ID A0A168QVJ6_ABSGL Unreviewed; 425 AA.
AC A0A168QVJ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN Name=ABSGL_11503.1 scaffold 12295 {ECO:0000313|EMBL:SAM05628.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM05628.1};
RN [1] {ECO:0000313|EMBL:SAM05628.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM05628.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SHO1 family.
CC {ECO:0000256|ARBA:ARBA00009739}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000256|ARBA:ARBA00009083}.
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DR EMBL; LT554468; SAM05628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168QVJ6; -.
DR STRING; 4829.A0A168QVJ6; -.
DR InParanoid; A0A168QVJ6; -.
DR OrthoDB; 1365981at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd11855; SH3_Sho1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR HAMAP; MF_01364_A; Ribosomal_S14_2_A; 1.
DR InterPro; IPR001209; Ribosomal_uS14.
DR InterPro; IPR023676; Ribosomal_uS14_arc.
DR InterPro; IPR018271; Ribosomal_uS14_CS.
DR InterPro; IPR039744; RIbosomal_uS14_euk_arc.
DR InterPro; IPR043140; Ribosomal_uS14_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR12010; 40S RIBOSOMAL PROTEIN S29; 1.
DR PANTHER; PTHR12010:SF2; 40S RIBOSOMAL PROTEIN S29; 1.
DR Pfam; PF00253; Ribosomal_S14; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00527; RIBOSOMAL_S14; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 367..425
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 341..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47263 MW; 613569E0C9061A8D CRC64;
MAHANVWNSR PKTYGKGSRQ CRVCAHQAGL IRKYNLNICR QCFREYANDI GFHKVSLHMV
EGVGQGKGKQ TKWVLTITVN VLDHYNSTVK RNTLSPSYET SKVPFSNNES GIVSSSTLPL
IYIALLTRVS AWVSAKSLNW IQNKLKPITY KVPFVNIKIT HLIMSTLFSS SLILTLSLSH
SLSPDSRTMA GFTTFTLTNP IVLTISILAA IGWFILFVGG CVAAFHGITW WIIIYNLFVV
VLVFVGTGCA KLANYKNMVM ILLTISIVYL TYLIPILLAA EPIGARASAG GAIILIICEF
LWIFLFGSDE ESWVHQTAHR YNDAGPNITT PAVIQRQLNR SSLSGSRKNR NSPLPQFNNE
KNLSDNANLS QATALHNYQA SPDDPNELSF EKNEVLDILD RKGNWWQARK ADGSTGIVPS
NYFNS
//
