ID A0A0V0TLL0_9BILA Unreviewed; 804 AA.
AC A0A0V0TLL0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD {ECO:0000256|ARBA:ARBA00014344};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=ERCC2 {ECO:0000313|EMBL:KRX39411.1};
GN ORFNames=T05_306 {ECO:0000313|EMBL:KRX39411.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX39411.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX39411.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX39411.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000256|ARBA:ARBA00009146}.
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:KRX39411.1}.
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DR EMBL; JYDJ01000234; KRX39411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TLL0; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.10.275.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR010643; HBB.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR001945; RAD3/XPD.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF1; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF06777; HBB; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR PRINTS; PR00852; XRODRMPGMNTD.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX39411.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT DOMAIN 36..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 804 AA; 92250 MW; FE9504DB7FEB2017 CRC64;
MSQFSGSSNC CFAFIELYVR TSHNLGRITM RIDVDGLSVI FPYEFIYPEQ YYYMLQLKRT
LDARGHCLLE MPSGTGKTAS LLSLVIAYVK SYPSQLEKLI YCSRTIPEIS KVVEELRHLC
ESYEKETGES LNIVGLAMSA RKNMCIHPEV SKLRLGKIVD GHCLSLTSSF VRARRLDDPS
IPCCNYFEEF MEEGVESALP RGVYNLDDLK AYGRRMGWCP YFVARHALLR ADVIVYSYHY
LLDPKIAELI SKDLSRRSVV VFDEAHNIDN VCIESLSVTL KKRTIERCQE NLESLQKFVK
ETKERDVAHL DREYKRLVEG LREAKHLRDT DKILANPVLP DDILEEAVPG SIRNAEHFIA
FLRRFLNYVK HRMSSNSVMI ENPAVFLSDV QIRTAIERKP LRFCSERLAS LLRTLELSDT
SNFAPLILLA NFATLVSTYA KGFCLLFEPF DEKLPTVPNP VMTFSCMDAS IAIRPVFHRF
QSVLITSGTL SPLDMYPKIL NFDPAVMASF SMTLARPCIL PLIVAKGNDQ ITMTSKFEAR
DDTSVIRNYG TLLLELSRIV PDGIVCFFTS YMYMENTVAF WYKQGIIDRI MKNKLLFIET
QDIIETSLAL QNYIKACENG RGAILLSVAR GKVSEGVDFS DHLGRAVVML GVPYVYTESR
IIRARLEYLR DQFNIKENDF LTFDAMRQAA QCVGRALRNK TDYGLMIFAD KAFRMLNDRT
VLQRYSRSDK REKLPKWIQE QLSASNLDLS IEEALQISRR WLRTMAQPFT QNDQLGISML
NQTQITDEQM KRKLTNEAYL MELQ
//