ID A0A1E3HAB3_9TREE Unreviewed; 928 AA.
AC A0A1E3HAB3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=L202_08145 {ECO:0000313|EMBL:ODN72706.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN72706.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN72706.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN72706.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN72706.1}.
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DR EMBL; AWGJ01000014; ODN72706.1; -; Genomic_DNA.
DR RefSeq; XP_018988647.1; XM_019142984.1.
DR AlphaFoldDB; A0A1E3HAB3; -.
DR STRING; 1295533.A0A1E3HAB3; -.
DR GeneID; 30159454; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 445..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 651..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..379
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 102008 MW; EA9D18A862231A0D CRC64;
MPPKSPSTPR QRRGMRRGKQ PIASTPASPG EQAKQSKQQQ KHHHVVATAP VHLPLQKAGK
LSWTLLGLIF AILPWVFGRM HYALPEPLPP LDADGIPQPS EEVVRSHIQA LEDIGYRIVG
TPAALAGEQY VLDQVLELVE QCNARNVLNC EWWHQKGDGL HAFEILDHEV LKSYTGISNI
ILKISAFHPP SYDIHNPKPD KDAILLGAHI DSTFPSPGAA DDAIGVGVML DLARTLIHQN
NPFDNSIIFL FNGAEETLQD GSHLYSIEHS TRTQVKAVIN LEAAGSKGGA LLFQATSGEM
IEAYGKVPYP KGTVIAADVF SSGIIMSDTD FGQFEKYLGV SGLDMAIVGH SYFYHTHHDT
LSSIQPGSAQ HFTSNIHAVV SHLLSSSSPL SSTLPWSPPD KVYFGLFDKV FLYWDMKAAD
RWYTALAAVS GVMAVRRLKG EGWKVITTAS LATISGLAGG FIGPNLLAFT LTKLGKPLLW
FTHEHLAALI YIPTAFLSSL SIHLFFTHFL SPVERTKLEA VHYAVQMVWS SWMMLALQAV
RVRSAYLPAG ITLFLLIGAL GDGAVRVWGK EREGMNFKAT YLLPSIGLIA FFVEAITAAL
DIFTPLTGRM GKSAPAEHVI ATLTATCGLA LFPTLTPLFH RLPRQTQRKV VLVLKIWVAG
VVAGLGWVYD GEHPKRVGLN YNYNHTDQSH IIHIAFMDLG PIGTIPSSLH ARYALPSSPL
IHKDLEDEDH DWDAIYPVST FLDTYKFELD ISGQGSAQRL EGQEKEKEKG GWGGVEGVEN
FEWPEMGWSV KEKGGDGFRD VEITFNFTDL VWPVLSFHAH VLSWSFPAPA PPAEYMQHHI
KFANSVDSPL TTLKLRYKVE EPGQEKLGVH WSAFDVSQMN PFTTPHPGGG TGKPATVVLT
DMWDWIGEQW GGDLDLVTGG VVYGVVQI
//