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 Q2HA12

Entry ID Method Resolution Chain Position Source
AF-Q2HA12-F1 Predicted AlphaFoldDB

No variants for Q2HA12

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2HA12

No associated diseases with Q2HA12

3 regional properties for Q2HA12

Type Name Position InterPro Accession
domain Peptidase M24 257 - 570 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 424 - 436 IPR001131
domain Aminopeptidase P, N-terminal 93 - 226 IPR007865

Functions

Description
EC Number 3.4.11.9 Aminopeptidases
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
manganese ion binding Binding to a manganese ion (Mn).
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

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
MEFCDESYDL VNIDEFDALW VASRHGVAFG VPPCLLISDD DAIARSSIEL KSGPSSSNLS
70 80 90 100 110 120
PSTLSTEKTS SDSSGVICDP QLHETWREGL GKFPAKEHAR KVARELGADH GIIFLLGQDE
130 140 150 160 170 180
KYYEDSDMGP TFRQRRYFYY ITGADFPGCA VTYDILRDKL VLWIPRIEPR TVLWFGKVPT
190 200 210 220 230 240
PEECKAASDV DSVYYIDFLH EKQCPVFKRG QTIHVLHPDQ IPPELDHLGK FIRIDAVRLK
250 260 270 280 290 300
PAMDAARVIK TDYEIALIRR ANAVSSAAHK AVLRNIKRFT NEREIDALFR GYCIAHGAPI
310 320 330 340 350 360
QSYPVIAASG INASTLHYDD NNQSLKNRQL LILDAGAEVH CYASDITRTI PLPGSFTPLA
370 380 390 400 410 420
REIYRLVERM QDECIAQIKP GVRFSALHAH ACAVAVTGLL KLGILRGEEE EILARGTVAA
430 440 450 460 470 480
FFPHGLGHHV GLEVHDVSGT ERLLLNGGPG SGPGSGGGYG CGASTWRGYR LRRRVMTKRE
490 500 510 520 530 540
SLTPWEVAAL WEGAKPEKEK QQERWLLNNV PLDEVEAALT LASSSGARGQ KLAPGMVVTV
550 560 570 580 590
EPGIYFLPRV LEKYWNVGGV RIEDDILVTK KGYENLTTAP KGDEMMKCMG ESGLL