ID A0A0L0HTH4_SPIPD Unreviewed; 1155 AA.
AC A0A0L0HTH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=tubulin-glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00026108};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
GN ORFNames=SPPG_00353 {ECO:0000313|EMBL:KND04636.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KND04636.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KND04636.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KND04636.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] +
CC H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-
CC glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-
CC COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; KQ257450; KND04636.1; -; Genomic_DNA.
DR RefSeq; XP_016612675.1; XM_016748681.1.
DR AlphaFoldDB; A0A0L0HTH4; -.
DR STRING; 645134.A0A0L0HTH4; -.
DR GeneID; 27684086; -.
DR VEuPathDB; FungiDB:SPPG_00353; -.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; A0A0L0HTH4; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000053201; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF45; CYTOSOLIC CARBOXYPEPTIDASE NNA1; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000053201}.
FT DOMAIN 685..789
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 831..948
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 127741 MW; A54F780A5779FCB3 CRC64;
MSPAARSPSH KKTDKMVKKT SGSKKKAHGI GSLRPKKAAS MPELGECSGN IRSGRILNLP
KISKSRENFS SSVSQSIPIT NSTTGLSSPG CLRILEKLSE LITNPWSPSH PNGLPPRPPS
STSSRSSAST KTETASVRRA SDPPFTSARW KHDKRKTRSY PNVGLARRGS DGSLPELSIG
RHGVRRRSGS RSGDDETGVE VGGSRLRDGS GPVDGPRSAP GTPPISADVR NKIGKQFLAL
KRLMDKEGVH ADSPLQKTLF SKSSPNISLL VKCLRILLDV DICIIITNLL IRLTTTTDSN
ANNTAFMAKK GLAVALLKCL QSLHGEYLSG DIGVGPPNHH QRVDELMGNL FVLVVRVAKY
DTKIPLLARL HGAVPTTIMT IRRWNERKEY GLMMHGFQAL RIYATKNENN VVTIIKSNIA
TLMATMIKSP TSPIKLDCLL DLLTILAKSK PGAIQILSSF TIAHLISLFK NASTDAVQRA
VLKLLKAIVE TDEGKKAFVE DNGIAVLTEA LDGVIQASES SPSQIPTGQN TIPTLLVTLL
RSAVSQTDLP FLERYQYLSF PLPLAAEENG DNAEAKTDVD DDESTSLRQF CPELELHDGI
PSMTPLPMGN IQVRHVQPMS GRHLVSSKCV AETEGTYKRP MNLVRKSVYD QMTRVLHPNA
SQNQLIYDVM DETIAAGISG NTLQFESRFE SGNLQMAVKI SDYEYDLLLQ TDINSSPGKH
NQWFYFCVQR MVPNTPYKFN IVNMSKPNSQ FNQGMQPVMF SREEGCWRRV GDAIYYYKNH
YAFPTQYESE YTFATLTFTI TFSYAGDSCY FAYHYPYTYS DLQRSLFHLQ LSSTFGERCR
RQTLCRTLGG NECPLLTVTD FSPASTATNP ISERVYVLLS ARVHPGESNS SHIMHGLLNY
LLSDAETAID LRKRCVFKIV PMLNPDGVVN GSHRCSLAGV DLNRQWKRPD RRRAPTIWWV
KRLWKFLVDE GKRVLLTCDF HGHSRRKNMF IFGCENTPGS DVENLEKTFP TLLSTLSPTF
DMSLTRFDVT PSKETTARVV LWREMGILNS FTLESSYCGG DFGEKKGLQF QPADLRQAGI
DFCRALRAFL DIPPWNSSSP FPTAAPLVPS VRSASASVVK TSVVVESEVG QVEAEVHLEV
SAEISVGEEQ GNTLA
//
