ID U9UXP9_RHIID Unreviewed; 1494 AA.
AC U9UXP9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLOINDRAFT_15537 {ECO:0000313|EMBL:ESA23343.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA23343.1};
RN [1] {ECO:0000313|EMBL:ESA23343.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA23343.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI274845; ESA23343.1; -; Genomic_DNA.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_3_1; -.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; 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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 651..824
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 934..1106
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 312..339
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 540..576
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1494 AA; 171971 MW; 7DD8C1E6DD430FDC CRC64;
MPPKTKTKKK KQINSARAFS TTSTPSKNKE TLKNEIESQV SSPISEPSTT ELVVSSEQTK
VDNVEENINE EETYINSIIE NYQDLDLKRV DAYFKDSQEL ISLGNEMQVL KLDSNIEHKI
LNFIKKLGYH ELDQYRNLYT SNLSQEHIIS SLNKLYLILL RLGFSQENIK ECLININGAE
VKAALDWLCI HLSSEDLPAG FVDKIYYEKG MNISVTRSTS PTSQSPIKKG DVFKEKKSLV
QNSSSTSKPK RSNMVEKDMK DWILNSLEND ASDDSELEPV STYQPLSSSL KYATLKCELV
LQNKISSVLK KFNRSQEKQE QVNQRIDELQ KEIKSFEELG SYEFNSDEAE MEFKNLMKDK
DLEKEVKEIL GDEIEDGKEQ DKTIQIDENK QLEGDQKKDI MEKINDDDDD DLFGGLLDNV
PDDSTTSSES NVSSTIIMRE MIPKTFTGKL PKDQLKEFCR KKDDKVKISF DVDRGGSHYK
CSLKIRWSNE KKGQDKEWNM GNVACRKKIE AESYVATLAL FELTDLPIYL TFPTFFRELW
LELTEEKKSA ENKIKLAEEQ ERIKLLIDVI EEKKKENIIE EKSKISDELD QEQIYKEDKS
SIKHYNIVNK TSSEGEAMKK AFLNRQKNKT YMDMLEKRKQ LPIYSYKDQF LEKLNKNQVV
IISGETGCGK STQIPQFITE DMLMNGYGDK CNVICTQPRR ISAISIAYRV SAEIGDLPRT
IGTSKALVGY QIRLESKVAR GNILTFCTYG ILLRRLESDK LLKDVSHVII DEVHERSLES
DFLMIILKKI FERRSDLKVI LMSATIEASK ISRYFDHCPI IEIPGKIFPV EVKFLEDVIE
ETDYMIEADD EFARKVHRQI RDEGTITITG KGQTSHNIRL QYEEDIDSSY DLNIPQEYLE
QYSKKTQLAL SRIDETCINY DLIISLLNYI CNNPVAKQKN NIPEDGAILI FLPGMAEIRR
LNDQILSDIN FSDTTKFLVY PLHSTISSED QNLVFDIPPK GVRKIVLATN IAETGITIPD
VTIVVDTGKV NQIRYNERKK ITNLQEMFIS KANAKQRKGR AGRIREGICF HLFTKWKYER
EMHEHELPEI LRLPLQELCL KIKICELGNI EQVLSMALDV PLSQSIKNAI ITLQEVQAIT
AEEELTPLGI HLSHIPVDVH LGKMILFGSI FKCLDPILTI SAILNYKSPF LIPFGSESEA
EIVIKNKFKE GESDLLTMYK GYILWKELYE KEVINKGGKG WETVRRFCVN NFLSLQNLLM
IEDIKKQFLE LLVNIGFVKI DESSKNYLSR YRFQKSRLLC AIPSYYNQNS NSYAIINATI
LAGLYPKIIY QEPLKNQYFT VMDSGILTSG SSGIIKVNPK NVFIHPSSIV FKHDLKSQAK
ERNWFIYNTL IQTTKLYVRD VSKVDVVNLV LFGRDIEIKH EHKMVIIDKW IVLQCPGKTS
TILKYLRHQL NKILKYKIDY PTRDLEKEQE DWLNLILEVI KCSSNNTTTL SSSL
//
