ID A0A165TAP8_9APHY Unreviewed; 1412 AA.
AC A0A165TAP8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAEQUDRAFT_808686 {ECO:0000313|EMBL:KZT73163.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT73163.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT73163.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT73163.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV429038; KZT73163.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165TAP8; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000076727; 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; 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:SF443; MULTIDRUG-RESISTANCE LIKE PROTEIN 1, ISOFORM I; 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; 1.
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:UP000076727};
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 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..442
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 518..738
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 805..1080
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1118..1365
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 480..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 157104 MW; 3303E527E43B7F44 CRC64;
MTSQKRFKRF LHVPGVPVDP PPPKATLDDA DLIPEETANF YNILTFGWIT PLLGLGYARP
LEDTDLYKLQ DSRSSQLIAD KILASFDQRR EAADEYNARL AAGEIKPGWK GLWWTLRGNR
AEREKQWRQK DGRKHASLAF ALNDSVAWWF WSAGILKLIA DVTTTLSPLV VKALITFSTD
SYYAHQAGLY DDIPPIGRGV GLAIGLLLMQ VLTSLCTHHF FYRATSTGVL LRGGLITAIY
SRSMQLTTRA RTVLTNGKLV NHISTDVSRI DFCCGFMQMG MTAPVQMVIC LVILLVNLGP
SALAGFAFFV LCTPLQTMAM RRLMGLRMKS MGWTDKRSKL LQELIGGMKI IKYFSWEVPY
LRKVEELRAR EMGYVRDLLL IRSANNAIAI SLPTLASVLS FIVYSLTGHS LNAANIFSSL
TLFNLLRMPL MFFPLAISST ADAKNAIERL YGVFEAETIQ DTQVQDPTLP VAVDVVDASF
TWEEPPPEPE TSKKLRSTFG GRKNKKSKQG SPTATAPASG AQTPKVADRI FSMSDITLSI
PRGQLCAIVG PVGSGKTSLL QGLIGEMRRT NGRVAFNGRI AYCAQSAWIQ NATVRENICF
GRPFDEARYW RAVHDACLDA DLRLLPAGDM TEVGEKGISL SGGQKQRLNI CRAIYVGADI
QIFDDPFSAL DAHVGRSVFQ NVLLNAPAGT TRVLVTHALH FLPQVDYIYT VVDGRLAERG
TYAELLQSGG EFARFVREFG AKEKEEEEEE EAVEEAGEKK KDGKEVAPVG KATMMQAEER
TTGSVSGAIY RQYLHAGRGE ILIPFLVISV ALLQGIQVMS SYWLVYWEER KWPYGSGFYM
GIYAGLGVGQ AVFFFFMGSG FAMLTYLASK KLHSDALTRV MYAPMSFFET TPLGRIMNRF
AKDIDTVDNL LGDSLRMLVA TLANILGAII LIGIVIPWFL IAVAAILVCY VWAAFFYRAS
ARELKRLDAI LRSSLYSHFS ESLSGLATIR AYGETQRFLE ENQKRVDIEN RAYWLTVTNQ
RWLGIRLDFL GILLTFVVAI LSVASRYTIS PSQMGVVLSY IISVQQAFGW LVRQTAEVEN
DFNSVERIIY YANELEQESP HRLPDHTPPA PWPPVGAIQF NEIVLKYRPE LPAVIKGLSM
TIRPGEKVGI VGRTGAGKSS IMTALYRLVE LTSGSIVIDG VNISTLGLED LRQSLAIIPQ
DPLLFSGTLR SNLDPFGYHD DARLWDALRR AYLVEDHKPG SIDGTDESVS TGNRFSLDSP
VEDEGGNLSI GQRSLVSLAR ALVKESKILI LDEATASVDY ETDRKIQDTI AVEFRDRTIL
CIAHRLRTII GYDRICVMDA GGIAEFDTPA NLFHRPDGIF RSMCERSTIT LEDILYAAKA
RMIDDEKRTY VETRKSSQSE FEEKAYVEVD EV
//
