ID J8ZVN3_EDHAE Unreviewed; 1656 AA.
AC J8ZVN3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 2.
DT 08-NOV-2023, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJW03718.2};
GN ORFNames=EDEG_01987 {ECO:0000313|EMBL:EJW03718.2};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW03718.2, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW03718.2, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW03718.2,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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:EJW03718.2}.
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DR EMBL; AFBI03000032; EJW03718.2; -; Genomic_DNA.
DR STRING; 1003232.J8ZVN3; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_01987; -.
DR HOGENOM; CLU_002902_0_1_1; -.
DR InParanoid; J8ZVN3; -.
DR OMA; LNMPAKC; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000003163; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003163}.
FT DOMAIN 82..321
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..792
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1175..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1656 AA; 191531 MW; 08EEBF2C75DAE9A6 CRC64;
MINDDLFDVF EDTTALAIAP EAPKFEQNIN SDDHFTLNNT THISFYPKDV KYEKLDVEKM
YNGTIFKKEY PFELDTFQKL SVAAIDRNEN LLISAHTSAG KTVVAEYAIA HCALNNQRCI
YTSPIKALSN QKFRELSMLC DSQKLYNAEY FNSLHDGITI ESKKGDFDIV SGNNLHMHNS
EDNSKNNCDN IDGESSGQNS EFDVYGENVF CNSYASSFPT VISPSVGLMT GDVTINPNAS
ILVMTTEILR NMLYKGNTML KEVNYVIFDE IHYLKDAERG VVWEEAIILS PSHFRFVFLS
ATIPNADEFA KWVVSISKVC CHVIGTDKRP TPLEHFLWVR ERPYKILYNI PDNQSNTKDD
STFLADSNVG NKTVKRSING NDSTDKNDKD VYGVNNLSTT ANKSNSNINN LNTNNSVDIK
YNIEEKNPNK SNNTINNLYN SIDNKYNIEE KNANKSNNTI NNLYNSIDNK YNIEEKNANK
SNNTINNLYN SIDNKYNIEE KNANKSNTNK NNLYNTINNL DNIEEKNANK SNTSKKNFNN
NCNASECDDK FRIQQKMNIV YHKNSTKMVS PEKTTYFDKK VFLSAIKNVS NRKRTEENDV
KNLIMHVSSQ GLLPCIVFSF SRKECERYAL TLQDGFTDDN QKEKITLIFN AAIANLRDEE
KNLDLIQSIL PMLQRGVGIH HAGLLPIIKE IVEILFQENL LFVLFATETF AIGLNMPAKC
VVFTSLKKFD GESKRLVSSG EYIQMSGRAG RRNLDTKGIV FSLMNEYITL KKAVKLFSGQ
ADKLSSAFKL SYNMILNLMR IVDVDPVFLI KRSFFYFQSQ NNLEETYYKI EKMKNDVVGI
LLPRLKEQIC SKNDFIILEK IFEEQNLGLN FIRNDCNEKS NNNQFGCIAN NLIDIDCIHC
TTNNNSNIEN KHKNSSNNVL QKKFVEIYKE LKTNNQNSHS RNTIFTDEFL SAPINLNLKI
IDPLLKQKIS KKNIDDLSPY EIQNILKGYG KLRLKRNKIA CKFYNKQNCL ENDRVVDIFI
NNDGNFYTIR KCIIRKHSKD TNADAQSAKT NAKPIGVVYF DKCTQFFSVD YENIDAVYDL
RVMNLKALNE SAKRKVDKLY LDDVIKNYDY LVKFLNKFDE ETAIKHEKNS LNSLSKNFDK
EFCESSDENN IINKKQKEKA ISDVNNTKYS KSRMNITNFD KKNNDNSKSS SITNNKNENN
LIDYLDKSNL VNRKNDLVRD PEIEELIYLE TVIWLIKTKI IHFLPSNCCF ICGKSKFDVD
CLQNKCLDES EIADYIQEKD FLKYFSKNIN QKINKENHSS RSQKFPQSNN TINNTFSHKK
YNDRNIDCYK NNFSSTSSNF HNNDMLYSQR NRNNDNYNIS KYQNKFSEGN NNTDTYNMEN
RDHRKFKNYN QHRDISHDNK NRHSSPNKNI IERRNSHQED LQTNKYYQIL HNLHLEDTFI
RIYQDNLNQY INLTNIYHLS ECKKMMQVLR RLAYYDKSIT IKGRVACEIS TADELILTEL
IFNGKFLKMD IDEAVALLSC LIFHEFDNES TINEKNKQNY NTLTDIIKKL VAVMTECGIE
IKETDLLKKY SWEMMDIAMA WVNGKSFIEI CSMSKIFEGS IIRAFRRLEE LLKQLCAAAR
EIGNNDLENL LQLVSLKSKE ISCLLQVYMS KKYLTI
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