| Type | Description |
|---|---|
| Definition | poly(A) polymerase Cid1 |
| Date | Results | Publications |
|---|---|---|
| 2015-06-27 10:16:00 | Data show that a hinge region (N164-N165) of terminal uridylyltransferase Cid1 is essential for catalytic activity. | 25712096 |
| 2014-05-24 10:34:00 | Structural analysis of Cid1 bound to a non-hydrolyzable nucleotide UMPNPP and bound to its minimal pseudo-product ApU revealed new key residues for the substrate/product recognition. | 24322298 |
| 2013-01-26 11:44:00 | This work demonstrates that Cid1 is able to accommodate all 4 tested ribonucleotide triphosphates (NTP) in the active site, but there are differences in recognition that suggest UTP is the preferred NTP. | 22885303 |
| 2012-10-27 10:12:00 | describe crystal structures of cytoplasmic terminal uridylyl transferase Cid1 in apo conformers and bound to UTP, and demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP | 22751018 |
| 2012-10-20 11:48:00 | Cid1 RNA binding properties, a feature with critical implications for miRNAs, histone mRNAs, and, more generally, cellular RNA degradation | 22608966 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
CID1_SCHPO
UniprotKB:
O13833
UniParc:
UPI0000127999
EMBL:
AF105076,
CU329670
EnsemblGenome:
SPAC19D5.03
KO:
spo:SPAC19D5.03
|
| Nucleutide sequences |
EMBL-CDS:
AAD16889.1,
CAB50789.1
Gene_ORFName:
SPAC19D5.03
EnsemblGenome_TRS:
SPAC19D5.03.1
|
| Protein sequencees |
EnsemblGenome_PRO:
SPAC19D5.03.1:pep
RefSeq:
NP_594901.1
|
| Others |
UniRef100:
UniRef100_O13833
UniRef90:
UniRef90_O13833
UniRef50:
UniRef50_O13833
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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