A1DF27

PR
Gene name
ampp (NFIA_079250)
Protein name
Probable Xaa-Pro aminopeptidase P
Names
AMPP, Aminopeptidase P, Aminoacylproline aminopeptidase, Prolidase
Species
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
KEGG Pathway
nfi:NFIA_079250
EC number
3.4.11.9: Aminopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

169-249 (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 A1DF27

Entry ID Method Resolution Chain Position Source
AF-A1DF27-F1 Predicted AlphaFoldDB

No variants for A1DF27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1DF27

No associated diseases with A1DF27

5 regional properties for A1DF27

Type Name Position InterPro Accession
domain Creatinase, N-terminal 49 - 183 IPR000587
domain Peptidase M24 361 - 577 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 519 - 531 IPR001131
domain Peptidase M24, C-terminal domain 590 - 652 IPR032416
domain Aminopeptidase P 361 - 587 IPR033740

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

1 GO annotations of cellular component

Name Definition
cellular anatomical entity A part of a cellular organism that is either an immaterial entity or a material entity with granularity above the level of a protein complex but below that of an anatomical system. Or, a substance produced by a cellular organism with granularity above the level of a protein complex.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
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
MLGFRSPIRL CKLSALGSAP LLPISRPKLF STAVARYAAD METVNTTERL ARLRQLMQEH
70 80 90 100 110 120
KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SMTKAALSTD GRYFNQASKQ
130 140 150 160 170 180
LDSNWELLKR GVENVPTWQE WTTEQAEGGK VVGVDPSLIT ASGARSLEET LKRNGSSLVG
190 200 210 220 230 240
ISQNLVDLVW GKDRPAPPRE KVRVHPDKFA GKTFQEKIAD LRKELEKKKT AGFVISMLDE
250 260 270 280 290 300
IAWLFNLRGS DIPYNPVFFA YAIITPTKAE LYIDDDKITP EVVAHLGQDV VIKPYNSIFA
310 320 330 340 350 360
DAKALSEARK QEAGETASKF LLSNKASWAL SLSLGGEEHV EETRSPIADA KAIKNEVELA
370 380 390 400 410 420
GMRACHIRDG AALIEYFAWL ENELVNKKTV LDEVDAADKL ERIRTKHDLF AGLSFDTISS
430 440 450 460 470 480
TGPNGAVIHY KPEKGTCSII DPDAIYLCDS GAQYLDGTTD VTRTFHFGKP TELEKKAFTL
490 500 510 520 530 540
VLKGLIAIDT AVFPKGTSGF ALDALARQYL WKEGLDYLHG TGHGIGSYLN VHEGPIGIGT
550 560 570 580 590 600
RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA
610 620 630 640 650
PIGRNLIQPS LLSDLELKWV NDYHAEVWDK THHFFENDEF TRSWLQRETA PITK