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Database: UniProt
Entry: K2RTI1_MACPH
LinkDB: K2RTI1_MACPH
Original site: K2RTI1_MACPH 
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}.
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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
//
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