ID A0A074ZLZ3_9TREM Unreviewed; 2358 AA.
AC A0A074ZLZ3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Replication factor C subunit 2 {ECO:0000256|ARBA:ARBA00040745};
GN ORFNames=T265_13940 {ECO:0000313|EMBL:KER26777.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER26777.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER26777.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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DR EMBL; KL596739; KER26777.1; -; Genomic_DNA.
DR RefSeq; XP_009169508.1; XM_009171244.1.
DR STRING; 6198.A0A074ZLZ3; -.
DR GeneID; 20328107; -.
DR KEGG; ovi:T265_13940; -.
DR CTD; 20328107; -.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000054324; 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:0008270; F:zinc ion 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 InterPro; IPR006564; Znf_PMZ.
DR InterPro; IPR007527; Znf_SWIM.
DR InterPro; IPR048324; ZSWIM1-3_RNaseH-like.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR Pfam; PF04434; SWIM; 3.
DR Pfam; PF21056; ZSWIM1-3_RNaseH-like; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00575; ZnF_PMZ; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50966; ZF_SWIM; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 497..538
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 1239..1280
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 1998..2039
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT REGION 136..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2358 AA; 267913 MW; FEEE45DE4F3056FD CRC64;
MLRCHTTMVY VKKIKKAYYN QSGHSFIQTI WIETDNTNVT DIHEQTYLAA SPNNWDHAAP
TLKETYNVVL AGDMNAQFGR LSSLEPHLGG HFGINARRTG NGERLLQLCQ ILNCFSQYEL
PCLTINVFGE LPESGGTPDQ QCLTDNEDGS SKPPENRRRP QTFRHWCLVT QEEFTECTME
SVVPNTKLSH DIPWVEKYRP VVLTDIVGNE ATILRLTAFS REGNVPNIII AGPPGCGKTT
SILCLAHALI GSSYKEAVLE LNASNDRGID VVRNKIKMFA QKKVTLPPGR QKIIILDEAD
SMTEGAQQAL RRTMEIYSRT TRFALACNDS SKLIEPIQSR CAVLRYARLT AAQIMARLLE
VCRAESVSYT DEGLEAIVFT ADGDMRQWAS CRIARVANYG IHDTNMVEAM HRCLKMELLN
GKIGLWEAIR VSRMSATYLI WNRQKTVSDA SRRDLCIVGH PELDRLCRRL MPYAISKMAS
DLSSTHPITV MSSDEHATIM MDRRRETITH ATRTCTCKKF VQFGIPCRHL LHFAMAQNGE
TTELPVCSRW TRENNGAIAV SFAQLDAPRS GTRNPSALLN MVLNDVRTLY QRMELEHFAV
YSAWHRSFVQ QAGPRESPPF IFPPPVNLST DTSIADYDQL PPSVLLNLDA PALVATEIPE
GLVTEAPEDS VVPGEVAVVD ISSLDDDGTI PAVQTGPRRA VGVYDARRDP RSETVDETPT
VPSLQDFLVD DTICAECGLE DPEENEGRTV NWVQCPYCTR WHHRSCLIQP PIVTIFWCFF
SLVAAAPVSA EEYTVDVTPL FASHLGSRVF GNVHELVHRI KQFERLSGWY CSVRNSKANS
SGEKTFIKYQ CHRKGFARPP NEGKRRRLLD HTHCEAFFNV GRLGTFFRVT KSHMVHNHEL
LGPEASRWFD RNRRLLPEEL EIIRPMLECR SRCFNIRFYV RSKFGKYLTT SDIGNIRARH
MFGRNNPSYI LDLESQFNEQ GRARCLRDGS NRVTHFIYST SEMLDLYRRF PDFLLIDSTF
STNQHKYFLY QLLIVDGCRK RLPVAIGFLW RETEADVRTF LLTFLEFVGS GSLVKCIISD
GTLSNVYHDR NHLRVFFVAM HTSRLWKYLA FLELIRLNDH PFFMCINSFL LPNASKWASC
RMPRVANYGI HDTNMVEAMH RCLKIGLWEA IRVSRMSATY VIWNRQKTVS DASRRDLRIV
GHPELDRLCR RLMPYAISKM ASDLSSTHPI TVMSSNEHAT IMMDRRRETI THATRTCTCK
KFVQFGIPCR HLLHFAMAQN GETTELPVCS RWTRENNGAI AVSFAQLDAA RSGTRNPSAL
LNMVLNDVRT LYQRMELEHF AVYAAWHRSF VQQAGPRESP PFIFPPPVNL STDTSIADYD
QLPPSVLLNL DAPALVATEI PEGLVTEAPE DSVVPGEVAV VDISSSDDDG TIPAVQTGPR
RAVGVYDARR DPRSEVVDET PTIPSLQDFL VDDTICAECG LEDPEENEGR TVNWVQCTLV
MASSSQSLVA AAPVSAEGYT VDVTPLFASH LGSRVFGNVH ELVHCIKQFE RLSGWYYSVR
NSKANSSGEK TFIKYQCHRK GFARPPNEGK RRRLLDHTHC EAFFNVGRLG TFFRVTKSHM
VHNHELLGPE ASRWFNRNRR LLPEELEIIR PMLECRSRCF NIRFYVRSKF GKYLTTSDIG
NIRARHMFGR NNPSYILDLE SQFNEQGRAR CLRDGSNRVT HFIYSTSEML DLYRRFPDFL
LIDSTFSTNQ HKYFLYQLLI VDGCRKSLPV AIGFLWRETE ADVRTFLLTF LEFVGSASLV
KCIMSDGALA IGNAIASVFP FAYHLLCRVH ILRNVIKRFP RSQSFTRFFV AMHTSRLWKY
LAFLELIRLN DPPFFMYINS FLLPNASKWA SCRMPRVANY GIHDTNMVEA MHRCLKMELL
NGKIGLWEAI RVSRMSATYL IWNRQETVSD APRRDLCIVG HPELDRLCRR LMPYAISKMA
SDLSSTHPIT VMSSDEHATI MMDRRRETIT HATRTCTCKK FVQFGIPCRH LLHFAMAQNV
ETTELPVCSR WTRENNGAIA VSFTPLDAPR YGMRTPSALL NMVLNDVRTL YQRMEPGHFA
VYAMWHRSFV QQAGTRELSP FTFPSPINLN TDTSIADYDQ LPPSTLLNLD APALLPTEIP
KGLVTAGPED SVVHDETAVV DISSSDEGGK QGLFQLSNLA RDEQLALNNL QSTHQGFGMV
TSENVFKVCD EPHPMLVKQL LDHCVKSDFT EAHKILRHLW TLGYSAEDIM SILFRVLKNH
PMEEYIKLEF LKNMQRILRL TTLSTTEDHL AYMVMPGASN SHLPSPPTLT LLVTIRLSNK
SWLYGSEASV LNTDVVCR
//
