ID A0A383W3J6_TETOB Unreviewed; 1104 AA.
AC A0A383W3J6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=BQ4739_LOCUS12428 {ECO:0000313|EMBL:SZX72237.1};
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX72237.1, ECO:0000313|Proteomes:UP000256970};
RN [1] {ECO:0000313|EMBL:SZX72237.1, ECO:0000313|Proteomes:UP000256970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNXT01001119; SZX72237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383W3J6; -.
DR STRING; 3088.A0A383W3J6; -.
DR Proteomes; UP000256970; 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; 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:UP000256970}.
FT DOMAIN 282..342
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 112988 MW; A93FB2DC705B1127 CRC64;
MDIRKFFQAA GVKPGAATQK KEKKQEASQP QAAAAAAAAA PAKAKPKSKS TPSPAKRSAG
KAAAGKAAAA AATPAASGGG SARKRKKKDA DSDSDVVLVS DDDDDDDDDV MSLDAEDDAS
DDDDFVDLED EDDDAAAKPK PAKRAKPSTP AATKSAGSTP GRKGAAAAAA PKGKAAGGRG
KATKHEMVIE KGSQEGSEKK RKVPGSMAGQ AAPVAPKSAK KEKAEKAQLS PEAAAAVAAV
DAAAKALPEL QPDELVFMKN EAFGGAVDME PSAPGSKTVP AGHPDAFTGK VFVFSGVLPS
LYREQATDLV AAHGGRSTKD VSGKSSFLVV GNNCSRRKFD KAIEKHCKVI DEDGFLALVG
ASKPPAAAAA AAAATQQQPS QGQQQQQQQG SAAAAAAPSG GAGAGSGRGA AVKAVAAAGF
YGTPAGAGSG GAAAAAAAGA GPSSSRAAAA QAPRGGTASE QLWVDKYKPR NAQELVGNPG
LVSTIKQWLF QWDAVHLHGA TPEQPSGGGG GKPKDMGKKA VLLSGPPGIG KTSSAHIIAR
ELGFQVVEVN ASDTRSKSDA KAGGGMAGKL SNVVREMVTS TALAAASGVK RRQVLVMDEV
DGMSGGDRGG VADLIATIKM SRIPIICICN DKYSQKLRSL RSHCLELDYR KPTWQQISSR
MSHVCRQEGL AVNEATLRTL IEGAQGDLRL ILGQLQMARL RSQSLDFTAA KAMGAGGKDA
DMSPFSAAGK LLEARGAGRP PSVGELTELA FADADLVPLL VAENYVNHRP DIVPPGNLAL
RLRALAKAAD AISAGDVVNV SVRRYGNWGL MPFGALLGCV VPAAYMHGPR ETFEMYENNF
TRFSAWFGNN SHQGKQKRLL AELSCNMAAA ESGATCSRGS VRLDYLPALR TVLTRPLVAD
GEEAIPRIIS TMQDYCINRE QWDFVLDITK CKSKAPWAAD PTEGLGSKVK SAFTRKFNQQ
GLVPRTNTMV ADIVKGRKGK AKAGNTAAGN GGGEGDELAG EGLAGDAEGG AALAEEAGVP
GDVQVKSEEE DEDELSPEQL ADRMKGEGIK FELKAPAASG KAGGPSGRGR GGGRSGRGGS
GRGGAASGGR GPASGRGRGR GRGK
//
