ID A0A182W135_9DIPT Unreviewed; 1243 AA.
AC A0A182W135;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000256|ARBA:ARBA00014190};
DE EC=3.4.11.1 {ECO:0000256|ARBA:ARBA00012565};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.13.23 {ECO:0000256|ARBA:ARBA00023625};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000256|ARBA:ARBA00030997};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|ARBA:ARBA00033172};
DE AltName: Full=Proline aminopeptidase {ECO:0000256|ARBA:ARBA00030930};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN004044-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN004044-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN004044-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000256|ARBA:ARBA00023511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000256|ARBA:ARBA00023511};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A182W135; -.
DR STRING; 112268.A0A182W135; -.
DR EnsemblMetazoa; AMIN004044-RA; AMIN004044-PA; AMIN004044.
DR VEuPathDB; VectorBase:AMIN004044; -.
DR OrthoDB; 1126684at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd00433; Peptidase_M17; 1.
DR CDD; cd16504; RING-HC_COP1; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR042755; COP1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR44080; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR PANTHER; PTHR44080:SF1; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR Pfam; PF00400; WD40; 3.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 57..95
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 551..593
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 637..671
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 133343 MW; 36CD6C4D942ACE89 CRC64;
MSSGTGGGAS SSSAGGGGAG IGGAGSSSSG SSSGKKRLAT LNGIPTSVDD KTNDFLCPIC
FDIINEAYIT RCGHTFCHQC IARSIDVAKK CPKCNYPLAS HEHIVPNFLL NELITKHRLK
GGGVSGGLLH RHNKSLPGEH SPQLHAGGGA CGGGDATAGG EGDTLKHFLA TESKKLSLSD
VNVMLEILTQ RKTLLEAESC AAQNRLLHEF LKHLLKQKEQ QQLQIANEIA LIRNDLLDVE
KVLKDVQSSC PTVAEVEQSV RDEKDENVVA IKREIIQIID TIDNITVPSN RSLIDDTCST
VSESYEGFNL HGTRRGQGGS VLGGSLSSTP SSFLARKQRM YQHFDDFVQC YFAARSEDLY
FGKDRSCSSD SLGVGERSTS SGASIGTGGG GGGGSLNSDR LMGGVQPAPT SNTSSQSNLD
NTRSSGRSSL DTFRESLIKF SKYSALRPLA TLNYSNDSNY VSTIVSSIEF DKDSEYFAIA
GVTKRIKIFD YYTAIRDAAV DINYPINEMT CNSKISCVIW NSYFKQVLAS SDYEGIVTIW
DVLTRTRTKT FEEHDKRCWC VDFNEVDTRL LASGSDDARV KLWSLNVDHS VATIEARANV
CCVKFNPKSS CHLAFGTADH CVNYYDLRNL KQPLCLFKGH RKAVSYVKFL NTDEIVSAST
DGQLKLWNIN SPPFCLRSFT GHINEKNFAG LATNNDYLAC GSEDNSLCVY YKGLSKQLFN
LKFSSGGSGS GSGGGSGSAA GTGSSSGIGN SSSRTSGLQS TDMERSNSEG NEFVSAVCWR
KQSNIIIAGN SEGVIKILEI VCGPVKAGQT RIFWDLGKFP AVAVAGLGDA SKWDELDEID
GAKENVRIAA AAGVRALSAN KMTEIVVEDM EHAQQAAEGA TLANYKFQAF KSKDKQTPLP
AVAFAEDASG KADWDRGVII AEAQNFARVL METPANHMTP SIFVDTVKQR LSAANVEVLV
HDEAWAREKK MGSFLSVTNG SDEPARFLEL TYRGSQDAKC VALVGKGITF DSGGISLKPS
ANMDQMRADM GGAANVVSTI LALAQLKAPV HVKGFVPLCE NMPSGRATKP GDVVYAMNGK
SICVDNTDAE GRLILADALC YASTFNPKFI LDIATLTGAI KVALGDCVSG VFSSNNKLWD
AIHEAGSQTG DRVWRMPLFK HYSEQMCDHN GYDLNNLGKG KGAGSCTAAA FLREFVPKDT
PWLHVDIAGV MGDCSDQSYT GSKGMTGRPM RTLVEFVTKA GSA
//
