O61142

PR
Gene name
SUB1
Protein name
Subtilisin-like protease 1
Names
EC 3.4.21.62 , PfSUB-1
Species
Rattus norvegicus (Rat)
KEGG Pathway
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

37-97 (Belt subunit) EV

Target domain

330-668 (Catalytic core of Sub1)

Relief mechanism

Cleavage

Assay

Deletion assay, Structural analysis

137-217 (Bacterial PD-like domain) EV

Target domain

330-668 (Catalytic core of Sub1)

Relief mechanism

Cleavage

Assay

Deletion assay, Structural analysis

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for O61142

Entry ID Method Resolution Chain Position Source
4LVN X-ray 225 A PDB
4LVO X-ray 226 A PDB
AF-O61142-F1 Predicted AlphaFoldDB

No variants for O61142

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O61142

No associated diseases with O61142

3 regional properties for O61142

Type Name Position InterPro Accession
domain Protein kinase domain 11 - 347 IPR000719
active_site Serine/threonine-protein kinase, active site 132 - 144 IPR008271
binding_site Protein kinase, ATP binding site 17 - 40 IPR017441

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-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
MATIQSETDC YDIIEVLGKG TFGEVAKGWR RSTGEMVAIK ILKNDAYRSR IIKNELKLLR
70 80 90 100 110 120
CVRGLDPDEA HVIRFLEFFH DALKFYLVFE LLEQNLFEFQ KENNFAPLPA RHIRTVTLQV
130 140 150 160 170 180
LRALARLKEL AIIHADLKPE NIMLVDQTRC PFRVKVIDFG SASIFSEVRY VKEPYIQSRF
190 200 210 220 230 240
YRAPEILLGL PFCEKVDVWS LGCVMAELHL GWPLYPGNNE YDQVRYICET QGLPKPHLLH
250 260 270 280 290 300
AARKAHHFFK RNPHPDATNP WQLKSSADYL AETKVRPLER RKYMLKSLDQ IETVNGGGAV
310 320 330 340 350 360
NRLSFPDREA LAEHADLKSM VELIKRMLTW ESHERISPSA ALRHPFVSMQ QLRSAHEATR
370 380 390 400 410 420
YYQLSLRGCR LSLQVDGKPP PPVIANAEDG PPYYRLAEEE ETAGLGGVTG SGSFFREDKA
430 440 450 460 470 480
PGMQRAIDQL DDLSLQEARR GLWSDTRADM VSDMLAPLKV ATTSHRVPDS GPEPILAFYG
490 500 510 520 530 540
SRLTGRHKAR KAPAGSKSDS NFSNLIRLSQ ASPEDAGSCR GSGWEEGEGH TTSTEPSAIP
550 560 570 580 590 600
QREGDGPSIK DRPMDAERSG PELFDPSGCP GEWLNEPEWT LEGIRGSRAQ GLPARHPHPH
610
GPPRTTSFLQ HVGGHH