ID A0A0M8P5B1_9EURO Unreviewed; 527 AA.
AC A0A0M8P5B1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=ACN38_g3667 {ECO:0000313|EMBL:KOS45428.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS45428.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS45428.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS45428.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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:KOS45428.1}.
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DR EMBL; LHQQ01000044; KOS45428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8P5B1; -.
DR STRING; 229535.A0A0M8P5B1; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000037696; 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:UP000037696}.
FT DOMAIN 368..507
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 28..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 56370 MW; 54CA88A3C815FE01 CRC64;
MASGGHMHNF TTLIKRLEAA TSRLEDMAMS YDESSTTKSL TSSPSSTPAV PPPPKPSPPP
PAAPVAAPVP PQIQDFDALI KGDVQNFVNL GEQIGGLVAE QSKAVLQAFQ AERTYLFVVT
KAKKPDTQPP ELMTDLHKAS DSINNIRESN RASPLFNHLS AVAEGIVALA WFFESKPAEF
VTDMIGGIEY YGNKVLKEYK DKDKAHVDYI KAYYQNFKAL AVYLKKHFPQ GLTWNNESGI
DALEALKQAK GGPVPVSGGA PPPPPPPVPA LNVPGGGAPP PPPPPGIPPA PAPAAPAADM
GAVFNQLNQG EGITSTLRKV DKSEMTHKNP NLRAGSIVPE SEGSSAVRGK SPAPNKKPKP
ENMRARKPPR KELEGSKWLI ENFDAPGEII EIPAQQNHSI LISRCNKTII KVSNKANAIA
IDNCVGLSLI VDSLVSSLDI IKCPKFAVQI DGTVPTLLLD QVDGATVYLS QQSLNTEVFT
SKCSAININL PPPEGTDEDT KECPLPEQFK SYIKNGVLVS EIVEHAG
//
