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

0 structures for P22602

Entry ID Method Resolution Chain Position Source

No variants for P22602

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P22602

No associated diseases with P22602

3 regional properties for P22602

Type Name Position InterPro Accession
domain Peptidase S30, polyprotein P1, potyvirus 41 - 284 IPR002540
domain Helper-component proteinase (HC-Pro) cysteine protease (CPD) domain 618 - 740 IPR031159
domain Potyviral polyprotein protein 3 771 - 856 IPR039560

Functions

Description
EC Number 3.4.22.45 Cysteine endopeptidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
cysteine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
serine-type peptidase activity Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATYMSTICF GSFECKLPYS PASCGHIVKE REVPASVDPF ADLETQLSAR LRKQEYATVR
70 80 90 100 110 120
VLKNGTFTYR YKTDAQIMRI QKKLERKDRE EYHFQMAAPS IVSKITIAGG DPPSKSEPQA
130 140 150 160 170 180
PRGIIHTTPK VRKVKTRPII KLTEGQMNHL IKQVKQIMSE KRGSVHLISK KTTHVQYKEI
190 200 210 220 230 240
LGATRAAVRT AHMMGLRRRV DFRCDTWTVG LLQRLARTDK WSNQVRTIHV RRGDSGVILN
250 260 270 280 290 300
TKSLKGHFGR SSGDLFIVRG SHEGKLYDAR SRVTQSVLNS MIQFSNADNF WKGLDGNWAR
310 320 330 340 350 360
MRYPSDHTCV AGLPVADCGR VAALTRHSIL PCYKITCPTC AQQYASLPVS DLFKLLHKHA
370 380 390 400 410 420
RDGLNRLGAD KDRFIHVNKF LMALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
430 440 450 460 470 480
NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAR ANWNLYLSCD
490 500 510 520 530 540
NQLDKNANFL WGQREYHAKR FFSNFFDEID PAKGYSAYEI RKHPNGTRKL SIGNLVVPLD
550 560 570 580 590 600
LAEFRQKMKG DYRKQPGVSR KCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
610 620 630 640 650 660
NSGDQKFVDL PKGDSEMLYI AKQGYCYINV FLAMLINISE EDAKDFTKKV RDMCVPKLGT
670 680 690 700 710 720
WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
730 740 750 760 770 780
QLILFANDEL ESDIKHYRVG GVPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPR
790 800 810 820 830 840
VMRQLLLDEP YLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
850
SAAETLVAQR IIIDAA