ID W6K7W2_MAGSQ Unreviewed; 2062 AA.
AC W6K7W2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=LamG-like jellyroll fold domain-containing protein {ECO:0000259|SMART:SM00560};
GN ORFNames=MGMAQ_1292 {ECO:0000313|EMBL:CCQ73214.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ73214.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ73214.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ73214.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
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DR EMBL; FO538765; CCQ73214.1; -; Genomic_DNA.
DR STRING; 1288970.MGMAQ_1292; -.
DR KEGG; magq:MGMAQ_1292; -.
DR HOGENOM; CLU_232952_0_0_5; -.
DR OMA; DNAFVDT; -.
DR Proteomes; UP000032733; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF00353; HemolysinCabind; 9.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51120; beta-Roll; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032733};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1802..1929
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2062 AA; 206808 MW; 42FE79E87D62E6EC CRC64;
MEKEQNQDFM SEGTTASEIE GTQGETLMPT DSGADSMSSL ELLLSGLATQ GGIESAVADV
VQAALAEALA SGIQPEVAQQ ASDAFVAALV EALGDGLSPQ AALDLAKGIF VQAQAQADQN
AQNLDETWLT ELSGRDADGR TVDQLSEIEV ADLLEASPDM LGEVAEVFAQ VLREALAQGS
TLQEALSEAR GAADGFLLNG LATAGGDSLL AALASGEGLD NEFMNSEAFR EALGEALASG
ADLGVALELA AAAQAQLARA GEESDLELDP AAAMIAALAE GEDVDATLND MVLAAGGDGG
YLDALGDALA KGLGAASLEE AGQTIKSIAE ARGDTQLTLS QVDQLLQTLA TGGDVASLIR
DMGGDVGAFE QALAEAMSNG QSLGTALPNA IAASQQVVES EALVDEGGSD ILNALATGNA
DGLNGGEDFE LALSTALEQG QDPDQAVTGA NDAAQQIADA LDGDTDTQVA ANDTDDELDT
FLDEGTAAGT EEPVVEEFVD DGTGDDEALP DEGFDEFETA AGGNDTPESN GNTWNGPSFG
GDGQNGGGPG SLIGGSGNGI PTTTESRGTN SGDDGGDSDP GDTTTPDTAT TPNLLPLVAG
PLVVNSNEQS GDQDVDLLAG ASDPDGGGAL VISNLTLVSG NGVGVTVTGS VLTIDTDAYV
YLAVGETEDL VYTYDITDGD GGSVTQTATL SVAGDNEQPT VSGVVTGPSG VTEDGTSFQI
DLLRNASDED LSDDLDTQSV SVNAVGGVLP LAPVAFTVDD GTGELDLDPA QFNYLAVGES
VDLEVSYNVV DGNGGSVPTT ATVTVNGAND GPAVSGVVTG PSGVTEDGAS FQIDLLGNAS
DEDLSDDLDT QSVSVNAVGG VLPLAPVAFT VDDGTGELDL DPAQFNYLAV GESVDLEVSY
NVIDGNGGSV PTTATVTING ANDAPTVSGV VVGPSGVTDD GSAIQIDLLG NASDDDLSDD
LDTASVAVAV TGGIAPTDAV VFTIDNDSGQ VSLDSTQFDY LAVGDSVDLE FSYDVIDGNG
GFVATTATVT INGANDAPVV SAPVVGPTDA TEQSAAYEID LLSNASDVDR GADLDTSTVS
ISVSSGPSPS NPVTFVVDNL TGVLTLDPSQ FAYLSGTESV TLEISYDVID NEGGITPTTA
TTTISGITAA YYAFAVADVG TGAADEIHGG SANGLTDSNV LRIEFDPDNM PTADLLTVLQ
AYNQSDTSAY TTDSPYAIAD LNINISGWTS IETVIVRDGV AYPIDTDPAA VFIGTPGNDD
GAGGGLDLDL ANILYGDRGS DEFSGGNESD ILDGGAGRDT LSGDDGNDLL QGGEDNDILI
GGSGDDVFGI TGTDQGFDDF DGGTGSDTIL GSQGDDTIGI FESFGPADSV ETIDGGDGYN
VVEGSYKNNQ LDFSATELHN IDLITGGAGV DDIIGSDGAD TITGGTSNDV LSGGGGDDVF
RIDGSAEGFD LYDGGQGTDT ILGGDGDDSI GIDQLFDPTQ SVEVIDGGAG YNVIQGSFNT
DVMDFSATEL LNIDLIDGGS RSDTIIGSDG DDTISGGVSD DSLSGGAGND VFLVSGSSEG
SDAYSGGAGV DTILGSSGDD TIGLSGTFNA TNGINVIDGG AGTDVIAGSS SANILDFSST
VLTNIESIDG GGGSDVITGT TGADVIGGGA GSDRINGGGG DDQLSGGNGS DTFVFSSAGH
ITITDYATGN NKLDFDAVFE TLGIDSGGQV VMLDDAGDGQ TVLSVADGAG NTAESLFTVT
LADTDWTQSQ AATKIASSRV VEDATDTVAQ VDMGLEDNQA LTFDGVDDMV TLADPAALSL
TGALTVEAWI RPDSLSGDAQ TILGNDEMAL QLDGGLLNFT LNAEGLDYTI ASNGALSEGE
WIHIAGVYDG TSGDMSLYIN GIAQDQTATP GTSVDIGGQA LEVGGLGGAS LFQGAVEEVR
LWNDVRSESE IQDTMGRQLN GDEADLAGYW NFNEGGGTTV ADGTGNGHDG TVTGGAKFTN
LSQPTVGQGE TYKGLLLGTD AAGDSLTYAM AVDPDHASAM TLSGNTYTYE NDGNSAADDS
FAVTVTDSAG NETTEIVQVD IT
//