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Database: UniProt
Entry: F4RCE4_MELLP
LinkDB: F4RCE4_MELLP
Original site: F4RCE4_MELLP 
ID   F4RCE4_MELLP            Unreviewed;       531 AA.
AC   F4RCE4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   22-FEB-2023, entry version 54.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=MELLADRAFT_115627 {ECO:0000313|EMBL:EGG09715.1};
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).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; GL883096; EGG09715.1; -; Genomic_DNA.
DR   RefSeq; XP_007406769.1; XM_007406707.1.
DR   AlphaFoldDB; F4RCE4; -.
DR   STRING; 747676.F4RCE4; -.
DR   EnsemblFungi; EGG09715; EGG09715; MELLADRAFT_115627.
DR   GeneID; 18925654; -.
DR   KEGG; mlr:MELLADRAFT_115627; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_115627; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   HOGENOM; CLU_015780_1_0_1; -.
DR   InParanoid; F4RCE4; -.
DR   OrthoDB; 1453907at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 1.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR018106; CAP_CS_N.
DR   InterPro; IPR036222; CAP_N_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR10652:SF0; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   Pfam; PF01213; CAP_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR   SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT   DOMAIN          373..509
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          46..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..296
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  56161 MW;  7599212853F9F11E CRC64;
     MANGIPTQGV GSLFTLIKRL EAATSRLEDI AVAQTSVGTP ALLNEGFSTH ASPSNVPGVS
     SGSASNPEAM ETPPSIKAFD ELLSGSLARY LTLSKDVGGP AQEQANHVEQ AFMAQREFLL
     VASACQKPSI DALMELLQPT SDPLNKVVEV KDAQRAEKRL FNGLTAVAEG IPGLGWVAVE
     TKPGPMVSDA KDSAQFWVNR VVKDNKDSDP QLADWAKSFI VVLEDLRKYI MQYHTTCLVW
     NPKGEDATSF AKRMSPAGSP SASTPRAPTG APSAPTPPRP GPPPPGPPPP PPMPSMNQAS
     GAAGGMDAVF AALNKGENIT SGLKRVDPSQ MTHKNPTLRT SSATGPSGGL TSPQGSIKRP
     TKPPKPQSFQ KRPPKTQLDG NKWAIEYHEN QSSIVIENTE INQIVNIFGC KNSTISIKGK
     VNAITLVSCT KTSVLLESVV SSLSITSSPS FTVQVLGKVP TVMVDATDGG QIYLSKESLD
     VEIVTAKTSA LNVSLPSEEE EGEFVERAMP EQLKTVVVNG KLVTSVLEHS G
//
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