ID A0A0C2NJN4_THEKT Unreviewed; 806 AA.
AC A0A0C2NJN4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Inner membrane protein YbhI {ECO:0000313|EMBL:KII74232.1};
GN ORFNames=RF11_04253 {ECO:0000313|EMBL:KII74232.1};
OS Thelohanellus kitauei (Myxosporean).
OC Eukaryota; Metazoa; Cnidaria; Myxozoa; Myxosporea; Bivalvulida;
OC Platysporina; Myxobolidae; Thelohanellus.
OX NCBI_TaxID=669202 {ECO:0000313|EMBL:KII74232.1, ECO:0000313|Proteomes:UP000031668};
RN [1] {ECO:0000313|EMBL:KII74232.1, ECO:0000313|Proteomes:UP000031668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuqing {ECO:0000313|EMBL:KII74232.1};
RX PubMed=25381665; DOI=10.1093/gbe/evu247;
RA Yang Y., Xiong J., Zhou Z., Huo F., Miao W., Ran C., Liu Y., Zhang J.,
RA Feng J., Wang M., Wang M., Wang L., Yao B.;
RT "The genome of the myxosporean Thelohanellus kitauei shows adaptations to
RT nutrient acquisition within its fish host.";
RL Genome Biol. Evol. 6:3182-3198(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC chloroplast inner membrane {ECO:0000256|ARBA:ARBA00004478}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004478}.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC DIT1 subfamily. {ECO:0000256|ARBA:ARBA00007349}.
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:KII74232.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JWZT01000495; KII74232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2NJN4; -.
DR EnsemblMetazoa; KII74232; KII74232; RF11_04253.
DR Proteomes; UP000031668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030676; CitT-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001898; SLC13A/DASS.
DR NCBIfam; TIGR00785; dass; 1.
DR PANTHER; PTHR42826:SF3; DICARBOXYLATE TRANSPORTER 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42826; DICARBOXYLATE TRANSPORTER 2.1, CHLOROPLASTIC; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plastid {ECO:0000256|ARBA:ARBA00022780};
KW Plastid inner membrane {ECO:0000256|ARBA:ARBA00022780};
KW Reference proteome {ECO:0000313|Proteomes:UP000031668};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..782
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 806 AA; 88182 MW; 98B836CC6F2934F6 CRC64;
MVGIYLAMLC GLVLRPFTDA VIMLIILGFA SLVLDPAPLF AGFGSPMVWF IISAFIICKA
FVITGLGKRI AYLLLKRYGK NTLTLGYLMM VTDTVLAPAT GSNMSRSGGI TYPIFRNIAE
ALGSKPDDGS RKIGAYLTIL MYVVSMGTSS LFLTGMATNS ITVSLANEIM KVNLEWMTWF
KAAVVPAGLV LLLAPWILYK IYAPELKVIN NVNEIAEKGL RELGPVKREE KLLIVFFILG
VLGWMTGSIT GIAFIPVGLA FLACLLLFGV LSWNDVVSEK SAWQTFVWYG AFYGCAVALS
KGGFYVFLVD VIKNYLDLSH LNEISAIAVL VFISLAVRYF FVSNSAFVVS FYPVLFTLGM
TTQAHPMYVA LSLAFSAGYG ALLTHYGNGA GVFTFSSGYV PQKTFWMLGT IMVVVNEHKM
KLDILIKNGL VADLDSRDYI NRNIGIIGDR IVDLNAVDDL QAETVIDAAG CIVLPGLIDF
HGHVFHGGTA ISVNPDIVCL PNGVTSMVDA GSSGWVNYQL FRNSVIHPAM VKIKSYLNVV
NVGLSTLGGG PTGYLENTNP ANYNEEKIAQ TLNGNRDNIL GLKLRYSQDI AKGKQYASDP
LLSTVSLARK LDTTICVHVT DSLLCADELI RYFNADDIYA HCFHGTGHSI LNEQGEVYAA
IKEAQSRGVI FDCSNGVAHF DFHVARTAME QGFYPDIIST DLTLRNSLRT DKVYSLLHVM
SKYLNMGMSF FDVVRAVTAT PARLMKIQGQ IGTLAPGAFA DVSIVKLQKE KIVFEDTQGV
KIEGDRYIDN CATLCNGQIV YRRLRF
//
