ID A0A0V1CTB8_TRIBR Unreviewed; 1733 AA.
AC A0A0V1CTB8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Integrator complex subunit 9 {ECO:0000313|EMBL:KRY52576.1};
GN Name=ints9 {ECO:0000313|EMBL:KRY52576.1};
GN ORFNames=T03_5273 {ECO:0000313|EMBL:KRY52576.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52576.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52576.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52576.1};
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 -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the BBS5 family.
CC {ECO:0000256|ARBA:ARBA00005822}.
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:KRY52576.1}.
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DR EMBL; JYDI01000102; KRY52576.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CTB8; -.
DR OrthoDB; 10261999at2759; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0034464; C:BBSome; IEA:InterPro.
DR GO; GO:0036064; C:ciliary basal body; IEA:TreeGrafter.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:TreeGrafter.
DR GO; GO:0060271; P:cilium assembly; IEA:TreeGrafter.
DR Gene3D; 3.40.50.10890; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR006606; BBL5.
DR InterPro; IPR014003; BBS5_PH.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR Pfam; PF07289; BBL5; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00683; DM16; 2.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51450; LRR; 2.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1733
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876144"
FT TRANSMEM 528..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1067..1207
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT DOMAIN 1423..1455
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
FT DOMAIN 1531..1585
FT /note="BBSome complex member BBS5 PH"
FT /evidence="ECO:0000259|SMART:SM00683"
SQ SEQUENCE 1733 AA; 195811 MW; AAB3ADDF9FB5B119 CRC64;
MRARWTRIDV FFGACLLTIS LNSAVNNVNC APCPDSCSCP SVETVLCRHL QPDEEFLTKN
WQLLVNARTL AFFSCPVGIP LLNLTEFCGL RKLSSLSLCE CGVERVEFSA SRSSPVVGLR
FFSLSGNSLI KLNASEHLVK FAPSLLSLDL GSNRLVEADL SGLLALERLD LSRNRFAKLP
KLPYRLQWLN ISENLIDSIS NFHHHRLHGM DLSGNRLTVL QNAGTYLTSL HHLNASRNSI
ISVRLTKMDK LVSLDLSWNQ LAELGRLEAA VLVELNLAGN KLQTVPSLGL ENLSSLILSN
LSVVSFSMAQ LTGLRKLVNL DLSGCVHLRT LTGGKLATYV PALSQLDVSD TALQSFEVDF
FQSSRLERLR VVGCRLHCDC RQLWRRWLSD QVFGRDPIPC SNMSVPNHCP VGVAEKSGRV
FKLRLGRVGY LQCGEYGYEQ PNVLWEIYRF QKAAYEPICQ WIPVADEIVR YQGYSDGLYC
LPGGLLALRL MHSDDASPVR CRAMNGAGNA TGITLIHFDY SHWWQLKMNS FICAIATMVG
LLVVNIFYIV VRRLIVWRIS KMERTSRVRR LLEAMEKYRQ RQLEALYEKY AQRTQQIVDN
YHQQVEQLKK GYMAQSERFR DYRAAQMESV THQIDSVRVA YAQQAQRFRD YSSRQMERLW
ESYERQLNRL RTFTLQQRLR VMRQYKFPQQ YINKLLENFY SDSANKIRVE YPFIDPNSFR
LPDLTSPEHQ LPVMLLVEMP GSSSDPQQQH KLQIELESIT SCEADSSKAN CVQIKQRLDE
ELMPVIKRKR TESNDLDFLT DSEVSSAQSS TVSHNVKLFV LTENPSEPCL MLKWPEKVIM
LDCPLNDLQL LSMTPVLLLK SSELINFDFN DAVSGLPTSK FTDVNAADII LVSNFNSALA
LPFITERSEF QGTVYATEPT VEFARCLMLD MVTYFERAKS ATHRKLTSAP FYTFEDVENC
LSKVNIVNYN ETVICPGFGH LTPTASGLSI GGCNWIVYLS SFTCVSTHAK AMAVDKFDNA
TAIVVGSLNQ YPKKNPATVM DEFCTVVANT IAAGGNVLIP SSPCGVTFDL IEYLFARVLS
RSPLPNCQVI FISETADTCF AFGNICGEWL CDSKKCRVFQ PQEPFVHGSF FFLKLCKLMS
RFACISTACS WWTCETDEIN KRSPYIVFAS HPSLRVGDAV QFLLLMKDNE KNTIILTDPE
FSPNEVLFPY KPISMKVAFC PIDVRMNTVE AVSLLSSLQP KALCLPIQEK NTVENFCNTS
EIVVRFSRSN TRYYSTSNIC PIPPDHRLVK IKLDPKLASA VTLFDLGCGK SIGRVAGRLI
LKEIGYYVES DENIEKTVYK NATLTCPSLK VAEQLLQKID FRASDPSLAN SNVEVAYENE
NAKFSMTKSM TRIFAKLDDL DTIEKLQDIE TFDLIHLKLR NGEFIVDKSH GIEDTKGNRG
QKAIGFNSIT AIRTRTTLSK LVGKTESLYV LTKPGSTRFE FIFSIINQAN AKLFASILIV
FRAYETSTSY REVKMRTPII VRETLKLLPL EEQCKRVEGT WNLYSDEGDL GVLIMTNVRV
VWFATVNESM NISIPYLHIK SCRIKNSKFG LALVIETSVQ SGSNIFGFRI DPQDRLEEVC
RQIISLHSMF QVNPVFGVEV VRSQRIVQDD NETIAIGLCT EDDIEIDSTG RADSLTAYFA
CGDPHRKSGE PVYNEELGVA IEALKEGFTL NDFRVFCLCQ ALKEQNDYST KFD
//
