ID A0A165BIW9_9APHY Unreviewed; 1603 AA.
AC A0A165BIW9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZT01143.1};
GN ORFNames=LAESUDRAFT_763968 {ECO:0000313|EMBL:KZT01143.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT01143.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT01143.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT01143.1,
RC ECO:0000313|Proteomes:UP000076871};
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).
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DR EMBL; KV427669; KZT01143.1; -; Genomic_DNA.
DR STRING; 1314785.A0A165BIW9; -.
DR InParanoid; A0A165BIW9; -.
DR OrthoDB; 6951at2759; -.
DR Proteomes; UP000076871; 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; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF36; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 5 ISOFORM X1; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Hydrolase {ECO:0000313|EMBL:KZT01143.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1019..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1058..1083
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1130..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1164..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1207..1228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..701
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1281..1512
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1603 AA; 175130 MW; 63AA51D068DD82B3 CRC64;
MPRSLFWRQF SALMRKNVIV LSKHPWLNVV RCILLPIGYG IFLAAAQFLL FRPNNDGLGT
AVPVQRLSDQ YDGSLTLLWA DGTNGAGSPS AEDIMAHITS GFNPWQLSNV QKVDSPSDVA
AHCPENWSGQ SQCFGALIFN SLPDSSNVSS ASQPYNYTLR VDYGLEYINV LKHTSSYEQR
MIPLQWAVDN AIIELTTNIS FPAPLEWPFT QETNAEQDTD VRLSFVRGTR NLIVLALFIC
YIGIAYQLPG SVMFERATQL TSHMKAMGLM DSARIISWHL TISLIYIPAW TLVSVIWHFQ
IFTGTNTGLV FAIHLLLGLS LASWSFFASV PFGRSPQLAA IASTVLAIGF AVLALVFQHA
STVSAFIYSL FFPPGFYIFA IRAVCGFEVH QIPTSVIRPD PDNHLRLLPL IFAAIINIFL
WPCIAVLLER YLYDAHNPSK LSWHFWGKQK RAVEDGISSL PAGTAISIRN LGKDFRTSTF
RRNKGVVTAV ADLSLDIPKT GIYVLLGSNG AGKSTTMSIL AGLLGRTRGT VLFEGGAERP
PLGTIGLVPQ KNVLFPELTC YETLRLWQAI KPLSDSSSKE DIEQLLHDCD LGKKVHYNAN
ALSGGQKRKL QLAIGLVGGS KILLVDECTS GVDPLSRRAL WRTLTSVRHE RTIVFTTHFL
DEADLLADTI AILAAPGKLV AQGTPVALKS QLGEGYAVHV TFPDDLEEGS AEPSELLERI
CLLAPFAFIS TSTPNGTSYQ LRSRDSSIVH EVLKMLEMER EEGFIDSYSV QSASIEDVFL
TLMHSNTETQ SATKEKVYDA TLSEGSFPIL GLTNGRKRSP VGQALTVFHK RILIARRSWL
TPLLLVLIAV GGACAPLFFI SGLPAQTCVQ AFPDVESLPL YAPYSPVVNQ AAKYGIFGAQ
VLASPPGILS TLGRTMETVP VYNISNNATF VEQVHQNYLS FPLGGVSFDL DSSSALVAWQ
ATPPGFTSLT MLNLASNVFL NHAVNASGKG IGVPRLIMAN LQRFAKFNFG ETLDTLKWVA
FYGAAMSAFP AFFSLYVSKE RRSSVQAMQF SNGLSNPVGL WLGHLMFDSI FSLIVATVMI
IIFATVSTQF AGLGLFWVVL VLYGVAAALF SYCVSLAVNS PLAAFALSAG YQIVTFLLYF
AAHLIIVTYA NVFDSSRDLS IIHFTLSVTA PVVSAVHAAF VSVNLFSLLC DGNQPATLPS
MGQLSRFGGP ILYLIGYSFA LFAILVWVDS GSIRPRRLKS HKRDSTTTKL ASGVEELRAA
CIRRHDVDDE AAAAAKSNDA LRVLNVVKAY GSPGNKVVDD VSFGVPKDTI FALLGPNGAG
KTTTFNMIRG DVIPNEGDVL INDVSIVNQP RAARLSLGVC PQFTAIDTAL TVREHLMIYG
RLKGLYRGEE VQRNVHALMH ATSLDMYADR LATSLSGGNQ RKLALAIALI GNPSVVLIDE
FSTGIDAKMK RDMWATLRTV ARGKAIVITT HSMEEASALA NKVGILAKKI LAVGTTESLA
ERYATYEVHF SCRSREEVAL AEKLMAQVPG ARMADDVATR FEVPIGHGMS LAKLFGVLSA
QKDFEYTVER ATLESVFLKV IRENDVLEED TASRTRRWWR LIF
//
