ANI1_EMEND
ID ANI1_EMEND Reviewed; 488 AA.
AC P03880;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Intron-encoded DNA endonuclease I-AniI;
DE AltName: Full=COB intron protein;
DE AltName: Full=mRNA maturase bI1;
DE Contains:
DE RecName: Full=Truncated non-functional cytochrome b;
DE Contains:
DE RecName: Full=DNA endonuclease/RNA maturase I-AniI;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=I-AniI;
OS Emericella nidulans (Aspergillus nidulans).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=yA2 pyroA4 cnxC3;
RX PubMed=7034966; DOI=10.1016/0092-8674(81)90354-8;
RA Waring R.B., Davies R.W., Lee S., Grisi E., Berks M.M., Scazzocchio C.;
RT "The mosaic organization of the apocytochrome b gene of Aspergillus
RT nidulans revealed by DNA sequencing.";
RL Cell 27:4-11(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-488.
RC STRAIN=yA2 pyroA4 cnxC3;
RX PubMed=6755468; DOI=10.1073/pnas.79.20.6332;
RA Waring R.B., Davies R.W., Scazzocchio C., Brown T.A.;
RT "Internal structure of a mitochondrial intron of Aspergillus nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6332-6336(1982).
RN [3]
RP FUNCTION, AND RNA SPLICING AND ENDONUCLEASE ACTIVITY.
RX PubMed=9256423; DOI=10.1073/pnas.94.17.8994;
RA Ho Y., Kim S.-J., Waring R.B.;
RT "A protein encoded by a group I intron in Aspergillus nidulans directly
RT assists RNA splicing and is a DNA endonuclease.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8994-8999(1997).
RN [4]
RP FUNCTION, AND BIOCHEMICAL CHARACTERIZATION OF MATURASE ACTIVITY.
RX PubMed=10512698; DOI=10.1006/jmbi.1999.3070;
RA Ho Y., Waring R.B.;
RT "The maturase encoded by a group I intron from Aspergillus nidulans
RT stabilizes RNA tertiary structure and promotes rapid splicing.";
RL J. Mol. Biol. 292:987-1001(1999).
RN [5]
RP FUNCTION, AND RNA AND DNA-BINDING.
RX PubMed=12758073; DOI=10.1016/s0022-2836(03)00426-1;
RA Chatterjee P., Brady K.L., Solem A., Ho Y., Caprara M.G.;
RT "Functionally distinct nucleic acid binding sites for a group I intron
RT encoded RNA maturase/DNA homing endonuclease.";
RL J. Mol. Biol. 329:239-251(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 237-488 IN COMPLEX WITH DNA.
RX PubMed=14633971; DOI=10.1101/gad.1109003;
RA Bolduc J.M., Spiegel P.C., Chatterjee P., Brady K.L., Downing M.E.,
RA Caprara M.G., Waring R.B., Stoddard B.L.;
RT "Structural and biochemical analyses of DNA and RNA binding by a
RT bifunctional homing endonuclease and group I intron splicing factor.";
RL Genes Dev. 17:2875-2888(2003).
CC -!- FUNCTION: Mitochondrial DNA endonuclease and mRNA maturase involved in
CC intron homing and required for splicing of the cytochrome b (cobA) gene
CC intron, containing its own coding sequence. The protein stimulates the
CC intrinsic ribozyme activity of the intron through binding to and
CC stabilizing specific secondary and tertiary structure elements in the
CC RNA. As an endonuclease it introduces a specific double-strand break at
CC the junction of the two exons the cobA gene and thus mediates the
CC insertion of an intron, containing its own coding sequence (group I
CC intron), into an intronless gene. Recognizes with limited specificity
CC and cleaves the sequence 5'-GAGGAGGTTTCTCTGTA-3'. The proteins RNA and
CC DNA recognition and binding surfaces are independent.
CC {ECO:0000269|PubMed:10512698, ECO:0000269|PubMed:12758073,
CC ECO:0000269|PubMed:9256423}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14633971}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: The mature protein may arise from proteolytic cleavage of an in-
CC frame translation of cobA exon 1 plus intron, containing the I-AniI
CC open reading frame. Cleavage may take place close to Met-213 resulting
CC in an active endonuclease/maturase of about 30 kDa (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Residues 237 to 488 are sufficient for endonuclease,
CC intron homing, and RNA maturase activity.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG
CC endonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA31737.1; Type=Erroneous gene model prediction; Note=The cobA ORF was not predicted to be expressed alternatively as a fusion with intron 4, and intron 4 CDS was not annotated.; Evidence={ECO:0000305};
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DR EMBL; J01388; AAA31737.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J01389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A04513; QXASBI.
DR PDB; 1P8K; X-ray; 2.60 A; Z=237-488.
DR PDB; 2QOJ; X-ray; 2.40 A; Z=237-488.
DR PDB; 3EH8; X-ray; 2.70 A; A/D/G=237-488.
DR PDBsum; 1P8K; -.
DR PDBsum; 2QOJ; -.
DR PDBsum; 3EH8; -.
DR AlphaFoldDB; P03880; -.
DR SMR; P03880; -.
DR MoonProt; P03880; -.
DR PRIDE; P03880; -.
DR EvolutionaryTrace; P03880; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR Pfam; PF00033; Cytochrome_B; 1.
DR Pfam; PF00961; LAGLIDADG_1; 2.
DR SUPFAM; SSF55608; SSF55608; 2.
DR SUPFAM; SSF81342; SSF81342; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Intron homing; Mitochondrion;
KW mRNA processing; mRNA splicing; Nuclease.
FT CHAIN 1..?
FT /note="Truncated non-functional cytochrome b"
FT /id="PRO_0000013491"
FT CHAIN ?..488
FT /note="DNA endonuclease/RNA maturase I-AniI"
FT /id="PRO_0000013492"
FT REGION 1..169
FT /note="cobA exon 1 encoded"
FT REGION 170..488
FT /note="cobA intron encoded"
FT CONFLICT 295
FT /note="I -> R (in Ref. 6)"
FT /evidence="ECO:0000305"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2QOJ"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:2QOJ"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 429..437
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:2QOJ"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:2QOJ"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:2QOJ"
SQ SEQUENCE 488 AA; 55395 MW; 40B106A275535E27 CRC64;
MRILKSHPLL KIVNSYIIDS PQPANLSYLW NFGSLLALCL GIQIVTGVTL AMHYTPSVSE
AFNSVEHIMR DVNNGWLVRY LHSNTASAFF FLVYLHIGRG LYYGSYKTPR TLTWAIGTVI
LIVMMATAFL GYVLPYGQMS LWGATVITNL MSAIPWIGQD IVEFIWGGLY TDEPQCGDVL
LKILLNAGKS PILGFAYDLF FIIVLLIGVK IAMTRGKSAG VRSLHTSEAS QRLHAGDLTY
AYLVGLFEGD GYFSITKKGK YLTYELGIEL SIKDVQLIYK IKKILGIGIV SFRKINEIEM
VALRIRDKNH LKSFILPIFE KYPMFSNKQY DYLRFRNALL SGIISLEDLP DYTRSDEPLN
SIESIINTSY FSAWLVGFIE AEGCFSVYKL NKDDDYLIAS FDIAQRDGDI LISAIRKYLS
FTTKVYLDKT NCSKLKVTSV RSVENIIKFL QNAPVKLLGN KKLQYLLWLK QLRKISRYSE
KIKIPSNY
