Protein Family Models for Protein (Select 489417458) - Protein Family Models

Select item 4250961.

This domain is found in conserved virulence factors [1]. It is often found in association with Pfam:PF02985 and Pfam:PF08712. [1]. 15853881. Silkworm pathogenic bacteria infection model for identification of novel virulence genes. Kaito C, Kurokawa K, Matsumoto Y, Terao Y, Kawabata S, Hamada S, Sekimizu K;. Mol Microbiol. 2005;56:934-944. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF025142.5
Method:: HMM

Select item 4225252.

HEAT repeat domain-containing protein

This family includes multiple HEAT repeats. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF025030.5
Method:: HMM

Select item 4192383.

NifU N-terminal domain-containing protein

This domain is found at the N terminus of NifU and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the the assembly of iron-sulphur clusters [1][2]. [1]. 12886008. Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. Tong WH, Jameson GN, Huynh BH, Rouault TA;. Proc Natl Acad Sci U S A. 2003;100:9762-9767. [2]. 14993221. Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein. Dos Santos PC, Smith AD, Frazzon J, Cash VL, Johnson MK, Dean DR;. J Biol Chem. 2004;279:19705-19711. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF020295.5
Method:: HMM

Select item 4145544.

HEAT repeat protein

The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see Pfam:PF00514). [1]. 7550332. HEAT repeats in the Huntington's disease protein. Andrade MA, Bork P;. Nat Genet 1995;11:115-116. [2]. 9989501. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D;. Cell 1999;96:99-110. (from Pfam)

GO Terms:

Molecular Function:: protein binding (GO:0005515)

Date:: 2024-10-16

Family Accession:: NF014979.5
Method:: HMM

Select item 4137745.

PBS lyase HEAT-like repeat

This family contains a short bi-helical repeat that is related to Pfam:PF02985. Cyanobacteria and red algae harvest light energy using macromolecular complexes known as phycobilisomes (PBS), peripherally attached to the photosynthetic membrane. The major components of PBS are the phycobiliproteins. These heterodimeric proteins are covalently attached to phycobilins: open-chain tetrapyrrole chromophores, which function as the photosynthetic light-harvesting pigments. Phycobiliproteins differ in sequence and in the nature and number of attached phycobilins to each of their subunits. This family includes the lyase enzymes that specifically attach particular phycobilins to apophycobiliprotein subunits. The most comprehensively studied of these is the CpcE/F lyase Swiss:P31967 Swiss:P31968, which attaches phycocyanobilin (PCB) to the alpha subunit of apophycocyanin [1]. Similarly, MpeU/V attaches phycoerythrobilin to phycoerythrin II, while CpeY/Z is thought to be involved in phycoerythrobilin (PEB) attachment to phycoerythrin (PE) I (PEs I and II differ in sequence and in the number of attached molecules of PEB: PE I has five, PE II has six) [2]. All the reactions of the above lyases involve an apoprotein cysteine SH addition to a terminal delta 3,3'-double bond. Such a reaction is not possible in the case of phycoviolobilin (PVB), the phycobilin of alpha-phycoerythrocyanin (alpha-PEC). It is thought that in this case, PCB, not PVB, is first added to apo-alpha-PEC, and is then isomerised to PVB. The addition reaction has been shown to occur in the presence of either of the components of alpha-PEC-PVB lyase PecE or PecF (or bo. TRUNCATED at 1650 bytes (from Pfam)

Date:: 2024-08-14

Family Accession:: NF015114.5
Method:: HMM

Select item 4005256.