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Database: UniProt
Entry: Q5ZHL1_CHICK
LinkDB: Q5ZHL1_CHICK
Original site: Q5ZHL1_CHICK 
ID   Q5ZHL1_CHICK            Unreviewed;       359 AA.
AC   Q5ZHL1;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=RCJMB04_37a17 {ECO:0000313|EMBL:CAG32782.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAG32782.1};
RN   [1] {ECO:0000313|EMBL:CAG32782.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAG32782.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAG32782.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; AJ721123; CAG32782.1; -; mRNA.
DR   RefSeq; NP_001006550.1; NM_001006550.2.
DR   AlphaFoldDB; Q5ZHL1; -.
DR   GeneID; 424958; -.
DR   KEGG; gga:424958; -.
DR   CTD; 5984; -.
DR   VEuPathDB; HostDB:geneid_424958; -.
DR   OrthoDB; 275853at2759; -.
DR   PhylomeDB; Q5ZHL1; -.
DR   Reactome; R-GGA-265976; Homologous DNA pairing and strand exchange.
DR   Reactome; R-GGA-351451; Homologous recombination repair of replication-dependent double-strand breaks.
DR   Reactome; R-GGA-351468; Processing of DNA double-strand break ends.
DR   Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          68..200
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  39323 MW;  A2F635D887AA8C2E CRC64;
     MQAFLKGPSS ISSKPPAAKE RSAAGSSGEG NKLKPVPWVE KYRPKNVDEV AFQDEVVAVL
     KKSLEGADLP NLLFYGPPGT GKTSTILAAA RELFGPELFR QRVLELNASD ERGIQVIREK
     VKAFAQLTAS GSRADGKVCP PFKIVILDEA DSMTSAAQGA LRRTMEKESK TTRFCLICNY
     ISRIIEPLTS RCSKFRFKPL SDKIQQQRLL DVSEKENVKI TSEAVSYLVK VSDGDLRKAI
     TYLQSATRLM GGKEITEKTV TEIAGVIPRE TIDGLLSACS SGSFEKLETV AKNLINEGYA
     VAQLVNQLHD IVVESEDFSD KQKSIIVEKL AEVDKCLADG ADEYLQLISL CALVMQQLT
//
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