ID K8EQB2_9CHLO Unreviewed; 1313 AA.
AC K8EQB2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Regulator of telomere elongation helicase 1 {ECO:0000313|EMBL:CCO20251.1};
GN OrderedLocusNames=Bathy16g00860 {ECO:0000313|EMBL:CCO20251.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO20251.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO20251.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO20251.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FO082263; CCO20251.1; -; Genomic_DNA.
DR RefSeq; XP_007508634.1; XM_007508572.1.
DR STRING; 41875.K8EQB2; -.
DR GeneID; 19011179; -.
DR KEGG; bpg:Bathy16g00860; -.
DR eggNOG; KOG1132; Eukaryota.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000198341; Chromosome_16.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 1.
DR Pfam; PF06733; DEAD_2; 2.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CCO20251.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 23..423
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 80..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1313 AA; 143811 MW; EA93930B1CC52538 CRC64;
MFPPPKSRAH PPPPIQIIVQ NVSYSVKFPF PEPYPSQIVM MEKILFALRE GTNALLESPT
GTGKTVCLLC ATLAFAEHEE KQRIKQKNTK KKNTKKRKDT EKEEKEEKEE DLELKRTKGV
KEEYTGGEPS KVTIVYVSRT HSQLQQVISE LKATEYAPRS SVVGSRKQLC VNEWVAEAAK
KMGDGNKRGA EKLCKIACNS GKCDKKRNVG THMERVFGID VVNGWFANQW GGEFNGGSLG
YGRTTNHHDF GTKERAGSIL SQLPNEDVLS SKSSKSGGGD GGGDDDGKGK GSIMDIEDLV
KEGKRANGPC PYYLAREMTR GAEIIFAPYS YILDAGVRKR ALGDTVMNWH NSIVIFDEAH
NAESACEEAA SRDLTAVHVA NAIKDADAAF QYYSMIEESM EGLSKEEKKD SKKTGTYPTR
SAGDYLTLRG IFAALEREIA IVCAQDQERV RKGETLPSSR DGWFIFDLLA KVNINMDTYA
QMIEVCEDAA NVVSMRAEEI GKGSGAGLER VKDFLDRAFE AKQKGLIECY RSRVGPPEEE
FSSTWNKKND DGRENKRLAK GPTMSFWCMV PGVIVNELCE LGVKSLLLAS GTLSPMDSFA
SELRAPFPVR LENPHVIPQE NVWAGAFLKG PSNAVSLNSS YRFRDTEQYK NELGLLILRV
ARVTPDGVLV FFPSYGVMAK CIEFWKTRTS IWNDIARTTK KTLVVEPKES DAFLEAFESF
NKALERSKTN SWSKVGLTNT DGSAKDDETA VTLAAKGGAM FLAVCRGKVS EGIDFADKAG
RAVILTGIPY APKASARVRY KREFLDAAIM VHKRNNTHQS CNITSGEQWY SQTAMRATNQ
AIGRVIRHKD DFGAVILADE RFAYRNHQSQ LSLWLRPAMQ TFDTFERGIE SLSAFFERCG
NPNSALMLAA AEKSAKKKKR KGPLLQRKSE NDKTADFAGQ RQKKSSNTNG EQQQQQHHAR
RDTNFSKKSR ASDTSLPFAL MNALNNNNDD NTNKNENEVD EEKERRNFLF SGGGGGGGGG
GGGSLASRLL KSGGNRDNTT KLAGGGVGNI RGSGALGNAN VVDKAMLAKQ KLVKRARAEL
PPEDFPKFVE VMKSAVSADS SDVALHESMK TLAKLCKIEK RGVGPSTLWA AIGTSLALKD
AAKKAYDGFE ENAKRKMAEK TTTTAAATAA TIPPLVQSSQ PPPPPKPKID AGVENIFGRL
ARPPKEDSIS GELKSILTTK PSSSSQAPQK AAKKKTSCDH CKASKCDRPF QSIVCGHFAC
YKCFNAVFAK SSAEAKKAPN NNKNNTTSSS SSSGPCPTCS TLVTKKSLKK MYL
//
