|
Name |
Accession |
Description |
Interval |
E-value |
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
595-727 |
6.95e-44 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 154.36 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAFDHVRKVYVGQGDSGVAYVKFDYEK-DGKKETQEHGKMTLSGTEEFEVD-SDDYITSMEVYVDKVYGYKSEI 672
Cdd:pfam01419 1 GASWDDGVYDGVRKVYVGQGGDGITYIKFEYVKgGGKVEGDEHGKKGLLGPEEFEIDyPDEYITSVEGTYDKVFGSDSEV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 673 VIALTFKTFKGETSPRFGIETENKYEVKdGKGGKLAGFHGKASDVLYAIGAYFIP 727
Cdd:pfam01419 81 ITSLTFKTNKGRTSPFFGTPSGTKFSLE-VKGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
441-572 |
7.73e-41 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 145.88 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGtDHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGRGGTSTIEISHPDEYLVSVEGLYD-----SSN 515
Cdd:pfam01419 1 GASWDDG-VYDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKGLLGPEEFEIDYPDEYITSVEGTYDkvfgsDSE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694415 516 IIQGIQFQSNK-HTSQYFGYEyygDGTQFSLQVNEKKIIGFHGFADSHLNSLGAYFVP 572
Cdd:pfam01419 80 VITSLTFKTNKgRTSPFFGTP---SGTKFSLEVKGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
441-570 |
6.51e-39 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 140.39 E-value: 6.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGTDHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGrGGTSTIEISHPDEYLVSVEGLYDS---SNII 517
Cdd:cd09612 1 GSAWDDGVFPDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGG-GTPEEIVLDYPDEYITSVSGTYGPvsgSNVI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1063694415 518 QGIQFQSNKHTSQYFGYEyygDGTQFSLQVNEKKIIGFHGFADSHLNSLGAYF 570
Cdd:cd09612 80 TSLTFKTNKRTYGPFGVE---SGTPFSLPVEGGKIVGFHGRSGDYLDAIGVYV 129
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
595-727 |
2.98e-38 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 138.13 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAFDHVRKVYVGQGDSGVAYVKFDYEKDGKKETQEHGKMTLSgTEEFEVDSDDYITSMEVYVDkvygyKSEIVI 674
Cdd:smart00915 1 GTEWDDGAFDGVRKIYVGQGGEGIKSIQFDYDKGGKVWGDEHGGKGGT-GEEILLYPGEYITSVEGTYD-----KSGVIT 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063694415 675 ALTFKTFKGETSPRFGIETENKYEVKDGKGGKLAGFHG-KASDVLYAIGAYFIP 727
Cdd:smart00915 75 SLTFKTNKGRTSPFGGYEGGTKFVLESKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
441-572 |
8.22e-37 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 134.28 E-value: 8.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGtDHDGVMKIHVAVGGLGIEQIRFDYVKnGQLKEGPFHGvkGRGGTSTIEISHPDEYLVSVEGLYDSSNIIQGI 520
Cdd:smart00915 1 GTEWDDG-AFDGVRKIYVGQGGEGIKSIQFDYDK-GGKVWGDEHG--GKGGTGEEILLYPGEYITSVEGTYDKSGVITSL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 521 QFQSNK-HTSQYFGYEyygDGTQFSLQ-VNEKKIIGFHG-FADSHLNSLGAYFVP 572
Cdd:smart00915 77 TFKTNKgRTSPFGGYE---GGTKFVLEsKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
586-724 |
9.43e-37 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 144.33 E-value: 9.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 586 KVKAQGGSYGETFDDGAFDHVRKVYVGQGDSGVAYVKFDYeKDGKKET--QEHGKMTLSGTEEFEVDSDDYITSMEVYVD 663
Cdd:PLN02193 4 KLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEY-VNGSQVVvgDEHGKKTELGVEEFEIDADDYIVYVEGYRE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063694415 664 KVYGYKSEIVIALTFKTFKGETSPRFGIETENKYEVkdgKGGKLAGFHGKASDVLYAIGAY 724
Cdd:PLN02193 83 KVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVL---QGGKIVGFHGRSTDVLHSLGAY 140
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
595-725 |
1.18e-31 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 119.59 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAF-DHVRKVYVGQGDSGVAYVKFDYEKDGKK-ETQEHGKMTLsGTEEFEVD-SDDYITSMEVYVDKVYGykSE 671
Cdd:cd09612 1 GSAWDDGVFpDGLRKITVRSGENGIDSIKFEYDKDGQHvVGPWHGGGGG-TPEEIVLDyPDEYITSVSGTYGPVSG--SN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063694415 672 IVIALTFKTFKGeTSPRFGIETENKYEVKdGKGGKLAGFHGKASDVLYAIGAYF 725
Cdd:cd09612 78 VITSLTFKTNKR-TYGPFGVESGTPFSLP-VEGGKIVGFHGRSGDYLDAIGVYV 129
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
2-126 |
4.38e-31 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 118.10 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 2 SWDDGKHTKVKRVQLTFD-DVIRSIEVEYD-GTSLKSQPRGTAGTKIDGFTLSSDEYITEVNGYYKTTfsgEVITSLTFK 79
Cdd:smart00915 3 EWDDGAFDGVRKIYVGQGgEGIKSIQFDYDkGGKVWGDEHGGKGGTGEEILLYPGEYITSVEGTYDKS---GVITSLTFK 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1063694415 80 TNK-RTYGTYGNKTSSYFSVAAPKDNQIVGFLG-SSSHALNSIDAHFAP 126
Cdd:smart00915 80 TNKgRTSPFGGYEGGTKFVLESKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
2-125 |
1.33e-27 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 108.04 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 2 SWDDG-KHTKVKRVQLTFDD-VIRSIEVEYDGTSLKSQPR--GTAGTKIDGFTL-SSDEYITEVNGYYKTTFSGEVITSL 76
Cdd:cd09612 3 AWDDGvFPDGLRKITVRSGEnGIDSIKFEYDKDGQHVVGPwhGGGGGTPEEIVLdYPDEYITSVSGTYGPVSGSNVITSL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1063694415 77 TFKTNKRTYGTYGNKTSSYFSVAApKDNQIVGFLGSSSHALNSIDAHFA 125
Cdd:cd09612 83 TFKTNKRTYGPFGVESGTPFSLPV-EGGKIVGFHGRSGDYLDAIGVYVS 130
|
|
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
1-126 |
3.54e-27 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 106.98 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 1 MSWDDGKHTKVKRVQLTFD-DVIRSIEVEYDGTSLKSQ-----PRGTAGTKIDGFTLSsDEYITEVNGYYKTTFSG--EV 72
Cdd:pfam01419 2 ASWDDGVYDGVRKVYVGQGgDGITYIKFEYVKGGGKVEgdehgKKGLLGPEEFEIDYP-DEYITSVEGTYDKVFGSdsEV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 73 ITSLTFKTNK-RTYGTYGNKTSSYFSVAApKDNQIVGFLGSSSHALNSIDAHFAP 126
Cdd:pfam01419 81 ITSLTFKTNKgRTSPFFGTPSGTKFSLEV-KGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
431-569 |
2.62e-17 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 85.39 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 431 QKLEAQGGNGGNQWDDGTdHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGRGGTSTIEIShPDEYLVSVEGL 510
Cdd:PLN02193 3 QKLEAKGGETGDVWDDGV-YDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEID-ADDYIVYVEGY 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 511 YD-----SSNIIQGIQFQSNK-HTSQYFGYEyygDGTQFSLQVNekKIIGFHGFADSHLNSLGAY 569
Cdd:PLN02193 81 REkvndmTSEMITFLSFKTYKgKTSHPIEKR---PGVKFVLQGG--KIVGFHGRSTDVLHSLGAY 140
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
130-443 |
5.81e-06 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 49.91 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 130 PGS-TGAKPGASGIGSDSG--SIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSA 206
Cdd:NF033609 565 PGSdSGSDSSNSDSGSDSGsdSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 207 GTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNI-----G 281
Cdd:NF033609 645 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdS 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 282 DTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGA 361
Cdd:NF033609 725 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 362 GGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGT-SPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGNG 440
Cdd:NF033609 805 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNA 884
|
...
gi 1063694415 441 GNQ 443
Cdd:NF033609 885 SNK 887
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
40-452 |
8.23e-06 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 49.38 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 40 GTAGTKIDGFTLSSDEYITEVNGYYKTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNS 119
Cdd:COG3210 816 GSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGT 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 120 IDAHFAPAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGS 199
Cdd:COG3210 896 LTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSS 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 200 KPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSN 279
Cdd:COG3210 976 AVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISG 1055
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 280 IGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNP 359
Cdd:COG3210 1056 GNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTA 1135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 360 GAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGN 439
Cdd:COG3210 1136 STEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTN 1215
|
410
....*....|...
gi 1063694415 440 GGNQWDDGTDHDG 452
Cdd:COG3210 1216 VTTTTTLTASDTG 1228
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
3-134 |
1.95e-05 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 47.64 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 3 WDDGKHTKVKRVQL-TFDDVIRSIEVEY-DGTSLKSQPRGTAGTK--IDGFTLSSDEYITEVNGYYKTTF--SGEVITSL 76
Cdd:PLN02193 16 WDDGVYDNVRKVYVgQGQYGIAFVKFEYvNGSQVVVGDEHGKKTElgVEEFEIDADDYIVYVEGYREKVNdmTSEMITFL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063694415 77 TFKTNK-RTYGTYGNKTSSYFSVAAPKdnqIVGFLGSSSHALNSIDAHFAPAPPPGSTG 134
Cdd:PLN02193 96 SFKTYKgKTSHPIEKRPGVKFVLQGGK---IVGFHGRSTDVLHSLGAYISLPSTPKLLG 151
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
167-409 |
3.44e-05 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 46.92 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 167 NAGGSKPSSGSAGTNPGASAVGNGETEKNaGGSKPSSGSAGTNPGASAGGNGeteKNVGGSKPSSGKAGTNPGANAGGNG 246
Cdd:cd21118 119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGT-GGPWASGGNYGTNSLGGSVGQG---GNGGPLNYGTNSQGAVAQPGYGTVR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 247 GTEKNAGGsksssgsarTNPGASAGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTE 326
Cdd:cd21118 195 GNNQNSGC---------TNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 327 SDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIEGTENNVG--GKETNPGASGIGNSDGSTGTSPEGTES 404
Cdd:cd21118 266 NGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRmaGGGGSQGSKESSGSHGSNGGNGQAEAV 345
|
....*
gi 1063694415 405 NADGT 409
Cdd:cd21118 346 GGLNT 350
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
111-429 |
6.89e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 46.44 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 111 GSSSHALNSIDAHFAPAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNG 190
Cdd:NF033609 583 GSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDS 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 191 ETEKNAGGSKPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASA 270
Cdd:NF033609 663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 271 GGNGETVSNiGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGS 350
Cdd:NF033609 743 DSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 351 NDGSTGTNPGAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKES---------NTG 421
Cdd:NF033609 822 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEakdskeplpDTG 901
|
....*...
gi 1063694415 422 SESNTNSS 429
Cdd:NF033609 902 SEDEANTS 909
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
181-434 |
1.01e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 181 NPGASAVGNGETEKNAGGSKPSSGSAGTNPGASAGGNGETEKNvgGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSG 260
Cdd:TIGR00927 640 HTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESE--GEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEH 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 261 SARTNPGAS-------AGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTE---SDAG 330
Cdd:TIGR00927 718 EGETEAEGTedegeieTGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEmkgDEGA 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 331 GSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGstGTSPEgtESNADGTK 410
Cdd:TIGR00927 798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDG--GDSEE--EEEEEEEE 873
|
250 260
....*....|....*....|....
gi 1063694415 411 TNTGGKESNTGSESNTNSSPQKLE 434
Cdd:TIGR00927 874 EEEEEEEEEEEEEEEENEEPLSLE 897
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
65-426 |
1.06e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.60 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 65 KTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSV-----AAPkdNQIVGfLGSSSHALNSIDAhfapappPGSTGakPGA 139
Cdd:pfam05109 401 KTLIITRTATNATTTTHKVIFSKAPESTTTSPTLnttgfAAP--NTTTG-LPSSTHVPTNLTA-------PASTG--PTV 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 140 SGigSDSGSIGSAGTNPGADGTRETEknaggSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSAGTNPGASAGGNGE 219
Cdd:pfam05109 469 ST--ADVTSPTPAGTTSGASPVTPSP-----SPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 220 TEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGSKSN------ 293
Cdd:pfam05109 542 TSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTpvvtsp 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 294 -DGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSG---------NGGTN--DGASGIGSNDGSTGTNPGA 361
Cdd:pfam05109 622 pKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHmplltsahpTGGENitQVTPASTSTHHVSTSSPAP 701
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 362 GGGTDSNIEGTENNvgGKETNPG----ASGIGNSDGSTGTSPEGtESNADGTKTNTGGK-ESNTGSESNT 426
Cdd:pfam05109 702 RPGTTSQASGPGNS--STSTKPGevnvTKGTPPKNATSPQAPSG-QKTAVPTVTSTGGKaNSTTGGKHTT 768
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
111-357 |
1.37e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 111 GSSSHALNSIDAHFAPAPPPGST--GAKPGASGIGSDSG---SIGSAGTNPGADGTRETEKNAGgSKPSSGSAGTNPGAS 185
Cdd:PHA03307 170 RQAALPLSSPEETARAPSSPPAEppPSTPPAAASPRPPRrssPISASASSPAPAPGRSAADDAG-ASSSDSSSSESSGCG 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 186 AVGNGETEK-----------NAGGSKPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGG 254
Cdd:PHA03307 249 WGPENECPLprpapitlptrIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 255 SKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKT 334
Cdd:PHA03307 329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
|
250 260
....*....|....*....|....*.
gi 1063694415 335 NS---GNGGTNDGASGIGSNDGSTGT 357
Cdd:PHA03307 409 AGrprPSPLDAGAASGAFYARYPLLT 434
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
595-727 |
6.95e-44 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 154.36 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAFDHVRKVYVGQGDSGVAYVKFDYEK-DGKKETQEHGKMTLSGTEEFEVD-SDDYITSMEVYVDKVYGYKSEI 672
Cdd:pfam01419 1 GASWDDGVYDGVRKVYVGQGGDGITYIKFEYVKgGGKVEGDEHGKKGLLGPEEFEIDyPDEYITSVEGTYDKVFGSDSEV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 673 VIALTFKTFKGETSPRFGIETENKYEVKdGKGGKLAGFHGKASDVLYAIGAYFIP 727
Cdd:pfam01419 81 ITSLTFKTNKGRTSPFFGTPSGTKFSLE-VKGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
441-572 |
7.73e-41 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 145.88 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGtDHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGRGGTSTIEISHPDEYLVSVEGLYD-----SSN 515
Cdd:pfam01419 1 GASWDDG-VYDGVRKVYVGQGGDGITYIKFEYVKGGGKVEGDEHGKKGLLGPEEFEIDYPDEYITSVEGTYDkvfgsDSE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694415 516 IIQGIQFQSNK-HTSQYFGYEyygDGTQFSLQVNEKKIIGFHGFADSHLNSLGAYFVP 572
Cdd:pfam01419 80 VITSLTFKTNKgRTSPFFGTP---SGTKFSLEVKGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
441-570 |
6.51e-39 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 140.39 E-value: 6.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGTDHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGrGGTSTIEISHPDEYLVSVEGLYDS---SNII 517
Cdd:cd09612 1 GSAWDDGVFPDGLRKITVRSGENGIDSIKFEYDKDGQHVVGPWHGGGG-GTPEEIVLDYPDEYITSVSGTYGPvsgSNVI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1063694415 518 QGIQFQSNKHTSQYFGYEyygDGTQFSLQVNEKKIIGFHGFADSHLNSLGAYF 570
Cdd:cd09612 80 TSLTFKTNKRTYGPFGVE---SGTPFSLPVEGGKIVGFHGRSGDYLDAIGVYV 129
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
595-727 |
2.98e-38 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 138.13 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAFDHVRKVYVGQGDSGVAYVKFDYEKDGKKETQEHGKMTLSgTEEFEVDSDDYITSMEVYVDkvygyKSEIVI 674
Cdd:smart00915 1 GTEWDDGAFDGVRKIYVGQGGEGIKSIQFDYDKGGKVWGDEHGGKGGT-GEEILLYPGEYITSVEGTYD-----KSGVIT 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063694415 675 ALTFKTFKGETSPRFGIETENKYEVKDGKGGKLAGFHG-KASDVLYAIGAYFIP 727
Cdd:smart00915 75 SLTFKTNKGRTSPFGGYEGGTKFVLESKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
441-572 |
8.22e-37 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 134.28 E-value: 8.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 441 GNQWDDGtDHDGVMKIHVAVGGLGIEQIRFDYVKnGQLKEGPFHGvkGRGGTSTIEISHPDEYLVSVEGLYDSSNIIQGI 520
Cdd:smart00915 1 GTEWDDG-AFDGVRKIYVGQGGEGIKSIQFDYDK-GGKVWGDEHG--GKGGTGEEILLYPGEYITSVEGTYDKSGVITSL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 521 QFQSNK-HTSQYFGYEyygDGTQFSLQ-VNEKKIIGFHG-FADSHLNSLGAYFVP 572
Cdd:smart00915 77 TFKTNKgRTSPFGGYE---GGTKFVLEsKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
586-724 |
9.43e-37 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 144.33 E-value: 9.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 586 KVKAQGGSYGETFDDGAFDHVRKVYVGQGDSGVAYVKFDYeKDGKKET--QEHGKMTLSGTEEFEVDSDDYITSMEVYVD 663
Cdd:PLN02193 4 KLEAKGGETGDVWDDGVYDNVRKVYVGQGQYGIAFVKFEY-VNGSQVVvgDEHGKKTELGVEEFEIDADDYIVYVEGYRE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063694415 664 KVYGYKSEIVIALTFKTFKGETSPRFGIETENKYEVkdgKGGKLAGFHGKASDVLYAIGAY 724
Cdd:PLN02193 83 KVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVL---QGGKIVGFHGRSTDVLHSLGAY 140
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
595-725 |
1.18e-31 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 119.59 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 595 GETFDDGAF-DHVRKVYVGQGDSGVAYVKFDYEKDGKK-ETQEHGKMTLsGTEEFEVD-SDDYITSMEVYVDKVYGykSE 671
Cdd:cd09612 1 GSAWDDGVFpDGLRKITVRSGENGIDSIKFEYDKDGQHvVGPWHGGGGG-TPEEIVLDyPDEYITSVSGTYGPVSG--SN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063694415 672 IVIALTFKTFKGeTSPRFGIETENKYEVKdGKGGKLAGFHGKASDVLYAIGAYF 725
Cdd:cd09612 78 VITSLTFKTNKR-TYGPFGVESGTPFSLP-VEGGKIVGFHGRSGDYLDAIGVYV 129
|
|
| Jacalin |
smart00915 |
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a ... |
2-126 |
4.38e-31 |
|
Jacalin-like lectin domain; This entry represents a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B- cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
Pssm-ID: 214909 [Multi-domain] Cd Length: 128 Bit Score: 118.10 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 2 SWDDGKHTKVKRVQLTFD-DVIRSIEVEYD-GTSLKSQPRGTAGTKIDGFTLSSDEYITEVNGYYKTTfsgEVITSLTFK 79
Cdd:smart00915 3 EWDDGAFDGVRKIYVGQGgEGIKSIQFDYDkGGKVWGDEHGGKGGTGEEILLYPGEYITSVEGTYDKS---GVITSLTFK 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1063694415 80 TNK-RTYGTYGNKTSSYFSVAAPKDNQIVGFLG-SSSHALNSIDAHFAP 126
Cdd:smart00915 80 TNKgRTSPFGGYEGGTKFVLESKEGKKIVGFHGrSSGDGLDSLGAYFSP 128
|
|
| Jacalin |
cd09612 |
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains ... |
2-125 |
1.33e-27 |
|
Jacalin-like plant lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. The family was initially named after an abundant protein found in the jackfruit seed. Jacalin specifically binds to the alpha-O-glycoside of the disaccharide Gal-beta1-3-GalNAc, and has proven useful in the study of O-linked glycoproteins. Jacalin-like lectins in this family may occur in various oligomerization states.
Pssm-ID: 187708 [Multi-domain] Cd Length: 130 Bit Score: 108.04 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 2 SWDDG-KHTKVKRVQLTFDD-VIRSIEVEYDGTSLKSQPR--GTAGTKIDGFTL-SSDEYITEVNGYYKTTFSGEVITSL 76
Cdd:cd09612 3 AWDDGvFPDGLRKITVRSGEnGIDSIKFEYDKDGQHVVGPwhGGGGGTPEEIVLdYPDEYITSVSGTYGPVSGSNVITSL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1063694415 77 TFKTNKRTYGTYGNKTSSYFSVAApKDNQIVGFLGSSSHALNSIDAHFA 125
Cdd:cd09612 83 TFKTNKRTYGPFGVESGTPFSLPV-EGGKIVGFHGRSGDYLDAIGVYVS 130
|
|
| Jacalin |
pfam01419 |
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 ... |
1-126 |
3.54e-27 |
|
Jacalin-like lectin domain; Proteins containing this domain are lectins. It is found in 1 to 6 copies in these proteins. The domain is also found in the animal prostatic spermine-binding protein.
Pssm-ID: 396138 [Multi-domain] Cd Length: 134 Bit Score: 106.98 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 1 MSWDDGKHTKVKRVQLTFD-DVIRSIEVEYDGTSLKSQ-----PRGTAGTKIDGFTLSsDEYITEVNGYYKTTFSG--EV 72
Cdd:pfam01419 2 ASWDDGVYDGVRKVYVGQGgDGITYIKFEYVKGGGKVEgdehgKKGLLGPEEFEIDYP-DEYITSVEGTYDKVFGSdsEV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 73 ITSLTFKTNK-RTYGTYGNKTSSYFSVAApKDNQIVGFLGSSSHALNSIDAHFAP 126
Cdd:pfam01419 81 ITSLTFKTNKgRTSPFFGTPSGTKFSLEV-KGKKIVGFHGRAGNALNALGAYFAP 134
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
431-569 |
2.62e-17 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 85.39 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 431 QKLEAQGGNGGNQWDDGTdHDGVMKIHVAVGGLGIEQIRFDYVKNGQLKEGPFHGVKGRGGTSTIEIShPDEYLVSVEGL 510
Cdd:PLN02193 3 QKLEAKGGETGDVWDDGV-YDNVRKVYVGQGQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEID-ADDYIVYVEGY 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063694415 511 YD-----SSNIIQGIQFQSNK-HTSQYFGYEyygDGTQFSLQVNekKIIGFHGFADSHLNSLGAY 569
Cdd:PLN02193 81 REkvndmTSEMITFLSFKTYKgKTSHPIEKR---PGVKFVLQGG--KIVGFHGRSTDVLHSLGAY 140
|
|
| Jacalin_ZG16_like |
cd09611 |
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ... |
22-123 |
1.78e-06 |
|
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.
Pssm-ID: 187707 [Multi-domain] Cd Length: 128 Bit Score: 47.70 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 22 IRSIEVEYDGTSlkSQPRGTAGTKIDGFTLSSDEYITEVNGYYKTtfsgeVITSLTFKTNKRTYGTYGNKTSSYFS-VAA 100
Cdd:cd09611 30 IKGIQVRYGSNW--SDVYGGRGGNEQEIVLEPGESITKVSGSYKI-----YLHGLVFTTNKGRYLSFGKLRGRSFNaTPP 102
|
90 100
....*....|....*....|....
gi 1063694415 101 PKDNQIVGFLGSSSHA-LNSIDAH 123
Cdd:cd09611 103 PSNYVLRGISGRYGGLgIKSIGFH 126
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
130-443 |
5.81e-06 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 49.91 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 130 PGS-TGAKPGASGIGSDSG--SIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSA 206
Cdd:NF033609 565 PGSdSGSDSSNSDSGSDSGsdSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 207 GTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNI-----G 281
Cdd:NF033609 645 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdS 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 282 DTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGA 361
Cdd:NF033609 725 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 362 GGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGT-SPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGNG 440
Cdd:NF033609 805 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNA 884
|
...
gi 1063694415 441 GNQ 443
Cdd:NF033609 885 SNK 887
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
40-452 |
8.23e-06 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 49.38 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 40 GTAGTKIDGFTLSSDEYITEVNGYYKTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNS 119
Cdd:COG3210 816 GSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGT 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 120 IDAHFAPAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGS 199
Cdd:COG3210 896 LTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSS 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 200 KPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSN 279
Cdd:COG3210 976 AVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISG 1055
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 280 IGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNP 359
Cdd:COG3210 1056 GNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTA 1135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 360 GAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGN 439
Cdd:COG3210 1136 STEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTN 1215
|
410
....*....|...
gi 1063694415 440 GGNQWDDGTDHDG 452
Cdd:COG3210 1216 VTTTTTLTASDTG 1228
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
131-466 |
1.31e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 48.61 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 131 GSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSAGTNP 210
Cdd:COG5295 257 SGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTAS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 211 GASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGS 290
Cdd:COG5295 337 GASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAAGG 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 291 KSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIE 370
Cdd:COG5295 417 AAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIAGATATGAG 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 371 GTENNVGGKETNpGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGNGGNQWDDGTDH 450
Cdd:COG5295 497 AAAGGAGAGAAG-GAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANSVALGAGS 575
|
330
....*....|....*.
gi 1063694415 451 DGVMKIHVAVGGLGIE 466
Cdd:COG5295 576 VASGANSVSVGAAGAE 591
|
|
| Jacalin_like |
cd09302 |
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ... |
445-567 |
1.63e-05 |
|
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
Pssm-ID: 187706 Cd Length: 128 Bit Score: 45.09 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 445 DDGTDHDGVMKIHVAVGGLgIEQIRFDYvkngQLKEGPFHGvkGRGGTSTIEIS-HPDEYLVSVE---GLYDSSNIIQGI 520
Cdd:cd09302 6 DTGGDGARLTEIRVRSGGA-VDAIRVVL----RDYTDGRHG--GNGGPNTSSVFlDPGEYITITSvssGDNGGGTRIDAI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063694415 521 QFQSNKHTSQYFGYEYYGDGTQFSLQVNeKKIIGFHGFADSHLNSLG 567
Cdd:cd09302 79 QFTTNKGRSGTYGTTSGALGTEFTVPVG-GEIVGIYGRAGDDVDAFG 124
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
3-134 |
1.95e-05 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 47.64 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 3 WDDGKHTKVKRVQL-TFDDVIRSIEVEY-DGTSLKSQPRGTAGTK--IDGFTLSSDEYITEVNGYYKTTF--SGEVITSL 76
Cdd:PLN02193 16 WDDGVYDNVRKVYVgQGQYGIAFVKFEYvNGSQVVVGDEHGKKTElgVEEFEIDADDYIVYVEGYREKVNdmTSEMITFL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063694415 77 TFKTNK-RTYGTYGNKTSSYFSVAAPKdnqIVGFLGSSSHALNSIDAHFAPAPPPGSTG 134
Cdd:PLN02193 96 SFKTYKgKTSHPIEKRPGVKFVLQGGK---IVGFHGRSTDVLHSLGAYISLPSTPKLLG 151
|
|
| Jacalin_like |
cd09302 |
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ... |
5-113 |
2.35e-05 |
|
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.
Pssm-ID: 187706 Cd Length: 128 Bit Score: 44.32 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 5 DGKHTKVKRVQLTFDDVIRSIEVEY-DGTSLKSQPRGTAGTKIdgFTLSSDEYITEVNGYYKTTFSGEVITSLTFKTNKR 83
Cdd:cd09302 8 GGDGARLTEIRVRSGGAVDAIRVVLrDYTDGRHGGNGGPNTSS--VFLDPGEYITITSVSSGDNGGGTRIDAIQFTTNKG 85
|
90 100 110
....*....|....*....|....*....|.
gi 1063694415 84 TYGTYGNKTSS-YFSVAAPKDNQIVGFLGSS 113
Cdd:cd09302 86 RSGTYGTTSGAlGTEFTVPVGGEIVGIYGRA 116
|
|
| griffithsin_like |
cd09614 |
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin ... |
3-125 |
3.05e-05 |
|
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.
Pssm-ID: 187710 Cd Length: 128 Bit Score: 44.31 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 3 WDDGKHTKVKRVQLTFDDVIRSIEVEYDGTSLKSQPR--GTAGTKIDGFTLSSDEYITEVNGYYkttfsGEVITSLTFKT 80
Cdd:cd09614 7 GSDFDILTVSAIQLRSGSYVDQIITDYQDLNGTQNFHhgGGGGNLSPTLNFSSGEYITEVTGRS-----GDRVDQVQFTT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1063694415 81 NKRT-YGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNSIDAHFA 125
Cdd:cd09614 82 NYGGrTLPGGGGGGSAFTWTVPDNQKVIGFAGRSGSYLDQLQVYYL 127
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
167-409 |
3.44e-05 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 46.92 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 167 NAGGSKPSSGSAGTNPGASAVGNGETEKNaGGSKPSSGSAGTNPGASAGGNGeteKNVGGSKPSSGKAGTNPGANAGGNG 246
Cdd:cd21118 119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGT-GGPWASGGNYGTNSLGGSVGQG---GNGGPLNYGTNSQGAVAQPGYGTVR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 247 GTEKNAGGsksssgsarTNPGASAGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTE 326
Cdd:cd21118 195 GNNQNSGC---------TNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 327 SDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIEGTENNVG--GKETNPGASGIGNSDGSTGTSPEGTES 404
Cdd:cd21118 266 NGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRmaGGGGSQGSKESSGSHGSNGGNGQAEAV 345
|
....*
gi 1063694415 405 NADGT 409
Cdd:cd21118 346 GGLNT 350
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
111-429 |
6.89e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 46.44 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 111 GSSSHALNSIDAHFAPAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNG 190
Cdd:NF033609 583 GSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDS 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 191 ETEKNAGGSKPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASA 270
Cdd:NF033609 663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 271 GGNGETVSNiGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGS 350
Cdd:NF033609 743 DSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 351 NDGSTGTNPGAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKES---------NTG 421
Cdd:NF033609 822 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEakdskeplpDTG 901
|
....*...
gi 1063694415 422 SESNTNSS 429
Cdd:NF033609 902 SEDEANTS 909
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
40-462 |
1.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 45.54 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 40 GTAGTKIDGFTLSSDEYITEVNGYYKTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNS 119
Cdd:COG4625 70 GGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 120 IDAHFAPAP-PPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGG 198
Cdd:COG4625 150 GGGGGGGAGgAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 199 SKPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVS 278
Cdd:COG4625 230 GGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 279 NIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSK-TNSGNGGTNDGASGIGSNDGSTGT 357
Cdd:COG4625 310 GGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGgGGGGGGGGGGGSGGGGAGGGGGSG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 358 NPGAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQG 437
Cdd:COG4625 390 GGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGS 469
|
410 420
....*....|....*....|....*
gi 1063694415 438 GNGGNQWDDGTDHDGVMKIHVAVGG 462
Cdd:COG4625 470 GSGAGTLTLTGNNTYTGTTTVNGGG 494
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
66-429 |
1.86e-04 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 45.14 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 66 TTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNSIDAHFAPAPPPGSTGAKPGASGIGSD 145
Cdd:COG3210 348 TGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 146 SGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSAGTNPGASAGGNGETEKNVG 225
Cdd:COG3210 428 TTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 226 GSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGSKSNDGANNGASGIES 305
Cdd:COG3210 508 NGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTS 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 306 NAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIEGTENNVGGKETNPGA 385
Cdd:COG3210 588 ATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTA 667
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1063694415 386 SGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSS 429
Cdd:COG3210 668 GGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTG 711
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
138-374 |
2.40e-04 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 44.22 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 138 GASGIGSDSGSIGSAGtNPGADGTreteknaGGSKPSSGSAGTNPGASAVGNGeteKNAGGSKPSSGSAGTNPGASAGGN 217
Cdd:cd21118 125 GGHGAYGSQGGPGVQG-HGIPGGT-------GGPWASGGNYGTNSLGGSVGQG---GNGGPLNYGTNSQGAVAQPGYGTV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 218 GETEKNVGGSKP--SSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGG-NGETVSNIGDTESNAGGSKSND 294
Cdd:cd21118 194 RGNNQNSGCTNPppSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGnNGSSSSNSGNSGGSNGGSSGNS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 295 GANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNdGASGIGSNDGSTGTNPGAGGGTDSNIEGTEN 374
Cdd:cd21118 274 GSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGG-GSQGSKESSGSHGSNGGNGQAEAVGGLNTLN 352
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
131-412 |
3.81e-04 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 43.99 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 131 GSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSAGTNP 210
Cdd:COG5295 320 AAALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 211 GASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGS 290
Cdd:COG5295 400 GSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 291 KSNDGANNgASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIE 370
Cdd:COG5295 480 AATSSAAI-AGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAV 558
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063694415 371 GTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTN 412
Cdd:COG5295 559 GNNTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDT 600
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
40-378 |
5.10e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 43.40 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 40 GTAGTKIDGFTLSSDEYITEVNGYYKTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSVAAPKDNQIVGFLGSSSHALNS 119
Cdd:COG3468 99 GGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 120 IDAHFAPAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGS 199
Cdd:COG3468 179 GGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGGGA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 200 KPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNpgaNAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSN 279
Cdd:COG3468 259 AGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGG---GGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 280 IGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGGTNDGASGIGSNDGSTGTNP 359
Cdd:COG3468 336 GGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGG 415
|
330
....*....|....*....
gi 1063694415 360 GAGGGTDSNIEGTENNVGG 378
Cdd:COG3468 416 LTLTGGTLTVNGNYTGNNG 434
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
181-434 |
1.01e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 181 NPGASAVGNGETEKNAGGSKPSSGSAGTNPGASAGGNGETEKNvgGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSG 260
Cdd:TIGR00927 640 HTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESE--GEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEH 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 261 SARTNPGAS-------AGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTE---SDAG 330
Cdd:TIGR00927 718 EGETEAEGTedegeieTGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEmkgDEGA 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 331 GSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNIEGTENNVGGKETNPGASGIGNSDGstGTSPEgtESNADGTK 410
Cdd:TIGR00927 798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDG--GDSEE--EEEEEEEE 873
|
250 260
....*....|....*....|....
gi 1063694415 411 TNTGGKESNTGSESNTNSSPQKLE 434
Cdd:TIGR00927 874 EEEEEEEEEEEEEEEENEEPLSLE 897
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
65-426 |
1.06e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.60 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 65 KTTFSGEVITSLTFKTNKRTYGTYGNKTSSYFSV-----AAPkdNQIVGfLGSSSHALNSIDAhfapappPGSTGakPGA 139
Cdd:pfam05109 401 KTLIITRTATNATTTTHKVIFSKAPESTTTSPTLnttgfAAP--NTTTG-LPSSTHVPTNLTA-------PASTG--PTV 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 140 SGigSDSGSIGSAGTNPGADGTRETEknaggSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSGSAGTNPGASAGGNGE 219
Cdd:pfam05109 469 ST--ADVTSPTPAGTTSGASPVTPSP-----SPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 220 TEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGSKSN------ 293
Cdd:pfam05109 542 TSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTpvvtsp 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 294 -DGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSG---------NGGTN--DGASGIGSNDGSTGTNPGA 361
Cdd:pfam05109 622 pKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHmplltsahpTGGENitQVTPASTSTHHVSTSSPAP 701
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 362 GGGTDSNIEGTENNvgGKETNPG----ASGIGNSDGSTGTSPEGtESNADGTKTNTGGK-ESNTGSESNT 426
Cdd:pfam05109 702 RPGTTSQASGPGNS--STSTKPGevnvTKGTPPKNATSPQAPSG-QKTAVPTVTSTGGKaNSTTGGKHTT 768
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
111-357 |
1.37e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 111 GSSSHALNSIDAHFAPAPPPGST--GAKPGASGIGSDSG---SIGSAGTNPGADGTRETEKNAGgSKPSSGSAGTNPGAS 185
Cdd:PHA03307 170 RQAALPLSSPEETARAPSSPPAEppPSTPPAAASPRPPRrssPISASASSPAPAPGRSAADDAG-ASSSDSSSSESSGCG 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 186 AVGNGETEK-----------NAGGSKPSSGSAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGG 254
Cdd:PHA03307 249 WGPENECPLprpapitlptrIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 255 SKSSSGSARTNPGASAGGNGETVSNIGDTESNAGGSKSNDGANNGASGIESNAGSTGTNFGAGGTGGIGDTESDAGGSKT 334
Cdd:PHA03307 329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
|
250 260
....*....|....*....|....*.
gi 1063694415 335 NS---GNGGTNDGASGIGSNDGSTGT 357
Cdd:PHA03307 409 AGrprPSPLDAGAASGAFYARYPLLT 434
|
|
| PPE |
COG5651 |
PPE-repeat protein [Function unknown]; |
125-340 |
2.01e-03 |
|
PPE-repeat protein [Function unknown];
Pssm-ID: 444372 [Multi-domain] Cd Length: 385 Bit Score: 41.03 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 125 APAPPPGSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETekNAGGSKPSSGSAGTNPGASAVGNGETEKNAGGSKPSSG 204
Cdd:COG5651 169 QPPPTITNPGGLLGAQNAGSGNTSSNPGFANLGLTGLNQV--GIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 205 SAGTNPGASAGGNGETEKNVGGSKPSSGKAGTNPGANAGGNGGTEKNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTE 284
Cdd:COG5651 247 AAAAAGAGASAALASLAATLLNASSLGLAATAASSAATNLGLAGSPLGLAGGGAGAAAATGLGLGAGGAAGAAGATGAGA 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694415 285 SNAGGSKSNDGANNGASGIE--SNAGSTGTNFGAGGTGGIGDTESDAGGSKTNSGNGG 340
Cdd:COG5651 327 ALGAGAAAAAAGAAAGAGAAaaAAAGGAGGGGGGALGAGGGGGSAGAAAGAASGGGAA 384
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
131-454 |
2.89e-03 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 40.75 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 131 GSTGAKPGASGIGSDSGSIGSAGTNPGADGTRETEKNAGGSKPSSGSAGTNpgasAVGNG-ETEKNAGGSKPSSGSAGTN 209
Cdd:cd21118 58 SSGIQNALGQGHGEEGGSTLGSRGDVFEHRLGEAARSLGNAGNEIGRQAED----IIRHGvDAVHNSWQGSGGHGAYGSQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 210 PGASAGGNGETEKNvGGSKPSSGKAGTNPGANAGGNGGtekNAGGSKSSSGSARTNPGASAGGNGETVSNIGDTesNAGG 289
Cdd:cd21118 134 GGPGVQGHGIPGGT-GGPWASGGNYGTNSLGGSVGQGG---NGGPLNYGTNSQGAVAQPGYGTVRGNNQNSGCT--NPPP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 290 SKSNDGANNgaSGIESNAGSTGTnfgaggtggigdtesdaggSKTNSGNGGTNDGASGIGSNDGSTGTNPGAGGGTDSNI 369
Cdd:cd21118 208 SGSHESFSN--SGGSSSSGSSGS-------------------QGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 370 EGTENNVGGKETNPGASGIGNSDGSTGTSPEGTESNADGTKTNTGGKESNTGSESNTNSSPQKLEAQGGNGGNQWDDGTD 449
Cdd:cd21118 267 GGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVG 346
|
....*
gi 1063694415 450 HDGVM 454
Cdd:cd21118 347 GLNTL 351
|
|
| griffithsin_like |
cd09614 |
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin ... |
438-570 |
4.85e-03 |
|
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.
Pssm-ID: 187710 Cd Length: 128 Bit Score: 37.76 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 438 GNGGNQWDDgTDHDGVMKIHVAvGGLGIEQIRFDYVKNGQLKEGpFHGVKGRGGTSTIEIShPDEYLVSVEGLYDSSniI 517
Cdd:cd09614 1 GFGGSPGSD-FDILTVSAIQLR-SGSYVDQIITDYQDLNGTQNF-HHGGGGGNLSPTLNFS-SGEYITEVTGRSGDR--V 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063694415 518 QGIQFQSNkhTSQYFGYEYYGDGTQFSLQVNEK-KIIGFHGFADSHLNSLGAYF 570
Cdd:cd09614 75 DQVQFTTN--YGGRTLPGGGGGGSAFTWTVPDNqKVIGFAGRSGSYLDQLQVYY 126
|
|
| Jacalin_ZG16_like |
cd09611 |
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a ... |
437-533 |
6.02e-03 |
|
Jacalin-like lectin domain of the zymogen granule protein 16 and related proteins; ZG16p is a conserved secreted vertebrate protein with tissue-specific expression profiles, which might play a role in glycoprotein secretion, perhaps as a linker protein that participates in the formation and/or transport of the zymogen granule. Its paralog ZG16b (PAUF) has been associated with roles in gene regulation and cancer. This domain family also contains mammalian proteins labelled as prostatic spermine-binding protein (SBP) and salivary-gland specific secreted proteins.
Pssm-ID: 187707 [Multi-domain] Cd Length: 128 Bit Score: 37.69 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694415 437 GGNGGNQWDDGTDHDG-VMKIHVAVGGLGIEQIRFDYVKNgqlkegpFHGVKGRGGTSTIEIS-HPDEYLVSVEGLYDss 514
Cdd:cd09611 1 GSGGGKYFSDVGEGGGpITGIRVSVGNNYIKGIQVRYGSN-------WSDVYGGRGGNEQEIVlEPGESITKVSGSYK-- 71
|
90
....*....|....*....
gi 1063694415 515 NIIQGIQFQSNKHTSQYFG 533
Cdd:cd09611 72 IYLHGLVFTTNKGRYLSFG 90
|
|
| |
