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Database: UniProt
Entry: A0A0B2UR55_TOXCA
LinkDB: A0A0B2UR55_TOXCA
Original site: A0A0B2UR55_TOXCA 
ID   A0A0B2UR55_TOXCA        Unreviewed;       353 AA.
AC   A0A0B2UR55;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Replication factor C subunit 4 {ECO:0000313|EMBL:KHN73486.1};
GN   Name=Rfc4 {ECO:0000313|EMBL:KHN73486.1};
GN   ORFNames=Tcan_11712 {ECO:0000313|EMBL:KHN73486.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN73486.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN73486.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN73486.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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:KHN73486.1}.
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DR   EMBL; JPKZ01003105; KHN73486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2UR55; -.
DR   STRING; 6265.A0A0B2UR55; -.
DR   OMA; GCQSGSF; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT   DOMAIN          60..193
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   353 AA;  39819 MW;  BD9D13955C3AC232 CRC64;
     MEAFFGRKEA SSAKPTVAET HRHSQAIIPW MEKYRPKKVD DIVFQEEVVS VLKKVLEGAD
     LPNLLFYGPP GTGKTSAAVA LCRELFKNVD TYHDRVLEMN ASDERGIDIV RTKIKEFARR
     AVCSKLPDGS PVIGLKVIIL DEADAMTGAA QAALRRTMEK ESRTTRFFLI CNYISRIISP
     LTSRCAKFRF KPLSMESQKE RLEYICREEN VNVEPAALIE LIELCGGDMR KSVTYLQTIS
     SCQAKLTPSD VRELSGAVPD SVVKDLLNVC ERMNFDEMCT YVESIKRQGY GVYQLMTQLF
     SLILHSTQLL DTHKSAIFEK MAECELRLLD GADELLQLLD LSAAIIEQYK TII
//
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