O17403

PR
Gene name
cpsf-2 (F09G2.4)
Protein name
Probable cleavage and polyadenylation specificity factor subunit 2
Names
Cleavage and polyadenylation specificity factor 100 kDa subunit, CPSF 100 kDa subunit
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F09G2.4
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

500-570 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O17403

Entry ID Method Resolution Chain Position Source
AF-O17403-F1 Predicted AlphaFoldDB

No variants for O17403

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O17403

No associated diseases with O17403

5 regional properties for O17403

Type Name Position InterPro Accession
domain Metallo-beta-lactamase 17 - 222 IPR001279
domain Zn-dependent metallo-hydrolase, RNA specificity domain 563 - 619 IPR011108
domain Beta-Casp domain 242 - 368 IPR022712
domain Cleavage and polyadenylation specificity factor 2, C-terminal 642 - 840 IPR025069
domain CPSF2, metallo-hydrolase domain 10 - 203 IPR035639

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mRNA cleavage and polyadenylation specificity factor complex A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.

1 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.

4 GO annotations of biological process

Name Definition
mRNA 3'-end processing Any process involved in forming the mature 3' end of an mRNA molecule.
mRNA 3'-end processing by stem-loop binding and cleavage Any mRNA 3'-end processing that involves the binding to and cleavage of a stem-loop structure. For example, histone mRNAs contain a highly conserved stem-loop sequence at the 3' end of the mRNA with a 6 base pairs (bp) stem and a 4-nt loop. The mRNA is cleaved between these two elements, after the fourth or fifth nucleotide, which is typically an adenosine.
mRNA polyadenylation The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
pre-mRNA cleavage required for polyadenylation The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12102 CFT2 Cleavage factor two protein 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9V3D6 Cpsf100 Probable cleavage and polyadenylation specificity factor subunit 2 Drosophila melanogaster (Fruit fly) PR
Q9P2I0 CPSF2 Cleavage and polyadenylation specificity factor subunit 2 Homo sapiens (Human) PR
O35218 Cpsf2 Cleavage and polyadenylation specificity factor subunit 2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MTSIIKLKVF SGAKDEGPLC YLLQVDGDYI LLDCGWDERF GLQYFEELKP FIPKISAVLI
70 80 90 100 110 120
SHPDPLHLGG LPYLVSKCGL TAPVYATVPV YKMGQMFIYD MVYSHLDVEE FEHYTLDDVD
130 140 150 160 170 180
TAFEKVEQVK YNQTVVLKGD SGVHFTALPA GHMLGGSIWR ICRVTGEDIV YCVDFNHKKE
190 200 210 220 230 240
RHLNGCSFDN FNRPHLLITG AHHISLPQMR RKDRDEQLVT KILRTVRQKG DCMIVIDTAG
250 260 270 280 290 300
RVLELAHLLD QLWSNADAGL STYNLVMMSH VASSVVQFAK SQLEWMNEKL FKYDSSSARY
310 320 330 340 350 360
NPFTLKHVTL CHSHQELMRV RSPKVVLCSS QDMESGFSRE LFLDWCSDPR NGVILTARPA
370 380 390 400 410 420
SFTLAAKLVN MAERANDGVL KHEDRLISLV VKKRVALEGE ELLEYKRRKA ERDAEETRLR
430 440 450 460 470 480
MERARRQAQA NESDDSDDDD IAAPIVPRHS EKDFRSFDGS ENDAHTFDIM AKWDNQQKAS
490 500 510 520 530 540
FFKTTKKSFP MFPYIEEKVK WDDYGEVIKP EDYTVISKID LRKGQNKDEP VVVKKREEEE
550 560 570 580 590 600
EVYNPNDHVE EMPTKCVEFK NRVEVSCRIE FIEYEGISDG ESTKKLLAGL LPRQIIVVHG
610 620 630 640 650 660
SRDDTRDLVA YFADSGFDTT MLKAPEAGAL VDASVESFIY QVALSDALLA DIQFKEVSEG
670 680 690 700 710 720
NSLAWIDARV MEKEAIDNML AVGTSNLMID DKNREEDVND QEENGATEGE GNAEPMEIGE
730 740 750 760 770 780
NGSQESLAIS ESGKEVENGH TNDSRTKKGT KGKIRGNLIL DPLPKRLIPI HQAVFVNDPK
790 800 810 820 830 840
LSDFKNLLTD KGYKAEFLSG TLLINGGNCS IRRNDTGVFQ MEGAFTKDYY KLRRLFYDQF
AVL