ID A0A194VMR2_9PEZI Unreviewed; 985 AA.
AC A0A194VMR2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Heavy metal tolerance protein {ECO:0000313|EMBL:KUI65454.1};
GN ORFNames=VM1G_00704 {ECO:0000313|EMBL:KUI65454.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI65454.1};
RN [1] {ECO:0000313|EMBL:KUI65454.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI65454.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM003098; KUI65454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VMR2; -.
DR OrthoDB; 2876209at2759; -.
DR Proteomes; UP000078559; Chromosome 1.
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:SF586; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 6; 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.
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 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 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 358..646
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 680..916
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 276..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 110806 MW; BEFFCC7E4E912CD5 CRC64;
MAREVAWRLS GYTAAEVLFL DAEVIYPFLL LLSYGIIFAV HSVIASQGQE DVEKPSVTGP
GGKPLPVTRI KVEKSATRNT VVREFSRLSH LFFKAGTTAV ILTFVANALH IIHQCARARW
ENIQRYCNDE LLVYITGGIF YWGYIGFSLI SQNDKPNAVH FSIWCIGLVF ELIILAAFLV
AFNDKLDRLQ SIEFHSWDSK LKSNAHQIPS DTALLSSFVI RVCFLLGMVV VYGSLRGHLP
SFWPTWKCQK KEEPIAMTTD ETTPLLNSLA TGLENGNGHT NGHANGNGAV ARSTRRRMSE
ARRVNGTAKG SRQKQAEFAF YRPEKLPHRS WWEYLRGYHV FFPYLWPAKK VKLQLLVLLC
FVLVILQRAV NVLVPIQLGV LVKALTEAAK LGADAMPWKQ LFIFLGLKLM QGPSAILGSL
RSILWIPVTQ HSYVSLQTAA FEHVHSLSLD FHLGKRTGEL LSALNKGGSV NQFLEQTTFQ
VAPMLMDLFI AIGFFWVEFG PLYALWATII TFSYLVLTIR MASTRADQRR DMVNADREEE
AVKNDSITAY ETVKYFNAEA FEFKRYHHAI KAFQNAEARV TFGMNLMNMW QTVVFISGML
IVMAIAAYEV VLGRRTVAEF VMIMTYLNQL QGPLNFFGSF YRTVQQAMIS GERLLELFKI
QPNMVDRPGV PPLRGCQGHI RWNHVDFDYA NSPALTDLTF ECRPGTTTAF VGESGGGKST
IFRLMFRYYN CKSGTIEIDG HDVKDLTIDS VRRAIGVVPQ ETILFNDTIM YNLKYANPEC
SNEEIYEACR AASIHERIMS FADGYQTRVG DRGMRLSGGE KQRVAIARTI LKKPRIIMLD
EATSALDSET EQQIQHKLFK NKELGEGKTL LIIAHRLSTI THAEQILVLH RGKIVERGTH
DELLNKHGRY HSMWEKQAKA EMAAKAANMA KEKAERAMRE ARLAAKDSGD DHSDDGGDSM
ASSCHIPTAP ATPAHELPGL NMIVH
//
