zinc finger HIT (zf-HIT) found in Box C/D snoRNA protein 1 (BCD1) and similar proteins; The zf-HIT domain-containing family includes BCD1 and its yeast counterpart Bcd1p, both of which have been characterized as assembly factors for box C/D snoRNPs. BCD1, also known as serologically defined breast cancer antigen NY-BR-75 or zinc finger HIT domain-containing protein 6 (ZNHIT6), is required for the accumulation, processing, transport, and biogenesis of box C/D snoRNAs, specifically U3 and U8, in the nucleoplasm. Bcd1p is essential for cellular viability in Saccharomyces cerevisiae and contributes to the specific stability of box C/D snoRNAs. Members of this family contain a zf-HIT domain, characterized by a fold in "treble-clef" through interleaved CCCC and CCHC ZnF motifs that both bind a zinc atom. The zf-HIT domain of Bcd1p is necessary but not sufficient for yeast growth, and although it lacks direct RNA-binding capacity, it helps Bcd1p maintain steady-state levels of box C/D snoRNAs. Additionally, the zf-HIT domain of Bcd1p is functionally interchangeable with that of Hit1p, another box C/D snoRNP assembly factor belonging to the zf-HIT family.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 334182298 256 SVCEECKQNPWKYKCPGCSIRSCALPCVKAHKQRTGCTGK 295
Cdd:cd23023    1 GLCEVCGENEAKYTCPRCGARTCSLACVKAHKEETGCSGK 40

Chloroplast import apparatus Tic20-like; Chloroplast function requires the import of nuclear encoded proteins from the cytoplasm across the chloroplast double membrane. This is accomplished by two protein complexes, the Toc complex located at the outer membrane and the Tic complex located at the inner membrane. The Toc complex recognizes specific proteins by a cleavable N-terminal sequence and is primarily responsible for translocation through the outer membrane, while the Tic complex translocates the protein through the inner membrane. This entry represents Tic20, a core member of the Tic complex. This protein is deeply embedded in the inner envelope membrane and is thought to function as a protein- conducting component of the Tic complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182298   94 RRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEF---LTYPFLGAIGRL 170
Cdd:pfam16166   1 RRPTTLCRSASKDSLSAFDFPELAEKPEWWWRTLSCVPYLLPLFNGWQYGDTGYYLHPFLEQFPPfglLIYPIPGAINRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182298  171 PSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIR 250
Cdd:pfam16166  81 PSWFSMVYFFTLYFGVVRNKNLPHYFRFHVMMAMLLDVLLQVVLLTSNFNPLIGFGGKFGMYYWTGVFLFYIFTLLYCIR 160

                  ....
gi 334182298  251 CALA 254
Cdd:pfam16166 161 CALA 164

HIT zinc finger; This presumed zinc finger contains up to 6 cysteine residues that could coordinate zinc. The domain is named after the HIT protein. This domain is also found in the Thyroid receptor interacting protein 3 (TRIP-3) that specifically interact with the ligand binding domain of the thyroid receptor.

                          10        20
                  ....*....|....*....|....*...
gi 334182298  257 VCEECKqNPWKYKCPGCSIRSCALPCVK 284
Cdd:pfam04438   4 LCSVCG-NPSKYRCPRCGVRYCSLECYK 30

Chloroplast import apparatus Tic20-like; Chloroplast function requires the import of nuclear encoded proteins from the cytoplasm across the chloroplast double membrane. This is accomplished by two protein complexes, the Toc complex located at the outer membrane and the Tic complex located at the inner membrane. The Toc complex recognizes specific proteins by a cleavable N-terminal sequence and is primarily responsible for translocation through the outer membrane, while the Tic complex translocates the protein through the inner membrane. This entry represents Tic20, a core member of the Tic complex. This protein is deeply embedded in the inner envelope membrane and is thought to function as a protein- conducting component of the Tic complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182298   94 RRKTLLTPRASKDVPSSFRFPPMTKKPQWWWRTLACLPYLMPLHETWMYAETAYHLHPFLEDFEF---LTYPFLGAIGRL 170
Cdd:pfam16166   1 RRPTTLCRSASKDSLSAFDFPELAEKPEWWWRTLSCVPYLLPLFNGWQYGDTGYYLHPFLEQFPPfglLIYPIPGAINRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182298  171 PSWFLMAYFFVAYLGIVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSKWMPLGVYWGKFGMHFWTAVAFAYLFTVLESIR 250
Cdd:pfam16166  81 PSWFSMVYFFTLYFGVVRNKNLPHYFRFHVMMAMLLDVLLQVVLLTSNFNPLIGFGGKFGMYYWTGVFLFYIFTLLYCIR 160

                  ....
gi 334182298  251 CALA 254
Cdd:pfam16166 161 CALA 164

zinc finger HIT (zf-HIT) found in zinc finger HIT domain-containing protein 2 (ZNHIT2), 3 (ZNHIT3) and similar proteins; ZNHIT2 and ZNHIT3 are members of the zf-HIT domain-containing protein family that play crucial roles in various biological processes. ZNHIT2 acts as a bridging factor between the R2TP/PFDL complex and U5 snRNP, while ZNHIT3 interacts specifically with the ligand binding domain of the thyroid receptor and is involved in small nucleolar ribonucleoprotein particle assembly, transcriptional regulation, and snoRNP assembly. ZNHIT3 is also associated with HNF-4alpha and may play a role in MODY, while its dysfunction is linked to PEHO syndrome. Both proteins contain the zf-HIT domain and interact with other proteins through their HIT-type zinc finger in the presence of ATP, ADP, or other factors.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 334182298 256 SVCEECKQNPWKYKCPGCSIRSCALPCVKAHKQrtGCTG 294
Cdd:cd23024    1 RLCGVCNKNESKYKCPRCNIPYCSLACYKSHKE--SCSE 37

zinc finger HIT (zf-HIT) domain; The zinc finger HIT (zf-HIT) is a novel zinc-binding domain with about 50 amino acids. It is characterized by a fold in "treble-clef" through interleaved CCCC and CCHC zinc finger motifs that both bind a zinc ion. zf-HIT domain may function as a protein-protein interaction domain. It is mainly found in nuclear proteins involved in gene regulation and chromatin remodeling. The zf-HIT family includes six proteins containing zf-HIT domain present in human and three in yeast proteome, all belonging to multimodular RNA/protein complexes.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 334182298 257 VCEECKQNPWKYKCPGCSIRSCALPCVKAHK 287
Cdd:cd23020    1 TCGICGGYPGKYKCPRCGVPYCSLECYRKHL 31