ID A0A165ZZ27_9AGAM Unreviewed; 646 AA.
AC A0A165ZZ27;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 24.
DE SubName: Full=Fimbrin {ECO:0000313|EMBL:KZT34785.1};
GN ORFNames=SISSUDRAFT_1052301 {ECO:0000313|EMBL:KZT34785.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT34785.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT34785.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT34785.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV428165; KZT34785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZZ27; -.
DR STRING; 1314776.A0A165ZZ27; -.
DR Proteomes; UP000076798; 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; cd21300; CH_FIMB_rpt3; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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:UP000076798};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 113..233
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 261..364
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 388..521
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 534..646
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 441..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 72077 MW; D137C4FE65F9946B CRC64;
MQAIKLQRKY PQVTQEEMYD LINRFNSIDT NTPGRVDKAA VISALQSQGQ AYDQVRETLK
HVSVDASGKV ELEDWVELNA KLKSQKAASV LPTKAGKVTV AGSNANVSHT INEEERREFT
SHINGVLEGD PDVGSRLPVP TDTMQLFDEC RDGLILCKLI NDSVPDTIDP RVLNKPTLRK
PLNAFQITEN NNIVITSAKA IGCSVVNIGS SDISEGREHL ILGLIWQIIR RGLLSRVDIK
LHPELYRLCE EDETIDDLLR LTPDQILLRW FNYHLKQANW KRRVNNFSKD VSDGENYTVL
LNQLKPAECS LGPLQTQDLK TRAEQVLQNA DAIGCRKYLT PPSLLSGNPR LNLAFVANLF
NTWPGLAPLD EQEAKDYGVV DDFDAEGERE ARVFTLWLNS LEVEPGVHNL FENLKDGLVI
LQVFDKVIPG SVVWRRVSKP KATSPTQPSF STEAGEEEEE TGITPNQPKL SRFKCVENTN
YAIDLARQNK LHLVGIQGAD IVDGSKTLVL GLVWQLMRLN ITQTLTKLSG SGRPITDQEI
LKWANTTAQK SQFSGRAVRS FKDPSLTTGL FFLDILDAIR PGIVDPALVL NVNESSSYDD
RRSNAKLAIS IARKMNALIF LVPEDIVDIR PRLILTFVAS LMSIQT
//
