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 Q8YRP3

Entry ID Method Resolution Chain Position Source
AF-Q8YRP3-F1 Predicted AlphaFoldDB

No variants for Q8YRP3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8YRP3

No associated diseases with Q8YRP3

5 regional properties for Q8YRP3

Type Name Position InterPro Accession
domain Orn/DAP/Arg decarboxylase 2, N-terminal 139 - 390 IPR022644
binding_site Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site 146 - 164 IPR022653
conserved_site Orn/DAP/Arg decarboxylase 2, conserved site 322 - 338 IPR022657
domain Arginine decarboxylase, helical bundle domain 416 - 497 IPR040634
domain Arginine decarboxylase, C-terminal helical 624 - 677 IPR041128

Functions

Description
EC Number 4.1.1.19 Carboxy-lyases
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
arginine decarboxylase activity Catalysis of the reaction: L-arginine + H(+) = agmatine + CO(2).
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
arginine catabolic process The chemical reactions and pathways resulting in the breakdown of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
spermidine biosynthetic process The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKHRGQEEMG VESTATSDEV VKVPANGNKL EGKNHKQKKL LPTNTPGDVS RVWKIEDSEA
70 80 90 100 110 120
LYRIEGWGQP YFSINAAGHV TVSPKGDRGG SLDLFELVNA LKQRSLGLPL LIRFSDILED
130 140 150 160 170 180
RIERLNACFA KAIARYNYPG VYRGVFPVKC NQQRHLIEDL VRFGRPHQFG LEAGSKPELM
190 200 210 220 230 240
IALALLDTPG SLLICNGYKD REYVETAMLS QRLGQTPIIV LEQVEEVDLV IAASHQLGIK
250 260 270 280 290 300
PILGVRAKLS TQGMGRWGTS TGDRAKFGLT IPEIIQAVDK LRDADLLDSL QLMHFHIGSQ
310 320 330 340 350 360
ISAINVIKDA IQEASRIYVE LASLGANMKY LDVGGGLGVD YDGSQTNFYA SKNYNMQNYA
370 380 390 400 410 420
NDIVAELKDT CAEKQIPVPT LISESGRAIA SHQSVLIFDV LSTSDVPRDN PEPPKEGESP
430 440 450 460 470 480
VINYLWETYQ SINKENYQEF YHDATQFKEE AISRFNLGIL RLRERAKAER LYWACCQKIL
490 500 510 520 530 540
DIIRQHDYVP DELEDLEKIM ASIYYINLSV FQSAPDCWAI DQLFPIMPIH RLDEEPTQRG
550 560 570 580 590 600
ILADLTCDSD GKIDRFIDLR DVKSVLELHP FQPGEPYYMG MFLNGAYQEI MGNLHNLFGD
610 620 630 640 650 660
TNAVHIQLTP KGYQIEHVVK GDTMSEVVSY VQYDSEDMVE NIRQRCERAL EEKRITLAES
670
QRLLQTYEQS LRRYTYLNS