LOCUS CAY39372 519 aa linear INV 20-JAN-2011 DEFINITION cytochrome c oxidase subunit I, partial (mitochondrion) [Radopholus similis]. ACCESSION CAY39372 VERSION CAY39372.1 GI:257143738 DBSOURCE embl accession FN313571.1 KEYWORDS . SOURCE mitochondrion Radopholus similis ORGANISM Radopholus similis Eukaryota; Metazoa; Nematoda; Chromadorea; Tylenchida; Tylenchina; Tylenchoidea; Pratylenchidae; Radopholinae; Radopholus. REFERENCE 1 AUTHORS Jacob,J. TITLE Plant-parasitic nematodes: from genomics to functional analysis JOURNAL Unpublished REFERENCE 2 AUTHORS Jacob,J., Vanholm,B., Vanleeuwen,T., Devreese,B. and Gheysen,G. TITLE The mitochondrial genome of Radopholus similis JOURNAL Unpublished REFERENCE 3 (residues 1 to 519) AUTHORS Jacob,J. TITLE Direct Submission JOURNAL Submitted (07-APR-2009) Jacob J., Ghent University, Molecular Biotechnology, Coupure Links 653, 9000 Gent, BELGIUM FEATURES Location/Qualifiers source 1..519 /organism="Radopholus similis" /organelle="mitochondrion" /db_xref="taxon:46012" /country="Uganda" Protein 1..>519 /product="cytochrome c oxidase subunit I" Region 12..466 /region_name="Cyt_c_Oxidase_I" /note="Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of...; cd01663" /db_xref="CDD:29934" Site order(12,92,96,98,105,145,149,167,171,191,198,201,209, 218..220,225..226,228,238,276,279,282..283,287) /site_type="other" /note="Subunit I/III interface [polypeptide binding]" /db_xref="CDD:29934" Site order(21,82,93,100,103,157..158,164,168) /site_type="other" /note="D-pathway" /db_xref="CDD:29934" Site order(27,31,34,38,118..119,401) /site_type="other" /note="Subunit I/VIIc interface [polypeptide binding]" /db_xref="CDD:29934" Site order(41,44..45,409,412..413,446,464) /site_type="other" /note="Subunit I/IV interface [polypeptide binding]" /db_xref="CDD:29934" Site order(57,228,266,269..270,295..297,300,303,311,319,322, 329..331,343,361..362,364,366..370,434..435,439..441, 450..451) /site_type="other" /note="Subunit I/II interface [polypeptide binding]" /db_xref="CDD:29934" Site order(63,379,383,425,462) /site_type="other" /note="Low-spin heme (heme a) binding site [chemical binding]" /db_xref="CDD:29934" Site order(116,119) /site_type="other" /note="Subunit I/VIIa interface [polypeptide binding]" /db_xref="CDD:29934" Site order(137,214..217) /site_type="other" /note="Subunit I/VIa interface [polypeptide binding]" /db_xref="CDD:29934" Site order(191,198,238,276,279,282..283,287) /site_type="other" /note="Dimer interface" /db_xref="CDD:29934" Site order(228,233..234,365,369..370,439) /site_type="other" /note="Putative water exit pathway" /db_xref="CDD:29934" Site order(241,291..292,377) /site_type="other" /note="Binuclear center (heme a3/CuB) [ion binding]" /db_xref="CDD:29934" Site order(241,245,256,291..292,317,320) /site_type="other" /note="K-pathway" /db_xref="CDD:29934" Site order(267,271) /site_type="other" /note="Subunit I/Vb interface [polypeptide binding]" /db_xref="CDD:29934" Site order(292,369..370,439..440) /site_type="other" /note="Putative proton exit pathway" /db_xref="CDD:29934" Site 297 /site_type="other" /note="Subunit I/VIb interface" /db_xref="CDD:29934" Site 330 /site_type="other" /note="Subunit I/VIc interface [polypeptide binding]" /db_xref="CDD:29934" Site order(378,439..440) /site_type="other" /note="Electron transfer pathway" /db_xref="CDD:29934" Site 410 /site_type="other" /note="Subunit I/VIIIb interface [polypeptide binding]" /db_xref="CDD:29934" Site order(446,450) /site_type="other" /note="Subunit I/VIIb interface [polypeptide binding]" /db_xref="CDD:29934" CDS 1..519 /gene="cox1" /coded_by="FN313571.1:6113..>7669" /transl_table=5 /db_xref="GOA:C7TQN6" /db_xref="InterPro:IPR000883" /db_xref="UniProtKB/TrEMBL:C7TQN6" ORIGIN 1 mfynnyyqyn avnhkyigsm yfvfaffsmm mgvslsllir lelgnpgfll gngqlfnsii 61 tghalimiff fvmpmlmgff gnmliplllm sadmawprvn nqsfwflpaa milmmmsmii 121 dqgsgtswtl ypplsssghl ggsvdfsifs lhvagfssla gsmnflssmk slrsmtisle 181 mmdlflwstl vtvfllilsl pvlaggitml lfdrnfnsnf fevgsggnsl mfqhlfwffg 241 hpevyililp afglvsqttl lisgkkmvfg svamisammv igfigclvwa hhmftvgldf 301 dsrayftaat mviavptgik vfswmmtlyg syminnmmve wlygfiflft lggltglvls 361 nssldillhd tyyvvahfhy vlslgavfgi iigffvyygy fyglvlnkil vnsfykmifl 421 gvnmtffplh faglqgfprk yvdyidiysi wniissfgsi lstysmfffi ylfyesffnf 481 rlvylnffes nylllvknmy lhsfydslvy yynwfilvk //