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Database: UniProt
Entry: A0A1Q9EAN7_SYMMI
LinkDB: A0A1Q9EAN7_SYMMI
Original site: A0A1Q9EAN7_SYMMI 
ID   A0A1Q9EAN7_SYMMI        Unreviewed;      1981 AA.
AC   A0A1Q9EAN7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative serine protease HhoA {ECO:0000313|EMBL:OLQ04473.1};
GN   Name=hhoA {ECO:0000313|EMBL:OLQ04473.1};
GN   ORFNames=AK812_SmicGene12419 {ECO:0000313|EMBL:OLQ04473.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ04473.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ04473.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ04473.1,
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   -!- SIMILARITY: Belongs to the DeSI family.
CC       {ECO:0000256|ARBA:ARBA00008140}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:OLQ04473.1}.
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DR   EMBL; LSRX01000209; OLQ04473.1; -; Genomic_DNA.
DR   OrthoDB; 1046951at2759; -.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00989; PDZ_metalloprotease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.90.1720.30; PPPDE domains; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   InterPro; IPR008580; PPPDE_dom.
DR   InterPro; IPR042266; PPPDE_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF05903; Peptidase_C97; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM01179; DUF862; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51858; PPPDE; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OLQ04473.1};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1352..1374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          560..595
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          725..865
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51858"
FT   DOMAIN          1400..1552
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          1468..1524
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1892..1948
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   1981 AA;  216509 MW;  DDF7300E2E3DAA9B CRC64;
     MKGCQIELVE LDAQKFGRSH DWVLLCADKL GELATAQGDS WRAEAMFRRS YEARLADSQD
     AEDTDIANSA YNLAVCLAQQ GKDTVAEQYY RKAVEDQGRL DEAEKLYKEL SQTTALIPLD
     SKQRRMAAHG PLELNMPSAD TLQAESSLMM CRTAIQQVVK EHLPKDGLCV VFVETKRGAD
     SLEIELHKAL AAFKTGANPI LVATDVAARG QGAPEMIAGP NLWFNLYLTF EHGDEASSLA
     LSDGSLDEFL VGCEHSGTAV AFVNERCAYL HDLYDILIEA KQDTPIWFEE MVRQARRPTG
     GKGGRRAERF GGLGIASVSA IVSYGIVTVS FVAAGQYAMR CDVPCSGIAD SGLKLVVLSW
     QFLCDAETSF RRIFAHPSRL IWAYSLQEEK TLGEPASDQE VLLVLFHAVS ARRLRISVCT
     MAPPAILSRG EYLSRLAESR KQCRSGPLMS TQLDCAQHSV PTVPLPRDVF ARAGTSLVSH
     TTGTLCRIRG AMDEEDGQED DDDELFLKLP RDSEEEECQL PITLNRDSAL EDDRLPLTLP
     KSCESSLEVF LSSDQVALNS VLTNILSKFS ELDADGSGAI TMDELASHWL AAATEVCKRP
     LSDSEKELIG GSVQRAFDVM DVEQDGKINK HEWLHTALLD MHPPGPVATE IITQKLRDSD
     TPDIVSTLVY TWLSADEMVC GIVTRQMLSI NPCGDAELLD VMNSTGSDSI TYAEFVANVL
     RLTFRPVELY YYDLSKSFAS VLSPILLGQY EDGIWHTSVG VFGQELYFFG YILTCYPGQS
     AFGQPRKSVQ LGYTLRTVEE LNAEIKRVYF DYRPDLYDAF DHNCNDLSNH MVQFLLGRSI
     PDSVRLMSER LKSSSLVKVL RPLLNRMLGN RQSRGKQDGE DKILELEATA RARRNGARRN
     SGSAMKLSEP EPEVVSVDSL KLDLEDDEEL RAGVAIAVAG QDATTQQLTG MVLFRSMGAS
     APVVAQVEME HPDGTFDIGW FDQAGSKQQA TAVPGASLEP YMPALQASAL LQDVFSKVAG
     QVPPSLERWS SMDIGKGDIQ RAAVTCLDGH ALVRSQPSYW SSSVQCRFCL DAIPAGQVRM
     HCYSCNYSLC GKCFLQNQNP HVGQNPAGFE EIRHSLAIWP RCDNGHSLER FGGGTADGGA
     SCSSCSQPEI GSTGPFFLIC RFCQQQLCHD CSRRSLCTLL DAAYEPRVAR ADAVDSDAVR
     RLFAAQGRRK KMKLTSMMLM IQRGGPCGIA TMPLSIADPR KGGVPGVSNH HPDKQGSVSK
     ARQVKDNFVN RVAEKCGAAV VRIQTEQKVE IPSIGNADIF SFFFGIKPEI NQQERKIKGQ
     GSGFCVDGAV GVVSRSATPL KFDLCWRMEA EVLAAILVSV LLVVLVLLWL LIFFSGFGPT
     KLHSWQSRTI RLCKKRKRWS WTKIEEGLFL GSVPRSQDHL IELQGEKVGA IVTLNEAWEL
     PVSCASMEEF GMKHLHLPTP DFFAPCLDDI TKAVDFITEC RQQGIGVYVH CNGGRGRSAV
     CVLCYLIKTG WPAMKAFQHV KSKRNIANML FLGGRFHKQW RAVLSWQRRE LGGPTRAQGR
     KVAPADAVKV LTNAHVVQGA DRILASFPGR RAAIECEILE TDEVIDLAAL RVKDKSQLPL
     PSMALGASET VKTGDWTIVL GNPLGLQNTC TLGIVSSLER STGETGFDWM RHPLIQTDAA
     VNQGNSGGPM LNEIGEVIGM ISMRALFGEG IGFAIPADSI RTALPSLLAG RKVPRSYIGV
     KMAMQDHSGH EAAITLVMTV WASTEQFVDS GLYSDDSCTN RTSGGLFPVG SCTVARTMVT
     VEGTEITTIS YATADCSGDQ LGNFTSTDGS CASNRGMYTK NSIFTAASAT VENFGDETCS
     GNATSTLTFP VDTCYPLGDT ESLKYQCDGC AVVDVVLDGS PAAEAGVQVG DQILEVGGRK
     VRHFDEVQLA VRALPVDNRL KLKVRRGEKS TTLVVTTADI RRLREASPAS PGGRHRVVLL
     P
//
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