ID A0A0V0XAC8_9BILA Unreviewed; 1029 AA.
AC A0A0V0XAC8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=lgc-50 {ECO:0000313|EMBL:KRX84954.1};
GN ORFNames=T06_12584 {ECO:0000313|EMBL:KRX84954.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84954.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX84954.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX84954.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
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:KRX84954.1}.
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DR EMBL; JYDK01000003; KRX84954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XAC8; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd17752; BRCT_RFC1; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 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; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF6; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..388
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 65..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 114426 MW; 277D4B3230F295D8 CRC64;
MHFIIMLVSC KLIGVSIKFI VALCASYYIS STMLDEKATK VTVVEVEEQS GRKIRGSKKR
VIIESDESQF EDSPKKVQAE PSKKKKSKRL ESEEKNESLK PITVSDYFSQ SSQKHGKAFS
KVLDEAMADF DSPGASGPRK RGKKKATTPD IIDEILTGAQ PMNVVETAAL SSPKASKSKR
SAVESQSKEK KKIPPDNKKT IDSNDGKKAA TKKKPVQLAE SVEKKGRGKD GKSTMNKKSC
SPKTPVKSDS SVETPKKVKQ TSKPVTPSSS AEKRKGKDEN EKLSGRPGYQ RFLQREGPRA
LGTREIPKGA ENCFQGLTFV LSGILETVDR EDVKLLIQKY GGRVTGAVSK KTDYLVAGRD
CGETKTKKAK ELRVTILDED GFFDLLSKLP SKSTDNGLTT TVSPESKISG TPKKKAKVMM
IDEISSDVKL DSTADGGQAV MWVDKYKPKS IKQVIGQHGP KSCLNKLLNW LRHWNHYHGD
GQRKKSVDKR SSHATDDGAQ FKAALLSGAP GIGKTTTAQL CCQELGIPYL ELNASDSRNK
KLIEEHFSES IKSRSIDQYF RVNSSDGTER RSSNTFFDHV LIMDEVDGMS GNEDRAGVQE
LIDLIKRTRV PIICICNDRQ SQKLRTLANY CFDLRFHRPQ TLQIRSALMT VAYKEGLKIP
PQALDQLIEG ANHDIRQVLH HLSLLAAQNR GIDFDQARQA ALQAKKDTTQ NIFESTRLLF
KHSDGSQKSS FDDRMELFFS DYSAVPLFVQ ENYLNCVPKD ALDQLQKMEL LSDAAELIAL
GDIVDRQIRT LSNWSLLTVQ GMFSTALPCE LLKGFIQGQI AFPAWFGKNS KYSKLKRILQ
QLSTHMGLHI SATSDDLNVE YLPRLRSAVV KLLVDNDAKG AVEQCQAYDL TREDVEAMME
LGIWPNRPDP MSSVASKSKA AFTRAFNSSN HLLPYSNDAA VVGRRKKMLS AAFDGIQEEA
EDPFDNGEKN RMKNPPSDSE DEEDASVEMF RVTKQKKDHQ GKGKNKINDD EDAKPAKSST
NKPRKTKKS
//
