ID A0A166A2S7_9AGAM Unreviewed; 1551 AA.
AC A0A166A2S7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZV63334.1};
GN ORFNames=PENSPDRAFT_758018 {ECO:0000313|EMBL:KZV63334.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV63334.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV63334.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV63334.1,
RC ECO:0000313|Proteomes:UP000077086};
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; KV424686; KZV63334.1; -; Genomic_DNA.
DR STRING; 1314672.A0A166A2S7; -.
DR InParanoid; A0A166A2S7; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000077086; 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; cd18596; ABC_6TM_VMR1_D1_like; 1.
DR CDD; cd18604; ABC_6TM_VMR1_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:SF356; ATP-BINDING CASSETTE TRANSPORTER ABC4; 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 Hydrolase {ECO:0000313|EMBL:KZV63334.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
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 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1009..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1048..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1152..1170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1235..1256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 307..663
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 707..951
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1016..1293
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1330..1551
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 397..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1551 AA; 169821 MW; FA162394692C3385 CRC64;
MDLQVVVNAV AYAVTPKEAP VPLWRDTRLL PVYVGGVSVV IALLSAIFGT LRNVLSNARD
NNARPQDAGR KNIRAHITSL GGMTIFAFRV ARALCVFTLL GLYAYDLIRD ADAHTRPESV
TKNELRELVV LLTYLYASGL ALLNIVAQAP LARTAAPHLV LILLASCAVY GVRDIWPLMT
YTLRPLDARE GTLLWIKITL IALAGIIIPL TVPRQYIPLD RENPSDEPNP EQTCSLLSLL
TYSFLDKPIY TAYKYPQLAT ETLPAIADYD RTAHLVNRSF KHLDVFSGAR RQHMFFALMR
VFRWEYVVLS CMMALRACTA LFAPIGINRL LTYLETGGEG ALVQPWVWCL LMFLGPTVGT
VLMQYYTFTT TAAMVRAEGM ITQLIFEHSL RLRVKSESAS TPAPSAAPTP DNASIAESDA
GTAVADGSES TASHSGEASS STAVSSSSQS DGKGAGKTGD KKENDGKDEK KEDNFAGKIN
NLVTTDLQSI VNGRDFTMVA VFTPVMVAIS LYFLYLVLGW STFVGMAIMV ACLPIPGYLA
KMLQTVQKTL MKKTDARVQT ATEMMNVLRM IKMFGWEGKI AERLSTKRAE ELRWLRFSEM
IDLGNDGVTL FIPVLQMVAT YGTFTLVMGG RLTPSIVFPS MSVFMILRNQ IGMLFYFASP
LIKAKVSLDR VTEFLRETEL LDEYAHVNDA QPVESQLLGK PADDLTIGMC DASFTWSVAS
SSADGTVTPS RRTFTLRVPG ELTIPRGKIN IIVGPTGSGK TSLLMALLGE MHFTPQAAGA
WVNLPRAGGV AYAAQESWVQ NETIRDNILF GAPYDEVRYK KVIHQCGLKR DLSLFEAGDK
TEVGEKGLTL SGGQKARVTL ARAIYSSADI LLLDDVLAAL DVHTAKWIVD KCFKGDLVRG
RTVLLVTHNV ALAGSIADYV IAFGNDGAIA ARGSYKEVLA KDKGLAQEAA QEEEILAKAD
EEIEEPEDLN EPESKADGKL IVKEEVAEGH VSLHALKLFW WALGGRHPVL FWVTFLVGVF
GYHILASSQS FWLGRWAEAY TRPGPVDVTY YMVSFVLLVF VTTVTFVIAM GTYVFGVIRA
AKTIHALLID SILGTTLRWL DQTPVSRVIT RCTKDIKALD GQFAGEFRWL VSVSAQLITQ
LVAIALVTPA VILPGIGIFL VGAFFGNIYM KAQLPVKREM SNKKAPVLGH FGAAITGLTS
IRAYGAQDAF RQESYKRIEN YTRSGRMFYN LNRWISTRSD ALGALFSSGL GVYMVYGPGG
AAIGPSNVGF SLAMAAAFSN MILWWVRIFN DFEVEGNSLE RIQAYMEIEQ EPKPVKEKTP
PAAWPTSGDL RVEGLSARYS PDGPKVLHDL SFSVKSGERV GIVGRTGSGK SSLTLSLLRC
IYTEGDVYYD GVNTANLNLD VLRTNVTIIP QVPELLSGTL RENLDPFNEH DDAVLNSALR
ASGLFSLQSE TDEGRITLDS QISSGGGNLS VGQRQILALA RALVRGSKLL ILDEATSSID
YETDTIIQSS LRNELGGDVT LLTVAHRLQT IMDADKIMVL DAGRIVERER R
//
