Terrisporobacter hibernicus strain MCA3 plasmid unnamed, complete sequence.
Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae; Terrisporobacter.
Terrisporobacter hibernicus sp. nov., isolated from bovine faeces in Northern Ireland
Submitted (11-AUG-2021) Centre for Food Safety, University College Dublin, UCD Centre for Food Safety, College of Health and Agricultral Sciences, R1.25, Science Centre South, Dublin, Leinster D04 V1W8, Ireland
REFSEQ INFORMATION: The reference sequence is identical to\nCP081136.1.\nBacteria and source DNA available from UCD Centre for Food Safety.\nThe annotation was added by the NCBI Prokaryotic Genome Annotation\nPipeline (PGAP). Information about PGAP can be found here:\nhttps://www.ncbi.nlm.nih.gov/genome/annotation_prok/\n\n##Genome-Assembly-Data-START##\nAssembly Date :: JUL-2021\nAssembly Method :: Trycycler v. v0.4.1\nAssembly Name :: T. hibernicus\nGenome Representation :: Full\nExpected Final Version :: Yes\nGenome Coverage :: 100.0x\nSequencing Technology :: Oxford Nanopore MinION\n##Genome-Assembly-Data-END##\n\n##Genome-Annotation-Data-START##\nAnnotation Provider :: NCBI RefSeq\nAnnotation Date :: 02/06/2023 17:46:44\nAnnotation Pipeline :: NCBI Prokaryotic Genome\n Annotation Pipeline (PGAP)\nAnnotation Method :: Best-placed reference protein\n set; GeneMarkS-2+\nAnnotation Software revision :: 6.4\nFeatures Annotated :: Gene; CDS; rRNA; tRNA; ncRNA\nGenes (total) :: 4,037\nCDSs (total) :: 3,904\nGenes (coding) :: 3,876\nCDSs (with protein) :: 3,876\nGenes (RNA) :: 133\nrRNAs :: 12, 12, 12 (5S, 16S, 23S)\ncomplete rRNAs :: 12, 12, 12 (5S, 16S, 23S)\ntRNAs :: 93\nncRNAs :: 4\nPseudo Genes (total) :: 28\nCDSs (without protein) :: 28\nPseudo Genes (ambiguous residues) :: 0 of 28\nPseudo Genes (frameshifted) :: 9 of 28\nPseudo Genes (incomplete) :: 19 of 28\nPseudo Genes (internal stop) :: 6 of 28\nPseudo Genes (multiple problems) :: 6 of 28\nCRISPR Arrays :: 1\n##Genome-Annotation-Data-END##\nCOMPLETENESS: full length.
type strain of Terrisporobacter hibernicus
COORDINATES: similar to AA sequence:RefSeq:WP_018590498.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
proline reductase-associated electron transfer protein PrdC
Derived by automated computational analysis using gene prediction method: tRNAscan-SE.
COORDINATES: similar to AA sequence:RefSeq:WP_018590499.1
COORDINATES: similar to AA sequence:RefSeq:WP_018590500.1
GO:0050485 - oxidoreductase activity, acting on X-H and Y-H to form an X-Y bond, with a disulfide as acceptor [Evidence IEA]
glycine/sarcosine/betaine reductase component B subunit
COORDINATES: similar to AA sequence:RefSeq:WP_018590501.1
COORDINATES: similar to AA sequence:RefSeq:WP_018590502.1
aminotransferase class V-fold PLP-dependent enzyme
COORDINATES: protein motif:HMM:NF040786.1
selenium metabolism-associated LysR family transcriptional regulator
COORDINATES: similar to AA sequence:RefSeq:WP_005339037.1
GO:0003746 - translation elongation factor activity [Evidence IEA]
GO:0001514 - selenocysteine incorporation [Evidence IEA]; GO:0006414 - translational elongation [Evidence IEA]
selenocysteine-specific translation elongation factor
COORDINATES: similar to AA sequence:RefSeq:WP_018590487.1
GO:0004125 - L-seryl-tRNASec selenium transferase activity [Evidence IEA]
GO:0016260 - selenocysteine biosynthetic process [Evidence IEA]
COORDINATES: similar to AA sequence:RefSeq:WP_012159590.1
GO:0004756 - selenide, water dikinase activity [Evidence IEA]
GO:0001887 - selenium compound metabolic process [Evidence IEA]
COORDINATES: similar to AA sequence:RefSeq:WP_018590489.1
COORDINATES: ab initio prediction:GeneMarkS-2+
Derived by automated computational analysis using gene prediction method: GeneMarkS-2+.
COORDINATES: similar to AA sequence:RefSeq:WP_018590491.1
COORDINATES: similar to AA sequence:RefSeq:WP_003230776.1
COORDINATES: protein motif:HMM:NF013930.2
GO:0003677 - DNA binding [Evidence IEA]; GO:0003896 - DNA primase activity [Evidence IEA]; GO:0008270 - zinc ion binding [Evidence IEA]
GO:0006260 - DNA replication [Evidence IEA]
CHC2 zinc finger domain-containing protein
COORDINATES: similar to AA sequence:RefSeq:WP_012157915.1
D-proline reductase (dithiol) protein PrdB
COORDINATES: similar to AA sequence:RefSeq:WP_018590496.1
CBO2463/CBO2479 domain-containing protein
COORDINATES: similar to AA sequence:RefSeq:WP_004607309.1
GO:0050002 - D-proline reductase (dithiol) activity [Evidence IEA]
D-proline reductase (dithiol) proprotein PrdA