDDSSDTE NNDELVPADS TPKLDLQSDK KKGIQVQLDL KSNGNGSSGK
KAPAARSRAT GSSGKAAAGG SAGKRKR
//
