ID A0A1L9NNF6_ASPTC Unreviewed; 1479 AA.
AC A0A1L9NNF6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPTUDRAFT_139132 {ECO:0000313|EMBL:OJI90732.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI90732.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV878176; OJI90732.1; -; Genomic_DNA.
DR STRING; 767770.A0A1L9NNF6; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_139132; -.
DR OMA; CWQMIIT; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF269; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184304};
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 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1141..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 280..558
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 629..856
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 919..1199
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1236..1466
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1479 AA; 162708 MW; 3670F9153E5F20EC CRC64;
MAALLSCQQV DNTLHIPPSY CRSGFDFSLL FEELILGVLP LGVVLLLIPF QVGHLLGRPR
KVVASWLAWA KTVSWLTLSV INLVLTVLWA LPSATRTDAS VAANAVLTVG ILLLCLFSYA
EHNLSVRPSF LLNVYLGATL LFDIAKTRTL WLRHPEGINQ VIAIITSVGA GLKVLLLILE
ATEKRYILRH PYQNYPSEAL AGIYNRSFFW WLNSLFRRGF SKVLGVDDLF ALDKQLESKR
LHRILKGVVA KDRENGGSSL LSACLKAFKW PILAVIPPRI MLAALNICQP LLLERSLSFS
EQPKSTSTDN IGYGLIGAYI LVYVGLGVTM GQYQHLTYRS ITMVRGGVVS MIYEKACTLS
TKDADPASSV TLMSADIERI VQGWQTMHDI WGNALEIGLA IYLLERQLGL SCVVPVGVAI
VALVGSLIAM SFVMSRQARW LEAIERRISS TSSMLGSMKG IKMLGLQSAL LKSVHGLRLD
ELSISRKFRK LLVWNMALAW LTRIFAPIFA FGAFVGISHD RGNDAALTTS VVYTSLSLFS
LLSDPLLSLV MALMNYAGSV GSFKRIEEFL EQKEHIDPRN KSTGLSSYAL DEKSHLALIK
DTEVSTTESR SISFPSSKES LPSSVRDVVT IQNGAFGWDT TKEPLLKNLT MSIPQGGLTL
LIGPSGCGKS TLLKAFLGEV PCLQGNIQLS LNSLSFCEQT PWHMNGTIRD CIVAMSAFDS
QWYKSVIYAC ALAEDFEQLP RGDQTVIGSK GVALSGGQSQ RIALARAVYS RKSVIILDDV
FSSLDATTED HIFHHLIGNQ GLLRSIDSTI IFASSSVKRA PYADHIVVLD KNGHVIEQGS
FKALDATGGY VSSFALGLPD WGYKADLFPA SGVQVETKEK PKIASTETEP GADTETQGKG
GDLSIYLYYV KAIGWIPTIV FIVAIASFVF CISFPSIWVN WWASSNEAEP GKHTGYYLGI
YAMLGVIGML CLMVGCWQMV ITMVPRSGEV FHRKLLTTVL SAPMLFFSKT DSGAILNRFS
QDLQLIDMEL PIAAINTFAT LALCIAQMIL IAVASKYAAI SFPLVILIVY LIQKMYLRTS
RQLRLLDLEE KAPLFSHFTD CLSGLVTLRA FGWQQALQEK NDMLLDRSQR PFYLLYAIQR
WLTLSLDMVV AGIAVLLIVL VVVLRGSISA GYVGVALLNV IQFSQSIKLL ITFWTNLETH
IGSIHRVRTF TEDVQSEDLP TENREIPPEW PSNGEIEFKS VSAEYRASEP VLQEVSLTIH
GGEKVGICGR TGSGKTSLIM SMFRMVDITT GHLLIDGLDI SQLPRQGIRS RINGVSQSPL
LMKGSVRANA DPTGCFSDEA ITHALKSVGL YSKVQEKGGL DVDIDDLFLS HGQQQLFCLA
RAILRPGNIL VLDEATSSVD TKTDEIMQRI IREKFSSHTI LTVAHKLDTI LDYDKVVVLD
AGRIVECGNP HTLLCSDKSH FSRLYASLAM DEQEESPQA
//
