ID A0A2T2N237_CORCC Unreviewed; 986 AA.
AC A0A2T2N237;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BS50DRAFT_509128 {ECO:0000313|EMBL:PSN59098.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN59098.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN59098.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN59098.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ678166; PSN59098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2N237; -.
DR STRING; 1448308.A0A2T2N237; -.
DR Proteomes; UP000240883; 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; cd18573; ABC_6TM_ABCB10_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 1.
DR CDD; cd02223; cupin_Bh2720-like; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 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; IPR013096; Cupin_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF07883; Cupin_2; 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 SUPFAM; SSF51182; RmlC-like cupins; 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 Reference proteome {ECO:0000313|Proteomes:UP000240883};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 185..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..474
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 507..744
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 106331 MW; EE7DC69D1DF66128 CRC64;
MRGLSAFSAK AWHGPGNGAL FSHIQSRVNL LSPLSLRGSA ARTNCADEIA SQARCLATRG
PLAVRPALLH LHAPAGLARR NGVPQPSRAF SASRAAFEAQ KATKQPVKAR KSYKDEMKEK
GVVNVEEQEP ESEEMGFVKS ERASAAAQVN LSAKLSKDGS GGGTPGGMRE MWRLIKIARP
EMGTLSWAFL FLLLSSAVSM SVPFSIGKIL DIATQPEGSK ELLFGMDITT FYAVLAGVLA
TGAACNFGRI IILRIVGERI VARLRSQLYR KTFNQNAEFF DANRVGDLIS RLGSDTIIVG
KSITQNLSDG LRSLVSGAAG FAMMGWVSIK LTGILAIIGP PVAVVAFLSG RSLRNISRKI
QKNLGTLTKI AEERLGNVRT SQAFVGEVQE AGRYNRQIKR IFALGKKEAL VAASFYGSTG
LMGNMTVIAV LYVGGGMVKS GAISIGELSS FLMYTAYAGG SMVGLSGFYG EMMKGVGAAS
RLFELQDRNP TLSPTKGEPV KSARGPIEFK NVTFSYPTRP AVTIFKDLNF KIDQGMNVAI
VAPSGAGKST VASLLLRFYV PNEGLITING RDITKLNAKQ LRRKIGYVGQ EPVLFSGTIA
ENIAYGVPNA TRAEIVAAAR KANCQFISDF PDGLETHVGA RGTQLSGGQK QRIAIARALI
KKPDILILDE ATSALDAESE TLVNQALGKL LEERNTTISI AHRLSTIKRS DRIICIGADG
QVAEEGTYHE LSNNPNGAFS KLMEWQLSGG DAEPTVNNPR PTEVEEIERE LEIEEAEEEK
TRSKTLNLST TVPLSHPSSS INSSRSASTT SLRSPSQERR SKMADFKNVG NKANQPPKHE
MVHFKGLLSG KRKFKEFRRV LHTGLYSQLV AMEVPVNGEI GDEVHTVDQI LLFTSGRGRA
TVAGKDQDVA AGDVVVVPAG TQHQFVTVGE EPLKLVTVYS PAEHDPATVH RTKEEGDEEE
EPGWSGRGKK QNEDDGLVKF DGVYQE
//
