ID A0A093VD95_TALMA Unreviewed; 712 AA.
AC A0A093VD95;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=High osmolarity signaling protein SHO1 {ECO:0000256|ARBA:ARBA00017350};
DE AltName: Full=High osmolarity signaling protein sho1 {ECO:0000256|ARBA:ARBA00016255};
DE AltName: Full=Osmosensor SHO1 {ECO:0000256|ARBA:ARBA00029697, ECO:0000256|ARBA:ARBA00030785};
GN ORFNames=GQ26_0071890 {ECO:0000313|EMBL:KFX50482.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX50482.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX50482.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX50482.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX50482.1}.
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DR EMBL; JPOX01000007; KFX50482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VD95; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR CDD; cd20824; C1_SpBZZ1-like; 1.
DR CDD; cd11912; SH3_Bzz1_1; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035459; Bzz1_SH3_1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..177
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 382..432
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 554..614
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 654..712
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 432..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 433..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 78782 MW; 1FF621990EF49F27 CRC64;
MAEVNVNPQF GAELKVSNGI AWLDDIQQFY RERSAIEREY ASKLSALCKK YSDRKAKKIS
SLSVGDTPTM TPGSLESASL TTWSTQLNTV ESHAAVRDKF GLDLISQVAD PLKNIATRYE
ELRKSHVEYH ARLEKERESQ LSELKKVKGK YDGVCQEVEN RRKKTESSFD YNKTKAQAAY
HQQLLEMGNS KFYHEYVPEV LDSLGDLNET RVQKLNAFWS LAAQLEKGAS TQSTELMTRL
GNEIPRNNPK LDSLMFLQHN TSQSQEPPNL AFEPSPVWHD DDQMITDEPA KVFLRNMLMK
SKSQVKELKA EAEKQQREVE GAKRVRDNIR QGKDKRDEVD IVKAIFNLQE KLHEIERKKM
TAEVETLTIL AVVGDLSLGA KNHNFRSQTF KIPTNCDLCG ERIWGLSAKG FDCVDCGYTC
HSKCQMKVPA ECPGEQTKEE KKKLKAERQE QAQSTPVVSE SAPSHGNNGT MTEMPALTRK
DTMNSLSSGY AHSAHRSVSG SISSSKPSGE EPAELSAAPP RNSTSTTKRN RILAPPPTQY
VSSPTAAEAP VSKKNEQRGK MVYAYQATGD GEVTVNEGQN IVVLEPDDGS GWMRVKAGSQ
EGLVPSAYAE LAPAPSPALT ERPASAYSNS SVSLAGSTTA KKVGPTVAPR RGAKKLQYVE
ALYDYEARSD AEHSMSEGDR FVLITKDSGD GWAEVEKGGQ VKSVPANYIQ EV
//
