SRP19_PYRFU
ID SRP19_PYRFU Reviewed; 100 AA.
AC Q8TZT9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Signal recognition particle 19 kDa protein {ECO:0000255|HAMAP-Rule:MF_00305};
DE Short=SRP19 {ECO:0000255|HAMAP-Rule:MF_00305};
GN Name=srp19 {ECO:0000255|HAMAP-Rule:MF_00305}; OrderedLocusNames=PF1894;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Binds directly to 7S RNA and
CC mediates binding of the 54 kDa subunit of the SRP. {ECO:0000255|HAMAP-
CC Rule:MF_00305}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. Archaeal SRP consists of a
CC 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and
CC SRP19. {ECO:0000255|HAMAP-Rule:MF_00305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00305}.
CC -!- SIMILARITY: Belongs to the SRP19 family. {ECO:0000255|HAMAP-
CC Rule:MF_00305}.
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DR EMBL; AE009950; AAL82018.1; -; Genomic_DNA.
DR RefSeq; WP_011013033.1; NZ_CP023154.1.
DR PDB; 3DLU; X-ray; 1.80 A; A/B/C/D=1-100.
DR PDB; 3DLV; X-ray; 1.87 A; A/B=1-100.
DR PDBsum; 3DLU; -.
DR PDBsum; 3DLV; -.
DR AlphaFoldDB; Q8TZT9; -.
DR SMR; Q8TZT9; -.
DR STRING; 186497.PF1894; -.
DR TCDB; 3.A.5.7.2; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAL82018; AAL82018; PF1894.
DR GeneID; 41713714; -.
DR KEGG; pfu:PF1894; -.
DR PATRIC; fig|186497.12.peg.1965; -.
DR eggNOG; arCOG01217; Archaea.
DR HOGENOM; CLU_169299_1_0_2; -.
DR OMA; FVVWPSE; -.
DR OrthoDB; 121943at2157; -.
DR PhylomeDB; Q8TZT9; -.
DR EvolutionaryTrace; Q8TZT9; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 3.30.56.30; -; 1.
DR HAMAP; MF_00305; SRP19; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR InterPro; IPR036521; SRP19-like_sf.
DR InterPro; IPR022938; SRP19_arc-type.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Signal recognition particle.
FT CHAIN 1..100
FT /note="Signal recognition particle 19 kDa protein"
FT /id="PRO_0000135223"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3DLU"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:3DLU"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3DLU"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3DLU"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3DLU"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3DLU"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3DLU"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:3DLU"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:3DLU"
SQ SEQUENCE 100 AA; 11645 MW; 648EF600402C9CD6 CRC64;
MGRFVVWPSE LDSRLSRKYG RIVPRSIAVE SPRVEEIVRA AEELKFKVIR VEEDKLNPRL
SGIDEELRTF GMIVLESPYG KSKSLKLIAQ KIREFRRRSA
