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 Q59536

Entry ID Method Resolution Chain Position Source
AF-Q59536-F1 Predicted AlphaFoldDB

No variants for Q59536

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q59536

No associated diseases with Q59536

3 regional properties for Q59536

Type Name Position InterPro Accession
domain Peptidase S9, prolyl oligopeptidase, catalytic domain 464 - 679 IPR001375
active_site Peptidase S9, serine active site 509 - 539 IPR002471
domain Peptidase S9A, N-terminal domain 4 - 403 IPR023302

Functions

Description
EC Number 3.4.21.83 Serine endopeptidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 GO annotations of molecular function

Name Definition
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
MKLPIAKRIP HPHELHGDVR EDDYYWLKDR DNTEVIQYLE EENRYYHEIM RPLQEQTEQI
70 80 90 100 110 120
YESMVDRVPD SEMKVPVQHG QFFYYSRLDK NKQYPIYARK QAASRALLQD ATEEVVLDLN
130 140 150 160 170 180
ELAEEDDYLS VTVQRMTTDH SRLAYLENRD GTDRYTIYIK DLNTGELLSD RVPNVYIYGS
190 200 210 220 230 240
MEWCRCGDYI FYTTVDEHQR PCQLWRHRLG SDVESDELIF EEKDDTFTLF ISKSQSGKFI
250 260 270 280 290 300
FVYSSSKTTS EIHMIDTDSP LSPLQLVDER RDGILYDVEH WEDDLLILTN EGALNFQLLR
310 320 330 340 350 360
CPLNDLSSKV NVVEYNEERY LQEMYPFRDK LLIAGRENGL TQIWVVHDGE LQQISWDEPL
370 380 390 400 410 420
YTVAVLSEQS YDTNEVLIQY ESLLTPKTTF GLNLQTGEKQ CLQVAPVSGE YDRSQFRQEQ
430 440 450 460 470 480
LWATGRSGVK VPMTAVYLEG ALDNGPAPLI LYGYGSYGSN SDPRFDPYRL PLLEKGIVFV
490 500 510 520 530 540
TAQVRGGSEM GRGWYEDGKM QNKRNTFTDF IAAAKHLIDQ NYTSPTKMAA RGGSAGGLLV
550 560 570 580 590 600
GAVANMAGEL FKVIVPAVPF VDVVTTMLDT SIPLTTLEWD EWGDPRKQED YFYMKSYSPY
610 620 630 640 650 660
DNVEAKDYPH MYITTGINDP RVGYFEPAKW VARLRAVKTD NNTLVMKTNM GAGHFGKSGR
670 680
FNHLKEAAES YAFILDKLGV EAEEKVLNHR