ID   SRP72_SCHMA             Reviewed;         707 AA.
AC   P49965;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Signal recognition particle subunit SRP72;
DE            Short=SRP72;
DE   AltName: Full=Signal recognition particle 72 kDa protein;
GN   Name=SRP72;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7731929; DOI=10.1007/bf00931628;
RA   McNair A., Zemzoumi K., Lutcke H., Guillerm C., Boitelle A., Capron A.,
RA   Dissous C.;
RT   "Cloning of a signal-recognition-particle subunit of Schistosoma mansoni.";
RL   Parasitol. Res. 81:175-177(1995).
CC   -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC       ribonucleoprotein complex that mediates the cotranslational targeting
CC       of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC       (By similarity). The SRP complex interacts with the signal sequence in
CC       nascent secretory and membrane proteins and directs them to the
CC       membrane of the ER (By similarity). The SRP complex targets the
CC       ribosome-nascent chain complex to the SRP receptor (SR), which is
CC       anchored in the ER, where SR compaction and GTPase rearrangement drive
CC       cotranslational protein translocation into the ER (By similarity).
CC       Binds the signal recognition particle RNA (7SL RNA) in presence of
CC       SRP68 (By similarity). Can bind 7SL RNA with low affinity (By
CC       similarity). The SRP complex possibly participates in the elongation
CC       arrest function (By similarity). {ECO:0000250|UniProtKB:O76094,
CC       ECO:0000250|UniProtKB:P38688}.
CC   -!- SUBUNIT: Component of a signal recognition particle (SRP) complex that
CC       consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC       subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9.
CC       {ECO:0000250|UniProtKB:P38688}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76094}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:O76094}.
CC   -!- SIMILARITY: Belongs to the SRP72 family. {ECO:0000305}.
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DR   EMBL; L32975; AAA69689.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49965; -.
DR   SMR; P49965; -.
DR   STRING; 6183.Smp_207010.1; -.
DR   eggNOG; KOG2376; Eukaryota.
DR   HOGENOM; CLU_061313_0_0_1; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR   InterPro; IPR026270; SRP72.
DR   InterPro; IPR031545; SRP_TPR-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14094; PTHR14094; 1.
DR   Pfam; PF08492; SRP72; 1.
DR   Pfam; PF17004; SRP_TPR_like; 1.
DR   PIRSF; PIRSF038922; SRP72; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Endoplasmic reticulum; Reference proteome; Ribonucleoprotein;
KW   Signal recognition particle.
FT   CHAIN           1..707
FT                   /note="Signal recognition particle subunit SRP72"
FT                   /id="PRO_0000135236"
FT   REGION          564..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  79508 MW;  1ED1C8956397CE18 CRC64;
     MANEKAFNLQ SAYSDLNKAC SAQAYDKIIN ISGKILTKFP GETKAFQCKV VALIRAEKYE
     DCLSFLKKNP TLSSHVIFEK AYVEYRLNRL TEAAKTLESE EASDSKVQEL KAQVLYRKGD
     FAGAYAYLRT VIRNSQDDYS EERLANLTAV AAAESCFNNA NLDLDVNPQM YEGKFNLACY
     HLGRGDCYLA SRSLDDAENT CNLCLSEDPE LTEEERNEEL APIRVQRAYI LQLNKEEEEA
     NQVYQSVIRQ RASDPALLAV AANNIVCINQ DQNIFDSRKR IKMASTDGLQ FKLFSRQRTD
     MLINQALFYW YTNQMEACTA KLRTVSQEEL SPRALLLSAT QLIKEKNVDK AVLLLQSYLS
     NFAGSQIDAE IPLALAQLNL RRTSANNLGT GSPQPKNALN VAQMLENILP QHLIHSPGVL
     STRIALYLLA SSGENAVQTR PDSMKQIVNC IESTLHYYEE LGEQNEIYSH LLDNCAAFLL
     QQGEAKLAAE LLEKQLARLE SNICQEKQNS LIKQVLVARL VRAYAQFDRP KAEQTCKSLQ
     AKESLSEADV DTLETTFLYG AKSLKRLGKP SEPTDTSDKG KSKRSQIKKS ISDIPSSEDP
     GAQPVISRPK RKKRKVRLPK NYQPGVMPDP NRWLPRRERT HYRGKRRDKR FAPTRGPQGQ
     ITGESEWDAA IRSPKVKIPE DGSAGSTPKQ MSNTAKQQQK KGRKKGR