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Database: UniProt
Entry: A0A0V1CWX5_TRIBR
LinkDB: A0A0V1CWX5_TRIBR
Original site: A0A0V1CWX5_TRIBR 
ID   A0A0V1CWX5_TRIBR        Unreviewed;      1652 AA.
AC   A0A0V1CWX5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=glutaminyl-peptide cyclotransferase {ECO:0000256|ARBA:ARBA00012012};
DE            EC=2.3.2.5 {ECO:0000256|ARBA:ARBA00012012};
GN   Name=Qpctl {ECO:0000313|EMBL:KRY53797.1};
GN   ORFNames=T03_8676 {ECO:0000313|EMBL:KRY53797.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53797.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY53797.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY53797.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-
CC         [peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736,
CC         Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722,
CC         ChEBI:CHEBI:87215; EC=2.3.2.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000001};
CC   -!- SIMILARITY: Belongs to the glutaminyl-peptide cyclotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006014}.
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:KRY53797.1}.
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DR   EMBL; JYDI01000079; KRY53797.1; -; Genomic_DNA.
DR   STRING; 45882.A0A0V1CWX5; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03880; M28_QC_like; 1.
DR   Gene3D; 3.40.33.10; CAP; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR040233; CCD97-like_C.
DR   InterPro; IPR037457; M28_QC.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR040234; QC/QCL.
DR   PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR   PANTHER; PTHR12283:SF6; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF09747; CCD97-like_C; 2.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; PR-1-like; 2.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY53797.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1050..1072
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          124..255
FT                   /note="SCP"
FT                   /evidence="ECO:0000259|SMART:SM00198"
SQ   SEQUENCE   1652 AA;  189798 MW;  1F41D1833000E039 CRC64;
     MSDFGGKNCC LDVPSRRKLC VDKSRKQWQT HIRQQLKRNT LLWIGKRMHT DGITSVKTKS
     RLTPEKVQTK LSYKIASCKN YRRILWHNDQ LLFVFLSFIR SKPTLSSTSQ NLFVKGTPKP
     FNDLGKLMMV SVHNTVRGDA TDQSNMQCLT NWDSTLESYA QRLANSCNRT APANPPYGLA
     YSSEISEAII TPQSFVETLG NSFSLFYDPT ANQCDPADKA DCDTGRQIVW YQGDKVGCGK
     ANCTGRDFVV CAYTFQSSLQ TRPYSRDPLG PCSSCPSDKT VCTAKLCCIP DSDSSSTPST
     SVTSCGEKPA NLVNLVRFWS DALTQNYLVT SQSEISSLSA QSRTSNLGAV GKIPVQTSTA
     CPYLTPIYKL YAASATSNYY MIDSSLRQQR LTEGYTDQGV IGYAVPAQHL CNASVAIYEF
     YSPGNGATPV SFSEAEKIDL FFNSDQVKCN IPHGIRGHCK FQWDASLEKY AQTMANSCSS
     IKMTESSAMK NFSNLFYRNY DCHANISEEN LLKNHNQDVE IFWSEVEKLG CGRSICENGI
     SIVCAYSTAN NNSIMHVSLE MNKKNFQKET MCNSTASSST LDNSLTTSHL HYLDKPLGSC
     GSVLNNLVNL HRFWSDRRTQ NYLVTNPAEI ERLRKRKKMI DLGIIGKLAF GPSLACPYLL
     PVYRLFARRA TSNYYMVNRD LMNRRLQEGY VLKEIIGYAV PAQHLCGASM PMYEFYAKNS
     GIIQVEPATA IGALDGIPNP FVGAEQAELV TYHNLYRADF TAQNSECFRG WQNKFARIAQ
     QLANTCQRVR PDNITYGISF SNITTTEVSP INFVQDVWQD FQNIYTYNDD KCSTADNERA
     NFHNRPFLYY PGSGPCIFCS SKKSSCITNL CCKVRSFLFS KTTSLLLQVP KVLVVLILAV
     HNRPMSRNVL DTADYRILLW QITSGTSDLG IIGKVAKFND ESCPFLKPIY QLYSFHFNSN
     YYVIDKNLLK QRIADGWVPQ GKIGYAVNGE NVCNATIPVY EFFNSRYGIL QVQNTTDISD
     LLARRKYPEY IWHGISFWIW EGDSRGNLHI SYNFIIIMFL IFGTLFLFSF SFCEPSQNNW
     KLTQATHQIR NYEQEQLLQL CALSDHERFR NYLKYILIPR PVGSRNHKKV QEFITQSLEA
     LGYKVESTTF TQQTVVGQKT FTNIVGTLDP LIPRRLILAC HYDSKDFRPN FEFFGATDSA
     VPCAMLLDIA ASLRNVIYNR KSKDLTLQLI FFDGEESFRE WSDTDSLYGS RYMVKELEKR
     PYPEYYSPRS RDLDRIDLFV LLDLIGAKGS TFYYHYPYSV LNAYTVLPET ERQLKASRNC
     IYDLPTIFHD LMINTFIQDD HLPFLEKGVR ILHLIATPFP SEWHTVKDNE DILHFPTIYN
     ILSILQFLYY RLIILIKSET KYSRYTLVNT EQNCRGMIGI NDKDSCSFEN TCDLAERLHN
     LFKRIANIPE AFFRDQQRGE ADFTFEQRLN IVRSTYEQMP VKFLSKYSCY IEKGELDLFE
     PYSDQTMEYH IERIKNSDTK EAAFRIKNRR FSKLKQLISE GTYFSDREMR QRDPWLYYHM
     IGRFLTENES KALFYSQNSQ YKFNETKKTE TTISEEEKER LRKEFVIIMH ESFLEGRDKE
     FDYSEVDENS KYDDYVRINQ DAEDKYFEDS DD
//
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