ID A0A1V8TDG8_9PEZI Unreviewed; 2820 AA.
AC A0A1V8TDG8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=B0A48_04824 {ECO:0000313|EMBL:OQO09426.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO09426.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000006};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC {ECO:0000256|ARBA:ARBA00009252}.
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:OQO09426.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NAJO01000010; OQO09426.1; -; Genomic_DNA.
DR STRING; 1507870.A0A1V8TDG8; -.
DR InParanoid; A0A1V8TDG8; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000192596; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR034300; PNTB-like.
DR NCBIfam; TIGR00561; pntA; 1.
DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR Pfam; PF02233; PNTB; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2248..2268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2280..2302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2308..2328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2348..2368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2374..2391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2398..2419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2425..2443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2455..2478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2484..2506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2526..2545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2606..2628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1818..1964
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 1973..2137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 181..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2820 AA; 303767 MW; FF651A7213C9AC29 CRC64;
MADQNDHGRT VDGVPPNRWQ RAPTVREALP FTPFSSIVPF NPGIIPAPLV TSSHGPDIGL
GSHRQVRQIL QELSAGATSA EYASERCQKT LRDVQQLLRP EHLMRYTFKT PRNLADPAKP
PTKRAREYQP PKLSAFAQMA LDQTVIPIRY LTPESPESKP KPLANGHATK QEVQWKLLTP
SSDAKLPNGQ RTPQALQPVQ QTAGAQRADH DKTTPYSSQQ GKVLLRQDEL APAERAQYQY
VDGNSVSMRP VVSSGQRQQS DAALQSLQVL LDDVLEAEEH LRSGGMESDI GGLLCMVDLD
DGSAVVMQPA ARERLDTAIL AVTKVSRLDE ISVDTLLRIQ KLCHSSLSST INLDLQIDEA
WSTDDTHDWA NKTTEAASAL LAARTLLRIM TAGREEQQLQ SEELVGAVLK LLNNAIEAGL
VPIIEERSFI GEKIRGGDKP RPNPKFETAM HNRDALRVLL NSVTKTLRLL GTLLSKVDID
ESALSNTVSM AKALIFAENA TNDKDSVFGV QSVESVRKSA MDILGRIFTK YTDQRQFVID
EVLFSLEKLP ATKQSARQFR IPDMKPIQLV SALLMRLVQT SATRSSTALH LHSSTGDEED
DEQDSEDESE DEDAEAASDD DEIKISPSKS RKAPGDLLTL VKPLHDAATT DASHIIRILT
NRALTTSKNS DEPYRKLLDI FTEDFLQVLG SSEWPAAELL LRMLLGQMLQ IAQNPKNPQA
SRNLALELIG TMGSGMLQLQ IQARNAAHSL TTDTSTVATE LVNTFERMEG GDHDNSTLLA
FDGPYRVVLE YIHARDGGSE AQLQTARGFH LVQWAQALCG GREGSVDSER GDGSGGSKDL
QGKLRSMIMN PQWLESNHDF PAVPAATGRF AAILVTLNTT FCRAFTHVLS VLLNALADEH
PTVKSRALKS VIIILEKDPS VLDRNKSILH HIFRCAEDKS ALVRDSALRL ISKCTSLRPA
LDATVLPQII FRSEDPQVGV RKTAIKMLKD IYLRNEDINL RSTVANACIS RLRDSEESVA
ELARSVMEEI WFAPYYPAQV QHEGGVQTRL RFQSQAALLV RTVDLGEDVS NLLVSSFRDL
MAKSKTSTDN AKVCKTLIEV LSDGIIDPSD IPGSPSQDLI LETLAVFARS CPTFITANHL
ERLEPYTQNL ATDDDLAVYR SVLTILRFTM PHVHTLRSDF LQKLQVSLMS SIQRLPKPEI
AEVASCLWTI DGQLKNTAKL VNLVISALAG IRGMVGKPLS DDAKMVNRIG KLMNIVGQFG
RACDLEAHIG TFRASEKLSS PNAKSVSELA IDILCAFTGT GQILAVREAA LDAICAICLR
WPNQYLRPGV TKAFGLVHKE RNPSLEMIFL SGLEAFFAAQ ELPADRQEGK DGAATGREGL
ESTYIATDQD GASSALAQRF LKDILRLALA SSDDLALTAT KLIASIVQQG LPHPKECGPS
LVALETSPNP AIAKLAFVEH RVMHQKHETT VEKEYIRAMQ QAFAYQQSVV GSTNGYIGQP
PASKLKLFWE VLKEGKLKVR QKLLNNICQK FDFEAADLKL QNGRSPHLDF VRFCCENLAF
FEYDRTDDLL LLLAALDKTF ASNGTTVAQA IEQNVLQLNI DALTNGGAAS QDMTNGTAHQ
SVSNDSAQLS VYATSSQVLL VVQETRSYLQ RVWNLQRMAK KAKGATKENS KAPSRSSNAS
AMAEAYLSKV EQIIASPTTP DAQRSICKQF VDVMTTDHDV KVPEEDELVG DFDDATTNSE
TASRRSLSVT PTANGKGKKR KSISAAGSTP RKKARPSLAK TKSGSKALDE DEDGAAQSSP
SPEAEPVPSI PYSELTIGVP LEVRSGERRV AMTPQNAALL LKKGFKQVLV ENGAGFAAQF
SGHAYEEAGA TLVNASRVWY DSNIILKIRP PRITSRGLVG TNNYLEGFRK GGVLIGTLQP
NIDRNKPVVD SMVRKGLTSF SMDMIPRITR AQTFDVLSSM ANIAGYKAVL EASNHFGRYM
TGQTTAAGKI PPCKVLVIGA GVAGLSAIAT ARRMGAIVRG FDTRSAAREQ VQSLGAEFIE
VEVKEAGDGG GGYAKVMSKE FHDAEMALFL EQAKDVDIII TTALIPGRPA PTLITEEMVS
AMKPGSVIVD LAAENGGNCE ITVPGQLTDY KGVTVIGYTD LPSRLPTQAS TLYSNNITKF
LLSISPKEGH FGIDMNDEVV RRSIVTHNGE LIPALPPIAP PAPAAKPAEV AKEEIKAVTP
WQKAVREVST VTGGMGTALV LGKYTGPLFM GNFFTFSLAA LIGYRVVWGV QPALHSPLMS
VTNAISGMVG IGGFFIMGGG YLPQTIPQFL GAASVLLAFV NVSGGFIISK RMLDMFRRRT
DPPEYAWLYT LPAVLFGGGF IAAASTGLGG LVQAGYLVSS ILCIGSLTGL ASQATARAGN
ILGMLGVGSG VLASLAAVGF PVETLVQWAG VAGIGSIIGA LVARRITPTE LPQMVAALHS
VVGLAAVLTS IGSVMAAVSH LDALHMVTAY LGVLIGGVTF TGSIVAFMKL SGRMSSRPTI
LPGRHLINIG LLGSNIATFG AFLTMAPGAP VIAAGCLAAN TAFSFAKGFT TTAAIGGADM
PVVITVLNAY SGFALVAEGF MLNSPILTTV GSLIGVSGSI LSYIMCVAMN RSITNVLFGG
IAAPGKTDFK MEGEITQTTV DETVTSLKDA QKVVIVVGYG MAVAKAQYPI ADFVAYLRAQ
GVEVKFAIHP VAGRMPGQCN VLLAEANVPY DIVLEMDEIN EEGFDDVDVT LVIGANDTVN
PVALEKDSPI AGMPIINAYK SKQVIVMKRG MGSGYANTKM LFGDAKATCD AIKAALDASK
//
