ID T0LM42_COLGC Unreviewed; 751 AA.
AC T0LM42;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Actin {ECO:0000313|EMBL:EQB52766.1};
GN ORFNames=CGLO_07593 {ECO:0000313|EMBL:EQB52766.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52766.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|RuleBase:RU000487}.
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:EQB52766.1}.
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DR EMBL; AMYD01001518; EQB52766.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LM42; -.
DR STRING; 1237896.T0LM42; -.
DR eggNOG; KOG0681; Eukaryota.
DR HOGENOM; CLU_008246_1_0_1; -.
DR OMA; CYVSQDY; -.
DR OrthoDB; 196861at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.420.40; -; 4.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF16; ACTIN-RELATED PROTEIN 5; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..358
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 498..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 85237 MW; CE5065ECC43CAF69 CRC64;
MAPSATEALP PLKGPPERTY PPAKIFPVKE AKFEKPIAVQ HDGREKAAAH PGAAIVIDNG
SSAVRAGWSF EEKPRLNIPP IMSKYRDRKA GKTYSFAGSD CYADTTARSH IRYAFEQGTG
IVSNWDVMEH LLDYIFLKLG LNGDDASIDV PIVMTEAVAN LPYSRKSMTE IVFECYGAPS
VAYGIDSLFS YRHNKGNTGI VVSSSYTSTH VIPVYNHKAM LSQATRLNWG GWHAAEYLLK
LIRLKYPAFT GKLNVSQAEH MLRDHAYVSE DFDNELRGYL DWTGLEDRDI VIQYPFTEEV
VVQKTEEELA RIAERKKESG RRLQQQAAKM RLEKLMRKEN ELEHYKKLQA KLEQQTNKKE
VRRLLDSNDL KDEAALEKAI AVLDKAVKKA RTKDVGGDAE EDQQEPVFDL LDVPDEELDD
AGLKAKRQQK LMKSNHDARA RAKAEKEAEK ARIEEEKRLD QERRENDLEG WLEEKRQRRD
LTLQKMKERE RLKQDLGNRK SLASQIRMKS IANLASDNPT KKRRRGGDDD NFGANDDDWG
VYRQIVVGDN SDDEQEEEDL NANLKIYEEE LLRYDPDFTY EDTHEAQTDW SKSMLHAFAR
GPRPFDAGSQ AELNQIHLNV ERIRVPEVVF QPSIAGVDQS GLVEIIGDIL NQRLGAVPNR
DDFLKDIFLT GGNTMFQGFD ERLRSGLTPL LPADSPLHIR RAQDALLDAW KGAAGWAGSA
AWKAATITRE EYQEKGSEYI KEHDLGNTSY V
//
