SMART: PAM domain annotation

The domain within your query sequence starts at position 144 and ends at position 312; the E-value for the PAM domain shown below is 4.29e-68.

LLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDD
YSTAQRITYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRSSQKNKRMILIYLLPVKMLLG
HMPTIELLRKYHLMQFSEVTKAVSEGNLLLLNEALAKHETFFIRCGIFL

PAM PCI/PINT associated module

SMART accession number:	SM00753
Description:	-
Family alignment:	View or

There are 0 PAM domains in 0 proteins in SMART's nrdb database.

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Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

Ciccarelli FD, Izaurralde E, Bork P
The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold.
BMC Bioinformatics. 2003; 4: 64-64
Display abstract
BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. The characterization of their domain composition and organization provides useful information on the specific role of each region of their sequence. RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. This module is an around 200 residue long domain with a predicted TPR-like all-alpha-helical fold. CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins.

Aravind L, Ponting CP
Homologues of 26S proteasome subunits are regulators of transcription and translation.
Protein Sci. 1998; 7: 1250-4
Display abstract
Single copies of an alpha-helical-rich motif are demonstrated to be present within subunits of the large multiprotein 26S proteasome and eukaryotic initiation factor-3 (eIF3) complexes, and within proteins involved in transcriptional regulation. In addition, p40 and p47 subunits of eIF3 are shown to be homologues of the proteasome subunit Mov34, and transcriptional regulators JAB1/pad1. Finally, the proteasome subunit S5a and the p44 subunit of the basal transcription factor IIH (TFIIH) are identified as homologues. The presence of homologous, and sometimes identical, proteins in contrasting functional contexts suggests that the large multisubunit complexes of the 26S proteasome, eIF3 and TFIIH perform overlapping cellular roles.

Hofmann K, Bucher P
The PCI domain: a common theme in three multiprotein complexes.
Trends Biochem Sci. 1998; 23: 204-5

Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

PDB code	Main view	Title
3jck		3JCK
3jco		3JCO
3jcp		3JCP
3t5v		Sac3:Thp1:Sem1 complex
3t5x		PCID2:DSS1 Structure
3txm		Crystal structure of Rpn6 from Drosophila melanogaster, Gd(3+) complex
3txn		Crystal structure of Rpn6 from Drosophila melanogaster, native data
4cr2		Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
4cr3		Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
4cr4		Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
4d10		4D10
4d18		4D18
4trq		4TRQ
4wsn		4WSN
5a5b		5A5B
5g5p		5G5P
5gjq		5GJQ
5gjr		5GJR
5l3t		5L3T
5l4k		5L4K
5t0c		5T0C
5t0g		5T0G
5t0h		5T0H
5t0i		5T0I
5t0j		5T0J

The domain within your query sequence starts at position 144 and ends at position 312; the E-value for the PAM domain shown below is 4.29e-68.

PAM

3D Structures of PAM domains in PDB