ID Q8PTX1_METMA Unreviewed; 755 AA.
AC Q8PTX1;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Putative surface layer protein {ECO:0000313|EMBL:AAM32283.1};
GN OrderedLocusNames=MM_2587 {ECO:0000313|EMBL:AAM32283.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM32283.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM32283.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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DR EMBL; AE008384; AAM32283.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PTX1; -.
DR KEGG; mma:MM_2587; -.
DR PATRIC; fig|192952.21.peg.2969; -.
DR eggNOG; arCOG02496; Archaea.
DR eggNOG; arCOG02507; Archaea.
DR HOGENOM; CLU_326164_0_0_2; -.
DR Proteomes; UP000000595; Chromosome.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR048433; YNCE-like_beta-prop.
DR InterPro; IPR011964; YVTN_b-propeller_repeat.
DR NCBIfam; TIGR02276; beta_rpt_yvtn; 5.
DR PANTHER; PTHR47197:SF3; PE-PGRS FAMILY PROTEIN PE_PGRS17; 1.
DR PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR Pfam; PF05048; NosD; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF21783; YNCE; 1.
DR SMART; SM00710; PbH1; 7.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 387..448
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 755 AA; 79127 MW; C143EDDF8AB38339 CRC64;
MASAKEIIVD DDYGADFISI QEAVNNSVTG DIIIVRSGTY TENVLVDVTG ITIRSESNNG
SVQVKPLNES TGTLLITADN ITVSGLNITG ASKDSYKNAI FTYGDMNNVT GNTVENGSIF
LGSCTLENLT GILYGEMNNV TGNIIENGSI FLGPEISDNL IAENKISNGE EGVHISCCGI
NNTVSGNTIS NCSTGIYEYD QGANIHNNRI TDCDYGISLS FASGGIDNNV ILNCNTGIFL
REACYVDIIN NTIASCAECG IFDQENNNGK RIYNNYFNSS LNIRFGAGEG ENTWNSSLAS
GTNIAGGPYT GGNFWAKPDG TGFSQICVDL DWDGIGDLPY NIYEDEFDYL PLVSRSGPQN
SVTPSANFTA SVTNGIAPLV VEFTDLSKSA VAWNWDFDSD GIPDSTKQNP VYVYRNQGNY
TVNLTASNGL TASSKTADIS VEKRVAPTWP FVYMTGGLNT LRTVSVIDIR TGIVITKVKT
GKHPSGIAVT PDGKTAYVTN SWDNNVSVID TATNTVIDSV KVGSYPCGVA VSPDGTEAYV
TNCGSNNVSV IDTGANTVTA TVPVGNWPEG IAVTPDGKKA YVANSGNITA PEDTVSVINT
INDTVTDTIP AGRHPCGVAV TPDGKKVYVA NTYGGTVSVV DAATDTVTAT VDTGNSPFKV
AVNPAGTLAY VANEGGTVSV IDTSNDTVIA TVDVAGGRLE GLAITPDGKK VYVAHYGSSD
NSTLSVIDAL NNTNTVTSSV DVEVYPGKIA IIPEP
//
