ID A0A5N4EFB3_CAMDR Unreviewed; 936 AA.
AC A0A5N4EFB3;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=Cadr_000002146 {ECO:0000313|EMBL:KAB1282077.1};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1282077.1, ECO:0000313|Proteomes:UP000299084};
RN [1] {ECO:0000313|EMBL:KAB1282077.1, ECO:0000313|Proteomes:UP000299084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1282077.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB1282077.1};
RX PubMed=30972949; DOI=.1111/1755-0998.13020;
RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA Burger P.A.;
RT "Improving Illumina assemblies with Hi-C and long reads: an example with
RT the North African dromedary.";
RL Mol. Ecol. Resour. 19:1015-1026(2019).
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:KAB1282077.1}.
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DR EMBL; JWIN03000002; KAB1282077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N4EFB3; -.
DR STRING; 9838.ENSCDRP00005011796; -.
DR Proteomes; UP000299084; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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:SF36; 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; 3.
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:UP000299084}.
FT DOMAIN 296..374
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 104930 MW; EA65D42676FD4723 CRC64;
MVKLKSDEED DFVCKKAASK SKENGGSTNS YLGASNMKKN EEYTKTKNKP LSPIKLTPTS
VLDYFGTGSV QRSDKKMVAS RRKEPPQNAD DSRLKDEAIA RQLQLDEDAE LERQLHEDEE
FARTLAMLDE EPKSKKALKD PEEREMFSSV QANLCKAVKP KYPHKVKAEQ FSDERKNCSP
KKRTKCESSK ESQHSRSSAH KTGETSSPKA SSKLAALKKR EESSYKKTEP LGSKRKENAI
ELKETRTPKK IKSSPAKQES ISPEDSEKRR SNYQAYRSYL NREGPKALGS KEIPKGAENC
LEGLTFVITG VLESIERDEA KSLIERYGGK VTGNVSKKTN YLVRGRDSGQ SKSDKAAALG
TKIIDEDGLL NLIRTMPGKK SKYEIAAEAE MKKEKSKLER TPQKNDRGKR KISPTKKESE
SKKCQLTPQR ESSIKSIKKE TSVFRRGLDF KEQVAEETNG DSRARNLADD SSENKVENLL
WVDKYKPTSL KTIIGQQGDQ SCANKLLRWL QNWHKSPSED KKCGDFTTSF IFVCVSAKVG
KFAGKDDGSS FKAALLSGPP GVGKTTTASL VCQELGYSYV ELNASDTRSK NSLKEIVAES
LNNTSIKGFC SSMWSFVQFS FEGDNSFPFV KFQGAMMSIA FKEGLKIPPP AMNEIILGAN
QDIRQVLHNL SMWCARSKAL TYDQAKADSH RAKKDIKLEN YIHVKPVAAG GDMKKHLMLL
SRAADSICDG DLVDRQIRNK QNWSLLPTQA IYASVLPGEL MRGYMTQFPT FPSWLGRHSS
MGKHDRIVQD LALHMSLRTY SSKRTVNVDY LSHIRDALVQ PLTSQGIEGV QDVVALMDAY
YLMKEDFENI MEISSWGGRP SPFSKLDPKV KAAFTRAYNK EVHLTPYSLQ VVKTHRLSTG
PALDSEYNEE LNEDDSQSDE KDQDTLETDA MIKVVF
//
