ID A0A090L0Z0_STRRB Unreviewed; 362 AA.
AC A0A090L0Z0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Replication factor C subunit 4 {ECO:0000313|EMBL:CEF63346.1, ECO:0000313|WBParaSite:SRAE_1000160800.1};
GN ORFNames=SRAE_1000160800 {ECO:0000313|EMBL:CEF63346.1,
GN ECO:0000313|WBParaSite:SRAE_1000160800.1,
GN ECO:0000313|WormBase:SRAE_1000160800};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63346.1};
RN [1] {ECO:0000313|EMBL:CEF63346.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000160800.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF63346.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000160800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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; LN609528; CEF63346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L0Z0; -.
DR STRING; 34506.A0A090L0Z0; -.
DR EnsemblMetazoa; SRAE_1000160800.1; SRAE_1000160800.1; WBGene00258216.
DR WBParaSite; SRAE_1000160800.1; SRAE_1000160800.1; WBGene00258216.
DR WormBase; SRAE_1000160800; SRP04086; WBGene00258216; -.
DR eggNOG; KOG0989; Eukaryota.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF20; REPLICATION FACTOR C SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035682}.
FT DOMAIN 61..198
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 40701 MW; 111DE5DEF0A949B2 CRC64;
MNFFLSKQPG DKSRKNDGEH GTVQTSSRLP WVEKYRPKKV SDVVQQEEVV SVLKQCLSGA
DLPNLLFYGP PGTGKTSVAI AVCNEIFPSE ASFRDRVLEL NASDERGINV VRSKIKDFAR
RAVSVHTNQP GGPKLALKII ILDEADAMTS AAQAALRRTM ETESRTTRFF LICNYISKII
EPLTSRCAKF RFKLLSPELQ RARLKYIGES EGISIEDEAL DELIKITKGD LRRSITIFQS
LSFNKEIINV NQVREMTAFV PNEIIEELFI KPSELKTSDL VKYVQSFNRN GYSVYQIILQ
MVDYLTSEKS SGIGEIVKAK ILLKIGSIEN MILNDCDEYL AFLSLLGCIK TAISYGNELY
SK
//