ID A0A1Q9DPD7_SYMMI Unreviewed; 1118 AA.
AC A0A1Q9DPD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 2 {ECO:0000313|EMBL:OLP97018.1};
GN Name=Kcnh2 {ECO:0000313|EMBL:OLP97018.1};
GN ORFNames=AK812_SmicGene20685 {ECO:0000313|EMBL:OLP97018.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP97018.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP97018.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP97018.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OLP97018.1}.
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DR EMBL; LSRX01000448; OLP97018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9DPD7; -.
DR OrthoDB; 180795at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR47823; ION_TRANS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47823:SF9; K+-CHANNEL ERG AND RELATED PROTEINS; 1.
DR Pfam; PF00026; Asp; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1118
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012254886"
FT TRANSMEM 676..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 864..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 563..598
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 995..1118
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 1118 AA; 123812 MW; 50043930E9FE742D CRC64;
MAKIAGFAAL FLAFVTTVLA DLAGTVLRTR TPAPEPQLGT EPLVVRLQRV EGLHSSHFYV
GRLSLGQPRP QELQVLFDTA SGHLLVPHSA CASKACNKHK HYSPFLSSTA MDVNTNGKPV
REKERLVTGK AVRDAVTVEF TQADLGEGAA QAVLVHDDVC LGTEFGHQVC TNLDIMAAVK
MDDELFEAMP YDGMLGLSMA GLSTGTGCVF FQRLMESNPS MLPQFGLSFG AQSGEIFFGG
HDSSRMAENL KWFPVLHPDD GFWEVAIKSV RLGNLTVDAC NHGCRGIIDT GSSRLGVQEN
NFQALRAALS HSQALVGGGC QGPDLEFNLG DMALRLRVED YATGSNCEPQ LGSLELDPKD
YHGVYAFGET VLRRYYAAFD WQERRIGFAP VAQRRVQLGK AYVLTDLPGT SSSILERLPG
LEALQKMTCE ASAACFLVPS DSLTEFTNKA VNVGDERATK SQLLEKIDEA SLSLLLAEEQ
VKPISEEESQ TLIDIGSEIC DVSGGKPLRP TAPPVPDGPT EEQMEAIEEV WNQLDDGGDA
SDAPSNYSKF STKSTSLPEA LAQNRSMLID LFHKLDLDKS GVIDAAELRR GLRAVGQHPG
RAHRLLATLD TNKNGKIELA EWVSSIDSVA VRERRSGTIE SFARAIVKQA QAGTLVLSQD
EEKGWFMLSF RSSKRLLWDC FLTLLLLYIA LILPFRLAFY ELEEGIESFW GVLELLIDLC
FVLDILLTFR TSYSDDEGEE VFQWHKVMVH YLRTWFFVDF VTAVPLEYFV QGSPSTDGIK
LLKGSKVLKV LKLLRAIKFL KIFQGTELGS RLEDIILLSN VTRALEGFRI FISCCVLGHL
LACLLPILAG GFLERYREPV SSRYITTLYW AMTTVTTVGY GDITPQDDEE RVFTMFAMII
GGAFYGYVIG NISVILASRD VNRQAHKERL RLIHAWLVHH RFPNPLKHRV WAYYKTLVTN
KAALEDSTIF NDLSPELRQD VARYLVPPDL LNHLLFQNIP SSVIVRLVPI IQQITAQPNE
RITSRGEIGS GMFVVLDGIA LMDQSDPEVP NRHSKAPEVL RAGDSFGEEI LLGSEKEYGY
TVSATSRVTM LFIPADDFMT QFAALPEILS IMRHNFSI
//
