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Database: UniProt
Entry: T1IRJ8_STRMM
LinkDB: T1IRJ8_STRMM
Original site: T1IRJ8_STRMM 
ID   T1IRJ8_STRMM            Unreviewed;      1724 AA.
AC   T1IRJ8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR003692-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR003692-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995}.
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DR   EMBL; JH431367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 126957.T1IRJ8; -.
DR   EnsemblMetazoa; SMAR003692-RA; SMAR003692-PA; SMAR003692.
DR   eggNOG; KOG1192; Eukaryota.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_240180_0_0_1; -.
DR   OrthoDB; 382054at2759; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   CDD; cd09823; peroxinectin_like; 1.
DR   CDD; cd11655; rap1_myb-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR015010; Rap1_Myb_dom.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR11475:SF106; CURLY SU; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 2.
DR   Pfam; PF00201; UDPGT; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1724
FT                   /note="BRCT domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004579447"
FT   TRANSMEM        466..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1166..1227
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1338..1359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         917
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1724 AA;  196026 MW;  BA63EF2E54DF6008 CRC64;
     MLKHFLILLL IFNVTTAGDV LMLVPFGSMS HKICFDPIAR ELGARGHNVT LISVFEPTKT
     YPNVNEIVIP AMVHLHRQLQ DGHVRVGKEG VTYAIWSMFG DICGELCDNF FQTGMLQEWL
     KNGRKFDAII VDSVMAECLV SVAHLLSPAV VLWNTAFLLP WVAIPSDIPT PSSYNPYSFD
     GSIAQMSLWQ RMWNVVAHEK SQLLFNHAMY PPMDRAVFRH FPQATSIVEA MRRLSLILVN
     GNAVLSTPRA EMPVVVNVGG LHLTPSKPLT PDFAQLVDSA VNNGVVIFSL GTIFDALLTP
     DREEIIFKTQ ISNYMEIQKK FENTPKNIKI FEWIPQKDLL AHKNIRAFIT HAGLLSLQEA
     FHNQVPTVTL PVFADQPQNT AFLTSLNLTI PLSWDTLSVE NIIDAVTRAA EDETLRQNVA
     RVSRIFKDTS ESPLNKSVFW MEYIMRHKGA PLLQPAAKEL NLIQYFIIDV LLFLFFILVL
     VVLCNGLMAF LAENERDVFP VEYLPNIDDL LVDRVVDIAK RQIEDEAKLN VDSHFHSKRN
     GKVKEEVWEI HKQVSIGARA VDILSSEQNL TREASDHIVK RAPPRNGINF NVLCEDRRFQ
     CNRFAKFRNL DGSCNNHANP DWGMAVHKQN RLLAAKYGDG FNTPRVAKSG RRLPLSRFVR
     TTTIPDISAE SDRITHMIVQ FGQFMNHDIT STPDRTDLTN CCSNPNRMDC LPLLIPRDDP
     DLSQLQIGCM EFSRSIRACG NGVRQQINQN TAFIDGSQIY GSSEAESSSL RTFRQGLLQS
     SNNGENLPVN PTDQGCATRG TGTNFCFRAG DNRLNIQPGL SSMHTLFMRE HNRIARILLR
     FGPRFNDETL FQETRRVVIA ELESITFNEF LPLVLGPDLM KQYDLTLPKT GTATNYKSNV
     DPRIINSFTS AAFRFGHSQI LNFGQLGTFR NGFALKDNFN DPTVVHRAGA DSVLVGSVIQ
     KAEGMDNFMV EAVTKFLFKQ GNNPVGLDLG AFNIERGREH GIPSYNDFRE FCELPRIKTF
     EGLSDVFKDS RAPRAFELAY EDVDDIDLFP GGIAEKSVPG GLVGPTFACI IGTQFHRLFH
     GDRHFYTHGN QPGSFTSDER AMLSKRTLSS VMCDNLDVES VQLNAFLASN NSKNPLDIKM
     EKYTHNPYLF YLDDQPLRFS MRPCDERIKL KPVVEHGGAT ITSKSTKDTF RLVPPGAIVS
     TDDCISTKWI WDCVKENKLL STEDYIVKQR VESDVSDIDE GDNVVRMVNK KRKSPKGTRK
     EYLLCEDMAI INYLFDNRRI GEVKARAMWQ EMERVNVVPD RSWQSLKERY NKQIADNLQS
     YNLTKEKLKY LKYKETINRT PPKRPPLRPK STPSPTASEI SFTRRQTRLY TVEEDTKLIY
     YVLDEDDHRA IMGNIFWKKA AARKVLDRTW QSMRERFLKY IVYDMKKYKI KYEYRKSLGR
     LLHQVGVVYD SPIEISDDED GKIVKNKEKN VLKSPNVEIL IENTEDDELI REAEEDIRDQ
     RNDLESPDLQ LRLEESDDEV ENNHRMEKIC LEESPEIGKF VLERSKSPEV ENKDEICDKN
     TAAILEKIIT DDNENLVVLD YVTSTNGSPK LEITLFHLIR VNSSAQTQDL VGESSINNQP
     VVKNGEMNGD NTGKRKRLAI PNANLNFKRL NSGKMARPSD DEEEDFAKVA DEIERLGQQN
     LDEVDTNIKV LSVLFGLTED QTWQLLESVD FDRSTLLKEI CGIL
//
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