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Database: UniProt
Entry: A0A1H6S5M5_9EURY
LinkDB: A0A1H6S5M5_9EURY
Original site: A0A1H6S5M5_9EURY 
ID   A0A1H6S5M5_9EURY        Unreviewed;       813 AA.
AC   A0A1H6S5M5; A0A2H4Q4S5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Xanthine dehydrogenase, molybdenum binding subunit apoprotein {ECO:0000313|EMBL:SEI60097.1};
GN   ORFNames=SAMN05444271_103152 {ECO:0000313|EMBL:SEI60097.1};
OS   Halohasta litchfieldiae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halohasta.
OX   NCBI_TaxID=1073996 {ECO:0000313|EMBL:SEI60097.1, ECO:0000313|Proteomes:UP000198888};
RN   [1] {ECO:0000313|EMBL:SEI60097.1, ECO:0000313|Proteomes:UP000198888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22187 {ECO:0000313|EMBL:SEI60097.1,
RC   ECO:0000313|Proteomes:UP000198888};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNYR01000003; SEI60097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6S5M5; -.
DR   STRING; 1073996.SAMN05444271_103152; -.
DR   OrthoDB; 57164at2157; -.
DR   Proteomes; UP000198888; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198888}.
FT   DOMAIN          57..173
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  87470 MW;  1F14E099A0A8C114 CRC64;
     MSRPNTPNEN GRPDESTSAD TAPHGAGDEQ PRGRKPKDER ESVSSRTEKS DARKIVTGEA
     TYTADHAAAF PNLAEAAVVR SEIAHGVVTD IETSAAAEMD GVYAVITPDS PSVPDKPYTS
     AGQSYPEPSP LDLHVLRKRV RYVGDPIAAV AAEDAATARA AARQITVTYD EYDAVFDTET
     ATDEAAPQIH DRDDIENPQP GAAYERNIEA HALGEIGDVD DAFEAAATRD DRTVVETEWE
     TPYQSHCVPE PHTTIAHRDE DNRYHLVTST QVPYHVRRQL AHLFDVPIRD VRVTKPQVGA
     GFGGKQSMVI EPITLALSLA ADRPVKLEAT RREEFHAMRL RRPSRIEVRS VVTDDGELDA
     LDMSVVTNSG AYGPHGLTAA GAIGKKPLPL YTHTPNIRFE MDAVHTNLPI AGAMRGYGAP
     QGHFAVEGHM DEVARELEID PIEFRARNYI GEGDLDIASG ILKDGEYGRK IRSCGLEECI
     ERGKTAIGWD EVDQPDAEHL HRGCGMALAT QGSGIPGDEL GAAHIKMNED GSFILQTGAV
     DIGTGADTAM SQIAAEVLGT SPEDIVVQPS DTDISPFDYG AYASSTTYVT GQAVQKAALD
     AREQLFEFAA QLLDESVEKL VARDGAVSSK RTGESVTLEE IGYASIYGDE VRAQIMGEAS
     HSTDESPPPF GAQFADITVD ERTGEFEVHE LAFAVDCGVA INPDLAEGQV TGAMHMSYEL
     ATGADLSFDD DGTPETLGFR HYGMPRTSDQ PPLTPILVET HEPTGPFGAK SIAEIPTNAV
     PPALSNAIRR AVDVRISDLP ITAGKIKTEL DKQ
//
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