ID K2SQP1_MACPH Unreviewed; 1722 AA.
AC K2SQP1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ABC transporter-like protein {ECO:0000313|EMBL:EKG18985.1};
GN ORFNames=MPH_03675 {ECO:0000313|EMBL:EKG18985.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG18985.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18985.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18985.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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}.
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:EKG18985.1}.
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DR EMBL; AHHD01000167; EKG18985.1; -; Genomic_DNA.
DR STRING; 1126212.K2SQP1; -.
DR VEuPathDB; FungiDB:MPH_03675; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; K2SQP1; -.
DR OrthoDB; 5473955at2759; -.
DR Proteomes; UP000007129; 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; cd03233; ABCG_PDR_domain1; 1.
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; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
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; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
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; 2.
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:UP000007129};
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 766..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 842..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 935..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1018..1036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1436..1453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1465..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1504..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1544..1565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1572..1592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1696..1717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 398..656
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1093..1338
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 17..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1722 AA; 190412 MW; 6682D3DF0E68285D CRC64;
MDRLDPDQLQ AEAIRRLSQQ SGGFDPNTLQ VFTTTSPGGD MTEVRSIRTT HSETRSVVHS
ETHSVIRSES RSELQGSGSQ LDLQLSGSQS FIRPGSQLRN ESFSADSLSE LHASGSNSHL
RESGSQSALR SGSMTALQSS GSLAALQEAD DQAASHANIT LFAGPAADAQ SSAQGPESNS
AFRSARNGSE DATLATKSSA FALGSGSEAN GSARQGSTSV SARPDSQDAS TTLHTANSAY
FDAADASNNN DKEIAPASHE FRSVVKADAH SLPSEKPGSE DGATLNSKSS DIVHVNDGVN
VARAEHEFQE LSKELSRLSR SQSHKNKNGA TDLEKAASAS DASEHEQFDL EAVLRGRKDE
AEESGIKPKK VGVIWDGLTV SGIGGVKNYI KTFPQAFVSF FNVYETAKGL LGVGKKGREF
DILKDFKGVA RPGEMVLVLG RPGSGCTTFL KVIANQRFGY TKVDGEVTYG PFDANTFEKR
YRGEAVYNQE DDIHHPTLTV GQTLDFALET KVPGTRPGGL SRQQFKERVI DMLLKMFNIE
HTKNTIVGNP FVRGVSGGER KRVSIAEMMI TNACICSWDN STRGLDASTA LDYAKSLRIL
TDIHQVTTFV SLYQASESIF KVFDKVMVID SGRCVYYGPA QQARSYFEGL GFLEKPRQTT
PDYLTGCTDP FEREYKAGRS ENDVPSTPEA LVEAFNKSDI SARNDREMEE YRAEIAQEKQ
VWDDFQTAVA QGKRHASNRS VYTIPFHLQV WALVRRQFFL KWQDKFSLTV SWATSIVVAI
ILGTVWLDLP TTSAGAFTRG GLLFISLLFN AFEAFSELAS TMTGRPIVNK HRAYTFHRPS
ALWIAQIMVD TVFASAKILV FSIMVYFMCG LVLDAGAFFT FVLIIISGYL SMTLFFRTVG
CLCPDFDVAI RLAATIITFF VLTSGYLIQW QSEQVWLRWI FYINALGLGF SALMMNEFKR
LTLTCTSDSL VPTGGSYNDI AHQSCTLAGS TPGTDQISGS AYIEQGFAYH PSDLWRNWGI
MVVLIVGFLA ANALLGEHIK WGAGGKTVTF FAKENAETKK LNEDLQRKKE RRNRKEQTTD
AGDGLKINSK AILTWEDLCY DVPHPSGNGQ LRLLNNIFGY VKPGQLTALM GASGAGKTTL
LDVLAARKNI GVISGEKLID GKAPGIAFQR GTAYAEQLDV HEPAQTVREA LRFSADLRQP
YEVPQSEKYA YVEEVISLLE MEDIADAVIG DPENGLAVEQ RKRVTIGVEL ASKPELLLFL
DEPTSGLDSQ SAFNIVRFLR KLAAAGQAIL CTIHQPNSAL FESFDRLLLL QRGGQCVYFG
DIGKDAQVLL QYFHRYGADC PADLNPAEWM LDAIGAGQTP RIGNKDWGEI WRDSEEFAKV
KSDIVRMKEE RIKEVGAAPE VHQQEYATPM WYQIKRVNAR QHLSFWRTPN YGFTRLFNHV
IIALFTGLAF LQLDDSRASL QYRVFVIFQV TVLPALILAQ VEPKYGISRM ISFREQSSKA
YKTFPFALSM VLAEMPYSIL CAVGFFLPLY YIPGFQSASS RAGYQFFMVL ITEIFSVTLG
QLIAAITPDP FIAAYMNPFI IIVFALFCGV TIPKPQIPKF WRSWLYQLDP FTRLIGGMLV
TELHGRSVEC TSSEYNRFDS PPGQTCGDYM QDFFAAGGPG YILNNQTSNC EYCAYKVGDE
FYQPLGYEFT NRWRDLGILI AFIGSNLILL FTAARFLNFN RR
//
