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NU4C_ANTAG
ID   NU4C_ANTAG              Reviewed;         501 AA.
AC   Q85BG0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase chain 4, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase, chain 4;
DE   AltName: Full=NADH-plastoquinone oxidoreductase chain 4;
GN   Name=ndhD;
OS   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Yoshinaga K.;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 12 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 20 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 33 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 46 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 49 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 73 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 99 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 102 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 129 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 135 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 137 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 178 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 179 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 206 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 242 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 261 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 273 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 293 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 295 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 308 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 309 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 322 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 333 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 334 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 345 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 348 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 375 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 402 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 439 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 479 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 483 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 492 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The initiator methionine is created
CC       by RNA editing. The nonsense codons at positions 33, 333 and 439 have
CC       been modified to sense codons.;
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; AB086179; BAC55401.2; -; Genomic_DNA.
DR   EMBL; AB087485; BAC55501.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_777464.1; NC_004543.1.
DR   AlphaFoldDB; Q85BG0; -.
DR   SMR; Q85BG0; -.
DR   GeneID; 2553497; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_00491; NDH1_NuoM; 1.
DR   InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR43507; PTHR43507; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..501
FT                   /note="NAD(P)H-quinone oxidoreductase chain 4,
FT                   chloroplastic"
FT                   /id="PRO_0000118010"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  55853 MW;  21375F1067BF75DF CRC64;
     MSNFPWLTII VLLPISAGLL IPLLPNKGNR IIRWYTLGIC LVEFLLITYI FCNYFHFDNQ
     FIELKEDYNW INLLDFHWRL GIDGLSIGLI LLTGFITTLA TLAAWPITRN PRLSYFLMLA
     MYSGQVGLFA SQDILLFFFM WELELIPVYL LLSMWGGKRR LYAATKFILY TAGSSVFLLM
     GALTMGLYGS DGPTLDFENL ANRSYPIGLE IILYLGFFIA YAVKLPMVPL HTWLPDTHGE
     AHYSTCMLLA GILLKMGGYG LIRINMELLS HAHSIFAPWL VVIGAIQIVY SALTSLSQLN
     LKRRIAYSSV SHMGFVLIGI GSTTDIGVNG AILQMISHGL IGAALFFSAG VTYDRTRTLF
     LNQMGGIATS IPKIFTMFSS FSMASLALPG LSGFVAELMI FLGIVSSQNF SFLFKVVIII
     VAATGIILTP IYLLSMLRQM FYGYRIIKNL TSYVTDAGPR EIFIFICLFF PIIGIGFYPK
     LVLSLSNSKV ESIISGNFSS K
 
 
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