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
//