ID A0A0V1NLJ1_9BILA Unreviewed; 782 AA.
AC A0A0V1NLJ1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein RFT1 homolog {ECO:0000256|ARBA:ARBA00017957};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN Name=rft1 {ECO:0000313|EMBL:KRZ84842.1};
GN ORFNames=T08_14908 {ECO:0000313|EMBL:KRZ84842.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ84842.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ84842.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ84842.1};
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=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000256|ARBA:ARBA00026071}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RFT1 family.
CC {ECO:0000256|ARBA:ARBA00010288}.
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:KRZ84842.1}.
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DR EMBL; JYDM01000158; KRZ84842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NLJ1; -.
DR STRING; 92180.A0A0V1NLJ1; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03762; proteasome_beta_type_6; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR007594; RFT1.
DR PANTHER; PTHR13117; ENDOPLASMIC RETICULUM MULTISPAN TRANSMEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR13117:SF5; PROTEIN RFT1 HOMOLOG; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF04506; Rft-1; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 582
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 782 AA; 87584 MW; 44BFF40CAAE92545 CRC64;
MATTESSQND VGIFLKTTSY NVLLQIAFRS LTFLVNAILL HLIPISVLGV VNVRLMLLYG
TVYYFSREPF RRSCLQREEN SLRIQTINVM WLCPAVSFCL SLLFTFIWVF LLPDPSEDTS
TKYYGISACI YALSTVIETF AEPLCIIAQN LKQFHVKMIF EAVQMIIRQF FSLFLVYFFP
NLSLLAFAFG MVVSSSAYAV LYYLYFLNGF FKAKGRQINE LHEQNTVSVF PQFSKGFDSE
TLTLVYGFWK HGMIKQLLTE GERYVMTFFN LLNFRDQGVF DVVSNLGSLV ARVVLAPLEE
NAYIYFSQHL IRGMPINAQP KALFDEFAVV HDTFSNLLKL VSMIGLTSLV FGQAYSYPLL
KLYGGRSLII ASGPSLLRMY SFYVLLIALN GITECFMFSI MRLIEVDRHK LWLFYFCLVF
LLSAVLLCQL FGSIGFIMAN CINMIFRVAY SCWFIARFYR GKDSSLSCAL WNIIPSFHIL
SVMLISLFAT SISSVIFCCD GFFNTAAHIV IGGLLFALLF GSVYNSEPQL IVFAKKFMIK
SKQEKIICKV EVQLETTMTD AKLLAASGFP AYNPHEKISD GTTLVACEFE HGVIIAADTR
TSSGSLVVSR VSNKISPVSE YICCMRSGSS ADTQAVADIA KYQISVYEME HKCSIPVSIA
AEIFRSICYR YRNDITAGII VCGWDSVNGG QIYSIPISGM IMKQSWTAGG SGSVYAIGYL
DTNFKPNMTE EEANNFIRKA LAIAISRDGS SGGCIRLCSI TEKGMEHSVI PADQVADLLK
SS
//
