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Database: UniProt
Entry: A0A1V8TXT4_9PEZI
LinkDB: A0A1V8TXT4_9PEZI
Original site: A0A1V8TXT4_9PEZI 
ID   A0A1V8TXT4_9PEZI        Unreviewed;       822 AA.
AC   A0A1V8TXT4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=C2 domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=B0A51_16040 {ECO:0000313|EMBL:OQO16087.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO16087.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQO16087.1}.
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DR   EMBL; NAEU01001274; OQO16087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8TXT4; -.
DR   STRING; 1974281.A0A1V8TXT4; -.
DR   Proteomes; UP000192386; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd08681; C2_fungal_Inn1p-like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037791; C2_fungal_Inn1.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR47052; CONSERVED SERINE PROLINE-RICH PROTEIN (AFU_ORTHOLOGUE AFUA_2G01790); 1.
DR   PANTHER; PTHR47052:SF3; INGRESSION PROTEIN 1; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT   DOMAIN          21..179
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          154..271
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          294..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..529
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         822
FT                   /evidence="ECO:0000313|EMBL:OQO16087.1"
SQ   SEQUENCE   822 AA;  91123 MW;  4451263FD93E0AD2 CRC64;
     MSDEPSMATN EETNPWQSAR LTYRAIEPED EEFIHEVESH PATFINLQPA LKRPQSKADT
     KKSFDHYVNE CLLAVVICIT AEDLKPIGVI NLEGPEPDHD HHRYSDMGLG LSPSEQGKGH
     GSEAIRWALQ WGFESAGLHR ISVKAFEYNV GAMRLAGIFA DMTVDGPEIG TFVMIVDRAK
     NLPNRKTMGK QNPYCAARLG KEAKKTETDK RGGQTPRWDQ ELRFTVHDSP DYYTLKVSVF
     SEDKRTDLIG EAFVSLSDVI IPGGGKRDVW QGLNCKGKYA GEVRIEMTYY DSRPKPEISR
     ESSFGDEDAR TISGSGKVKR RPLPGLNGSR GMTPGTLSDP FAPSPMPGRA KHGPRELGMP
     ARANSMPPEM PYHDEIPHRA SSGALQYHPQ QFAQNDQGSY DEPQTYDDSY AYDELPREQQ
     YAQPDFLPQL PPSNRSRGTT PHQSQGLQHT HSAPQIPTME SDYHPGFSLH TEAPQPLPDL
     DFQHQHLRHR QYDAPQEWGN PYESSYDVER PMEDGAGQPP PPPPQHSHSA PVVPQYSPTR
     SPAGSPYGAA PSPAQPYVSN ASPLQSIEQE YGQARYTPAR SYASRAHSID EHASPGPHNA
     SRNSTPQSLV IGHSPSPAAR SPAARVMAHR HSVADPYQAT PPRPHPLSQE VPRARTSNPS
     SPYHIRPDQA PTPDRDDSRG PIVGWDGREI DPSDHLPVDS WAPEPIKKTP TKTYGLGRDK
     DFGPRSGENS PGMGQRLSKD TVVKFGRKSA TQAPPPQLPE LSPPNSRNRL RKATSETARG
     APTMPLREHT NFNAIPDPYA QQEYSRGFHG DSPRGYEHQQ PR
//
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