ID A0A0V0WI64_9BILA Unreviewed; 563 AA.
AC A0A0V0WI64;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN Name=hmu {ECO:0000313|EMBL:KRX75351.1};
GN ORFNames=T06_8248 {ECO:0000313|EMBL:KRX75351.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75351.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75351.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75351.1};
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=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRX75351.1}.
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DR EMBL; JYDK01000125; KRX75351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WI64; -.
DR STRING; 92179.A0A0V0WI64; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.1450.10; Tetraspanin; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SUPFAM; SSF48652; Tetraspanin; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 343..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..563
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 63565 MW; 5E8291DE13EB5842 CRC64;
MVVGVCYLTE TGRQFLAKSV TVSCVLVMIL SFGYASTAYI MGRKFSSTIA HILETDDNHS
FASRKAIKYN FISACAVFGY SLIIMFCSSN NGSVRGRWTE KRVGTTCSLG SLFTLLVILL
SGAVIAGNVF ATQEMTVALA SGISNAMINY DTWRKNENKQ LRQYLDNMQY EYECCGIFDW
TDWLQPKYLL HTSTRRVLNV SEGTFSCNPK EPCYVPWSCC ARYTTESSCY NMAIGQNLDY
KRFSGGFHEK GCYSKLMDKY KRFLGFGVNV FAAIAFSAII IFISWRLLFT SICSWYYLQL
DLITDPTHPG VAPGWILSGC GYPASIYLGE DNKEVDNEEW GIALQPPSTT SDDKDDSDDS
DDDDDSDDDS EDSDDDDDDD DDDDDDDDDD TSSSSSSSTS SSSTDGGGGG SGGATDDGDD
DDDDDDDDDK KKDKKKKKKK KSKLKKKKSK KKKKKKSKKK KKKSKKKKKK SKKKKKKSKK
KKKKSKKKKK KSKKKKKSKK KKKKSSKKKK KKSKKSKKSK SKKKKKGLLW KARGKGGRKR
KAKKMRIKKP RAKIRLPKMR FKR
//
