ID A0A164Y6E1_9AGAM Unreviewed; 1611 AA.
AC A0A164Y6E1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZS96624.1};
GN ORFNames=SISNIDRAFT_482423 {ECO:0000313|EMBL:KZS96624.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS96624.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS96624.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS96624.1,
RC ECO:0000313|Proteomes:UP000076722};
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; KV419398; KZS96624.1; -; Genomic_DNA.
DR STRING; 1314777.A0A164Y6E1; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000076722; 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; 3.
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; 3.
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:KZS96624.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
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 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1134..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1158..1179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1242..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1274..1293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..669
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 718..953
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1018..1284
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1334..1597
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 388..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1611 AA; 177060 MW; 957920B04D6188F3 CRC64;
MEQQPILLYQ NLLHPFLDAN YPVATNGSIW TDPRIIPVYL SAISLFLLGL HAIIPETRLR
RFYSFFVDVS YRVKELQDPA YKESIAWSIL QSVRIVASLA LLAIQLVLIN QNFNVINLTL
LAFFAYTALL SPVPIFGTSK WKYLVSSHLS FLHLIILFIY VLRDIAPVAA GRLPLDYQEG
ALGWTRFAVL ILTGFFVPAN LPRRYIPADP ENPIPPTITQ TASYLSLAFF SHLDPLIYKA
FKNSTLTIDD LPTLADDDTA GYIEKSGFKT LDPVQLGRKQ WSFIWATIFY FKKQYAVMSA
LSIVQAINEF ASPVAINRIL SYLEGDHDAL RPWVWIVWLT VGPIINSICQ QTYLYFSTKV
VIRRSAIITH LVFVHSLRVR LSTAVKKEDA PSSKKTKKAP AAPLEAIQSP APTPVESQAI
DAADAAHVTG IPAEMMDGAD PAGTAPSSVA ATEVAVKAAE TNKPKEELRV EEKKPEEKSQ
DQIGKITNMI SSDLRILQGG ADWLTPVFLV VRLGICIALL YIILGWSAFV GMAIFICMIP
VPGWLAKLGM KLQATKMKKS DARIAAINQV MNVLRMIKIF AWEDKVEKHL SEKREEELGY
ILKTQWLSTG TWMLNSIFPL MTMIATYATY TLILKKSLTA STIYSSIAVF NIFQEHLFGL
FHYLPNMLRA IVSLNRVGDF VNNGELYSES GKEALVSTGA GEESSGIKIC KSAFTWEKQS
DSATGAQTPS TGRRNFKLQI DGDLVFKHGE LNIICGPTGS GKTSMLMALL GEMYYQPLGP
DSQWSLPREQ GVAYAAQESW VLNETIRDNI LFGAKYDKER FDKVIYQCAL TRDLSLFEAG
DLTEVGEKGI TLSGGQKARL TLARAVYSSA QTLLLDDVLS ALDVHTARWV ADKCLGGDLL
RGRTTILVTH NVLLVEPYAA YVISLSVDGR IVSQGTVAEA LRKNDRLRAE IELEEAQARK
EGYLGEDHKE SEASDEDKDA SKAAGKLIVP EEMAQGHLSW RAMKMWLVEF GGPFFFTLCL
VGIFADSVMS IAAKWFLGYW AMQYDAIDHA EVPVPKYLAI YAGILVAGLI FVGFANGYWA
WGSVRASRAL HRKLVHSILT STFRWLDTTP ISRVLSRCSQ DCQMIDGPLA EMSIGFLYIT
SGLICTIIAV ITQAGLTALI SAFVVVALGM LSGQLYMAAQ LPVKRDMSNA RSPVLSHVGA
ALTGLVSIRA YGAQAAFHDE SLRRIDRYTR AARVYWNLNR WIGVRMDTLG GLFTGIVAAY
VVYGRPTTSG NVGFTLALMS GFSFELLVWI RLFNEVEVQG NSLERIQDFL DIDHEPPSTK
DASPPAYWPA SGELIVENLS AKYSLDGPEV LKNINFVLKS GERMGIVGRT GAGKSTVALA
LLRAIPTTGT VLYDGLDTDK INLCALRSNV TVIPQHPELL AGTLRENLDP FGDHDDALLN
EVLNAAGLNR TQTSNTTAGP STGAPQRANV GEAPADNAGK SGESGTIGLD TEVASGGSNF
SQGQRQIIAL ARAILRRSRV VILDEATAAI DYETDRVIQE SLKTEFKDAT VITVAHRLQT
IMGSDKILVL DAGEIKELDS PKALLKRQGS FFKGLVDESS DKEALYSAAG L
//
