ID I1CJM9_RHIO9 Unreviewed; 745 AA.
AC I1CJM9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=signal-recognition-particle GTPase {ECO:0000256|ARBA:ARBA00035672};
DE EC=3.6.5.4 {ECO:0000256|ARBA:ARBA00035672};
DE AltName: Full=Signal recognition particle 54 kDa protein homolog {ECO:0000256|ARBA:ARBA00034905};
GN ORFNames=RO3G_13370 {ECO:0000313|EMBL:EIE88659.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE88659.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE88659.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450}.
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DR EMBL; CH476743; EIE88659.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CJM9; -.
DR STRING; 246409.I1CJM9; -.
DR VEuPathDB; FungiDB:RO3G_13370; -.
DR eggNOG; KOG0780; Eukaryota.
DR InParanoid; I1CJM9; -.
DR OMA; GMTGQDA; -.
DR OrthoDB; 1110531at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd17875; SRP54_G; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135}.
FT DOMAIN 521..534
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 83337 MW; DF745184DDCF9740 CRC64;
MLRRVDQQTK RTNENEVETK ESLITNKTSK KGLGVSDKSL NTPPLLRSDS GLKLFKNTNA
QEKKLQVFND KPSNTTIPTK RTNAEVDIEA DYEPEGLDLD FTVFDDHLDE SAYESIQDPY
EEEFSTQRLF KQIQAASQTV THPTETTEPS FPDTVEYGPP REQEQPFVPE DPDTIVDMSV
FTDFADLDGY ELIHLFHEEE EDDFLHLSYS EDLNQLPLLL IDEDALEFSN ESLLLSENEL
ELDETQVDDF HIMVLADLGR KINSALSDLT KAPVIDEKVL DSLVKQICAA LLASDVNVML
VQKLRTNIKK SVNLEELANS ANKKRLIEKA VMDELSRLVD PEVEPYKPVK RRTNIFMMVG
LQGAGKTTTC TKIASFYQRK GWKVALVCAD TFRAGAFDQL KQNATKAKIP YYGSYTETDP
VTIAVEGVEK FRAEKFEIII VDTSGRHKQE TELFEEMKQI SSSVKPDTTI FVMDGTIGQA
AESQAKAFKE AAGFGSIIIT KMDGHAKGGG AISAVAATHS PIIFLGVGEH LQDMDRFEPK
SFIRKVLGVQ DMRDVIEHVQ DSINLNDNKK LIKNIEKAIP GMPAEMLAGA EQEGGKRMKR
MMCIMDSMTD EGNKDVDNPL KLNPLTIELD GDDKPFKEMK RVIRVARGSG TTVCEVQEII
FQYTKFAEMV KSIGGKNGLM QNMQNMNNMD PRRMNNIAEM AKSFGMNPNQ KDLMNAAKQM
GNMFGGRGGG GGMPNMAELM KAMKF
//
