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Database: UniProt
Entry: A0A0M0BFL8_9ARCH
LinkDB: A0A0M0BFL8_9ARCH
Original site: A0A0M0BFL8_9ARCH 
ID   A0A0M0BFL8_9ARCH        Unreviewed;       563 AA.
AC   A0A0M0BFL8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein fwdA {ECO:0000313|EMBL:KON27140.1};
GN   ORFNames=AC480_04790 {ECO:0000313|EMBL:KON27140.1};
OS   miscellaneous Crenarchaeota group archaeon SMTZ1-55.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1685133 {ECO:0000313|EMBL:KON27140.1, ECO:0000313|Proteomes:UP000037456};
RN   [1] {ECO:0000313|EMBL:KON27140.1, ECO:0000313|Proteomes:UP000037456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-55 {ECO:0000313|EMBL:KON27140.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KON27140.1}.
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DR   EMBL; LFWX01000085; KON27140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BFL8; -.
DR   PATRIC; fig|1685133.3.peg.656; -.
DR   Proteomes; UP000037456; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01304; FMDH_A; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR012027; Formylmethanofuran_DH_asu.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03121; one_C_dehyd_A; 1.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   PIRSF; PIRSF006453; FwdA; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          42..498
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   563 AA;  63059 MW;  E18E0AEA546A798B CRC64;
     MSLLLKNGFV YDPLNGVEGE VMDIAVDHGK IVETPLSQVQ KILDVTGMLV MPGGVDIHAH
     IAGSEVNAGR LLRPEDHFKD VEVRGKRTRS GVGYSVPSTF TTGYRYSKMG YTTVMVPSMP
     PLEARHTHEE MDDTPMIDKA AYPLLGDWWF ALEYLQDGLL DECAAHIAWM MRATKGYAIK
     IVNPGGLESW GFGKNVHSID DPVPNFDITP RQILRGLCQV NTILNLPHTI HVHTNNLGRP
     GNYYTALKTM DCVQDLAKGK QPIIHVTHCQ FSAFKGSDWS NMHSGAEGIA RYLNRHTHVT
     IDVGQVCFTN TTTMTADGPF QYGLYQLSGN KWVNHDVETE TSSGIVPFRY KRKSYVHATQ
     WTIGLELALL INSPWKVFLT TDHPNAAPFI TYPQIISWLM SRRARAKLLN KINRKARKRS
     ALASLDREYD FHEVAIMTRA GTARALGLTE KGHLGEGADA DIAVYNVNPE TINPSTEYAT
     IQRAFERTAY TLKAGEIVSR NGEIVKPVQG STYWADVQTR EPQEAAADLK QRFGKYWTIQ
     YANYSIPERY LHHSKPIAIK AEV
//
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