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Database: UniProt
Entry: F4S9M6_MELLP
LinkDB: F4S9M6_MELLP
Original site: F4S9M6_MELLP 
ID   F4S9M6_MELLP            Unreviewed;       625 AA.
AC   F4S9M6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Actin binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MELLADRAFT_95521 {ECO:0000313|EMBL:EGF98674.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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DR   EMBL; GL883171; EGF98674.1; -; Genomic_DNA.
DR   RefSeq; XP_007418074.1; XM_007418012.1.
DR   AlphaFoldDB; F4S9M6; -.
DR   STRING; 747676.F4S9M6; -.
DR   EnsemblFungi; EGF98674; EGF98674; MELLADRAFT_95521.
DR   GeneID; 18937267; -.
DR   KEGG; mlr:MELLADRAFT_95521; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_95521; -.
DR   eggNOG; KOG3655; Eukaryota.
DR   HOGENOM; CLU_013085_2_0_1; -.
DR   InParanoid; F4S9M6; -.
DR   OrthoDB; 101008at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd11281; ADF_drebrin_like; 1.
DR   CDD; cd11819; SH3_Cortactin_like; 2.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR   PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00102; ADF; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS51263; ADF_H; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          3..132
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000259|PROSITE:PS51263"
FT   DOMAIN          455..516
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          566..625
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          212..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..252
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..416
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..562
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  66751 MW;  B67904A2486CFF71 CRC64;
     MAQVRISDPA ISQAYQSIIA SDPGIDYVLL SYVGQTNDLK VQEKGTGGLE ELEESWNDGR
     MQYAFVRVTD PGSKLTKFVF IAWCGDGVQE SRKGLFHSHT STVGQFLKGY HVQINARSEA
     DVDPQHILKK VIDSSGAKYS IHNEKPMKRE LPAPVGTNYQ PIGRPDIAAM TSKQKPTPPA
     PVGTSYTPMK NELAEIRAAR TAPSAASILS RAPVSRAMDD DGFEPTVKAT TISPSPPPPV
     LSSRPTPKAP TAPTPSNTDS NDGRPGYVGT AYTPVSLGKP GKLGDRMSAF MQPQATAYST
     SSNTSPGKKL TWAERQAANK RQAEEEEARS RAAIDNASSF KSPHVPSATR PPASTYAPPQ
     NRPVDDDFDA PSVREIHAEE QLSPVSVPPP PPPPPPPPPP PAPAPPSPPP PPIPEATFED
     HEVDHRAPEV EEAVMHQKME TLALASDLAD AAASGVGIRA VVSYEYEKAE ENEMDLVEGE
     IIEQIEMLDE GWWSGVGADG TKQGLFPANY VEVIVEEEPV SAPVPPVSAP VPPVSAPAPP
     APPAPPAPPA PPAPPAPPAT SEPEKDQGPC AIAAYEYEAG EDNEISFKEG EMIVEIEFSS
     EDWWTGTDPS GARGLFPANY VEMEE
//
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