DJ27A_XENLA
ID DJ27A_XENLA Reviewed; 273 AA.
AC Q7ZYF1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=DnaJ homolog subfamily C member 27-A;
DE AltName: Full=Rab and DnaJ domain-containing protein 1;
DE AltName: Full=Rab and DnaJ domain-containing protein A;
GN Name=dnajc27-a; Synonyms=rbj-a, rbj1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RX PubMed=14980719; DOI=10.1016/j.gene.2003.11.010;
RA Nepomuceno-Silva J.L., de Melo L.D., Mendonca S.M., Paixao J.C.,
RA Lopes U.G.;
RT "RJLs: a new family of Ras-related GTP-binding proteins.";
RL Gene 327:221-232(2004).
CC -!- FUNCTION: GTPase possibly involved in regulation of the MEK/ERK
CC pathway. {ECO:0000250|UniProtKB:Q8CFP6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8CFP6}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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; BC043812; AAH43812.1; -; mRNA.
DR EMBL; BK001288; DAA01327.1; -; mRNA.
DR RefSeq; NP_001080762.1; NM_001087293.1.
DR PDB; 6JMG; X-ray; 2.70 A; A/B=1-273.
DR PDBsum; 6JMG; -.
DR AlphaFoldDB; Q7ZYF1; -.
DR SMR; Q7ZYF1; -.
DR DNASU; 380455; -.
DR GeneID; 380455; -.
DR KEGG; xla:380455; -.
DR CTD; 380455; -.
DR Xenbase; XB-GENE-6253616; dnajc27.L.
DR OrthoDB; 1288652at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 380455; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..273
FT /note="DnaJ homolog subfamily C member 27-A"
FT /id="PRO_0000332981"
FT DOMAIN 217..273
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6JMG"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:6JMG"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6JMG"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:6JMG"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6JMG"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6JMG"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6JMG"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6JMG"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:6JMG"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:6JMG"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6JMG"
FT HELIX 254..273
FT /evidence="ECO:0007829|PDB:6JMG"
SQ SEQUENCE 273 AA; 30878 MW; D4115A003E329424 CRC64;
METNLQKRKD SRKALRIKVI SMGNAEVGKS CIIKRYCEKR FVPKYQATIG IDYGVTKVHI
KDREIKVNIF DMAGHPFFYE VRNEFYKDTQ GVILVYDVGH KETFESLDGW LAEMKQELGP
QGNIDNIVFA VCANKIDSTK HRSVDESEGR LWSESKGFLY FETSAQSGEG INEMFQAFYS
AIVDLCDNGG KRPVSAINIG FTKEQADSIR RIRNCKDSWD MLGVKPGATR DEVNKAYRKL
AVLLHPDKCM APGSEDAFKA VVNARTALLK NIK