ID L2GT55_VAVCU Unreviewed; 1274 AA.
AC L2GT55;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ELA46809.1};
GN ORFNames=VCUG_01709 {ECO:0000313|EMBL:ELA46809.1};
OS Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Vavraia.
OX NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA46809.1, ECO:0000313|Proteomes:UP000011081};
RN [1] {ECO:0000313|Proteomes:UP000011081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vavraia culicis strain floridensis.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; GL877432; ELA46809.1; -; Genomic_DNA.
DR RefSeq; XP_008074725.1; XM_008076534.1.
DR AlphaFoldDB; L2GT55; -.
DR STRING; 948595.L2GT55; -.
DR GeneID; 19879583; -.
DR VEuPathDB; MicrosporidiaDB:VCUG_01709; -.
DR HOGENOM; CLU_002902_0_2_1; -.
DR InParanoid; L2GT55; -.
DR OMA; LNMPAKC; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000011081; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; 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; 2.
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; IPR016438; SKI2-like.
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; 1.
DR Pfam; PF08148; DSHCT; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 3.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011081}.
FT DOMAIN 81..235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 487..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 272..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 143271 MW; FD24519F1DC2EEEE CRC64;
MDKKMKIDFT SAFKDTTTLQ VPQKKVTLHK KTHCTDKICR DNTSHEAIVP EGMPYTDIDL
AQPIDTEIFA YELDLFQRIS CIALERDENV LVCAHTASGK TAIAEYAIHL ALKRKQRVVY
TSPIKALSNQ KYRELKLKFD DVGLITGDST LNPKASVLVM TTEILRNMLY RSNELVGEIK
FVIFDEIHYM TDRERGVVWE ECIILSTFNC VFLSATLPNA NEFAEWVVNV QGRVCHIVSN
DRRVVPLIHY VFPVGGKSLF KIKGGGETDA VASDAAVDEE NDEDRVTGGY DGERTDRGCT
ARRTKEGALC GARNGKKGEK GRNMGDNRRN TESSSRRGTN VRYCGVDGTK MDNHTSTESS
DDRLAGGDER RGRGTRGNKR HDDTSGDRRR FNRGKGREEE KHKKSTNKKR NTKKVFKATK
KALKAHSPTS TVDFNVEMFN EAIQNIKKSR VDYADIKAII GLLTEKALLP VIVFNFRRKD
CENFATCLEE DYNSTEEKEH VTMIFNKALE TLRVEDRALT PIQSMLPLLL RGIGIHHSGL
LPVLKEIIEI LFSLNLIKVL FATETFSIGL NMPAKCVLFT TLFKFDGEKM RTITSGEYIQ
MSGRAGRRGI DKEGICISIL TEAINIESAV ALFNGRSNPL QSAFHLTYNM ILNLLKIEGL
DPVYVLERSF FHYQKIKGVE RLRDTVNYFY GLMSKVEGVK VSDEGIDKER SAVSNACANN
QLKDYAHNSN TLYDHLHENN DSNNDMHENG ERENSNTGEF EFVNDALSQR KLEDLSLSDL
LVKGRLIDVT LNVNGFPIYL QNCIISSVSG LKDKKKKGEK DVNLEVVVLL YNRTNKMKRK
CIRLCDISAI YDARVKINNK RLGRKYSLLY GTPVTGHYCT ICEEEVSAAC LEERCFFGVL
EQFMEGAGIE GLDEKMLEKE EEHPIEVNSA MTMEYKTDSV SNGDMSGYVN ASNGMSDSGA
LPNGSRSISR EDVYQDEKSG KRSCDGRVNG NTGSDGDQDR FNKLPSNKCL DRSDNESDVS
GAETADSDQS SGAKSEDEET SRDSSTSTSL PCTASPVLKN KILKYLNNVY NTKNSELFVA
SRIDHIDQCT KMIQVLRRLD YYDNNSVTVK GRVACELNTE ELVLTELIFN GHFLKLSVIE
VVSLLSCLVF TEKEDAEVSE QSLRNYKIIE EVVQNVVKVM NQVGLNVQVE DFPYSNELMD
VVRMWAAGAS FESVTARTQV FEGSIVRCLK RLDEMLRQLS CAARAIGNLE MERIFGEGIS
KIKRDIVFCN SLYL
//
