ID G9YAJ0_HAFAL Unreviewed; 1652 AA.
AC G9YAJ0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative molybdenum cofactor biosynthesis protein {ECO:0000313|EMBL:EHM39972.1};
GN ORFNames=HMPREF0454_03614 {ECO:0000313|EMBL:EHM39972.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM39972.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM39972.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM39972.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the intimin/invasin family.
CC {ECO:0000256|ARBA:ARBA00010116}.
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:EHM39972.1}.
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DR EMBL; AGCI01000087; EHM39972.1; -; Genomic_DNA.
DR PATRIC; fig|1002364.3.peg.3266; -.
DR HOGENOM; CLU_000210_1_2_6; -.
DR Proteomes; UP000005959; Unassembled WGS sequence.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 12.
DR Gene3D; 2.40.160.160; Inverse autotransporter, beta-domain; 1.
DR InterPro; IPR003344; Big_1_dom.
DR InterPro; IPR024519; IAT_beta.
DR InterPro; IPR038177; IAT_beta_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003535; Intimin/invasin_bac.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR39576; ATTACHING AND EFFACING PROTEIN HOMOLOG-RELATED-RELATED; 1.
DR PANTHER; PTHR39576:SF1; INVASIN-RELATED; 1.
DR Pfam; PF02369; Big_1; 11.
DR Pfam; PF11924; IAT_beta; 1.
DR PRINTS; PR01369; INTIMIN.
DR SMART; SM00634; BID_1; 12.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 12.
DR PROSITE; PS51127; BIG1; 12.
PE 3: Inferred from homology;
FT DOMAIN 363..456
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 459..549
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 557..659
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 667..756
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 764..853
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 861..950
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 958..1047
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 1055..1143
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 1151..1243
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 1251..1343
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 1351..1442
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 1450..1542
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT REGION 41..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 169702 MW; 9E0DCA40F95E9BA5 CRC64;
MKKVFSIRKS ELFRFFAWLQ ILLQVLFPLV SVLPHSAIAQ SSSSSSTNLS PFAVDRNGSS
TTKDTAALPY GDTMSSLASS LSSNGAEGVA SSAKSAATGY ASSSAQQWLS QFGTARVQLN
VDDNGNWDDS AIDFLAPLYD NKKSMLFTQL GLRAPDGRIT GNMGMGVRTF YVEDWMFGGN
VFFDDDFTGK NRRIGIGAEA WTNNLKLSAN TYVGTTEWHQ SRDFNDYNEK PADGYDVRAE
GYLPAYPQLG AKLMYEQYYG DKVALFDTDH LQSNPSAVTT GLSYTPIPLV QLAVNYKRGQ
DSMDDTQFQV NLRYDLGRPW AYQVDPESVR LERSLAGSRY DLVERNNQIV LQYQKKDQQS
VSNLNLQVTV DNSPSDGLTP NTAQVFATDK DGQPVRNAPI TWSTSGTAKL ATSTSVTNNS
GVASVNFTNT VPESVQVTAK SGSVTATQNS QFNAATVSNI TLKITKDNSV ADGKTPNHAV
ATVTDINNRP IANTQVKWGV DAPATLKSTQ TTTNASGQVN TDFTSTTAGA VMLTATAGDK
SASQQGHFIA NSASNVIDTM VVTKDGNAAN GTTANTVNIT VKDGNGAPVS NANVSLSADK
GTVIFGAALK AKAAKAAKTF QTDAQGALTV AFTDTVAETT QLTATLENGN TKTATANFVA
DSASAKVSDL TVTSGAVANG TATNQATVTV VDANNNPLSG VDVAWSQDGS AVFGTSAKTD
ANGKTTVKFT DTQAQTVNVT ATLASGSTLS KPSSFVADSS SAKVSDLTVT TGAIANGTAA
NQSTVTVMDA NNNPLSGVDV TWTQDGSAVF GASAKTDANG QTTVKFTDTK AQTVNVTATL
ASGSTLSKPS TFVADSSSAK VSDLTITSGA VANGTATNQA TVTVVDANSN PLSGVDVTWS
QDGSAVLGTS AKTDASGKTT VKFTDTTAQT VNVTATLASG STLSKPSTFV ADSASSKVSD
LTITSGAAAN GTATNQATVT VVDANNNPLS GVDVTWTQDG SAVFGTSTKT DANGQTTVKF
TDTKAQTVNV TATLASGSTL SKPSTFVADS SSAKVSDLTI TSGAVANGTA TNQATVTVVD
ANSNPLSGVD VTWTQDGSAV FGASAKTDAS GQTTVTFTDL KAQTVNITAA VNGNSLSKPS
SFVADATTAH VSTLTIDTDG SAANGTAQNS ATATVTDSNN NFLPNTTVNW TVTGSAGLAS
GTSTTNSNGQ AVMTFTDTKV EIVTLTAKAG SSDTGQSKTS SFVADAATAH VTTLTIDTDG
SAANGTSQNS ATATVMDSQN NILANTTVNW TTTGRAGLTS GTSTTNSSGQ AVMTFTDTKA
ETITLTAKAG SSDTGQSKTS TFIADVDTAK IDSLTITKDG SPADGSTANT ATVVVSDING
NPLSGMAVTW SADKSTVTMT PAGNTDSTGK ASVSFVDTTA ETLQLTSSLS NGSTLSQNSE
FVIDTAGLKI SQFYSASSAD IHDSTVLRLF VQDKFGKPVN GANVRLSVTG SAQLESTSGV
TSSTTSGNGT LLINITDAVV ETVTATATLD NNTSATAPVT FVQSLATAIN ITIVQDGKGI
DAPNIAVATA VDKHGFPVPG YEIRWGLGST YTSQFNFSEI SAATDSNGEV RTNIQSKSSS
FSPRTITLEA IGESYFQNNP TGETPMAFAK GS
//
