The domain within your query sequence starts at position 528 and ends at position 963; the E-value for the MMS19_C domain shown below is 3.9e-116.

PKLAEELHKGESDVARADGPTKCSRHFRCLQALSAVSTHPSIVKETLPLLLQHLCQANKG
NMVTESSEVVAVCQSLQQVAEKCQQDPESYWYFHKTAVPCLFALAVQASMPEKESSVLRK
VLLEDEVLAALASVIGTATTHLSPELAAQSVTCIVPLFLDGNTSFLPENSFPDQFQPFQD
GSSGQRRLVALLTAFVCSLPRNVEIPQLNRLMRELLKQSCGHSCPFSSTAATKCFAGLLN
KQPPGQQLEEFLQLAVGTVEAGLASESSRDQAFTLLLWVTKALVLRYHPLSACLTTRLMG
LLSDPELGCAAADGFSLLMSDCTDVLTRAGHADVRIMFRQRFFTDNVPALVQGFHAAPQD
VKPNYLKGLSHVLNRLPKPVLLPELPTLLSLLLEALSCPDSVVQLSTLSCLQPLLLEAPQ
IMSLHVDTLVTKFLNL

MMS19_C

MMS19_C
PFAM accession number:PF12460
Interpro abstract (IPR024687):

This entry represents the C-terminal domain of MMS19. This domain shares homology with some HEAT repeat sequences. MMS19 is a key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity [(PUBMED:22678362), (PUBMED:22678361)].

In humans, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription [(PUBMED:22678362), (PUBMED:22678361)]. It is also part of the MMXD (MMS19-MIP18-XPD) complex, which plays a role in chromosome segregation, probably by facilitating iron-sulfur cluster assembly into ERCC2/XPD [(PUBMED:20797633)].

In budding yeasts, the mms19 mutants were originally isolated in a screening for mutants hypersensitive to the alkylating agent methyl methanesulfonate (MMS) [(PUBMED:8943333)]. Different from human MMS19, Mms19 in budding yeasts (also known as Met18) does not participate directly in NER [(PUBMED:23585563)].

In fission yeast, Mms19 is part of a silencing complex named Rik1-Dos2 complex, which contains Dos2, Rik1, Mms19 and Cdc20. This complex regulates RNA Pol II activity in heterochromatin, and is required for DNA replication and heterochromatin assembly [(PUBMED:21725325)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MMS19_C