ID Q1DAE0_MYXXD Unreviewed; 988 AA.
AC Q1DAE0;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:ABF90852.1};
GN OrderedLocusNames=MXAN_2160 {ECO:0000313|EMBL:ABF90852.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90852.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF90852.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CP000113; ABF90852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1DAE0; -.
DR STRING; 246197.MXAN_2160; -.
DR EnsemblBacteria; ABF90852; ABF90852; MXAN_2160.
DR KEGG; mxa:MXAN_2160; -.
DR eggNOG; COG4932; Bacteria.
DR eggNOG; COG5184; Bacteria.
DR HOGENOM; CLU_313043_0_0_7; -.
DR OrthoDB; 5511510at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd00102; IPT; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 8.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR039163; EMC7.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR13605:SF4; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 7; 1.
DR PANTHER; PTHR13605; UNCHARACTERIZED; 1.
DR Pfam; PF13620; CarboxypepD_reg; 7.
DR Pfam; PF13540; RCC1_2; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 7.
DR PROSITE; PS50012; RCC1_3; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000313|EMBL:ABF90852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 749..807
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|Pfam:PF01833"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 102291 MW; 89141A3D4CFDC24C CRC64;
MECRRGADAP PPHACRGHSI PRNRRIHVPS GASPFPGSPS HSRFLRVALP MRLIRPSWLW
ALLLALSACS STSTTPSDAG TQPDSGTQLG RIEGQAILEG ASSHAGISVS VEGASLSTTT
ATDGRFVLEN VASGTHIVVA RMSGYSEARQ SVTVTTGATA SVRLDLGRGR GSILGNVQVE
GVLDSSGVTV TLVETGANTT TDATGLFTFS DLAQGTYTVA LQKTNYLATQ QTVEVRGTGS
TLVSLSLSRE RSSVTGVIQL EGSSNHAGAV VTLVEASLTA TTNAEGQFNI QNVMTGTYTL
RVRRENYVDA QQTVEVRANQ PSQVNLTLLL VRGDVAGTVQ LSDGATPSGV TITVTQTGAN
TTTNAQGQFT FTGLPLGTYN LTAQKEGYAV VQQSVTVRTG AAATVAFTLV RAQGRVEGTA
LLEGASSHGG ITVTLAETGA TTTTNGQGRF AFSSVAAGTY TVEARLSGYA VARESVQVQE
NQQATVSLSL ARERGNVAGV IQLEGGSSPV DINVTLAGTA FSARTNTAGQ FSLTGVPTGS
YTLEAQKDGF ATGQRTVEVR AGEQAQVSLT LSRARGSISG VVLLEDANTT SGISVALVES
NASVLTDAQG RFSFSGLIVG TYTLSAYWTG YEIQERSVVV RNQETTVVNI TLRRRPGVVT
GTIQLEGESH HEGVTVSLSG HGATAMTDAQ GHFVLEDVPQ GRHTLAASKA NYAKAEAALD
VREGEPLPVS LALSRLGALE VSAPKLAVQG GHLTLTGSGF GAERGPFTVT VGGEAVTDFI
SWSDTEVVAR VAHHVAPGER DVVVTPGVPW RRNTTTSVWV VPQKTVAYGE HWGVGVLASN
HVSVWGGPSL ADIHPIPAGL TDVVSVATSR RTAFALQADG TVVAWGGDLP SDLSVPADLT
EVVAIAGGDS FVLALKADGT VVAWGESAIA PSSDVRDVVG IAVTSNASQA FLAGGTVVTW
GQDNEGRATP AEQLYLPPHD LLLRIPAR
//
