Q11010

PR
Gene name
pepN
Protein name
Aminopeptidase N
Names
Alanine aminopeptidase, Lysyl aminopeptidase, Lys-AP
Species
Streptomyces lividans
KEGG Pathway
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

693-769 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q11010

Entry ID Method Resolution Chain Position Source
AF-Q11010-F1 Predicted AlphaFoldDB

No variants for Q11010

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q11010

No associated diseases with Q11010

3 regional properties for Q11010

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 230 - 445 IPR014782
domain ERAP1-like C-terminal domain 535 - 844 IPR024571
domain Aminopeptidase N-like, N-terminal domain 107 - 188 IPR045357

Functions

Description
EC Number
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
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds 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.
zinc ion binding Binding to a zinc ion (Zn).

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
MPGTNLTREE ARQRATLLTV DSYEIDLDLT GAQEGGTYRS VTTVRFDVAE GGGESFIDLV
70 80 90 100 110 120
APTVHEVTLN GDALDTAEVF QDSRIALPGL LPGRNILRVV ADCAYTNTGE GLHRFVDPVD
130 140 150 160 170 180
DQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPEGW TVISNSPTPE PKDNVWEFEP
190 200 210 220 230 240
TPRISSYVTA LIVGPYHSVH SVYEKDGQSV PLGIYCRPSL AEHLDADAIF EVTRQGFDWF
250 260 270 280 290 300
QEKFDYAYPF KKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAATILHEL
310 320 330 340 350 360
AHMWFGDLVT MEWWNDLWLN ESFATYAEAA CQAAAPGSKW PHSWTTFANQ MKTWAYRQDQ
370 380 390 400 410 420
LPSTHPIMAD ISDLDDVLVN FDGITYAKGA SVLKQLVAYV GEEAFFKGVQ AYFKRHAFGN
430 440 450 460 470 480
TRLSDLLGAL EETSGRDLKT WSKAWLETAG INVLRPEIET DADGVITSFA IRQEAPALPA
490 500 510 520 530 540
GAKGEPTLRP HRIAIGAYDL DGAGKLVRGD RVELDVDGEL TAVPQLVGKA RPAVLLLNDD
550 560 570 580 590 600
DLSYAKVRLD EQSLAVVTEH LGDFTESLPR ALCWASAWDM TRDAELATRD YLALVLSGIG
610 620 630 640 650 660
KESDIGVVQS LHRQVKLAID QYAAPTAREA LLTRWTEATL AHLRAAEAGS DHQLAWARAF
670 680 690 700 710 720
AATARTPEQL DLLDALLDGT QTIEGLAVDT ELRWAFVQRL AAVGRFGGSE IAAEYERDKT
730 740 750 760 770 780
AAGERHAATA RAARPTEAAK AEAWESVVES DKLPNAVQEA VIAGFVQTDQ RELLAAYTER
790 800 810 820 830 840
YFEALKDVWA SRSHEMAQQI AVGLYPAVQV SQDTLDRTDA WLASAEPNAA LRRLVSESRS
850
GIERALRAQA ADAAAAE