ID A0A317X4V5_9EURO Unreviewed; 644 AA.
AC A0A317X4V5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 03-MAY-2023, entry version 11.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
GN ORFNames=BO94DRAFT_533106 {ECO:0000313|EMBL:PWY93365.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY93365.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY93365.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY93365.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY93365.1}.
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DR EMBL; MSFK01000007; PWY93365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317X4V5; -.
DR STRING; 1450535.A0A317X4V5; -.
DR OrthoDB; 5475188at2759; -.
DR Proteomes; UP000246702; 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:UP000246702};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 135..256
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 284..387
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 408..518
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 533..641
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
SQ SEQUENCE 644 AA; 72361 MW; 8B07E3D479CE1B90 CRC64;
MNVIKLQRRF PQFEQSEIFS LQDAFRKLDI DDKGSLDEAT VIKATQQSER KPYDVVRQAL
KEVELDSSRR VELEDYVDLI SKLRFARTQN HAASTPAAVL PGNGAGPSRH VSKGSIGGRI
HVQGSSANVT HTINEDERTE FTRHINAVLA GDPDIGHFLP FPTDTFEMFD KCKDGLVLAK
LINDSVPDTI DERVLNKAGK KIKELNAFHM TENNNIVINS AKGIGCSVVN IGSGDIIEVR
EHLILGLIWQ IIRRGLLGKI DIKLHPELYR LLEDDETLEQ FLRLPPEQIL LRWFNYHLKN
AKWDRRVSNF SSDVKDGENY TVLLNQLVPE TCSRKPLQTQ DVVQRAEEVL TNADKLGCRK
FLTPSSLVAG NPKLNLAFVA NLFNTIPGLD PITDEEKLEV EDFDAEGERE ARVFTLWLNS
LDVQPAVNSL FDDLRDGTIL LQAYDKVIPG SVNWRHVNKQ PASGGEMMRF RAVENTNYAT
ELGKHIGFSL VGVQGADITD GQRTLTLGLV WQLMRRDITN TLSSLAKRMG KREITDSEMI
KWANEMSHRG GRSSSIRNFK DQSIASGLFL LDVLNGMKSS YVDYDLVTPG RNDEEAYANA
KLSISIARKL GATIWLVPED ICQVRSRLVT TFIGSLMATY EKMQ
//
