ID A0A1Q9EK91_SYMMI Unreviewed; 1653 AA.
AC A0A1Q9EK91;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic {ECO:0000313|EMBL:OLQ07863.1};
GN Name=CYP38 {ECO:0000313|EMBL:OLQ07863.1};
GN ORFNames=AK812_SmicGene8662 {ECO:0000313|EMBL:OLQ07863.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ07863.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ07863.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ07863.1,
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 peptidase C69 family. Secernin subfamily.
CC {ECO:0000256|ARBA:ARBA00005705}.
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:OLQ07863.1}.
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DR EMBL; LSRX01000130; OLQ07863.1; -; Genomic_DNA.
DR OrthoDB; 312201at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR GO; GO:0120013; F:lipid transfer activity; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006820; P:monoatomic anion transport; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.10.3520.10; Glycolipid transfer protein; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR005322; Peptidase_C69.
DR PANTHER; PTHR12994:SF17; LD30995P; 1.
DR PANTHER; PTHR12994; SECERNIN; 1.
DR Pfam; PF08718; GLTP; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR Pfam; PF03577; Peptidase_C69; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF110004; Glycolipid transfer protein, GLTP; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:OLQ07863.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..380
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 510..633
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|Pfam:PF00160"
FT DOMAIN 1000..1122
FT /note="Glycolipid transfer protein"
FT /evidence="ECO:0000259|Pfam:PF08718"
FT REGION 911..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 180625 MW; C173BDEBEC8CEBC1 CRC64;
MPEFEEIDGA EYGGTATPYQ ADMVEKAGQS SNKAQELVGK IEELMLPADY AAKERCDSAG
AKESPRMLHK LLAGHVETDD YRRRFAYFRS DWLTDVMKGK TVSGALFLFF ATFTSTLALG
KHINDAPWPA SKVIGINEYM IMNSLYMFII AATELSRFIK YVTAFTENIF ATFIGTAWGT
YTIRKALTIS VFVLAIVAAV LDANFFGVDF IDTSSTGLTT TDGREWMTDM GSISATGVLV
AAVAAIPIVM FFYLDQNISS LMCQKPEQML GKGAYFHSSF ACMALFNLLG PIWGLPFVTG
SLPHSPQFVS AMTETDEDYK PTGVVENRVA PFVGYLCEIL SSYSRMLGYL LMGVVLFLPD
LLNKLPETAV SGALIFVGLK VVGCWLCNIY IGLGFPVFVL GSAFIALEKN TGEVASLIPF
RFKVLPCLFK SEDIEALLTE EPEPPKGSKS DSDDSIENAM GEDVERAKVP AEYANLPRLD
GRAVLEWTLT RGPESGATKY VIDEELIEEA KFTMVIDGWS APLSAGNFLD LVNRKFYNGL
PIQRADGFII QTGDPGADKG NGFSPGPGQP VRTIPLEVGI RNRKEALYGE TIDEARLVGT
EVKIPFQADG TIALARREFD NDSASSQVFM FLFESVRNNT TPPSASVLGV RVSWKNTTPK
NIAQRAPLPT RFWLNYGVAE KLLELRRGPS DGGRTVVPMV RCFAVSLALL TGAGGFDIDG
CTSIVVNADA MADGSAIASH SNDCADCDWR MAYVPAKDHP PHSERIVYDA VWSTYPRIVD
PSRSKQYQPG AGITASKELG RIPQVNHTYA LWEASYGLMN EHGLGLGEST CPAFLVGKGV
SDGGAALFSI GNLMAIALER CKTARCAIQT MGDLGAKYGF YGEDPGYGGA GEATQGPTAE
EVVVPSLPKA MDDAAEETST QSPAPSMEAE STASPSSHVA AAMPEVDAAS GDETAEAPCQ
AARPAGMKPV HLVHETRFGL LMEKFKACEV RDESGTLTNI DMAKFFEACE LYRDMLSKLG
SATGFVLSDI ESNLKKAQVV YEQAPEERAT FSGYLKSSVV GVAWLLRGVQ FFLAMIKLMF
TQETGNAGVE AYKQTLMQYH GWMLQKTVKI GMRAMPGKDG IVKSDGLVLG DVSLEQRAKL
CERDAPGASA AGLKVVQWMV ETMKKEGKWA VTLVDRTGEA WVFHICGGVP NNATSAPWAG
QRGALWVAQR VPSGHVAVIA NSMIIRTVDL ADKKNFMAHP GIVDLLKESG LWDGFGPLDW
QRIVQPDLAT FSYFPGLAPI PMYSTLRMWG VYRQAAPNSG LQATPDLGSF PFSVPVEGKA
TVQDVMNWFR THYEGTEFDM RYGSLAGPWQ SPNRAEGGNG ARSVPGQFAR STSIPRTSYT
QIVQSGPIHQ PRVWFAPDCS ASSVFVPFFS SALADADGRF DVEAYGTGSQ KSFVFSKHDT
VRPAWWAFDF VANWMEISYQ NMSEQYVYTA VQSTQLRVVE ETEEALRKSD KMHAKSAAKH
LADFQSKLQR NITEEWWALA DTLVVRYNDM FYNYPPETPH QVSDIGYPAF WLEMIGFNQE
FYRPHWVLPS LVPPSLLPQM IKDQLSNLAP VLKWGVRGYG TSDSATSISA TSESPLVSVV
VASMMCLGTY ALGYWRGRHS APASHDGYHH LSA
//
