ID A0A0A1T200_9HYPO Unreviewed; 527 AA.
AC A0A0A1T200;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=VHEMI00463 {ECO:0000313|EMBL:CEJ80267.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ80267.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ80267.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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DR EMBL; CDHN01000001; CEJ80267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1T200; -.
DR STRING; 1531966.A0A0A1T200; -.
DR HOGENOM; CLU_015780_1_0_1; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000039046; 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:UP000039046}.
FT DOMAIN 368..503
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 24..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 56463 MW; 6EEDB2FDB0674CDE CRC64;
MAANSHMHNL TTLIKRLEAA TSRLEDIATS TEPAEDGAAR AHPDASPAGV VSAAGAPAPK
AAPVPEPEEL PEAIEDFDTF LNGPVTKFVS LSKELGGLVA KQAELVFSGF KEQRKFLFIT
TKAAKPDLSG AEMAVYQDLL KPINESLMAV TDIKESNRGD PMYTQLSAVG DGIMVLAWVT
VAHRPFTHVE EFLSSAQFFG NRVIKEYKDK DPKQVEWIQS FYAIFKDLRD LVKQHYPNGI
QWNPKGDSAS AVAKALAASS TNAPPAAPAA GGPPPPPPPP PGPPPVLDIK TESAPAAAPS
AAGGLGAVFS ELNKGESVTK GLRKVDKSEM THKNPSLRAA ATVSDSARPK SPAPGKKPKP
ESMRVKKPSK KELEGNKWTI ENFEKEAVPI EIEASLSHSI LISRCNNTTI IVKGKANQVT
IENSSRLSLV VDSLVSTVDV VKAQNFALQV MGTIPTVMMD QVDGAQIYFS KESTTTKIFH
SKSDGINLNV ISGPDEDYKE VPLPSQMCSY YDPDKNDLVN EIVAHAG
//
