Q9V3D6

PR
Gene name
Cpsf100 (CG1957)
Protein name
Probable cleavage and polyadenylation specificity factor subunit 2
Names
Cleavage and polyadenylation specificity factor 100 kDa subunit, CPSF 100 kDa subunit
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG1957
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

161-245 (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 Q9V3D6

Entry ID Method Resolution Chain Position Source
AF-Q9V3D6-F1 Predicted AlphaFoldDB

No variants for Q9V3D6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9V3D6

No associated diseases with Q9V3D6

6 regional properties for Q9V3D6

Type Name Position InterPro Accession
domain Metallo-beta-lactamase 17 - 223 IPR001279
domain Zn-dependent metallo-hydrolase, RNA specificity domain 539 - 600 IPR011108
domain Beta-Casp domain 243 - 369 IPR022712
domain Cleavage and polyadenylation specificity factor 2, C-terminal 617 - 655 IPR025069-1
domain Cleavage and polyadenylation specificity factor 2, C-terminal 660 - 753 IPR025069-2
domain CPSF2, metallo-hydrolase domain 7 - 204 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.

3 GO annotations of biological process

Name Definition
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
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
O17403 cpsf-2 Probable cleavage and polyadenylation specificity factor subunit 2 Caenorhabditis elegans PR
10 20 30 40 50 60
MTSIIKLHTI SGAMDESPPC YILQIDDVRI LLDCGWDEKF DANFIKELKR QVHTLDAVLL
70 80 90 100 110 120
SHPDAYHLGA LPYLVGKLGL NCPIYATIPV FKMGQMFMYD LYMSHFNMGD FDLFSLDDVD
130 140 150 160 170 180
TAFEKITQLK YNQTVSLKDK GYGISITPLN AGHMIGGTIW KIVKVGEEDI VYATDFNHKK
190 200 210 220 230 240
ERHLSGCELD RLQRPSLLIT DAYNAQYQQA RRRARDEKLM TNILQTVRNN GNVLIAVDTA
250 260 270 280 290 300
GRVLELAHML DQLWKNKESG LMAYSLALLN NVSYNVIEFA KSQIEWMSDK LTKAFEGARN
310 320 330 340 350 360
NPFQFKHIQL CHSLADVYKL PAGPKVVLAS TPDLESGFTR DLFVQWASNA NNSIILTTRT
370 380 390 400 410 420
SPGTLAMELV ENCAPGKQIE LDVRRRVDLE GAELEEYLRT QGEKLNPLIV KPDVEEESSS
430 440 450 460 470 480
ESEDDIEMSV ITGKHDIVVR PEGRHHSGFF KSNKRHHVMF PYHEEKVKCD EYGEIINLDD
490 500 510 520 530 540
YRIADATGYE FVPMEEQNKE NVKKEEPGIG AEQQANGGIV DNDVQLLEKP TKLISQRKTI
550 560 570 580 590 600
EVNAQVQRID FEGRSDGESM LKILSQLRPR RVIVIHGTAE GTQVVARHCE QNVGARVFTP
610 620 630 640 650 660
QKGEIIDVTS EIHIYQVRLT EGLVSQLQFQ KGKDAEVAWV DGRLGMRVKA IEAPMDVTVE
670 680 690 700 710 720
QDASVQEGKT LTLETLADDE IPIHNSVLIN ELKLSDFKQT LMRNNINSEF SGGVLWCSNG
730 740 750
TLALRRVDAG KVAMEGCLSE EYYKIRELLY EQYAIV