ID D2RSZ5_HALTV Unreviewed; 766 AA.
AC D2RSZ5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Blue (Type 1) copper domain protein {ECO:0000313|EMBL:ADB60875.1};
GN OrderedLocusNames=Htur_1991 {ECO:0000313|EMBL:ADB60875.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB60875.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB60875.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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DR EMBL; CP001860; ADB60875.1; -; Genomic_DNA.
DR RefSeq; WP_012943164.1; NC_013743.1.
DR AlphaFoldDB; D2RSZ5; -.
DR STRING; 543526.Htur_1991; -.
DR GeneID; 8742590; -.
DR KEGG; htu:Htur_1991; -.
DR eggNOG; arCOG02796; Archaea.
DR eggNOG; arCOG02921; Archaea.
DR eggNOG; arCOG02933; Archaea.
DR HOGENOM; CLU_012344_3_2_2; -.
DR OrthoDB; 6744at2157; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR Pfam; PF00127; Copper-bind; 1.
DR Pfam; PF07995; GSDH; 2.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 81..150
FT /note="Blue (type 1) copper"
FT /evidence="ECO:0000259|Pfam:PF00127"
FT DOMAIN 189..384
FT /note="Glucose/Sorbosone dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF07995"
FT DOMAIN 407..473
FT /note="Glucose/Sorbosone dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF07995"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..725
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 82097 MW; B07C3D7026F037C4 CRC64;
MSERSDERPN PVPESATDYT ATSRRHLLKA AAAAGGVVAL GDLAAAQGVE TIELGGETSG
WQGVAPDDIA GETNPTLELE AGTTYELTWE NLDGQPHNFV IESEGGEQLE RTDLLMEQGE
TQTLEFEATS EMAEYYCEPH SATMRGEISV GDGGGGGAEQ DEAAEEEPEA FFDPGAEIGV
RTLAEGMTAP TDMAVADEDE ERYFVADQTG ELWVVTGDGL QDEPFLDVSD RLVELGTFEG
DYADPNQDYD ERGLLGVEFH PEFAENGRFF VHYSAPPNDE TPEGWSHVEV VSELQATEDL
SAGDPDSERV LMEFQKPQYN HDAGPMAFGP DGYLYVPMGD GGGANDNMEG HVEDWYDGNE
GGNGQDVSEN LLGSVLRVDV DSEMSETSRD GSGDAADEEG EDRPYAIPED NPLVDSDEGL
DEHYAWGFRN PFGISFDSDG RLFVSDAGQD LFEEANLVEA GGNYGWNVKE GTHCFSTESP
SQPPEDCPDS APDEAPYDGQ ELQDPIVEYP HVYQEQVVGI TIIGGHVYEA GDIGDLDGKY
VFGDWTADPA RQSPQGRILA ASEPSDGAGG MTGDGGGNQT EGMSPDDQEM PENATPDEEG
IEGEGFENET NATNATNETP DDGAADVGGG GQEQVVPRDE LWDMEELQLA GSEDGSFPYF
VRQFGQDLDG NVYVLANQVG VPEGDTGTVF EIVPPGEGES LEPFEADEAV EPEEQETDEN
ATEDTQNESI AENATDNESV ADENVTDGEN ATDNETLSEN VTADGA
//
