ID F2UT47_SALR5 Unreviewed; 1320 AA.
AC F2UT47;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGD81306.1};
GN ORFNames=PTSG_11343 {ECO:0000313|EMBL:EGD81306.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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DR EMBL; GL832997; EGD81306.1; -; Genomic_DNA.
DR RefSeq; XP_004987702.1; XM_004987645.1.
DR STRING; 946362.F2UT47; -.
DR EnsemblProtists; EGD81306; EGD81306; PTSG_11343.
DR GeneID; 16068227; -.
DR KEGG; sre:PTSG_11343; -.
DR eggNOG; KOG4295; Eukaryota.
DR InParanoid; F2UT47; -.
DR OrthoDB; 5491086at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 3.30.60.30; -; 2.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF07648; Kazal_2; 2.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00264; Tyrosinase; 2.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00280; KAZAL; 2.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1279..1301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..246
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 881..931
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 1247..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 144763 MW; 19DC968DC183BDF1 CRC64;
MPTNITATGP DGSQAVRVTV RVWHAQYAGG SGDSACQSHG GEPPALWDQH DYVVAHHSCG
CPPGVGYVEC EEPDMCRTHR CLAHPRAACE VSHCGVCAVR FYAEKRSSYE GVAPLDCLPR
DKCTGECRKE FEACSQYTGC REALYRLVDE RASSGTCNGT CHERLAVPTE PGRTLFDRVW
SCYRTCEERE TVHTVCALPP RAGQCKGRMT RWYFDRITGK CRQFAYGGCG GNGNNFETRE
ACEQRCELGA CCTRRTVLDD VGYDANGYDQ FGYDRRGYAR DGFSRRPWTY AEFVRNTFDL
FGLDERGYDP RGLDGSGFSE PRQCIYQGRR YNYGETFRFA CQWCVCGTDG AVTCQCTPRR
RREIRDLTLD EVQTYIDAIW RLYNSGNRWN EFVNMHLSAS ASAHGNPSFL PWHREYMNQL
ELALREVTGN CDFTLPYWDW TIDSSSPETS PVWNLVGGDG TGENQCIEDG PFATFSPCIS
RDWDRSWHIP SFADVTNVLS NDDFRTMATR LEGIHGNTHT WIRGLMSTYS APYDPVFYLH
HAYVDKQWYD WQVVLGNGNK YPEELLHNTM DPFPKTPADV LDSEGQLCVV YEPPGRTPPC
NEALFGGTFE TKGYYAPGAR PQYDRDGYDR DGYDENGLDK LGRNRDGVRV GGVTATGFNT
AGVDSRGCSI MHPMPLYMRD VFQAQRELYR RIQANAYVQP ARTCSPLQPL PAWWKASMWM
SRGGLYGAIM DAYEAYLEEA LVRQPDEWQR DRTQSQPSIL EDLCFAADDL TLRQDDSWRP
GDDYQCPPGL PRQNCEWNPC ANATCPGSPD ATCWVNPCGR CRPEFYREDG SRARCYSTCP
VEEGTCTFDP CAYATCEANP EAVCETSPCG GCEVEWSDPE TGEPVTCDVE PDSCAAQGQT
YVCGEDGQTY DNVCYAREAG VKIAYGGLCV ACERLCPPEG MAAKACGEDW QTYASVCHAR
CAGVKVAYTG ACRPLPVTCE QVNFFKASDA GRQQLCNEHT SCLTTVARSA DNRCFWNEDT
RRCSCQPSDV VCTAGAHECA RCCNDDLRRC LRWGQDSVDT CWREAYVACT VQCAEEYDAA
KLPVAAASVG SVDDGDGGDG GDGGINIFLG GVDMVHSGND TNSTAPGPTG PLDTVVFRVG
LRGRPSTTMD AAQFAEATSL AVGRASFVPS AMRVVGASAM AAERLGNATA GVELEVNAES
SDGYAVQAAL EAAVVEGRLA KEVAIYTGSA TTDDVMLIGA VQVHAVPRPP DGPSTPFPTT
TDGGGGHPRP RKGGVPPGVL TGGAVGGIVF IGVVVALVVL FKHRANRSAS NKVGVSPVKM
//
