ID   CTF18_XENLA             Reviewed;        1000 AA.
AC   Q6NU40;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Chromosome transmission fidelity protein 18 homolog;
GN   Name=chtf18; Synonyms=ctf18;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chromosome cohesion factor involved in sister chromatid
CC       cohesion and fidelity of chromosome transmission. Component of one of
CC       the cell nuclear antigen loader complexes, CTF18-replication factor C
CC       (CTF18-RFC), which consists of ctf18, ctf8, dcc1, rfc2, rfc3, rfc4 and
CC       rfc5. The CTF18-RFC complex binds to single-stranded and primed DNAs
CC       and has weak ATPase activity that is stimulated by the presence of
CC       primed DNA, replication protein A (RPA) and by proliferating cell
CC       nuclear antigen (pcna). The CTF18-RFC complex catalyzes the ATP-
CC       dependent loading of pcna onto primed and gapped DNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of ctf18,
CC       ctf8, dcc1, rfc2, rfc3, rfc4 and rfc5. The CTF18-RFC complex associates
CC       with pcna (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin during S
CC       phase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. CTF18
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC068761; AAH68761.1; -; mRNA.
DR   RefSeq; NP_001084621.1; NM_001091152.1.
DR   AlphaFoldDB; Q6NU40; -.
DR   PRIDE; Q6NU40; -.
DR   DNASU; 414577; -.
DR   GeneID; 414577; -.
DR   KEGG; xla:414577; -.
DR   CTD; 414577; -.
DR   Xenbase; XB-GENE-987606; chtf18.L.
DR   OrthoDB; 307415at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 414577; Expressed in blastula and 16 other tissues.
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-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08519; RFC1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; DNA replication; DNA-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..1000
FT                   /note="Chromosome transmission fidelity protein 18 homolog"
FT                   /id="PRO_0000340083"
FT   REGION          53..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         396..403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1000 AA;  113222 MW;  82423AEBE4B9532F CRC64;
     MEEYDLYGVE DDFESQFASE LEVLAELEDD VSSRPGPQRS QLRTKLSFEE AISAGDPIRS
     NANSKPTGDS NGEALACIDT SKSKKRDASC IDFEEDEFSD SIYEPPITPK HKRARIEAVK
     KLDFGRDEYA GNSTALSDDI TPPPSPNHSP KKNERDSKFS SCEAFEVSDM APLQVTPTES
     EQKRVLKRPP VLEDYINVTS TDGSRVYMAL KEDNDGAQQK QGNLKWNSGQ QLHLLGVPFS
     YLKEQVNDEH RRKVLEESQR LTEMLNSQIN EEFGENDSEI LENDDNAGEE DDEDEPSSHS
     LWVDRFTPRH YTELLSDDYT NRCLLKWLKL WDTVVFGKER VVRKPKAIVD PRANHFKNQK
     EQQSKFKTKA QITEEILEAE LDHHNRPKNK VSLLCGPPGL GKTTLAHVIA RHAGYNVVEM
     NASDDRSPEA FRTRIEAATQ MKSVLGVDER PNCLIIDEID GAPTVSINML LSLVNRKDAK
     EAEGGTEATT GKKKKKEGGL LLRPIICICN DQYVPSLRQL RQQAFMLNFP QTMPSRLVQR
     LYEIAVKQGM KADTGALMAL CEKTENDIRS CINTLQFLHG RGKKELNMRS VQTMRIGLKD
     QNKGLFSVWQ EIFQLPKIQR KRIGQEVATN DLHLLLGSEN DSLGMLAKPP LNAVAQRFHH
     ILHLSTSTGE YEKLTMGLYD NFLNMKVKES NFSTVCLALD WLEFTDIVNS TIMHGQNFQL
     MRYLPFLPVA FHLLFAASNV PRIAYPSSHY EAQSKLNQMQ NLLNAMVSEI SPAIRTRVGP
     QSLVLDALCL LLDVLSPKLR PVNTQLFSTK EKQQLAELIN TMLAYNLTYH QERTMEGQYV
     YKLDPNVEDV CRFPDLPVRK PLTYQTKQLI AREIELERMR RTEAFQQARN AGRDNTTAAA
     AVKTADPKGA KSAAKPAALN HEQRLENIMK KATFEEKPEK DFFGRQIVKK VAAPVTASAN
     QEESVERRIG KAVGNSDVWF RFNEGVSNAV RRNIYIKDLL