Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A8XUS3

Entry ID Method Resolution Chain Position Source
AF-A8XUS3-F1 Predicted AlphaFoldDB

No variants for A8XUS3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8XUS3

No associated diseases with A8XUS3

5 regional properties for A8XUS3

Type Name Position InterPro Accession
domain Metallo-beta-lactamase 17 - 222 IPR001279
domain Zn-dependent metallo-hydrolase, RNA specificity domain 563 - 615 IPR011108
domain Beta-Casp domain 242 - 368 IPR022712
domain Cleavage and polyadenylation specificity factor 2, C-terminal 642 - 810 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.

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTSIIKLKVF SGAKDEGPLC YLLQVDNDYI LLDCGWDERF ELKYFEELRP YIPKISAVLI
70 80 90 100 110 120
SHPDPLHLGG LPYLVAKCGL TAPVYCTVPV YKMGQMFIYD LVYSHLDVEE FQHYSLDDVD
130 140 150 160 170 180
MAFEKVEQVK YNQTVVLKGD SGVNFTAMPA GHMIGGSMWR ICRITGEDII YCVDFNHRKD
190 200 210 220 230 240
RHLSGCSFDN FNRPHLLITG AHHISLPQMK RKDRDEQLVT KILRTVRQKG DCMIVIDTAG
250 260 270 280 290 300
RVLELAYLLD QLWANQDAGL STYNLVMMSH VASSVVQFAK SQLEWMDEKL FRYDSSSARY
310 320 330 340 350 360
NPFTLKNVNL VHSHLELIKI RSPKVVLCSS QDMETGFSRE LFLDWCADQR NGVILTARPA
370 380 390 400 410 420
SFTLAARLVE LAERANDGVL RNEDKHLSLL VRKRVPLEGE ELLEYKRRKA ERDAEETRIR
430 440 450 460 470 480
MERARRQAQA NESDDSDDDD IAAPIVPRLS EKDHRSFDAI ENDSHCFDIM AKWDNQQKAS
490 500 510 520 530 540
FFKSTKKSFP MYPYIEEKVK WDDYGEVIKP EDYTVISKID MRKGKNKDEP VVVHKREDEE
550 560 570 580 590 600
EVYNPNDHDE EMPTKCVEFR NRIEISCRVE FIEYEGISDG ESTKKMLAGL MPRQIIIVHG
610 620 630 640 650 660
SRDDTRDLYA YFTDNGFKKD QLNTPVANEL IDASVESFIY QVSLSDALLA EIQFKEVSEG
670 680 690 700 710 720
NSLAWIDARI QEKESIDNML VAGASQLTIE DSLQEDAVEV VEEDVIPMET FQDDQNKQEA
730 740 750 760 770 780
SEENVAEGEK SNGQSKENDE NASSIPIETQ PKIRGTLILT PLPKKQIPVH QAIFVNDPKL
790 800 810 820 830 840
SEFKNLLVDK GYKAEFFSGT LLINGGKCSI LVERLDSKWR VLSQKTFTNF GSCSTTSLLF
CK