ID ANI1_EMENI Reviewed; 488 AA. AC P03880; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 3. DT 31-OCT-2006, entry version 47. DE Intron-encoded DNA endonuclease I-AniI precursor (mRNA maturase bI1) DE (COB intron protein) [Contains: Truncated, nonfunctional cytochrome b; DE DNA endonuclease/RNA maturase I-AniI (EC 3.1.-.-)]. GN Name=I-AniI; OS Emericella nidulans (Aspergillus nidulans). OG Mitochondrion. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=82115341; PubMed=7034966; DOI=10.1016/0092-8674(81)90354-8; RA Waring R.B., Davies R.W., Lee S., Grisi E., Berks M.M., RA 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. RX MEDLINE=83065170; PubMed=6755468; RA Waring R.B., Davies R.W., Scazzocchio C., Brown T.A.; RT "Internal structure of a mitochondrial intron of Aspergillus RT nidulans."; RL Proc. Natl. Acad. Sci. U.S.A. 79:6332-6336(1982). RN [3] RP FUNCTION, AND RNA SPLICING AND ENDONUCLEASE ACTIVITY. RX MEDLINE=97404336; 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 RT directly 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 MEDLINE=99443883; 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 MEDLINE=22643283; 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 CC involved in intron homing and required for splicing of the CC cytochrome b (cobA) gene intron, containing its own coding CC sequence. The protein stimulates the intrinsic ribozyme activity CC of the intron through binding to and stabilizing specific CC secondary and tertiary structure elements in the RNA. As an CC endonuclease it introduces a specific double-strand break at the CC junction of the two exons the cobA gene and thus mediates the CC insertion of an intron, containing its own coding sequence (group CC I intron), into an intronless gene. Recognizes with limited CC specificity and cleaves the sequence 5'-GAGGAGGTTTCTCTGTA-3'. The CC proteins RNA and DNA recognition and binding surfaces are CC independent. CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- PTM: The mature protein may arise from proteolytic cleavage of an CC in-frame translation of cobA exon 1 plus intron, containing the I- CC AniI open reading frame. Cleavage may take place close to Met-213 CC resulting in an active endonuclease/maturase of about 30 kDa (By CC similarity). CC -!- MISCELLANEOUS: Residues 237 to 488 are sufficient for CC endonuclease, intron homing, and RNA maturase activity. CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG CC endonuclease family. CC -!- CAUTION: Ref.1 sequence differs from that shown because cobA was CC not predicted to be expressed alternatively as a fusion with CC intron 4, and intron 4 CDS was not annotated. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01388; AAA31737.1; -; 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; Z=237-488. DR REBASE; 3056; I-AniI. DR InterPro; IPR005797; Cytb_b6_N. DR InterPro; IPR001982; Endonuc_LAG/HNH. DR Pfam; PF00033; Cytochrom_B_N; 1. DR Pfam; PF00961; LAGLIDADG_1; 2. DR PROSITE; PS51002; CYTB_NTER; 1. KW 3D-structure; Endonuclease; Hydrolase; Intron homing; Mitochondrion; KW mRNA processing; mRNA splicing; Nuclease. FT CHAIN 1 ? Truncated, nonfunctional cytochrome b. FT /FTId=PRO_0000013491. FT CHAIN ? 488 DNA endonuclease/RNA maturase I-AniI. FT /FTId=PRO_0000013492. FT REGION 1 169 cobA exon 1 encoded. FT REGION 170 488 cobA intron encoded. FT CONFLICT 295 295 I -> R (in Ref. 6). FT TURN 237 238 FT HELIX 239 250 FT STRAND 251 258 FT TURN 259 260 FT STRAND 261 271 FT HELIX 272 274 FT HELIX 275 285 FT STRAND 289 293 FT TURN 296 297 FT STRAND 300 305 FT HELIX 308 321 FT TURN 327 328 FT HELIX 329 341 FT TURN 342 342 FT HELIX 346 348 FT HELIX 362 367 FT TURN 369 370 FT HELIX 371 382 FT STRAND 384 386 FT STRAND 389 394 FT STRAND 400 406 FT TURN 407 407 FT HELIX 409 418 FT TURN 419 420 FT STRAND 429 437 FT HELIX 440 451 FT TURN 452 452 FT STRAND 453 455 FT HELIX 460 474 FT HELIX 476 479 FT TURN 480 481 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 //