ID A0A150UW35_9PEZI Unreviewed; 673 AA.
AC A0A150UW35;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
GN ORFNames=M433DRAFT_7095 {ECO:0000313|EMBL:KYG42504.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42504.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG42504.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG42504.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG42504.1}.
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DR EMBL; JPDO01000444; KYG42504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UW35; -.
DR STRING; 766039.A0A150UW35; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
DR CDD; cd21294; CH_FIMB_rpt1; 1.
DR CDD; cd21297; CH_FIMB_rpt2; 1.
DR CDD; cd21300; CH_FIMB_rpt3; 1.
DR CDD; cd21303; CH_FIMB_rpt4; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961:SF18; FI19014P1; 1.
DR PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 4.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 145..266
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 294..399
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 420..546
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 561..669
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 84..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 74927 MW; 44560D842BAE0844 CRC64;
MNVLKLQKKY PQFQQSDIFG LTDAFRKLDV DDKGYIDEAT AIKSAQNSER QPYDVVRQAL
KEVELDSSRR VELDDYVDLI ARLRQSSPAQ QRMSTGPQRP RGTSNAQDST PTKPSHMSRG
SIGGGSGGRI TVSGATGGTQ HTINEDERTA FTSHINAVLA GDPDIGHLLP FPLDTFEMFD
ACKDGLVLAK LINDSVPDTI DERVLNRPGK KIKSLNAFHM TENNNIVIES SKGIGCSVVN
IGSGDIIEVR EHLILGLIWQ IIRRGLLGKI DIKLHPELYR LLEDGETLEQ FLRLPPEQIL
LRWFNYHLKN AKWHRRVQNF SNDVKDGENY TVLLNQLAPN VCSRSPLQTT DLLQRAEQVL
QNSDKLDPPC RKFLTPTSLV AGNPKLNLAF VANLFNNHPG LDPITEEEKQ EIEDFDAEGE
REARVFTLWL NSLDVKPAVV SFFDDLKDGT ILLQAYDKVI PGSVNWRHVN KPPANAAQPA
SQDPDEAYLT IKSGMSRFKA VENTNYAVEL GKQNRFSLVG IQGADITDGQ RTLTLGMVWQ
LMRRDITNTL TALAQRMGKR EISDTDMVQW ANSMASKGGN KSQIRSFKDA SLATAIPLLD
VLSGMKSSYV DYDLVAQGRT DDEKYQNAKL AISIARKMGA TIWLVPEDIT SLRSRLIVTF
IGSLMATAEK LGV
//