ID K2RTI1_MACPH Unreviewed; 641 AA.
AC K2RTI1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE SubName: Full=Actinin-type actin-binding conserved site {ECO:0000313|EMBL:EKG16002.1};
GN ORFNames=MPH_06824 {ECO:0000313|EMBL:EKG16002.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG16002.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG16002.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG16002.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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:EKG16002.1}.
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; AHHD01000287; EKG16002.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RTI1; -.
DR STRING; 1126212.K2RTI1; -.
DR VEuPathDB; FungiDB:MPH_06824; -.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_005217_0_2_1; -.
DR InParanoid; K2RTI1; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd21215; CH_SpAIN1-like_rpt1; 1.
DR CDD; cd21291; CH_SpAIN1-like_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.20.58.60; -; 2.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 2.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 10..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 124..230
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 484..519
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 641 AA; 73309 MW; 8BE988368A0A02A8 CRC64;
MAPLEQQWVI VQQKTFTKWL NSKISVRGLV IKDLCTDLSD GTLLIHLLEI LSQESLGKYA
SKPKLRVQKF ENVNKALDFI KGRSIQLVNM GAEDVVDGNR KIILGLIWTL ILRFTISDIS
DQGLSAKEGL LLWCQRKTAC YDDVEVRDFS SSWNDGLAFC ALLDIHRPDL IDYDALDKSD
HHGNMKLAFE IASNEIGIPD LLDVEDVCDV AKPDERSLMT YIAYWFHAFS QMEKVENAGR
RVEKFVQSMQ GAWEMQNSFE RRMRELLRQI AEQKKEWEEA VFDGTYADAK NQAGLFTSYR
RTKKREWVAE KSDLVSLLGN IKTKLSTYRL RPYTPPPELS LEALDQAWAG LMTAERARSS
VINETIRDIK NALRRSFADK ANDLALALNT LSVSLSGLEG DVEDQRQHTQ KLSENLQPLD
QFLEIIAGID KQCQEANIEE NDFTTYTYDE LDYELSLVKA SVAKKLAFLE NQMVARNMTN
LTPIQLEEFE SVFRHFDRDM SNSLTELEFS AALASLGLVY DEEEMHERFM ETSEGSNYVS
FEQFIRFMVS ETEDQNNAEQ VFESFREVAD GKPYVTELDL RHSLVPDEII EDLIRQMPEH
KGPDLQEDRE LPKYDYVTYM EKFIGGGGGS HGAERANGDA S
//