ID A0A0F4Z235_TALEM Unreviewed; 668 AA.
AC A0A0F4Z235;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=SRP54-type proteins GTP-binding domain-containing protein {ECO:0000259|PROSITE:PS00300};
GN ORFNames=T310_1391 {ECO:0000313|EMBL:KKA24579.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA24579.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA24579.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA24579.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC {ECO:0000256|ARBA:ARBA00008531}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA24579.1}.
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DR EMBL; LASV01000058; KKA24579.1; -; Genomic_DNA.
DR RefSeq; XP_013331191.1; XM_013475737.1.
DR AlphaFoldDB; A0A0F4Z235; -.
DR STRING; 1408163.A0A0F4Z235; -.
DR GeneID; 25313742; -.
DR OrthoDB; 5475029at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005785; C:signal recognition particle receptor complex; 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:0005047; F:signal recognition particle binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd14826; SR_alpha_SRX; 1.
DR CDD; cd17876; SRalpha_C; 1.
DR Gene3D; 3.30.450.60; -; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007222; Sig_recog_particle_rcpt_asu_N.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF04086; SRP-alpha_N; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 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; SSF64356; SNARE-like; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 641..654
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 132..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72258 MW; 43EA9FBCF80DE9D4 CRC64;
MLDAFEIITT SGVVLWSKSY APVGAHVVNS LINDVFIEEK VRPQDATADG VSPVYRKDKY
TLKWRRVKEF GLIFVAVYQS LLHLSWIDKL LDNIATIFVD LYKDQLKSSR SRVVEYPFDK
YFDQQVRELE DTAGGAVEET PGILEEERKN PLVSSDNGGP PPPPVPSLPK GKLRLCPASR
ILLTTEKAQH AAAQPVAISN ESSPSPTPDT SRSSTPLPNH ILPAKSGPGG RVSRRARKAA
HANANANVSS GDESARKGKS AKAGGKQMRK WDADGLVDEG DDENLDYSAR AGDEAPAPAV
EDVARDSWGR KTANGQFVLK DLGDEVHSIL ENADAEKAKA NASSGVVGSS FNAIGGLFRN
IVGGKTLTEA DLEKPLKAME DHLMKKNVAR EAAVRLCEGV KQELIGKKTG NFQSVDAALR
AAMEASLRKI LTPTSSLDLL HQIQAVTAPT NKQQAPRPYV ISIVGVNGVG KSTNLSKICF
FLLQNNYRVL IAACDTFRSG AVEQLRVHVR NLKELSAREN VGAVELYEKG YGKDAANVAK
DAVAYATANR FDVVLIDTAG RRHNDQRLMS SLEKFAKLAN PDKIFMVGEA LVGTDSVMQA
RNFNQAFGPG RHLDGFIISK CDTVGDMVGT LVSMVHATGI PIVFLGVGQH YGDLRGLSVP
WAVGLLMK
//
