ID A0A1S3JKT5_LINUN Unreviewed; 1066 AA.
AC A0A1S3JKT5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=LOC106174155 {ECO:0000313|RefSeq:XP_013411030.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013411030.1};
RN [1] {ECO:0000313|RefSeq:XP_013411030.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013411030.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_013411030.1; XM_013555576.1.
DR AlphaFoldDB; A0A1S3JKT5; -.
DR STRING; 7574.A0A1S3JKT5; -.
DR EnsemblMetazoa; XM_013555576.1; XP_013411030.1; LOC106174155.
DR GeneID; 106174155; -.
DR KEGG; lak:106174155; -.
DR InParanoid; A0A1S3JKT5; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000085678; Unplaced.
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-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; 2.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 346..424
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116795 MW; F8E42CC6D3DC8EA2 CRC64;
MEYCASTDLE QDDQSRDRSP DVDPIKAAFQ RQAQKAPTPK KTTPAKSTEE KKKQISVSDF
FGGGSVKKSE RKTAALKRKA PDGDTPSMDK EEHDDVDFQR TLELLDEQQA KKTKIESTKV
TPSKSSQSRR HDSTPSKSIT VAETPVRESP RRSSRTTTPQ KEESRSSSRT PRKEESRSSS
KTPQKQTLTS DQTPQKSRSS SKGRSRSEVS VVEETPERSS PRTRSRSRSC TPAKSDTSSE
QSVRQSPRRK ENESKTESSS LAKKLAAKAR SRELMNTKEE EEKELKKSTP QKKTPSKAKT
PVKATPEKTE SSPGTPATLE RKGSSYKSYL TRAGPSSLGA KEVPEGGDNC LEGLTFVITG
VLESFERDDM KSAIEKYGGK VTGSISKRTS YVVVGRDAGE SKLSKARQLG TKQLDEDGVL
DLIKTLPGKK SKYTVAAEKM VKEDSLNKSA VNEASGKKTS LKKEASVTTP GKTSLSESTP
TKSGQSEAKI GVDKPGESLL WVDKYKPTSM KQLIGQQGDK SNAKKLFHWL NNWHKNIASG
KKPVFSRFDS DGAGYRAALL SGPPGVGKTS AATVVCQEAG FSYIELNASD TRNKKSLEQE
VAEALSNHTL VDFFGSGQSG SSGQKHCLIM DEVDGMAGNE DRGGVQELVQ LLKKTKIPII
CMCNDRNHPK IRTLANYCFD LRFYKPRLEQ IKGPMLSLCF KEKIKVPPPA LNEIIAGANH
DIRQIIHNLA MWSASDKSLT YEQAKSDANQ AKKDMKIGPF DICRKVLVGG AETAGMTLAD
KQDLFFQDYD LTPLFVHENY LSTTPQAAQG NMKKHLRLIS QAVDSMCDGD MVSKVIRGQQ
RWSLLTSQSI FSSVIPGDLM RGSLPQMVSF PSWLGKNSSK NKVDRILQEL RTHMCLKVSA
NKEGLAMDYL PHLRSSLTQP LVQGDADGVP DVIHMMDEYS LLREDFDNIL EVTQWSGRKD
PMASVPSKVK SAFTRAYNKE AHMTPYAVSN MGKKGKKSVS SAEDYPGLGE EEGENGGGGG
GDEDEEEEED VTADAMIKVK KPSAAKGKGK GEGKGQGKGK GRGKKS
//
