ID Q22H07_TETTS Unreviewed; 1338 AA.
AC Q22H07;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Zinc carboxypeptidase family protein {ECO:0000313|EMBL:EAR84517.1};
GN ORFNames=TTHERM_00655450 {ECO:0000313|EMBL:EAR84517.1};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR84517.1, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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; GG662502; EAR84517.1; -; Genomic_DNA.
DR RefSeq; XP_001032180.1; XM_001032180.1.
DR MEROPS; M14.029; -.
DR EnsemblProtists; EAR84517; EAR84517; TTHERM_00655450.
DR GeneID; 7832788; -.
DR KEGG; tet:TTHERM_00655450; -.
DR eggNOG; KOG3641; Eukaryota.
DR HOGENOM; CLU_258593_0_0_1; -.
DR InParanoid; Q22H07; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000009168; 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; 3.40.630.10; Zn peptidases; 1.
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; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EAR84517.1};
KW Hydrolase {ECO:0000313|EMBL:EAR84517.1};
KW Protease {ECO:0000313|EMBL:EAR84517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 369..438
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 527..685
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 16..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 154904 MW; 7051480ED263E305 CRC64;
MDLYINNFLI SNQNQDAVSK TEMQEKESSN SSKNNESPIL NTETNQQNKD ALNEQFKSDN
TLKYEEEFAK NTAQQRKQKN SANSSFAMRK KVLNQSEDVI QNASFNRNIC SSRGQIESRN
DKSNLTVLNN TFMISKGFNS GQIDKELFSK EEASVLAVDD YDNDSLDEGD ELSYFELNYI
SQTGTNQQVK KIKRVKKTYL DQLPEANPIA KRELRGIEQL KSVYDYSLKF KEQQIVNSYL
ESFHMATENP EEFQKLVQRK EPLGVRNINA INTNYILGNN NPGISVNSDG SQTRQFIYQM
FTEENNIVYL KNPLLNNQVL CTLYKMSAIR NGEPYSDFKS KEASEITQQE RLEQMIKENL
TKKQKVLHFD SKFESGNLSI VSMKSSDEYN LLLQNDINTK GYTQWFFFSV KKTHRNQSVK
FNIVNFYKNG SLFNEGMKIS IFSKKKYDLT KVGWFKGATD IGYVKNNIVK QNDNYYYTLT
FKYTFEYNDD EVFFAYNIPY TYTQLNQFLH KCEMDPYKNQ FIYKKILCRT LIGNKLDLIT
ITNPCKNIQD EMSQRKGVII SARVHPGETV SSYIMEGIIE FLLQNTKEAH FLREKFIFKI
IPMMNPDGVI HGNYRCSLAG CDLNRRWKNP NQTLHPEIYY TKQMIFDFKQ KNDIAMVIDL
HGHSRKMNVF AYGCHDKKKP FECREFPFII SKLNSSFSFK DCNFKVQKNR EGTARIALYK
SLGIPNIYTI ESSFCGPSYL NTHFTAEHLK EMGHSICQSI LMKFQMANFQ QYLNQQEEQQ
DNQQQQQQNL EQENKTQQKK IEIPSFFSKV CSQQNLTSNK IFLDELYENP ENIDIGMKND
SGSDSEPSGD NMSDDELKKM FTSKTKKSKK LLDKNTKEVA TIQPQSQIKD PMSQTQTILK
RKTQSNFMTK SPEKKINSQQ GTSSSEVKPK AFNFDKAPSP IRSRTVIKNS FHQTGYNFVK
DQKNQKAEKE SQSQMKNMTV LEPKFVYFPL KVPDAFPNID KYKNSLRETK LRKLRENSQV
RQQMGNPQQT HRVIQMKLRQ SYNNGAAENQ SKIEKKPQLI SPREFKFNQA IPQPIENTVI
DSSLPVYNGI RDSINNTNKS QLGRILRTIM NTQTPDWIYG YSGNNSQYDT LNKSLVQEGS
QTLTRGGSKN MKQQQQLYNQ SPPQSNIVEK QQRSKSNDIS QYVFKMQKYD IFNGTFTNLP
DQSDVNKQSN RSLHENQFYQ PTFCDYKSLQ KTKFDQAFTG VPPTANSTTN SLNNSFASIN
NTLSKQQKII KPQSASRTVR KQLTTNQHLM NGIKLFQDQS KGDFEGSNIN NNGGNTVVVD
EKNINQQTVF QPIKIVYI
//
