ID M3CH44_SPHMS Unreviewed; 449 AA.
AC M3CH44;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540};
GN ORFNames=SEPMUDRAFT_148511 {ECO:0000313|EMBL:EMF13133.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF13133.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF13133.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF13133.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid. {ECO:0000256|RuleBase:RU003540}.
CC -!- SIMILARITY: Belongs to the annexin family.
CC {ECO:0000256|RuleBase:RU003540}.
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DR EMBL; KB456263; EMF13133.1; -; Genomic_DNA.
DR RefSeq; XP_016761254.1; XM_016904968.1.
DR AlphaFoldDB; M3CH44; -.
DR STRING; 692275.M3CH44; -.
DR GeneID; 27902105; -.
DR eggNOG; KOG0819; Eukaryota.
DR HOGENOM; CLU_025300_4_0_1; -.
DR OMA; VRGPLMQ; -.
DR OrthoDB; 1500773at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.10.220.10; Annexin; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR009117; ANX14.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10502; ANNEXIN; 1.
DR PANTHER; PTHR10502:SF102; ANNEXIN A7; 1.
DR Pfam; PF00191; Annexin; 4.
DR Pfam; PF00397; WW; 1.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01813; ANNEXINFUNGI.
DR SMART; SM00335; ANX; 4.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF47874; Annexin; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Annexin {ECO:0000256|ARBA:ARBA00023216, ECO:0000256|RuleBase:RU003540};
KW Calcium {ECO:0000256|RuleBase:RU003540};
KW Calcium/phospholipid-binding {ECO:0000256|RuleBase:RU003540};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU003540}.
FT DOMAIN 56..89
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 49087 MW; FD2080F548366458 CRC64;
MAHYQQSYGA PGGPQPYQQY PPGGGYYQQP MNHGFGQQQG FGGAPPGPPP PQGGGPPLPP
GWTSQFDPSS QRPYYISPTG ASQWDPPAPG FGGPPPGPPP PAQGGFGQSP YPQQQPGGFP
QQQQYGGPAA LPSPGYDLRQ RSHQDVTRAA DDLRASMKGF GTNETLLIKV MASLGPLEIA
AVKQVYQQRH KRDLLKDVHS ETSGYFREGL EAMIRGPLEQ DCWVIHESIK GLGTKESALN
DVLLARSNAD MNAIKQHYQH MYRKSLESDV KGDLSMKTER MFDMVMSARR AEESAPVIPQ
QTEQDIKDMY SATEGKTGTD QMTVCSILTS RSNGQIRAIV QAYQAKYHRS LQSVIKAEFS
GHMQDALLFI IGAAADPAKN DADLLEASMA GLGTKDQALV RRVVMIHWDK QRLHQCKAAY
KHFYKKDLAA RIASETSGDY KKLMVACVA
//
