ID A0A1Y2DSV2_9PEZI Unreviewed; 915 AA.
AC A0A1Y2DSV2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Heavy metal tolerance protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR38DRAFT_238250 {ECO:0000313|EMBL:ORY62351.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62351.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY62351.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62351.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY62351.1}.
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DR EMBL; MCFJ01000009; ORY62351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DSV2; -.
DR STRING; 1141098.A0A1Y2DSV2; -.
DR InParanoid; A0A1Y2DSV2; -.
DR OrthoDB; 2876209at2759; -.
DR Proteomes; UP000193689; 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; cd18583; ABC_6TM_HMT1; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF672; HEAVY METAL TOLERANCE PROTEIN; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:UP000193689};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 276..559
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 593..827
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 181..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 101405 MW; 58DD3B964A1E8E50 CRC64;
MKESREWLLA NLHYVYPVVI FLYFAVASAV AACTLQTSSP VIKTKHGRPK TIIGLLLLLT
LSYFGQLTAK IVEYMILQLW PKPDVIVGLL SCILVFGIEQ TSLGDASTTV WYPFYGSWLI
ALAFDPVILV LAILASPGTQ PEAANAFLWV DCGIIVARCV ILLTTILAYF IWRDRTQLPG
NDSERSPLIP KPDQRPNNGD ASTDSGYGTN SESNTEATNS PSDAESPWER QEREGREQME
KRLKSEGSWI AYAKGFMVFF PYVWPVKNRR LQIQAALVAV CLIIGNALNV LIPRQMGIVL
DTLNKPAGRN PWVEVMILAG LKLASSEAGI NFVRQLLWIP VEYHSSESLA IAAYSHVMNL
SSEFHDNMSS SDLIVAISNV QSVSSMLESV CFQALPMLID LVVAFIYLSA TFGPYEGFIT
VATGMAFIHV ATWMIARVKD KRKTMVKTFF EEHYRRQAGI QGWLTVSAFN QIPYEEERYE
VAAKAKNSSM KNLYYGYLAG HAFQYLILLC GLIAGAFLAV YQVIQQERTA GDFAMLLAYW
GQLTSPLRFF ASLGKSISQE LVYAERLLDV MLTKPTVVDK PNAKPLELKG GRVEFRNVNF
SYDKKQDILK GVKLSVPVGK TVAFVGATGA GKSTILKLLD RFYDVKGGSI QIDGQDIRDV
QLSSLRQSIG IVPQSPILFD DTIMNNIRYA RLTASDEEIY AACKAAAIHE HIMGFSEGYK
TRVGERGVKV SGGELQRIAI ARAILKRPDI VLLDEATSSV DTETEQKIQD GLRILCEGRT
TFIVAHRLST VMNADIIFVV SGGEVVEQGS HEDLLKKKGK YSELWSKQIF VKPKESQQDQ
EVEQAPQTES QQQQSEGTNE GQPANLPSTA STTNGNRRQN STPKLDTNMA SKANDEAVKT
PSGHTKEVDQ SKDRS
//