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Database: UniProt
Entry: S3DA25_GLAL2
LinkDB: S3DA25_GLAL2
Original site: S3DA25_GLAL2 
ID   S3DA25_GLAL2            Unreviewed;      1350 AA.
AC   S3DA25;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:EPE35282.1};
GN   ORFNames=GLAREA_10981 {ECO:0000313|EMBL:EPE35282.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE35282.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE35282.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily.
CC       {ECO:0000256|ARBA:ARBA00007577}.
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DR   EMBL; KE145354; EPE35282.1; -; Genomic_DNA.
DR   RefSeq; XP_008077361.1; XM_008079170.1.
DR   GeneID; 19470023; -.
DR   KEGG; glz:GLAREA_10981; -.
DR   eggNOG; KOG0055; Eukaryota.
DR   HOGENOM; CLU_000604_17_2_1; -.
DR   OMA; GFGQEEQ; -.
DR   OrthoDB; 1067095at2759; -.
DR   Proteomes; UP000016922; 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; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR   CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR   CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
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; 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   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF503; LP14331P; 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; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:EPE35282.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        103..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        767..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        827..849
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        895..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        923..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1009..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1041..1065
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..397
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          432..677
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          771..1070
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1105..1343
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1350 AA;  147421 MW;  9ECB80D1EAA4C33D CRC64;
     MGADFSEKPD RRSTGASSHG DSTSEHDSTR KEKAETSRLS SDRKAQSIAK ADSHVVQVKD
     KGEDDIYAHL PPAEAQILKN QVELPVVKAG VKILYRYATV NDYLIIAISA ICSIAAGAAL
     PLMTIIFGNL AGEFNSYFAG TTSRADFNDT INHMVLYFIY IGIAEFVTIY VSTVGFIYTG
     EHISGKIRWH YLEACLRQNI GFFDKLGSGE ITTRITADTN LVQDGISEKV GLTLNAVATF
     VTAFVIGFIK SWKLTLILSS TVVAITVSMG LGSTFIVKYS KQSLGSYALG GSIAEEVISS
     IRNAVAFGTQ DKLARQYDVH LAKAEKYGHR VKFVLAIMIG GMFCVIYLNY GLAFWMGSRF
     LVNNEITLSA ILTILMSIMI GAFAFGNVAP NAQAFTTAIS AAAKIYNTID RVSPLDPTSE
     KGEIIPEVKG TIELRNIKHI YPSRPEVTVM QDVSLVIPAG KKTALVGASG SGKSTIVGLV
     ERFYDPVGGQ VFLDGKDVST LNLRWLRQQI SLVSQEPTLF GTTIYENIRH GLIGTKHENE
     SADQQKELVL EAAKMANAHD FITALPEKYE TNVGERGFLL SGGQKQRIAI ARAMVSNPKI
     LLLDEATSAL DTKSEGVVQA ALEVAAAGRT TITIAHRLST IKDADNIVVM TQGRIVEQGT
     HNELLATRGA YYSLIEAQKI AAKEEMSAEE EAEIDHEDDK LVRKMTSKSG DFMEDPDDKN
     IANKLNRTQS EKSQSSVAMQ GRSENKIPEP SLWTLIKLIA SFNKKEMWWM LLGLSFSIIC
     GGGNPVQAVF FAKEIISLSY PLTDPRTGAE IPGAAHKIRS DVNFWSLMYL MLAIVQLIAY
     CGQGLAFAFC SEKLIHRVRD RAFRTMLRQD IAFFDKDENT AGALTSFLST QTTHVSGLSG
     VTLGTLLSVI TTLVAAIAVS TAIAWKLALV CVATIPVLLG CGFFRFWLLA QFQQRAKKSY
     EKSASFACEA TSAIRTVASL TRENDVLQQY VDSLEAQEKR SLNSVLKSSL LYAASQSLMF
     ACVALGFWYG GNRIADHEYS MFQFFVCFSA VIFGAQSAGT IFSFAPDMGK AKQAAAELKI
     LFDRQPTIDT WSEDGASLQN VEGHIEFRDV HFRYPTRPEQ PVLRGINLSV KPGQYIALVG
     ASGCGKSTTI ALLERFYDPL VGGIYIDGKE ISSLNINDYR SYIALVSQEP TLYQGTIREN
     VLLGADRQDV PDSAIEHACR EANIYDFIMS LPDGFSTVVG SKGSMLSGGQ KQRVAIARAL
     LRDPKVLLLD EATSALDSES EHVVQAALDK AAKGRTTIAV AHRLSTIQKA DIIYVFDQGR
     IVEQGTHMEL MSKGGRYSEL VNLQSLGKTG
//
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