The domain within your query sequence starts at position 31 and ends at position 363; the E-value for the NIF3 domain shown below is 1.9e-82.
ALLSSLNDFASLSFAESWDNVGLLVEPSPPHTVNTLFLTNDLTEEVMDEALQKKADFILS YHPPIFRPMKHITWKTWKECLVIRALENRVAVYSPHTAYDAAPQGVNSWLAKGLGTCTTR PIHPSRAPDYPTEGAHRLEFSVNRSQDLDKVMSTLRGVGGVSVTSFPARCDGEEQTRISL NCTQKTLMQVLAFLSQDRQLYQKTEILSLEKPLLLHTGMGRLCTLDESVSLAIMIERIKT HLKLSHLRLALGVGRTLESQVKVVALCAGSGGSVLQGVEADLYLTGEMSHHDVLDAASKG INVILCEHSNTERGFLSELQEMLGVHFENKINI
NIF3 |
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PFAM accession number: | PF01784 |
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Interpro abstract (IPR002678): | In Helicobacter pylori, GTP cyclohydrolase 1 type 2 converts GTP to dihydroneopterin triphosphate [ (PUBMED:23825549) ]. Nif3 interacts with the yeast transcriptional coactivator Ngg1p which is part of the ADA complex, the exact function of this interaction is unknown [ (PUBMED:11124544) (PUBMED:8663102) ]. This family includes GTP cyclohydrolase 1 type 2 proteins from bacteria and Nif3 from budding yeasts. The structure of the Methanocaldococcus jannaschii MJ0927 Nif3 protein has been determined [ (PUBMED:23295494) (PUBMED:25243119) ]. It binds to both single-stranded and double-stranded DNA [ (PUBMED:25243119) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry NIF3