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 Q96ZT9

Entry ID Method Resolution Chain Position Source
AF-Q96ZT9-F1 Predicted AlphaFoldDB

No variants for Q96ZT9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q96ZT9

No associated diseases with Q96ZT9

3 regional properties for Q96ZT9

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 199 - 415 IPR014782
domain ERAP1-like C-terminal domain 484 - 775 IPR024571
domain Aminopeptidase N-like, N-terminal domain 9 - 165 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
MVNVERYEIF LDFNEYSYEG MEKIKMKSDG EKVELDSVGL EIKEVKADGK QVKYETKNEK
70 80 90 100 110 120
LIVYSKVNEE LEIRFSGKAD NKSILGIYVA PYDGNYLITT QFEPIYARKF IPCFDSPDMK
130 140 150 160 170 180
AVFKLSVRVN RGQKVISNMP IISIRDDGEK IVYEFDETPR MSTYLLYLGI GDFEEISDES
190 200 210 220 230 240
KKPKIILATT PGKSKRGIFA IEVARKVIDY YEKYFEIPYQ LPKLHLIEIP EFAAGAMENW
250 260 270 280 290 300
GAITFRESAL LADESSSVSQ KLSVSAVIAH ELAHQWFGDM VTLKWWDDLW LNESFATFMA
310 320 330 340 350 360
YKSLKEIFPQ WESEGHFIYD ETLSALTEDS LLNTHPIETH VKDPHEIEEM FDNISYGKGA
370 380 390 400 410 420
SILRMIEAYV GEEVFRRGVV NYLNKFKFSN ASGSDLWNSI SEAYGSDISQ IMAEWITKPG
430 440 450 460 470 480
YPVITVNVEG DSVEFFQRRF TLLNVNDSTI YKVPLTFEVN GKRQTLLLDK ESVKLNFDNA
490 500 510 520 530 540
VSSIKVNLNR TGFYRVLYKP FELSFSSTLN SYEELGLVND YWNFLLAGLE SIKTYLTLIK
550 560 570 580 590 600
RFSNTRNSFL SREIAFELMT LYYINKDKYY SIARDFLLNQ IKIYRNAKDD LGKMAYSSII
610 620 630 640 650 660
RSLAIVDDDF ALGLSNLFQY YEQLDSNIKG AVAIAYAIST SDFNGLLDKY KSFNSDEEKL
670 680 690 700 710 720
RMIDAITNIR DKSIVEKLAM LVFNRTIKYQ EAPHVINSLS NNPYVREELC NFLQGNFDMI
730 740 750 760 770 780
KQFVVTVAGM WGLFYIIRGP MIMCGVNKPE ETIEFLDRIK TKEIARSVEI TKEYIKVYNR
VKNLDL