ID A0A139ISQ4_9PEZI Unreviewed; 1864 AA.
AC A0A139ISQ4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_6169 {ECO:0000313|EMBL:KXT17586.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT17586.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT17586.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT17586.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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 complex I NDUFA12 subunit family.
CC {ECO:0000256|ARBA:ARBA00007355}.
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:KXT17586.1}.
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DR EMBL; LFZO01000018; KXT17586.1; -; Genomic_DNA.
DR STRING; 113226.A0A139ISQ4; -.
DR Proteomes; UP000073492; 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 GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; 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 CDD; cd03244; ABCC_MRP_domain2; 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; IPR007763; NDUFA12.
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 Pfam; PF05071; NDUFA12; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
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 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 738..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1273..1293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1348..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 473..802
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 838..1081
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1188..1514
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1554..1839
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 200..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 207539 MW; 84EA8CC26B017355 CRC64;
MSTIMRTLRN LRSVGLKEYG HQLHYIGDTK RGALVGIDRY GNKYFENLDE ELPLRTRWVD
YKDHEFDPSQ IEPGWHAWMS YMVDKSPAED TLLQRQIRPW EPKKHVPVLT ASRSAFKTFN
TSDQEQSTAM DTKGSIEMSA LLDNSTTMFA RCKGAIWDSD DLSSCFQHDY LQTLLPLIAC
AISALFLACH ILRSAPRSRA EQDGYKHIPN GVRHDSPLHD SPDGSITDSS HDDEVQRNQD
LTLAKTKTNT SVLTVDRPRG EVWIPLVEEI TVLAELGVQV AALLVGAWGR DRTSAIAEVA
VWAYIAVLTS LRLLFSSTSK LSFPQLWYHT AILYCSQWIF TVLLFRSEII HPQSSISEAL
MSTHFSLTTL LAIIALSSRK GNRAVELEYE GEIEPSKEPL ASVFSLATFG WVDSIVWRGY
KAPLEMKDVW NLRPKDKAAE ILADYRQLKK TSILAWHLLR YFRRPLLEQA GWAAISGIVT
FVPTLLLKVI LQYVEDPSQT PKNAAWLYVI LLFVSGCINA LSSGQALWIG RRICIRLRAI
IIGEIYAKAL RRRAAAAPDK ILGQGDEKND ENESKQGALK KALSFGRKKY KKTNANGEPI
ANKPSPGGEE QVTSGAIINL MAVDSFKVAE ISAYLHFLWA ETPVQFILAI ALLYLFLGNS
SIVGIGMMAL LLPVNMFIAK QFTSVQKKIL AATDARIHTT NEVLTNVRII KYFAWEQRFL
AIVDEKRQVE LRHLRNRYIV WAAAATIWSG APVVITFLTF MVYTLVEKKD LIPSVAFTAL
SLFSLLRIPL DQLADMVAHV QESKVSVDRV EEYLNEPETD KYQQLRNDEY DECGEPLIGF
KQGTFSWGGR DAEDFKMIDL DLNFKVGQLN VVIGPTGSGK TSLLMALLGE MTLLSGSVYL
PGGPSREEVK RDPETGLTES VAYCAQQAWL MNGTIKENIV FASKFDARRY KNVIVACSLQ
RDLEILDGGD QTLVGEKGVT LSGGQKQRIS LARALYCDAR HVILDDVLSA VDSHTAKWIF
EKALMGPLMY NRTCILVTHN AALCLPQADF AVVLENGRTV AQGTAHDVIH SGTLAEEPSK
FDMKPRSAPA SKLPSRVPSD VGIDSQEVTT PSTANGHARE RIPRRDTEAS TLIGDPLTHV
ISKDIPGMNK PAEEKDIFNE KKATGAVKLS IISSYLRQMG GWIYWTTAAL CFGLQQLSQV
STTVWIQQWS NSYTRHEYLA RGLSHNHTFA VAHVRGGSSN CLRSGSCIWN MPFLSDAVHD
VKTMRIMNND VDIGYYLGVY AVLGLLYMGI TLLREGVLFG GSLTASRRIH RQLMERVTHA
KFRFFDSTPL GQIMNRFSKD VEAVDQEIAP VAVGVVHCLF SILTIVVLIS VITPGFLIAG
VFITILYFLI GRLYIASSRD LKRLESVQRS PLYQQFGETL SGMTTIRAYG DERRFIRENL
HRVNTHSRPF IYLWAANRWL ALRVDVVGAL VSFFTGVFVI LSVGRVDAGA AGLAMTYAVT
FTENVLWFVR LYASNEQNMN AVERVKEYLD VDQEAAPIIP ENRPEANWPS KGSVEFIGYS
TRYRSDFDFV LKNITFNIPP GEKVGVVGRT GAGKSSLALA LFRALEAEQG KILIDDVDIG
LIGLQDLREN IVMVPQDPTL FTGTIRSNLD PFGLFTDEEI FTVLRGVQLI GAPSASASQP
ASRPETPAGT LRKSTPNSSL NKQALTKVTE TPSSPATPTS PTALENKNIF KNLNSPVAEH
GSNLSQGQRQ LLCLARAMLK NPKVLLMDEA TASIDYATDS KIQDTIREIK NTTITIAHRL
QTIIDYDKVL VLDKGEVMEY GDPYDLITKE GGIFRGMCEM TGDFEVLEKD AKSAHNGRKL
VDDE
//
