ID J9IAC8_9SPIT Unreviewed; 639 AA.
AC J9IAC8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJY75194.1};
GN ORFNames=OXYTRI_03422 {ECO:0000313|EMBL:EJY75194.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY75194.1};
RN [1] {ECO:0000313|EMBL:EJY75194.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY75194.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY75194.1}.
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DR EMBL; AMCR01012573; EJY75194.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IAC8; -.
DR EnsemblProtists; EJY75194; EJY75194; OXYTRI_03422.
DR OrthoDB; 248389at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; METAL TRANSPORTER CNNM; 1.
DR PANTHER; PTHR12064:SF59; UNEXTENDED PROTEIN; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; CNNM; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..183
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 271..337
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 557..628
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 73321 MW; BF8CBCA72CE934F2 CRC64;
MIEWWIYLLI VVLQLLSAFF NGTNIGLMGL DPRYLELMQQ GPFETKEDEK NSYYAKKILP
LRNKGNQLLT TILIGCAATN SIISVLMAEI EGDISGFLIS TAIITVFGEI LPQAIANKYS
LEISTWLRFP MWFFYYATFI VTYPIGAILD KVLGEEAGNT LSKNQMKRMF EQYEKQALIK
PQERKILSAV LELKTKSIGQ VMTPIEKAFM IDINSNLNQQ LLKQIYSEGY SRIPVYEGDR
ENIVGLLMTR DLILINIEDQ IMTLKQLSSI LVRDVIAIDV NTKLEPVLTY FKQNKTHMGL
VTQSNKQIGS QMTLQKIGIV TIEDIVEEIL QEEIEDEREN ENIKGERKTM KNQIIYLFTD
NKAKDQLNDA EIIAICEFLQ LKVDNFGGGN ITKDQLYKLI RNSDVVDIES DSNPFSHILN
ENISYTRKPL TYINEYQNQD QLDFNQHLHK KETNGLLESH RKNKSNGSSV KTEANLLDNE
QYTDRDQIIL KFDQQKGSSN IMKNKDSNHN SNSKLNITNN TPYEDEDVPE EDLGHDQSMS
RDGILEDKLA NQLDPILFVK GVPADDFYLI LQGEVLVCSG SEGFFVKMGS YDYLGLNALV
QENYKPDFSA KVLNNARLLR IRYDHYQKYS KVFRQQNLL
//
