ID A0A1Q1FP38_9EURY Unreviewed; 932 AA.
AC A0A1Q1FP38;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
GN ORFNames=BV210_06735 {ECO:0000313|EMBL:AQL44497.1};
OS Halorientalis sp. IM1011.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=1932360 {ECO:0000313|EMBL:AQL44497.1, ECO:0000313|Proteomes:UP000187924};
RN [1] {ECO:0000313|EMBL:AQL44497.1, ECO:0000313|Proteomes:UP000187924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM1011 {ECO:0000313|EMBL:AQL44497.1,
RC ECO:0000313|Proteomes:UP000187924};
RA Zhao D., Kumar S., Zhou J., Wang R., Xiang H.;
RT "Isolation and genome sequence of Halorientalis hydrocarbonoclasticus sp.
RT nov., a hydrocarbon-degrading haloarchaeon.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP019067; AQL44497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q1FP38; -.
DR STRING; 1932360.BV210_06735; -.
DR KEGG; hali:BV210_06735; -.
DR Proteomes; UP000187924; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR021878; TgpA_N.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR42736; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR PANTHER; PTHR42736:SF1; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR Pfam; PF11992; TgpA_N; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000187924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..316
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 96163 MW; 256E1D21A2E09991 CRC64;
MGSLSGSGAS SGSGTQGAQG TGTGDGSGFG ALDPGQRTGV GSQGSPLSES LRSQSAEPHF
VVRSSAATYW RTGAYADYTG SGWTGQGETR QRGWPRNPGV AGGDRRTITQ EYRLLQPASA
LPAAWKPIDV NGPQAENVQV TGEGGLRYGE GRLPANATYT VTSAAPPRDP ARLRGAGTDY
PDGIEERYTA LPDSTSDRLT SFTDDLTSDS ETPYDTAVAI ESWLESNKGY SLNASHEGGT
VADEFVFEME QGYCEYFAST MAVMLRTQDI PARYAVGYST GEPRANGTYL VRAMNAHAWV
EVYVPDTGWV RFDPTPGQSR LDSEFRAYQR AAENGNAEAA ARRFLESASR EDGGNPFQPN
EGGESTGDQS SSDGQSGDGS GDGGNGTDGN ASEIAERYNH TESGSPGETF DVDGEGSAEV
SLVSDPVPGQ PVTVRVERGG DPLAGAVVAF DGRRIGTTNA SGKVTGEVPF SATLDVTVTV
PDGSDAPAGS AALALPSMTG SGLPRAAANG TNTTRSFDVP TNVAVGIEDE PAPGGTVTVN
ATIAGRPVPG ANVSVNGTAA GSTDADGRLD VSLPASEHAV VRVERGEAVG NRTLELANLS
VDVSGFALPG LSVTVSVTDD GEPVEGATVG VGDATATTGS DGTATVPLPL AAGATVTVET
AAGLTETEPV QMQFLTAGVL AGLALAVLAG AYLLRRRAVQ AGRSLREQVR VALHWLSGAF
VATLVALAVR GEAVLAALPE HLRRVRAALV SLARELAAAV RARQLDLDRL PGPRALLARL
LSALAGLFAG VRDSFPGSDG VAEPDGSMAT TADTTPDTPD ARERVRRAWR EFRAQVPVAD
HRTKTPGELA REGVDAGFPR SAVRTLRDAI RDVEYGRRDP AEYVDDVDDA RRELTPGTDG
GEETADAPDS TPHATDGGDA TAAGDPDGGD RS
//
