ID A0A135UV06_9PEZI Unreviewed; 1789 AA.
AC A0A135UV06;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=ABC transporter {ECO:0000313|EMBL:KXH64238.1};
GN ORFNames=CSAL01_09277 {ECO:0000313|EMBL:KXH64238.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH64238.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH64238.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH64238.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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:KXH64238.1}.
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DR EMBL; JFFI01000998; KXH64238.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135UV06; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000070121; 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 Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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:SF353; ABC TRANSPORTER ATP-BINDING PROTEIN_PERMEASE VMR1-RELATED; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 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 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:UP000070121};
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 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1170..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1197..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1288..1306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..652
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 690..937
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1064..1337
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1378..1654
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 55..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1789 AA; 197546 MW; 4091B6777873106E CRC64;
MGSFAQCSWP IWYIDDLTPC FQQDYLKILF PLIVIGFSFL HLSLQAFRSA AKNRKHGYEQ
VPEEHHHGHT DIPPEETEDD DDEALTMNGG GRLALVKTTT KGSIVQADSP PAQNLTILVE
ELGIAGLIAI HIIALVTGTV PGQHGFLVTI VGLVTWVYIA ILATLRLFLG NTKWRVPRIW
NHTATIYLFQ WLFTVGIFRS VLIHPSSRLA QTLVIVEFVL TSLLFGLAIT TRKGNKTVLL
EWEGDIEPSR EPLASLFSLV TFSWVDPIIT RGYKETLEMK SVWNLVPKEK AAAVLADYRA
MKRTTTLAWH LLKYFKGELL LQFALAAFAG IFTFAPTLLL KAILEYVEKP EGAPINVLWL
YVILLPVLDI IRSFADNYAL WIGRKICIRI RAIMVGEIYA KALRRKASAG KDKELGKKAP
AAGKQSLIGK IKAKLGFKKD KADAEAAANG AAKDPAKDDE QANLGTIINL MSVDSFKIAE
VTAYLHFICA SAPTQLVVAI ILLWDVMGLS AIPGLIVMAL LLPINYSFAR GFANTSKKIL
GATDKRINVT NEVLQNIRII KYFAWEAKFG RIVDEKRAAE LKALRSRYVI WSFAVAVWNS
VPVLITFFSF LMYTLIEHKP LYPSVAFTAI SLFMLLRVPL DQMGDMFAHV QETKVSLDRV
EEFLTEEETE KYEQLGEDNV DEDGNKVIGL RKANFIWGGK DVVADDGSMA FRLIDMDIDF
LIGKLNIISG PTGSGKTSML MALLGEMTLV EGKVYCPGGR SREDVRPDPE TGLADTVAYV
AQAAWLVNAN IKDNILFAAP YDEKRYRDVI VACALERDLE ILDNGDETLV GEKGITMSGG
QKQRISLARA IYSNSQHIFL DDCLSAVDSH TAQWIFNNAI KGPLMAGRTC ILVTHNLQLC
APSSHFVVCL ENGRVTAQGP SAELIAAGKL GEDVQKAAIN SASVSRIPSR VPSSVGEGGS
ETVVNPGDES ASDARSKKND KKKEQKDAME EKKAVGSVKW PVIQLYLSSM GAWWFWAVAL
TVFGLQQMSG VATNFWVREW ANQYVDEEVA HIGFSTASHS YSQQSLSPTY FASIANYGNR
ISSNFSTSTV ADVNVTYYLT VLAIIGLAGS VAAFIRDIWV FYGSLTASKK IHDDLVTRVS
RAKFKFFDVT PLGQLMNRFS KDLEAVDQEV APIAIGVFGC ALGILVTVVL ITIITPGFLI
AGVFITAAYY FVGAFYLRAS RDLKRLESVQ RSPLFQQFGE TLSGMTTIRA YGDERRFIRE
NLSKINVQAR PFIYLWAANR WLAFRTDVLG DTVSFFAGVF IIISLGTGTV DAGSAGISLS
YAIGFTENVL WLIRLYAINE QNMNSVERIK EYLDVEQEAE PIDEKNRPPK NWPSQGSVEF
INYSTRYRAD LDPVLRGLSF KINPKEKVGI VGRTGAGKSS LALAIFRALE ADEGKILIDD
IDVGLIGLRD LREAITIVPQ DPTLFMGTIR TNLDPFDAYT DEQIFEALRK VQLIGPNEST
SRPATRPTTP SAGSILPVTP NLGLIRGDSN SSPGSSIAPT NKNIFLNLSS TVSESGSNLS
QGQRQLLCLA RALLKRPNVL VMDEATASID YATDTKIQET IRELTSTIIT IAHRLQTIVD
YDKVLVLDKG AVVEYGHPYE LIRKENGSFR GMCDMSGELP SLLKAAKKKW DSGRLVDVDD
EEPDTQSTLV EGEAQKVTEE AKKNDEEQDK KKAEAEAEAR KRAEEDAKKA REAEEEAKKA
EEESKKKAEE DAKKKAADEE TKKQADEEAK KQAEDKAKAD EEAKKAGGG
//
