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Database: UniProt
Entry: A0A372QQ08_9GLOM
LinkDB: A0A372QQ08_9GLOM
Original site: A0A372QQ08_9GLOM 
ID   A0A372QQ08_9GLOM        Unreviewed;      1408 AA.
AC   A0A372QQ08;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:RGB30121.1};
GN   ORFNames=C1646_765746 {ECO:0000313|EMBL:RGB30121.1};
OS   Rhizophagus sp. MUCL 43196.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB30121.1, ECO:0000313|Proteomes:UP000263633};
RN   [1] {ECO:0000313|EMBL:RGB30121.1, ECO:0000313|Proteomes:UP000263633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB30121.1,
RC   ECO:0000313|Proteomes:UP000263633};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RGB30121.1}.
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DR   EMBL; QKKE01000374; RGB30121.1; -; Genomic_DNA.
DR   STRING; 1803374.A0A372QQ08; -.
DR   InParanoid; A0A372QQ08; -.
DR   Proteomes; UP000263633; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd18597; ABC_6TM_YOR1_D1_like; 1.
DR   CDD; cd18606; ABC_6TM_YOR1_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF442; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER SUR; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:RGB30121.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        142..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        822..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        901..931
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          98..387
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          490..714
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          821..1059
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1097..1358
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          432..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          701..728
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1378..1405
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        452..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1408 AA;  158464 MW;  D22934711A3092C3 CRC64;
     MPFWKSKPPP PPIPNQLLPE LNANIFSRIT FWWAESLMKL GYKRPLEKDD LYILNDARLA
     KNIISNFEKS WEKELTRKDG KPPSLIRALN RVFGYKFWIA GFFRFISDTL QVTSPLILQL
     ILQFAQESWM TKDAKDASPK SYMGYLFSVI LFIMQMSSTL FINSYFYYSM EVGILLRTAL
     ITAIYRKAMM LSGKARSMFT TGKVTNIMST DTTRLDFACG FLHVAWTAPI QLCIALGLLI
     RYLGPSALAG FAFLVIMGPL QGKVMKTLAK TRGKAAKITD DRVKLTQEVL QGIRVIKYYA
     WEESFLNALN KLRDKEMKYI RLLLIIRSGI TGVAMAIPMF ASILTFIVYS VTGGSLSADV
     IFPSLALFSI LRLPLILLPM VISTLTDSSV SIKRIQELLL AEELDSLPKV NPDSDSAIKV
     IDGEFIWESA PPEELSKDKQ KKNKKKQRKS KGLSKIENNE KNHVEEIKDK KENINEKDNN
     GTTSQSSTTL TPIDSTEKNS TTFTPYSHLR NINFSIPRGS LVAVVGSVGS GKSSLLSALI
     GEMKKVRGEI EFGGSVGYCP QSAWIQNATL RDNITFGLPF DEEKYRRVVK DCCLEPDLAV
     LPDGDMTEIG EKGINLSGGQ KQRVSVARAV YFNADIVMLD DPLSAVDAHV GNYLITNCIQ
     GSLKGKTRIL VTHHLHILPH VDYVICMKDG EIVEQGTYEE LMKAGNAFAK LIEEYGEAEE
     EEEEVEEIDV KPVNKDEIKK EKSKVVEKSS KTLMTTEERS TGSVDNAIYF AYIRAAGGYI
     LIPVLLFLLV MMQATNIGNN YWLTVWTNKQ LKISEAAYME IYFAWGIVQS IFSVLVGVTF
     SYAGAKAART LHRNAIKRVI RAPTRFFDTT PLGRIINRFS KDVDTCDNLL SESYRMFYTT
     LAVVIGTFVL ISVVFVLFLV PLVPLMILYY VAAVYYRSTN RELKRLDSIL RSSLYAHFSE
     TLTGLPTIRA YREQNRFISI NERFTDIENK AYFLTVVVQR WLGIRLESIA NALIFFTSLF
     TIIERYQVNP AVSGLVLSYA LQVTGTFNWC VRQYAEVEAN MNAVERLVYY SDSLDIEPAP
     IIPDHRPPPE WPVKGEVQIK DLVMAYAPEL PPVLKGVSLD ISSGEKVGIV GRTGCGKSTL
     ATSFFRFVEP TSGKIVLDGI DVTTIGLKDL RSKITIIPQD PVLFNGTLRS NLDPFNEHDD
     AKLWNALRRS HLIQENNDNV EESTITDKSG ALLITGETQP QQFKPEKLSL DSPVDENGGN
     FSQGQQQLIA LARALVRDSK LIIMDEATAS VDFRTDYLIQ TTIREEFKDS TVLTIAHRLR
     TVADYDKILV MDAGNILEYD SPYILMQKPN GIFKGMCERS GEFNELFEIA KGKFGSDQKV
     KKEEINNEKQ EVIKQESEII NFEEKSDN
//
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