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Database: UniProt
Entry: A0A162JJI4_9HYPO
LinkDB: A0A162JJI4_9HYPO
Original site: A0A162JJI4_9HYPO 
ID   A0A162JJI4_9HYPO        Unreviewed;       519 AA.
AC   A0A162JJI4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein SSH4 {ECO:0000256|ARBA:ARBA00017626};
DE   AltName: Full=Protein ssh4 {ECO:0000256|ARBA:ARBA00016528};
GN   ORFNames=BBO_03746 {ECO:0000313|EMBL:OAA45168.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA45168.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA45168.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA45168.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- FUNCTION: Components of the endosome-vacuole trafficking pathway that
CC       regulates nutrient transport. May be involved in processes which
CC       determine whether plasma membrane proteins are degraded or routed to
CC       the plasma membrane. {ECO:0000256|ARBA:ARBA00025244}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004639}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004639}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004576}.
CC   -!- SIMILARITY: Belongs to the SSH4 family.
CC       {ECO:0000256|ARBA:ARBA00006990}.
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:OAA45168.1}.
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DR   EMBL; AZHA01000009; OAA45168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162JJI4; -.
DR   OrthoDB; 5479594at2759; -.
DR   Proteomes; UP000076863; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd12910; SPRY_SSH4_like; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035780; SPRY_Ssh4-like.
DR   PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR   PANTHER; PTHR12864:SF54; SPRY DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..274
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          295..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  56371 MW;  25A71D89E3DA85EC CRC64;
     MSDPSSALTG VVIGLVSSFG SILLIGLVVF VFWASGCAGS GRILLDRLGR PGEYDDEQAF
     LREEEEALET MDEMARTDYL RAKAFVNANP PESLQTDISL SQYLAIQEKG VSAWEFEPEL
     EIANCFVEAR TEIEFYDSEC TVMCNLPVPK QNDVYYWEAK IYEKPESTLL GIGMATKPYP
     LFRLPGYHKY SVAYHSNGSR HYNQPFSEIP YGPRLVQGDV VGVGYRPRTG AIFFTRNGKK
     LEEVVHGLKS QNFFPAVGAN GPATVHVNLG QSGFVFIEAN VKKWGLAPVT GSLAPPPPYG
     SEQGSILLES GTKDGYAPPQ ERRHGHSFSG STYSVRGGQQ PANASHGRTR SGNFRILPTS
     PGPLRSPTDI SLAQLVRTDD GGETSSSAHQ QREEEHNENP LHLHLLDATN PPPDYTSPTG
     SDGDSSSRRQ STDSDDTPLI QVMNRSRGNS AAVPGTTVNN LPLPSYSDAV EQGAGQRRRS
     SFDSERSTSE AAEDDDSESS SDDSTNTVTP LSHNPTSAV
//
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