ID A0A1X7RZX7_ZYMTR Unreviewed; 1323 AA.
AC A0A1X7RZX7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ZT3D7_G8136 {ECO:0000313|EMBL:SMQ52983.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ52983.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ52983.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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DR EMBL; LT853698; SMQ52983.1; -; Genomic_DNA.
DR STRING; 1276538.A0A1X7RZX7; -.
DR Proteomes; UP000215127; Chromosome 7.
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; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR PANTHER; PTHR19241:SF685; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
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:UP000215127};
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 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1111..1135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1297..1317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 710..947
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1323 AA; 145963 MW; 6AF10D6648F990A8 CRC64;
MAADSSSRSA SRSRFRDWDA IFLPDLAPTP TTVAFKGMLP KPDAIVPVPT VASAVLSTIT
LPWRVGQRLF RLRRTHETPR NPTFSLFVRP GEMVLVASAE PAECTQLLRA IVRHVSYPGV
AVFCSAEDVH PHVLTVEQLL RFRLRARAVR SPGAEDDAVE LLLRLFRIES IRNTLIGNAV
VRGISGGERR RLSVAEALLS GANVLCFDDL TRGLDAATAL HCVQCLRSVV DAYRLTIFAS
LSAASDTIYA TFDQLVAIRD GHQVFGGPPT AIRPLRDDPQ TQPAPPLASY FDHLHARIAP
RASSPTTHDM ADAFRRSAHY ADTAVCLATY LAEEQASPGS SNQSPRHHQK RHATYRKVVA
LLQRQMLLAW KDRFALTVSW ILFLVLGCTI GLACFQLQRT GAGAQARGGL LYTCVLGIAV
SAQVEVAKTT LGRPLLRKVF AYRFERPATF WTAQIAVDTM LESMRVFIFA ICVYFLTALH
RTAPAFLYFL AVLLLLYMCN VLMNRAIGCM CRTFDSAIRT ATFVFVFYMI TAGYILSQAT
QPSWLKWTYY LNPLALAFSA LMMNEFEHIT IDCQSSVLSF PPTRPLPVNA LQSGVTCGLA
TSADRTFLVA GRTYLQLDFD YDTHDKVRTI LNLLALVGLF FIANLALAEI LDWDSPASSV
MVSVPKNIQP PQQTRTACMT AFVPTPPTPE FVQSPAAWTR GVSRLSFCRL RYDIATERGQ
QSRRLLDEVT GVLESGQLLA VMGASGAGKT TLLNLLSGRE HSGVRGGTVS ACTSRGLPPT
IGYAEQVDIH EPKSTVREAM LFSACLRQPK HVSFVEKRAW VDHLIPLLEL TPIQHAIIGV
VGSGSELSAR DRKRTTIAVE LAAKPDILFL DEPTTGLGSE GALAIARLLR KLADHGQAIA
CSIHQPSAST LENFDQVLFL HNGKMVYFGP LGSGLYRPAQ YIARQTCSSC PVGRDPVEWM
TTQVIGSSPA HHETWSDAWA SSEEADMLQA SLKPTSWSET SRAESMRGHP CQASVWYQIS
QLTLRNSTAL WRTPEYGFSR FVNHVALAVT IRIVLPHAGH SIRDMVHRVL TLWQTTMLPA
FILTTVEYRF HASRRLSLRE SATSTYSNTA LAVSAMLAEI PYCFLCTAGF VLPLFSLVGP
LVLSQVTYFA LAVFLVQIFC VTLAQAIATL SPYERISTLF NTPSITVFAL FCGISVPRSE
LPGFLRNWLY YLNPYTWLMS GLLTNSIHGF NVQCAGNELT DITVPLPQTC QQAMSLLSTL
HDPGYIAGNT SQVCHYCPLT TGDRYSESLG LSYAQRWKYL GVFSVFCVSN VGLILLAQQF
RRR
//
