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Database: UniProt
Entry: N1QM93_SPHMS
LinkDB: N1QM93_SPHMS
Original site: N1QM93_SPHMS 
ID   N1QM93_SPHMS            Unreviewed;       696 AA.
AC   N1QM93;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:EMF17013.1};
GN   ORFNames=SEPMUDRAFT_56981 {ECO:0000313|EMBL:EMF17013.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17013.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF17013.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF17013.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR   EMBL; KB456260; EMF17013.1; -; Genomic_DNA.
DR   RefSeq; XP_016765134.1; XM_016909421.1.
DR   AlphaFoldDB; N1QM93; -.
DR   STRING; 692275.N1QM93; -.
DR   GeneID; 27906558; -.
DR   eggNOG; KOG0781; Eukaryota.
DR   HOGENOM; CLU_009301_8_1_1; -.
DR   OMA; HLGWIDK; -.
DR   OrthoDB; 5475029at2759; -.
DR   Proteomes; UP000016931; 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   Hydrolase {ECO:0000313|EMBL:EMF17013.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          669..682
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          149..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  74870 MW;  F7F346F6A372F811 CRC64;
     MLDAFEIVTS SGIVLWRKHY APLSPHVINS LINDVFIEDR HVHTASTTAA AAAAASNPAS
     SLASSADTYR KDKYTLKYAT AKDVGLIFVA VYQSLLHLSW VDNLLTTAKA LFTRRYAADL
     KPQPQHQQHV ASIDTRDFDQ TFDALLGKLD TGSTRRAPSE VDSESQAELT PPSSTASQAD
     DQDGAPAPPV PLFKKPALAP PRDVAGDTTS PDDTPVATPD ASRPGTPLHA SSHLLAPKAG
     PGGLSRKQRK KANQFGTSAL PSSGDESDRR PKSSQGKTKA KRRWDASGVA QDDNDEVLDY
     SAAATPSTEQ DALDVEDVNA TRMGNRTVKG QFVLKDLDDE VEAILAESKR NADFTSTDKD
     VSGLIGTATS KLSGLFRNVV GGRALTKQDL EQPMQAMRNS LIEKNVAPEA AGRLCSSVET
     DLLNSKTASF TSIDKTIRES MGRALTKILT PTSSLDLLRN INNTIEGQNP RPYVISIVGV
     NGVGKSTNLS KIAYFLLQNK FRVLVVACDT FRSGAVEQLR VHVRNLTELS RREANAGTVE
     LFEKGYGKDA ADVAKQAVAF ASNAGGGNML YDVVLIDTAG RRHNDQRLMS SLTKFGQLAN
     PDKIFMVGEA LVGTDSVSQA RHFAEQFVDR KGQMRSNGKG MDGFIISKCD TVGDMVGTLV
     SMVHATGIPV VFLGVGQHYG DLRGLNVDWA VNKLMK
//
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