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DER_NEIG2
ID   DER_NEIG2               Reviewed;         485 AA.
AC   B4RKD2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN   OrderedLocusNames=NGK_0592;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
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DR   EMBL; CP001050; ACF29283.1; -; Genomic_DNA.
DR   RefSeq; WP_010357432.1; NC_011035.1.
DR   PDB; 6XRS; X-ray; 2.80 A; A/B/C/D=1-442.
DR   PDBsum; 6XRS; -.
DR   AlphaFoldDB; B4RKD2; -.
DR   SMR; B4RKD2; -.
DR   EnsemblBacteria; ACF29283; ACF29283; NGK_0592.
DR   GeneID; 66752763; -.
DR   KEGG; ngk:NGK_0592; -.
DR   HOGENOM; CLU_016077_6_2_4; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTP-bd_EngA.
DR   InterPro; IPR032859; KH_dom-like.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF14714; KH_dom-like; 1.
DR   Pfam; PF01926; MMR_HSR1; 2.
DR   PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Nucleotide-binding; Repeat; Ribosome biogenesis.
FT   CHAIN           1..485
FT                   /note="GTPase Der"
FT                   /id="PRO_1000099142"
FT   DOMAIN          3..167
FT                   /note="EngA-type G 1"
FT   DOMAIN          176..349
FT                   /note="EngA-type G 2"
FT   DOMAIN          350..434
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   REGION          435..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         56..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         182..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           98..108
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           132..136
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           152..160
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           188..196
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          223..228
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           248..257
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          259..266
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           273..284
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          288..294
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           301..314
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           316..318
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   TURN            328..331
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           337..348
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           354..367
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          379..387
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   TURN            388..391
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          392..399
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   HELIX           405..419
FT                   /evidence="ECO:0007829|PDB:6XRS"
FT   STRAND          427..431
FT                   /evidence="ECO:0007829|PDB:6XRS"
SQ   SEQUENCE   485 AA;  53956 MW;  C9141A08B63A57FD CRC64;
     MKPTIALIGR PNVGKSTLFN RLTRTKDALV HDLPGLTRDR HYGHGKVGSK PYFVIDTGGF
     EPVVDSGILH EMAKQTLQAV DEADAVVFLV DGRTGLTPQD KIIADRLRQS PRPVYLAVNK
     GEGGDRAVLA AEFYELALGE PHVISGAHGD GVYYLIEEIL ENFPEPEAEE ADAKHPVFAV
     IGRPNVGKST LVNAILGEKR VIAFDMAGTT RDSIHIDFER EGKPFTIIDT AGVRRRGKVD
     EAVEKFSVIK AMQAVEAANV AVLVLDAQQD IADQDATIAG FALEAGRALV VAVNKWDGIS
     EERREQVKRD ISRKLYFLDF AKFHFISALK ERGIDGLFES IQAAYNAAMI KMPTPKITRV
     LQTAVGRQQP PRAGLVRPKM RYAHQGGMNP PVIVVHGNSL HAISDSYTRY LTQTFRKAFN
     LQGTPLRIQY NVSENPYENA EDKPKKKPLR RVSLSNRIEK REGRKEEKNR FKKKTKVSVK
     KQFSK
 
 
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