|
Name |
Accession |
Description |
Interval |
E-value |
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
244-1066 |
8.18e-177 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
:
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 573.43 E-value: 8.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 244 LVGLKVNSEQFGSSMPSRSYLIRGLKIRVPSNYDENtntynGVWDGTFKLLSSSNPAWILFDLLTNARYGLGKFVSESMI 323
Cdd:COG4733 148 LVGLRFDAEQFNGSIPNVNALVRGRKIRVPSNYDPS-----GVWDGTFKWAWTNNPAWVFYDLLTGDRYGLGRRLTAADI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 324 DLGQLYQIGRYCDEEVDDGFGGKEKRFAINTQITSRQDAYRLIQDIAGAFRGMVFWAGGMVNIMQDSPSD-PVMLFTNAN 402
Cdd:COG4733 223 DKWSLYAIAQYCDQKVPDGGGGTEPRFTCNVYIQSQASAWDVLRDIAAAFRGMPYWDGGKLGVVADRPRDpPVATFTPAN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 403 VKDGLFTYKGSARKDRPSVALITYNNKQDGYKQNVEYVEDQEAMARYGERKTEAVAFGCTSRGQAHRVGLWLLYTARMES 482
Cdd:COG4733 303 VVDGSFTYSYSSRKERPNAALVSFSDPDNGYQQAEEPVEDPDLIARYGVNQTELTAPGCTSRGQAQREGRWALLTNRYRT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 483 DMITFTAGLDASFLMPGETVLIQNKYRAGKRNSGRIVSFTKNSITLDAPVSLKKSGSFIRIINQEGKIVERDIneTGDNI 562
Cdd:COG4733 383 RTVTFSVGLDGLVATPGDVIAVADDVLAGRRIGGRVSSVDGRVVTLDRPVTMEAGDRYLRVRLPDGTSVARTV--QSVAG 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 563 TKVTFKTALATAdqPVANGVWTITEPDLVPMRARVVAIAQGEtPGSFDITVVQNNASKYQAIDNGAALVPenttvldPTY 642
Cdd:COG4733 461 RTLTVSTAYSET--PEAGAVWAFGPDELETQLFRVVSIEENE-DGTYTITAVQHAPEKYAAIDAGAFDDV-------PPQ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 643 SKPSNLVISEGTYLSSPGNLSVKLMLAWEGK--SPEYWVSWRRSDegnvSNWQSARATEEQYEIVNVAENGRYDFQLYSV 720
Cdd:COG4733 531 WPPVNVTTSESLSVVAQGTAVTTLTVSWDAPagAVAYEVEWRRDD----GNWVSVPRTSGTSFEVPGIYAGDYEVRVRAI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 721 SFGGKKSEIITAV-YQVKGTMTPPGAPTSLTAVGDYRNVVLNWVNPDSVDLAQINVYASKTNKLDTATLI-AQAATTTFT 798
Cdd:COG4733 607 NALGVSSAWAASSeTTVTGKTAPPPAPTGLTATGGLGGITLSWSFPVDADTLRTEIRYSTTGDWASATVAqALYPGNTYT 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 799 HAGLGDNETWYYWIRAVNKRGMVGQPNSNLGTEATTRDVLSFLKDKITSSELGKElLDEIDSKATQEAVDNAIGEVQNSV 878
Cdd:COG4733 687 LAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQE-LDAIIQNATVAEVVAATVTDVTAQ 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 879 NESIQQVENDLAQTSSEIKAQVDSVnqslkedidTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDGDAALSQEI 958
Cdd:COG4733 766 IDTAVLFAGVATAAAIGAEARVAAT---------VAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 959 KKAQSSLTTSLSQTSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAkNELKTSIDSLSEVVTSGDENLARQISQIAAGT 1038
Cdd:COG4733 837 AAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTA-ADVSAVADSTAASLTAIVIAATTIIDAIGDGT 915
|
810 820 830
....*....|....*....|....*....|.
gi 556195944 1039 GEQFDSLK---IWYFDQDAEGWTEDDNGYTP 1066
Cdd:COG4733 916 TREPAGDIgasGGAQGFAVTIVGSFDGAGAV 946
|
|
| DUF1983 |
pfam09327 |
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized ... |
3763-3833 |
1.10e-16 |
|
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized domains are found in various bacteriophage host specificity proteins.
:
Pssm-ID: 430529 Cd Length: 75 Bit Score: 77.34 E-value: 1.10e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556195944 3763 QELKKTVVENGNVNSTWMVKMETNSNGKKYAAGIALGIDGKN--LQSQFLVQADRFGLINTSNGNTTTPFVVE 3833
Cdd:pfam09327 3 QKSTAVADLDGKLSAMYSIKAQVKANGQKYVAGIALGAESGGgvTTSQVLFMADRFAIVNPANGNVTPPFVVQ 75
|
|
| ILEI |
pfam15711 |
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ... |
3059-3140 |
8.35e-09 |
|
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.
:
Pssm-ID: 464817 Cd Length: 89 Bit Score: 55.34 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3059 DGSTV-IATSKTYDVFgSANNGATMSADIEALASGTYVCVLTFDEPTGN-RGKVLSALESLGgtSEVVNSLPYRGAYILL 3136
Cdd:pfam15711 9 DACTGkVLDSKSFDTY-SYSDSSRLANFLKSIPDGSIVLIATKDEASSKlSDEARKALESLG--SSKIDNLGFRDSWAFI 85
|
....
gi 556195944 3137 GRKG 3140
Cdd:pfam15711 86 GFKG 89
|
|
| DUF3672 super family |
cl13808 |
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is ... |
3872-3948 |
1.14e-05 |
|
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is typically between 126 and 146 amino acids in length. The family is found in association with pfam09327, pfam00041. There are two completely conserved G residues that may be functionally important. Many of the proteins in this family are annotated as fibronectin type III however there is little accompanying literature to confirm this.
The actual alignment was detected with superfamily member pfam12421:
Pssm-ID: 289206 Cd Length: 133 Bit Score: 47.65 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3872 VGKDGSSQFHNVIVRGHVEAESGSFKGTIDATDGVFRGTVQASRFVGDICSAGVFKQGVRPDITHYDSGSVGGTKTY 3948
Cdd:pfam12421 1 LTPDGHLTAKNGDFRGSINANSGTLNNVTIAENCTISGTLRAEKILGDIVKAGVWEFPYVREPASSNHRYFSGTLTV 77
|
|
| CBM_4_9 super family |
cl19911 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
3235-3345 |
2.29e-05 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
The actual alignment was detected with superfamily member pfam02018:
Pssm-ID: 418717 Cd Length: 134 Bit Score: 47.06 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3235 GNLIVNPSFE-RGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQ----KISFKKDRSYKIGIWAKQDpnttiq 3309
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTATWDGQiidiTIRLEKGTTYTVSFWVKAS------ 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 556195944 3310 STDNTKFRVAEGnGLIASKAYGPFTSNWQEVSWTWK 3345
Cdd:pfam02018 75 SGPPQTVSVTLQ-ITDASGNYDTVADEKVVLTGEWT 109
|
|
| FhaB super family |
cl27105 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
1874-3465 |
2.62e-05 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
The actual alignment was detected with superfamily member COG3210:
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 50.54 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1874 VNADTTITMAPGSRVFDDTGAVYVNGVRVAFGNASWNTVSFDLKAGWSTVEFLVNQWTGQAYINLGFKLSEKVAQLNSAL 1953
Cdd:COG3210 77 STGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1954 GMNALSNAISAVTSNVSTVGDRVTSTSQSVTDLRNSLEQTNANLENKADAQALSTLQNTVSKQRDTISSQGNSITNLNNT 2033
Cdd:COG3210 157 GAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2034 LTAARNAGDNLIPNYDFLQGATAWDTQYPAGVTFGNFGDGKAGVKLNRTTTTSPGIFSNNNKPLPLNGQRK--------- 2104
Cdd:COG3210 237 GAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGgtgvlgggt 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2105 -YRVVVKAKGVSGAMNMLIRRQNKIGQTDSNYEDKNVTLTSEWQTITWETGLTASNADGQNFKLYAHPANAEIWVDTFKV 2183
Cdd:COG3210 317 aAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2184 FDITDEVKIKANSDALSTLSSTVTQQGDKITSQGNSITKLTNDLEAADANIAKKADQSAVTTLTGRVEKTESGLTAANSN 2263
Cdd:COG3210 397 TTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2264 ITSLSSSLNQQSKRGANLLPDGTFESYAVGHNLSNNRVIVTTDDSHGGNKCIRVTRPNDYNANATDNSDNHIFSGFQVRD 2343
Cdd:COG3210 477 GNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTT 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2344 NAVFYMecWVKLDAKSTAMAENAQISIGLSLQYQDNSWQWPAVTKAAKDLSTAQWTKVSGYLKSTKSGIKQAMVRISIPN 2423
Cdd:COG3210 557 AASGSN--TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGL 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2424 VSSVKAGNSFLIDDLVITEVTDAYNAQSTADANANAISTLDSTVSQQGDQITSQGNSITKLTNDLSTTNSNVAKKADGAA 2503
Cdd:COG3210 635 TGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSIT 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2504 VTALTnrvteaeGNISSQSNQLATLSNSLAEGSLICNGGLNVDASFWEDSGPGSAFTYDANEKAIRTTTGSirvANLTRI 2583
Cdd:COG3210 715 VTGQI-------GALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANAN---GNTSAG 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2584 PVEAETTLTISFEMKASETISNVSSDSVGVIADLATPTNWISSVSPWLGGVSTNWQTKSVELTIPANFIGKYVYLRFAAG 2663
Cdd:COG3210 785 ATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAG 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2664 GWTPSNSARLYIRKVDVFSSTGVAKKANATAVSDLTSRVDSTEGKLASQSQALTKLQNDLATTNNNVSKKADANALTALT 2743
Cdd:COG3210 865 ANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTA 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2744 NRVTQTEKDINSTSSSVTNLNNKVDAISVGGTNLIKNSGDMTGWSNVVSDTYRGNAVIGATVKAGSGYRDLREITLESPV 2823
Cdd:COG3210 945 LSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTG 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2824 DAGEYVYSFYAKGGVAGQTMTAFFYNPNTTTSIETSQGAKGNNSDGRAQFTLTTSWARYWVKWKQTPTTGTKRLILCRIE 2903
Cdd:COG3210 1025 TTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATG 1104
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2904 SNTSKDQTVYINSPKFEVGNVVSDWNESPSDSASASAVDSLTTKVNQQGTSISSIGNRTTSLENGLSTAQNNIAKKADAS 2983
Cdd:COG3210 1105 TSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGG 1184
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2984 ALQDLRNTVTSQGDDLTAANSSITSLQASMNRRTVFTVTARGNGNSVTHGVFDESGKNLFTPGRSWALVTFAKHSDGSTV 3063
Cdd:COG3210 1185 ADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGA 1264
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3064 IATSKTYDVFGSANNGATMSADIEALASGTYVCVLTFDEPTGNRGKVLSALESLGGTSEVVNSLPYRGAYILLGRKGMKP 3143
Cdd:COG3210 1265 VSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTIN 1344
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3144 GDGLELRAPTGGDATAHISTSVEFVNGVMMGLGAAGGVMMKADANASAITTLQNTVKTQGDNIDSLSSSTTALENSLASS 3223
Cdd:COG3210 1345 TTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAG 1424
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3224 NASVDAASQIPGNLIVNPSFERGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQKISFKKDRSYKIGIWAKQD 3303
Cdd:COG3210 1425 TTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGT 1504
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3304 PNTTIQSTDNTKFRVAEGNGLIASKAYGPFTSNWQEVSWTWKATKDVVADVQFTAFLSAGAMYFDDFYVVDVTDSVETQA 3383
Cdd:COG3210 1505 STGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDT 1584
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3384 NSSAITNLDSRVTKTENDITSQGSQVTQLKNDLATTNTNVSKKADAAALTALTNRVTQNEKEIETQSSQTTSLKNSLSTV 3463
Cdd:COG3210 1585 GAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGA 1664
|
..
gi 556195944 3464 QA 3465
Cdd:COG3210 1665 GN 1666
|
|
| CALCOCO1 super family |
cl37761 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1196-1378 |
4.17e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
The actual alignment was detected with superfamily member pfam07888:
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1196 LQEEQQARANADTA-EAQARSTLAAQIRGSSESGNLDDIRSGLiyQEKNARITADAAEASAR----ESLQTEFNRNKASV 1270
Cdd:pfam07888 36 LEECLQERAELLQAqEAANRQREKEKERYKRDREQWERQRREL--ESRVAELKEELRQSREKheelEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1271 AEELHTLSTEQASQASKITGLQ---TSLGQKADASAVQ--TISQKVEEQGNTLKSQGAALSTLDNRVGSVESGVSANSKA 1345
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEediKTLTQRVLERETEleRMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190
....*....|....*....|....*....|...
gi 556195944 1346 ITGLQSTVTQQDKTLSSQSESITTLNNSLSDIQ 1378
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3629-3771 |
6.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3629 ITDAKEAQDSANANASA----LTSLTSRVTNVEGLVTSQASQLSSLTSQVNDASSKVDQmaqtitnnekTQSSLNTSLQS 3704
Cdd:COG4372 26 IAALSEQLRKALFELDKlqeeLEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----------LNEQLQAAQAE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3705 QIDAQASANIKNQtELNNATTSLAAIKSTQQTQATTISALSQQQTNLTAQVGGQSAELQELKKTVVE 3771
Cdd:COG4372 96 LAQAQEELESLQE-EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
|
| CBM_4_9 super family |
cl19911 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
1389-1507 |
1.18e-03 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
The actual alignment was detected with superfamily member pfam02018:
Pssm-ID: 418717 Cd Length: 134 Bit Score: 42.05 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1389 SNLLVNASFE-RDLAGWSAGNSVSSIIKASAPHSGSKILVCAAGT-----VQITQSVSVVEGRTYKLSSFVRcttdavIS 1462
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTatwdgQIIDITIRLEKGTTYTVSFWVK------AS 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 556195944 1463 SPGNNKLRI-----GAATLLKEIPIRPENLPKDetWKEVSDTWKATLTGK 1507
Cdd:pfam02018 75 SGPPQTVSVtlqitDASGNYDTVADEKVVLTGE--WTKLEGTFTIPKTAS 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
244-1066 |
8.18e-177 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 573.43 E-value: 8.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 244 LVGLKVNSEQFGSSMPSRSYLIRGLKIRVPSNYDENtntynGVWDGTFKLLSSSNPAWILFDLLTNARYGLGKFVSESMI 323
Cdd:COG4733 148 LVGLRFDAEQFNGSIPNVNALVRGRKIRVPSNYDPS-----GVWDGTFKWAWTNNPAWVFYDLLTGDRYGLGRRLTAADI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 324 DLGQLYQIGRYCDEEVDDGFGGKEKRFAINTQITSRQDAYRLIQDIAGAFRGMVFWAGGMVNIMQDSPSD-PVMLFTNAN 402
Cdd:COG4733 223 DKWSLYAIAQYCDQKVPDGGGGTEPRFTCNVYIQSQASAWDVLRDIAAAFRGMPYWDGGKLGVVADRPRDpPVATFTPAN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 403 VKDGLFTYKGSARKDRPSVALITYNNKQDGYKQNVEYVEDQEAMARYGERKTEAVAFGCTSRGQAHRVGLWLLYTARMES 482
Cdd:COG4733 303 VVDGSFTYSYSSRKERPNAALVSFSDPDNGYQQAEEPVEDPDLIARYGVNQTELTAPGCTSRGQAQREGRWALLTNRYRT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 483 DMITFTAGLDASFLMPGETVLIQNKYRAGKRNSGRIVSFTKNSITLDAPVSLKKSGSFIRIINQEGKIVERDIneTGDNI 562
Cdd:COG4733 383 RTVTFSVGLDGLVATPGDVIAVADDVLAGRRIGGRVSSVDGRVVTLDRPVTMEAGDRYLRVRLPDGTSVARTV--QSVAG 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 563 TKVTFKTALATAdqPVANGVWTITEPDLVPMRARVVAIAQGEtPGSFDITVVQNNASKYQAIDNGAALVPenttvldPTY 642
Cdd:COG4733 461 RTLTVSTAYSET--PEAGAVWAFGPDELETQLFRVVSIEENE-DGTYTITAVQHAPEKYAAIDAGAFDDV-------PPQ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 643 SKPSNLVISEGTYLSSPGNLSVKLMLAWEGK--SPEYWVSWRRSDegnvSNWQSARATEEQYEIVNVAENGRYDFQLYSV 720
Cdd:COG4733 531 WPPVNVTTSESLSVVAQGTAVTTLTVSWDAPagAVAYEVEWRRDD----GNWVSVPRTSGTSFEVPGIYAGDYEVRVRAI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 721 SFGGKKSEIITAV-YQVKGTMTPPGAPTSLTAVGDYRNVVLNWVNPDSVDLAQINVYASKTNKLDTATLI-AQAATTTFT 798
Cdd:COG4733 607 NALGVSSAWAASSeTTVTGKTAPPPAPTGLTATGGLGGITLSWSFPVDADTLRTEIRYSTTGDWASATVAqALYPGNTYT 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 799 HAGLGDNETWYYWIRAVNKRGMVGQPNSNLGTEATTRDVLSFLKDKITSSELGKElLDEIDSKATQEAVDNAIGEVQNSV 878
Cdd:COG4733 687 LAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQE-LDAIIQNATVAEVVAATVTDVTAQ 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 879 NESIQQVENDLAQTSSEIKAQVDSVnqslkedidTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDGDAALSQEI 958
Cdd:COG4733 766 IDTAVLFAGVATAAAIGAEARVAAT---------VAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 959 KKAQSSLTTSLSQTSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAkNELKTSIDSLSEVVTSGDENLARQISQIAAGT 1038
Cdd:COG4733 837 AAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTA-ADVSAVADSTAASLTAIVIAATTIIDAIGDGT 915
|
810 820 830
....*....|....*....|....*....|.
gi 556195944 1039 GEQFDSLK---IWYFDQDAEGWTEDDNGYTP 1066
Cdd:COG4733 916 TREPAGDIgasGGAQGFAVTIVGSFDGAGAV 946
|
|
| Phage-tail_3 |
pfam13550 |
Putative phage tail protein; This putative domain is found in the large gene transfer agent ... |
357-518 |
5.20e-32 |
|
Putative phage tail protein; This putative domain is found in the large gene transfer agent protein. These produce defective phage like particles. This domain is similar to other phage-tail protein families.
Pssm-ID: 433300 [Multi-domain] Cd Length: 163 Bit Score: 124.35 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 357 TSRQDAYRLIQDIAGAFRGMVFWAGGMVNIMQDSPsDPVMLFTNANVKDG----LFTYKGSARKDRPSVALITYNNKQDG 432
Cdd:pfam13550 1 DEQMSARDALEPLARAFGFDAVESGGTLRFRPRGV-APVATLTDDDLVDGsdgdPVERTRAAEAELPNAVRLTYTDPAND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 433 YKQNVEYVEDQEAMaryGERKTEAVAFGCTSRGQAHRVGLWLLYTARMESDMITFTAGLDASFLMPGETVLIQNKYRAGK 512
Cdd:pfam13550 80 YQPATVEARDAAGI---GERVSTVELPLVLSAGQAQRVAQRLLQEARAERETVTFSLPPSYLALEPGDVVELTDDGRAGR 156
|
....*.
gi 556195944 513 RNSGRI 518
Cdd:pfam13550 157 WRIDRI 162
|
|
| attach_TipJ_rel |
NF040662 |
host specificity factor TipJ family phage tail protein; Members of this family form a family ... |
151-532 |
1.52e-20 |
|
host specificity factor TipJ family phage tail protein; Members of this family form a family related to that of host specificity protein J of phage lambda, a tail tip protein that mediates attachment to LamB on the surface of E. coli. Binding of the phage tail to the LamB receptor triggers the injection of phage DNA into host cells. Proteins with this domain are likely also to be phage tail proteins.
Pssm-ID: 468628 Cd Length: 473 Bit Score: 98.51 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 151 TSVQFKFQLANGNGsfydVIATGESSSDVTLTAKKTGVYYRSYEIQLPKPGRaYKVRVLRLSADSNDQY--LFNDT-WVD 227
Cdd:NF040662 22 VSVEVEYRKVDDNG----VPGGAWTSLYGVGTAATRDTLGRTRRIKLPPPGR-GEVRVRRRRTRDNNSNsrARDEVkWYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 228 SIGEIVDTPMNYPNSVLVGLKVNSEQFGSSMPSRsylirglKIRVPSNydENTNTYNGVwDGTFKLLSSSNPAWILFDLL 307
Cdd:NF040662 97 LRAYLPRSPTVYPNVTLLAVRVRATDNLSSQSER-------KLNCIAT--RKLPVYNGG-GGWSDPTPTRSIAFALADLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 308 TNARYGLGkfvSESMIDLGQLYQIgrycDEEVDDGFGGkEKRFAINTQITSRQDAyrlIQDIAGAFRGMVFWAGGMVNIM 387
Cdd:NF040662 167 RDPVIGRG---LPDEIDLDTLYAL----DDEVWTGRGD-EFDYTFDDESVSFEEA---LQMIANAGRAEPYRDGGLLSFV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 388 QDSPSD-PVMLFTNANVKDGLF--TYKGSARKDRPSVALiTYNNKQDGYKQNVEYVEDQEAMarygeRKTEAV-AFGCTS 463
Cdd:NF040662 236 RDEPRTvPGALFNPRNIVPDSFkrSYTMPVEDDYDGVEV-EYVDPDTWKKETVRCRLPGSAG-----RNPKKIeLDGIRN 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556195944 464 RGQAHRVGLWLLYTARMESDMITFTAGLDASFLMPGETVLIQNKYRAGKRnSGRIVSFTKNSITLDAPV 532
Cdd:NF040662 310 RDQAWRRAMREARKLRYQRRSVSFTTELDGLLVNYGDRVAVADDIPGWTQ-SGEVTARDGLTLTTSEPL 377
|
|
| DUF1983 |
pfam09327 |
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized ... |
3763-3833 |
1.10e-16 |
|
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized domains are found in various bacteriophage host specificity proteins.
Pssm-ID: 430529 Cd Length: 75 Bit Score: 77.34 E-value: 1.10e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556195944 3763 QELKKTVVENGNVNSTWMVKMETNSNGKKYAAGIALGIDGKN--LQSQFLVQADRFGLINTSNGNTTTPFVVE 3833
Cdd:pfam09327 3 QKSTAVADLDGKLSAMYSIKAQVKANGQKYVAGIALGAESGGgvTTSQVLFMADRFAIVNPANGNVTPPFVVQ 75
|
|
| ILEI |
pfam15711 |
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ... |
3059-3140 |
8.35e-09 |
|
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.
Pssm-ID: 464817 Cd Length: 89 Bit Score: 55.34 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3059 DGSTV-IATSKTYDVFgSANNGATMSADIEALASGTYVCVLTFDEPTGN-RGKVLSALESLGgtSEVVNSLPYRGAYILL 3136
Cdd:pfam15711 9 DACTGkVLDSKSFDTY-SYSDSSRLANFLKSIPDGSIVLIATKDEASSKlSDEARKALESLG--SSKIDNLGFRDSWAFI 85
|
....
gi 556195944 3137 GRKG 3140
Cdd:pfam15711 86 GFKG 89
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
855-1013 |
2.75e-07 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 53.10 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 855 LDEIDSKAtQEAVDNAIGEVQNSVNESIQQ-VENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVNQTINTNI 933
Cdd:cd13769 3 LSELIQKA-QEAINNLAQQVQKQLGLQNPEeVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKLSETV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 934 SNVNSQIEAAKQSikdgdaalsQEIK-KAQSSLTTSLSQtSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAKNELKTS 1012
Cdd:cd13769 82 PELRKSLPVEEKA---------QELQaKLQSGLQTLVTE-SQKLAKAISENSQKAQEELQKATKQAYDIAVEAAQNLQNQ 151
|
.
gi 556195944 1013 I 1013
Cdd:cd13769 152 L 152
|
|
| DUF3672 |
pfam12421 |
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is ... |
3872-3948 |
1.14e-05 |
|
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is typically between 126 and 146 amino acids in length. The family is found in association with pfam09327, pfam00041. There are two completely conserved G residues that may be functionally important. Many of the proteins in this family are annotated as fibronectin type III however there is little accompanying literature to confirm this.
Pssm-ID: 289206 Cd Length: 133 Bit Score: 47.65 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3872 VGKDGSSQFHNVIVRGHVEAESGSFKGTIDATDGVFRGTVQASRFVGDICSAGVFKQGVRPDITHYDSGSVGGTKTY 3948
Cdd:pfam12421 1 LTPDGHLTAKNGDFRGSINANSGTLNNVTIAENCTISGTLRAEKILGDIVKAGVWEFPYVREPASSNHRYFSGTLTV 77
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
3235-3345 |
2.29e-05 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 47.06 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3235 GNLIVNPSFE-RGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQ----KISFKKDRSYKIGIWAKQDpnttiq 3309
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTATWDGQiidiTIRLEKGTTYTVSFWVKAS------ 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 556195944 3310 STDNTKFRVAEGnGLIASKAYGPFTSNWQEVSWTWK 3345
Cdd:pfam02018 75 SGPPQTVSVTLQ-ITDASGNYDTVADEKVVLTGEWT 109
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
1874-3465 |
2.62e-05 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 50.54 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1874 VNADTTITMAPGSRVFDDTGAVYVNGVRVAFGNASWNTVSFDLKAGWSTVEFLVNQWTGQAYINLGFKLSEKVAQLNSAL 1953
Cdd:COG3210 77 STGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1954 GMNALSNAISAVTSNVSTVGDRVTSTSQSVTDLRNSLEQTNANLENKADAQALSTLQNTVSKQRDTISSQGNSITNLNNT 2033
Cdd:COG3210 157 GAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2034 LTAARNAGDNLIPNYDFLQGATAWDTQYPAGVTFGNFGDGKAGVKLNRTTTTSPGIFSNNNKPLPLNGQRK--------- 2104
Cdd:COG3210 237 GAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGgtgvlgggt 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2105 -YRVVVKAKGVSGAMNMLIRRQNKIGQTDSNYEDKNVTLTSEWQTITWETGLTASNADGQNFKLYAHPANAEIWVDTFKV 2183
Cdd:COG3210 317 aAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2184 FDITDEVKIKANSDALSTLSSTVTQQGDKITSQGNSITKLTNDLEAADANIAKKADQSAVTTLTGRVEKTESGLTAANSN 2263
Cdd:COG3210 397 TTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2264 ITSLSSSLNQQSKRGANLLPDGTFESYAVGHNLSNNRVIVTTDDSHGGNKCIRVTRPNDYNANATDNSDNHIFSGFQVRD 2343
Cdd:COG3210 477 GNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTT 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2344 NAVFYMecWVKLDAKSTAMAENAQISIGLSLQYQDNSWQWPAVTKAAKDLSTAQWTKVSGYLKSTKSGIKQAMVRISIPN 2423
Cdd:COG3210 557 AASGSN--TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGL 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2424 VSSVKAGNSFLIDDLVITEVTDAYNAQSTADANANAISTLDSTVSQQGDQITSQGNSITKLTNDLSTTNSNVAKKADGAA 2503
Cdd:COG3210 635 TGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSIT 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2504 VTALTnrvteaeGNISSQSNQLATLSNSLAEGSLICNGGLNVDASFWEDSGPGSAFTYDANEKAIRTTTGSirvANLTRI 2583
Cdd:COG3210 715 VTGQI-------GALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANAN---GNTSAG 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2584 PVEAETTLTISFEMKASETISNVSSDSVGVIADLATPTNWISSVSPWLGGVSTNWQTKSVELTIPANFIGKYVYLRFAAG 2663
Cdd:COG3210 785 ATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAG 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2664 GWTPSNSARLYIRKVDVFSSTGVAKKANATAVSDLTSRVDSTEGKLASQSQALTKLQNDLATTNNNVSKKADANALTALT 2743
Cdd:COG3210 865 ANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTA 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2744 NRVTQTEKDINSTSSSVTNLNNKVDAISVGGTNLIKNSGDMTGWSNVVSDTYRGNAVIGATVKAGSGYRDLREITLESPV 2823
Cdd:COG3210 945 LSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTG 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2824 DAGEYVYSFYAKGGVAGQTMTAFFYNPNTTTSIETSQGAKGNNSDGRAQFTLTTSWARYWVKWKQTPTTGTKRLILCRIE 2903
Cdd:COG3210 1025 TTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATG 1104
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2904 SNTSKDQTVYINSPKFEVGNVVSDWNESPSDSASASAVDSLTTKVNQQGTSISSIGNRTTSLENGLSTAQNNIAKKADAS 2983
Cdd:COG3210 1105 TSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGG 1184
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2984 ALQDLRNTVTSQGDDLTAANSSITSLQASMNRRTVFTVTARGNGNSVTHGVFDESGKNLFTPGRSWALVTFAKHSDGSTV 3063
Cdd:COG3210 1185 ADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGA 1264
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3064 IATSKTYDVFGSANNGATMSADIEALASGTYVCVLTFDEPTGNRGKVLSALESLGGTSEVVNSLPYRGAYILLGRKGMKP 3143
Cdd:COG3210 1265 VSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTIN 1344
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3144 GDGLELRAPTGGDATAHISTSVEFVNGVMMGLGAAGGVMMKADANASAITTLQNTVKTQGDNIDSLSSSTTALENSLASS 3223
Cdd:COG3210 1345 TTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAG 1424
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3224 NASVDAASQIPGNLIVNPSFERGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQKISFKKDRSYKIGIWAKQD 3303
Cdd:COG3210 1425 TTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGT 1504
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3304 PNTTIQSTDNTKFRVAEGNGLIASKAYGPFTSNWQEVSWTWKATKDVVADVQFTAFLSAGAMYFDDFYVVDVTDSVETQA 3383
Cdd:COG3210 1505 STGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDT 1584
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3384 NSSAITNLDSRVTKTENDITSQGSQVTQLKNDLATTNTNVSKKADAAALTALTNRVTQNEKEIETQSSQTTSLKNSLSTV 3463
Cdd:COG3210 1585 GAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGA 1664
|
..
gi 556195944 3464 QA 3465
Cdd:COG3210 1665 GN 1666
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
842-1027 |
1.10e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 842 KDKITSSELGKELLDEIDSKATQEA--VDNAIGEVQNSVNESIQQVENDLAQTS---SEIKaqvdsvnqSLKEDiDTVNQ 916
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNqqKDEQIKKLQQEKELLEKEIERLKETIIknnSEIK--------DLTNQ-DSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 917 TIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDgdaaLSQEIKKAQSSL------TTSLSQTSKDLTAAI------QKET 984
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ----KQKELKSKEKELkklneeKKELEEKVKDLTKKIsslkekIEKL 529
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556195944 985 NDRIADVNDAAKQAADQLLSAKNELKTsiDSLSEVVTSGDENL 1027
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEI 570
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
853-1045 |
3.69e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 45.35 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 853 ELLDEIDSKATQ-EAVDNAIGEVQNSVNESIQQVE--NDLA----QTSSEIKAQVDSVNQSLKEDIDTVNQTI--VDNID 923
Cdd:smart00283 15 EQAEELEELAERmEELSASIEEVAANADEIAATAQsaAEAAeegrEAVEDAITAMDQIREVVEEAVSAVEELEesSDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 924 TVNQTIN-----TNISNVNSQIEAAKQSIK-DGDAALSQEIKKaqsslttsLSQTSKDLTAAIQ---KETNDRIADVNDA 994
Cdd:smart00283 95 EIVSVIDdiadqTNLLALNAAIEAARAGEAgRGFAVVADEVRK--------LAERSAESAKEIEsliKEIQEETNEAVAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556195944 995 AKQAADQLLSAKNELKTSIDSLSEVVTSGDENlARQISQIAAGTGEQFDSL 1045
Cdd:smart00283 167 MEESSSEVEEGVELVEETGDALEEIVDSVEEI-ADLVQEIAAATDEQAAGS 216
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1196-1378 |
4.17e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1196 LQEEQQARANADTA-EAQARSTLAAQIRGSSESGNLDDIRSGLiyQEKNARITADAAEASAR----ESLQTEFNRNKASV 1270
Cdd:pfam07888 36 LEECLQERAELLQAqEAANRQREKEKERYKRDREQWERQRREL--ESRVAELKEELRQSREKheelEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1271 AEELHTLSTEQASQASKITGLQ---TSLGQKADASAVQ--TISQKVEEQGNTLKSQGAALSTLDNRVGSVESGVSANSKA 1345
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEediKTLTQRVLERETEleRMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190
....*....|....*....|....*....|...
gi 556195944 1346 ITGLQSTVTQQDKTLSSQSESITTLNNSLSDIQ 1378
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3629-3771 |
6.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3629 ITDAKEAQDSANANASA----LTSLTSRVTNVEGLVTSQASQLSSLTSQVNDASSKVDQmaqtitnnekTQSSLNTSLQS 3704
Cdd:COG4372 26 IAALSEQLRKALFELDKlqeeLEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----------LNEQLQAAQAE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3705 QIDAQASANIKNQtELNNATTSLAAIKSTQQTQATTISALSQQQTNLTAQVGGQSAELQELKKTVVE 3771
Cdd:COG4372 96 LAQAQEELESLQE-EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
1389-1507 |
1.18e-03 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 42.05 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1389 SNLLVNASFE-RDLAGWSAGNSVSSIIKASAPHSGSKILVCAAGT-----VQITQSVSVVEGRTYKLSSFVRcttdavIS 1462
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTatwdgQIIDITIRLEKGTTYTVSFWVK------AS 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 556195944 1463 SPGNNKLRI-----GAATLLKEIPIRPENLPKDetWKEVSDTWKATLTGK 1507
Cdd:pfam02018 75 SGPPQTVSVtlqitDASGNYDTVADEKVVLTGE--WTKLEGTFTIPKTAS 122
|
|
| NTTRR-F1 |
NF033675 |
NTTRR-F1 domain; NTTRR-F1 (N-terminal To Repetitive Region - Firmicutes 1) is a homology ... |
3236-3277 |
7.09e-03 |
|
NTTRR-F1 domain; NTTRR-F1 (N-terminal To Repetitive Region - Firmicutes 1) is a homology domain found strictly as the N-terminal non-repetitive region of otherwise highly repetitive proteins of various Firmicutes. The repetitive region that follows typically is collagen-like, with every third residue a glycine.
Pssm-ID: 468135 Cd Length: 155 Bit Score: 40.23 E-value: 7.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556195944 3236 NLIVNPSFERGTegYTGWSGIATVVTLQVPHLGTKAAKLAAG 3277
Cdd:NF033675 4 NLIVNGGFETGS--LTPWSGVNASITSQFSHSGFYSARLLGG 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
244-1066 |
8.18e-177 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 573.43 E-value: 8.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 244 LVGLKVNSEQFGSSMPSRSYLIRGLKIRVPSNYDENtntynGVWDGTFKLLSSSNPAWILFDLLTNARYGLGKFVSESMI 323
Cdd:COG4733 148 LVGLRFDAEQFNGSIPNVNALVRGRKIRVPSNYDPS-----GVWDGTFKWAWTNNPAWVFYDLLTGDRYGLGRRLTAADI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 324 DLGQLYQIGRYCDEEVDDGFGGKEKRFAINTQITSRQDAYRLIQDIAGAFRGMVFWAGGMVNIMQDSPSD-PVMLFTNAN 402
Cdd:COG4733 223 DKWSLYAIAQYCDQKVPDGGGGTEPRFTCNVYIQSQASAWDVLRDIAAAFRGMPYWDGGKLGVVADRPRDpPVATFTPAN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 403 VKDGLFTYKGSARKDRPSVALITYNNKQDGYKQNVEYVEDQEAMARYGERKTEAVAFGCTSRGQAHRVGLWLLYTARMES 482
Cdd:COG4733 303 VVDGSFTYSYSSRKERPNAALVSFSDPDNGYQQAEEPVEDPDLIARYGVNQTELTAPGCTSRGQAQREGRWALLTNRYRT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 483 DMITFTAGLDASFLMPGETVLIQNKYRAGKRNSGRIVSFTKNSITLDAPVSLKKSGSFIRIINQEGKIVERDIneTGDNI 562
Cdd:COG4733 383 RTVTFSVGLDGLVATPGDVIAVADDVLAGRRIGGRVSSVDGRVVTLDRPVTMEAGDRYLRVRLPDGTSVARTV--QSVAG 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 563 TKVTFKTALATAdqPVANGVWTITEPDLVPMRARVVAIAQGEtPGSFDITVVQNNASKYQAIDNGAALVPenttvldPTY 642
Cdd:COG4733 461 RTLTVSTAYSET--PEAGAVWAFGPDELETQLFRVVSIEENE-DGTYTITAVQHAPEKYAAIDAGAFDDV-------PPQ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 643 SKPSNLVISEGTYLSSPGNLSVKLMLAWEGK--SPEYWVSWRRSDegnvSNWQSARATEEQYEIVNVAENGRYDFQLYSV 720
Cdd:COG4733 531 WPPVNVTTSESLSVVAQGTAVTTLTVSWDAPagAVAYEVEWRRDD----GNWVSVPRTSGTSFEVPGIYAGDYEVRVRAI 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 721 SFGGKKSEIITAV-YQVKGTMTPPGAPTSLTAVGDYRNVVLNWVNPDSVDLAQINVYASKTNKLDTATLI-AQAATTTFT 798
Cdd:COG4733 607 NALGVSSAWAASSeTTVTGKTAPPPAPTGLTATGGLGGITLSWSFPVDADTLRTEIRYSTTGDWASATVAqALYPGNTYT 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 799 HAGLGDNETWYYWIRAVNKRGMVGQPNSNLGTEATTRDVLSFLKDKITSSELGKElLDEIDSKATQEAVDNAIGEVQNSV 878
Cdd:COG4733 687 LAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELGQE-LDAIIQNATVAEVVAATVTDVTAQ 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 879 NESIQQVENDLAQTSSEIKAQVDSVnqslkedidTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDGDAALSQEI 958
Cdd:COG4733 766 IDTAVLFAGVATAAAIGAEARVAAT---------VAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 959 KKAQSSLTTSLSQTSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAkNELKTSIDSLSEVVTSGDENLARQISQIAAGT 1038
Cdd:COG4733 837 AAVVLAGVVVYGDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTA-ADVSAVADSTAASLTAIVIAATTIIDAIGDGT 915
|
810 820 830
....*....|....*....|....*....|.
gi 556195944 1039 GEQFDSLK---IWYFDQDAEGWTEDDNGYTP 1066
Cdd:COG4733 916 TREPAGDIgasGGAQGFAVTIVGSFDGAGAV 946
|
|
| Phage-tail_3 |
pfam13550 |
Putative phage tail protein; This putative domain is found in the large gene transfer agent ... |
357-518 |
5.20e-32 |
|
Putative phage tail protein; This putative domain is found in the large gene transfer agent protein. These produce defective phage like particles. This domain is similar to other phage-tail protein families.
Pssm-ID: 433300 [Multi-domain] Cd Length: 163 Bit Score: 124.35 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 357 TSRQDAYRLIQDIAGAFRGMVFWAGGMVNIMQDSPsDPVMLFTNANVKDG----LFTYKGSARKDRPSVALITYNNKQDG 432
Cdd:pfam13550 1 DEQMSARDALEPLARAFGFDAVESGGTLRFRPRGV-APVATLTDDDLVDGsdgdPVERTRAAEAELPNAVRLTYTDPAND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 433 YKQNVEYVEDQEAMaryGERKTEAVAFGCTSRGQAHRVGLWLLYTARMESDMITFTAGLDASFLMPGETVLIQNKYRAGK 512
Cdd:pfam13550 80 YQPATVEARDAAGI---GERVSTVELPLVLSAGQAQRVAQRLLQEARAERETVTFSLPPSYLALEPGDVVELTDDGRAGR 156
|
....*.
gi 556195944 513 RNSGRI 518
Cdd:pfam13550 157 WRIDRI 162
|
|
| attach_TipJ_rel |
NF040662 |
host specificity factor TipJ family phage tail protein; Members of this family form a family ... |
151-532 |
1.52e-20 |
|
host specificity factor TipJ family phage tail protein; Members of this family form a family related to that of host specificity protein J of phage lambda, a tail tip protein that mediates attachment to LamB on the surface of E. coli. Binding of the phage tail to the LamB receptor triggers the injection of phage DNA into host cells. Proteins with this domain are likely also to be phage tail proteins.
Pssm-ID: 468628 Cd Length: 473 Bit Score: 98.51 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 151 TSVQFKFQLANGNGsfydVIATGESSSDVTLTAKKTGVYYRSYEIQLPKPGRaYKVRVLRLSADSNDQY--LFNDT-WVD 227
Cdd:NF040662 22 VSVEVEYRKVDDNG----VPGGAWTSLYGVGTAATRDTLGRTRRIKLPPPGR-GEVRVRRRRTRDNNSNsrARDEVkWYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 228 SIGEIVDTPMNYPNSVLVGLKVNSEQFGSSMPSRsylirglKIRVPSNydENTNTYNGVwDGTFKLLSSSNPAWILFDLL 307
Cdd:NF040662 97 LRAYLPRSPTVYPNVTLLAVRVRATDNLSSQSER-------KLNCIAT--RKLPVYNGG-GGWSDPTPTRSIAFALADLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 308 TNARYGLGkfvSESMIDLGQLYQIgrycDEEVDDGFGGkEKRFAINTQITSRQDAyrlIQDIAGAFRGMVFWAGGMVNIM 387
Cdd:NF040662 167 RDPVIGRG---LPDEIDLDTLYAL----DDEVWTGRGD-EFDYTFDDESVSFEEA---LQMIANAGRAEPYRDGGLLSFV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 388 QDSPSD-PVMLFTNANVKDGLF--TYKGSARKDRPSVALiTYNNKQDGYKQNVEYVEDQEAMarygeRKTEAV-AFGCTS 463
Cdd:NF040662 236 RDEPRTvPGALFNPRNIVPDSFkrSYTMPVEDDYDGVEV-EYVDPDTWKKETVRCRLPGSAG-----RNPKKIeLDGIRN 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556195944 464 RGQAHRVGLWLLYTARMESDMITFTAGLDASFLMPGETVLIQNKYRAGKRnSGRIVSFTKNSITLDAPV 532
Cdd:NF040662 310 RDQAWRRAMREARKLRYQRRSVSFTTELDGLLVNYGDRVAVADDIPGWTQ-SGEVTARDGLTLTTSEPL 377
|
|
| DUF1983 |
pfam09327 |
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized ... |
3763-3833 |
1.10e-16 |
|
Domain of unknown function (DUF1983); Members of this family of functionally uncharacterized domains are found in various bacteriophage host specificity proteins.
Pssm-ID: 430529 Cd Length: 75 Bit Score: 77.34 E-value: 1.10e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556195944 3763 QELKKTVVENGNVNSTWMVKMETNSNGKKYAAGIALGIDGKN--LQSQFLVQADRFGLINTSNGNTTTPFVVE 3833
Cdd:pfam09327 3 QKSTAVADLDGKLSAMYSIKAQVKANGQKYVAGIALGAESGGgvTTSQVLFMADRFAIVNPANGNVTPPFVVQ 75
|
|
| ILEI |
pfam15711 |
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ... |
3059-3140 |
8.35e-09 |
|
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.
Pssm-ID: 464817 Cd Length: 89 Bit Score: 55.34 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3059 DGSTV-IATSKTYDVFgSANNGATMSADIEALASGTYVCVLTFDEPTGN-RGKVLSALESLGgtSEVVNSLPYRGAYILL 3136
Cdd:pfam15711 9 DACTGkVLDSKSFDTY-SYSDSSRLANFLKSIPDGSIVLIATKDEASSKlSDEARKALESLG--SSKIDNLGFRDSWAFI 85
|
....
gi 556195944 3137 GRKG 3140
Cdd:pfam15711 86 GFKG 89
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
558-834 |
5.90e-08 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 58.86 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 558 TGDNITKVTFKTALATADQPVANGVWTITEPDLVPMRARVVAIAQGETPGSFDITVVQNNASKYQAIDNGAALVPENTTV 637
Cdd:COG3401 133 GGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 638 LDPTYSKPSN--LVISEGTYLSSPGNLSVKLM------LAWEGKSPEYWVSWR--RSDEGNVSNWQSARATEEQYEIVNV 707
Cdd:COG3401 213 DTGGESAPSNevSVTTPTTPPSAPTGLTATADtpgsvtLSWDPVTESDATGYRvyRSNSGDGPFTKVATVTTTSYTDTGL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 708 AENGRYDFQLYSVSFGGKKSEIITAVyQVKGTMTPPGAPTSLTAVGDY-RNVVLNWVNPDSVDLAQINVYASKTNKLDTA 786
Cdd:COG3401 293 TNGTTYYYRVTAVDAAGNESAPSNVV-SVTTDLTPPAAPSGLTATAVGsSSITLSWTASSDADVTGYNVYRSTSGGGTYT 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 556195944 787 TLIAQAATTTFTHAGLGDNETWYYWIRAVNKRGMVGQPNSNLGTEATT 834
Cdd:COG3401 372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTAS 419
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
835-1083 |
9.49e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 58.05 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 835 RDVLSFLKDKITSSELGKELLDEIdsKATQEAVDNAIGEV---QNSVNESIQQVENDLAQTS-----SEIKAQVDSVNQ- 905
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESK--RETETGIQNLTAEIeqgQESLTENLEAIKEEIENIVgevelSKSSEELDSFKDt 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 906 --SLKEDIDTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDGD---AALSQEIKKAQSSLTTSLSQTSKDLTAAI 980
Cdd:COG5185 386 ieSTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATssnEEVSKLLNELISELNKVMREADEESQSRL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 981 QKETND-------RIADVNDAAKQAADQLLSAKNELKTSIDSLSEVVTSGDENLARQISQI--AAGTGEQFDSLKIWYFD 1051
Cdd:COG5185 466 EEAYDEinrsvrsKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkdFMRARGYAHILALENLI 545
|
250 260 270
....*....|....*....|....*....|....
gi 556195944 1052 QDAEGWT--EDDNGYTPMSVTSDGWLKANNPTST 1083
Cdd:COG5185 546 PASELIQasNAKTDGQAANLRTAVIDELTQYLST 579
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
855-1013 |
2.75e-07 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 53.10 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 855 LDEIDSKAtQEAVDNAIGEVQNSVNESIQQ-VENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVNQTINTNI 933
Cdd:cd13769 3 LSELIQKA-QEAINNLAQQVQKQLGLQNPEeVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTKLSETV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 934 SNVNSQIEAAKQSikdgdaalsQEIK-KAQSSLTTSLSQtSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAKNELKTS 1012
Cdd:cd13769 82 PELRKSLPVEEKA---------QELQaKLQSGLQTLVTE-SQKLAKAISENSQKAQEELQKATKQAYDIAVEAAQNLQNQ 151
|
.
gi 556195944 1013 I 1013
Cdd:cd13769 152 L 152
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
860-1041 |
1.67e-06 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 51.85 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 860 SKATQEAVDNAigevqNSVNESIQQVE---NDLAQTSSEIKAQVDSVNQSLKEDIDTVNQ--TIVDNIDTVNQTIN---- 930
Cdd:cd11386 4 SASIEEVAASA-----DQVAETSQQAAelaEKGREAAEDAINQMNQIDESVDEAVSAVEEleESSAEIGEIVEVIDdiae 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 931 -TNISNVNSQIEAA---KQSikDGDAALSQEIKKaqsslttsLSQTSKDLTAAIQK---ETNDRIADVNDAAKQAADQLL 1003
Cdd:cd11386 79 qTNLLALNAAIEAAragEAG--RGFAVVADEVRK--------LAEESAEAAKEIEElieEIQEQTEEAVEAMEETSEEVE 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 556195944 1004 SAKNELKTSIDSLSEVVTSGDEnLARQISQIAAGTGEQ 1041
Cdd:cd11386 149 EGVELVEETGRAFEEIVASVEE-VADGIQEISAATQEQ 185
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
518-824 |
1.92e-06 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 53.85 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 518 IVSFTKNSITLDAPVSLKKSGSFIRIINQEGKIVERDINETGDNITKVTFKTALATADQPVANGVWTITEPDLVPMRARV 597
Cdd:COG3401 3 SSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 598 VAIAQGETPGSFDITVVQNN-----ASKYQAIDNGAALVPENTTVLDPTYSKPSNLVISEGTYLSSPGNLSVKLMLAWEG 672
Cdd:COG3401 83 AVAAAPPTATGLTTLTGSGSvggatNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 673 KSPEYWVSWRRSDEGNVSNWQSARATEEQYEIVNVAENGRYDFQLYSVSFGGKKSEIITAVYQVKGTMTPPGAPTSLTAV 752
Cdd:COG3401 163 VAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTAT 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556195944 753 GDYRN-VVLNWVNPDSVDLAQINVYASKTNKlDTATLIAQAATTTFTHAGLGDNETWYYWIRAVNKRGMVGQP 824
Cdd:COG3401 243 ADTPGsVTLSWDPVTESDATGYRVYRSNSGD-GPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP 314
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
848-1006 |
1.02e-05 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 49.93 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 848 SELGKELLDEIDSKATQEA-----VDNAIGEVQNSVNESIQQVENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNI 922
Cdd:pfam06705 15 SGFHDKMENEIEVKRVDEDtrvkmIKEAIAHLEKLIQTESKKRQESFEDIQEEFKKEIDNMQETIKEEIDDMAANFRKAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 923 DTVNQTINTNISNVNSQIEAAKQSIK-----------DGDAALSQEI---KKAQSSLTTSLSQTSKDLTAAIQKETNDRI 988
Cdd:pfam06705 95 AELNDTINNVETNLQNEIAIHNDAIEalrkealkslnDLETGIATENaerKKMYDQLNKKVAEGFARISAAIDTEKNARD 174
|
170
....*....|....*...
gi 556195944 989 ADVNDAAKQAADQLLSAK 1006
Cdd:pfam06705 175 SAVSAATTELTNTKLVEK 192
|
|
| DUF3672 |
pfam12421 |
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is ... |
3872-3948 |
1.14e-05 |
|
Fibronectin type III protein; This domain family is found in bacteria and viruses, and is typically between 126 and 146 amino acids in length. The family is found in association with pfam09327, pfam00041. There are two completely conserved G residues that may be functionally important. Many of the proteins in this family are annotated as fibronectin type III however there is little accompanying literature to confirm this.
Pssm-ID: 289206 Cd Length: 133 Bit Score: 47.65 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3872 VGKDGSSQFHNVIVRGHVEAESGSFKGTIDATDGVFRGTVQASRFVGDICSAGVFKQGVRPDITHYDSGSVGGTKTY 3948
Cdd:pfam12421 1 LTPDGHLTAKNGDFRGSINANSGTLNNVTIAENCTISGTLRAEKILGDIVKAGVWEFPYVREPASSNHRYFSGTLTV 77
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
876-1036 |
2.09e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 876 NSVNESIQQVENDLAQTSSEIKAQVDSVnQSLKEDIDTVNQTIvDNIDTVNQTINTNISNVNSQIEAAKQSIKDGDAALS 955
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRI-RALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 956 QEIKKAQ-----SSLTTSLSQTS-----------KDLTAAIQ------KETNDRIADVNDAAKQAADQLLSAKNELKTSI 1013
Cdd:COG4942 108 ELLRALYrlgrqPPLALLLSPEDfldavrrlqylKYLAPARReqaeelRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180
....*....|....*....|...
gi 556195944 1014 DSLSEVVTSGDENLARQISQIAA 1036
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAE 210
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
865-1032 |
2.10e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 48.03 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 865 EAVDNAIGEVQNSVN----ESIQQVENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVNQTINTNISNVNSQI 940
Cdd:pfam01442 7 DELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 941 EAAKQSIKDGDAALSQEIKKAQSSLTTSLSQTSKDLTAAIQKETNDRIADVNDAAKQAADQLlsaKNELKTSIDSLSEVV 1020
Cdd:pfam01442 87 NADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEV---QAQLSQRLQELREKL 163
|
170
....*....|..
gi 556195944 1021 TSGDENLARQIS 1032
Cdd:pfam01442 164 EPQAEDLREKLD 175
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
3235-3345 |
2.29e-05 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 47.06 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3235 GNLIVNPSFE-RGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQ----KISFKKDRSYKIGIWAKQDpnttiq 3309
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTATWDGQiidiTIRLEKGTTYTVSFWVKAS------ 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 556195944 3310 STDNTKFRVAEGnGLIASKAYGPFTSNWQEVSWTWK 3345
Cdd:pfam02018 75 SGPPQTVSVTLQ-ITDASGNYDTVADEKVVLTGEWT 109
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
1874-3465 |
2.62e-05 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 50.54 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1874 VNADTTITMAPGSRVFDDTGAVYVNGVRVAFGNASWNTVSFDLKAGWSTVEFLVNQWTGQAYINLGFKLSEKVAQLNSAL 1953
Cdd:COG3210 77 STGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1954 GMNALSNAISAVTSNVSTVGDRVTSTSQSVTDLRNSLEQTNANLENKADAQALSTLQNTVSKQRDTISSQGNSITNLNNT 2033
Cdd:COG3210 157 GAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2034 LTAARNAGDNLIPNYDFLQGATAWDTQYPAGVTFGNFGDGKAGVKLNRTTTTSPGIFSNNNKPLPLNGQRK--------- 2104
Cdd:COG3210 237 GAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGgtgvlgggt 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2105 -YRVVVKAKGVSGAMNMLIRRQNKIGQTDSNYEDKNVTLTSEWQTITWETGLTASNADGQNFKLYAHPANAEIWVDTFKV 2183
Cdd:COG3210 317 aAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2184 FDITDEVKIKANSDALSTLSSTVTQQGDKITSQGNSITKLTNDLEAADANIAKKADQSAVTTLTGRVEKTESGLTAANSN 2263
Cdd:COG3210 397 TTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2264 ITSLSSSLNQQSKRGANLLPDGTFESYAVGHNLSNNRVIVTTDDSHGGNKCIRVTRPNDYNANATDNSDNHIFSGFQVRD 2343
Cdd:COG3210 477 GNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTT 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2344 NAVFYMecWVKLDAKSTAMAENAQISIGLSLQYQDNSWQWPAVTKAAKDLSTAQWTKVSGYLKSTKSGIKQAMVRISIPN 2423
Cdd:COG3210 557 AASGSN--TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGL 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2424 VSSVKAGNSFLIDDLVITEVTDAYNAQSTADANANAISTLDSTVSQQGDQITSQGNSITKLTNDLSTTNSNVAKKADGAA 2503
Cdd:COG3210 635 TGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSIT 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2504 VTALTnrvteaeGNISSQSNQLATLSNSLAEGSLICNGGLNVDASFWEDSGPGSAFTYDANEKAIRTTTGSirvANLTRI 2583
Cdd:COG3210 715 VTGQI-------GALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANAN---GNTSAG 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2584 PVEAETTLTISFEMKASETISNVSSDSVGVIADLATPTNWISSVSPWLGGVSTNWQTKSVELTIPANFIGKYVYLRFAAG 2663
Cdd:COG3210 785 ATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAG 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2664 GWTPSNSARLYIRKVDVFSSTGVAKKANATAVSDLTSRVDSTEGKLASQSQALTKLQNDLATTNNNVSKKADANALTALT 2743
Cdd:COG3210 865 ANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTA 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2744 NRVTQTEKDINSTSSSVTNLNNKVDAISVGGTNLIKNSGDMTGWSNVVSDTYRGNAVIGATVKAGSGYRDLREITLESPV 2823
Cdd:COG3210 945 LSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTG 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2824 DAGEYVYSFYAKGGVAGQTMTAFFYNPNTTTSIETSQGAKGNNSDGRAQFTLTTSWARYWVKWKQTPTTGTKRLILCRIE 2903
Cdd:COG3210 1025 TTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATG 1104
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2904 SNTSKDQTVYINSPKFEVGNVVSDWNESPSDSASASAVDSLTTKVNQQGTSISSIGNRTTSLENGLSTAQNNIAKKADAS 2983
Cdd:COG3210 1105 TSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGG 1184
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 2984 ALQDLRNTVTSQGDDLTAANSSITSLQASMNRRTVFTVTARGNGNSVTHGVFDESGKNLFTPGRSWALVTFAKHSDGSTV 3063
Cdd:COG3210 1185 ADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGA 1264
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3064 IATSKTYDVFGSANNGATMSADIEALASGTYVCVLTFDEPTGNRGKVLSALESLGGTSEVVNSLPYRGAYILLGRKGMKP 3143
Cdd:COG3210 1265 VSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTIN 1344
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3144 GDGLELRAPTGGDATAHISTSVEFVNGVMMGLGAAGGVMMKADANASAITTLQNTVKTQGDNIDSLSSSTTALENSLASS 3223
Cdd:COG3210 1345 TTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAG 1424
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3224 NASVDAASQIPGNLIVNPSFERGTEGYTGWSGIATVVTLQVPHLGTKAAKLAAGGSAGVGQKISFKKDRSYKIGIWAKQD 3303
Cdd:COG3210 1425 TTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGT 1504
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3304 PNTTIQSTDNTKFRVAEGNGLIASKAYGPFTSNWQEVSWTWKATKDVVADVQFTAFLSAGAMYFDDFYVVDVTDSVETQA 3383
Cdd:COG3210 1505 STGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDT 1584
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3384 NSSAITNLDSRVTKTENDITSQGSQVTQLKNDLATTNTNVSKKADAAALTALTNRVTQNEKEIETQSSQTTSLKNSLSTV 3463
Cdd:COG3210 1585 GAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGA 1664
|
..
gi 556195944 3464 QA 3465
Cdd:COG3210 1665 GN 1666
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
848-1002 |
5.28e-05 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 46.21 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 848 SELGKELLDEIDSKATQEAVDnaigEVQNSVNESIQQVENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIvdnidtvnQ 927
Cdd:pfam07464 3 EELQQSVQKQLGLPSQQEVVE----TIKENTENLVDQLKQVQKSLQEELKKASGEAEEALKELNTKIVETA--------D 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556195944 928 TINTNISNVNSQIEAAKQSIKDGDAALSQEIKKAQSSLTTSLSQTSKDLTAAIQKETNdriaDVNDAAKQAADQL 1002
Cdd:pfam07464 71 KLSEANPEVVQKANELQEKFQSGVQSLVTESQKLAKSISENSQGATEKLQKATKQAYD----DAVQAAQKLANQL 141
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
842-1027 |
1.10e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 842 KDKITSSELGKELLDEIDSKATQEA--VDNAIGEVQNSVNESIQQVENDLAQTS---SEIKaqvdsvnqSLKEDiDTVNQ 916
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNqqKDEQIKKLQQEKELLEKEIERLKETIIknnSEIK--------DLTNQ-DSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 917 TIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDgdaaLSQEIKKAQSSL------TTSLSQTSKDLTAAI------QKET 984
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ----KQKELKSKEKELkklneeKKELEEKVKDLTKKIsslkekIEKL 529
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556195944 985 NDRIADVNDAAKQAADQLLSAKNELKTsiDSLSEVVTSGDENL 1027
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEI 570
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
825-1027 |
3.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 825 NSNLGTEATTRDV-LSFLKDKITSSElgKELLDEIDSKA-TQEAVDNAIGEVQNSvNESIQQVENDLaqtsSEIKAQVDS 902
Cdd:TIGR04523 227 NNQLKDNIEKKQQeINEKTTEISNTQ--TQLNQLKDEQNkIKKQLSEKQKELEQN-NKKIKELEKQL----NQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 903 VNQSLKEDIDTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDgdaalsqeIKKAQSSLTTSLSQTSKDLtaaiqK 982
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ--------LKKELTNSESENSEKQREL-----E 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556195944 983 ETNDRIADV---NDAAKQAADQLLSAKNELKTSIDSLSEVVTSGDENL 1027
Cdd:TIGR04523 367 EKQNEIEKLkkeNQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
906-1041 |
3.48e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 43.85 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 906 SLKEDIDTVNQTIVD------------NIDTVNQTINTNISNVNSQIEAAKQSIKDgdaalsqEIKKAQSSLTTSLSQTS 973
Cdd:cd13769 2 QLSELIQKAQEAINNlaqqvqkqlglqNPEEVVNTLKEQSDNFANNLQEVSSSLKE-------EAKKKQGEVEEAWNEFK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556195944 974 KDLTaaiqkETNDRIADVNDAAKQAADQllsaKNELKTSIDSLSEVVtsgdENLARQISQIAAGTGEQ 1041
Cdd:cd13769 75 TKLS-----ETVPELRKSLPVEEKAQEL----QAKLQSGLQTLVTES----QKLAKAISENSQKAQEE 129
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
853-1045 |
3.69e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 45.35 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 853 ELLDEIDSKATQ-EAVDNAIGEVQNSVNESIQQVE--NDLA----QTSSEIKAQVDSVNQSLKEDIDTVNQTI--VDNID 923
Cdd:smart00283 15 EQAEELEELAERmEELSASIEEVAANADEIAATAQsaAEAAeegrEAVEDAITAMDQIREVVEEAVSAVEELEesSDEIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 924 TVNQTIN-----TNISNVNSQIEAAKQSIK-DGDAALSQEIKKaqsslttsLSQTSKDLTAAIQ---KETNDRIADVNDA 994
Cdd:smart00283 95 EIVSVIDdiadqTNLLALNAAIEAARAGEAgRGFAVVADEVRK--------LAERSAESAKEIEsliKEIQEETNEAVAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556195944 995 AKQAADQLLSAKNELKTSIDSLSEVVTSGDENlARQISQIAAGTGEQFDSL 1045
Cdd:smart00283 167 MEESSSEVEEGVELVEETGDALEEIVDSVEEI-ADLVQEIAAATDEQAAGS 216
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1062 |
4.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 846 TSSELGKELLDEIDskATQEAVDNAIGEVQNSVNEsIQQVENDLAQTSSEIKA---QVDSVNQSLKEDIDTVNQTiVDNI 922
Cdd:COG4372 28 ALSEQLRKALFELD--KLQEELEQLREELEQAREE-LEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQA-QEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 923 DTVNQ----------TINTNISNVNSQIEAAKQSIKDGDAALSQ---EIKKAQSSLTtslsqtskDLTAAIQKETNDRIA 989
Cdd:COG4372 104 ESLQEeaeelqeeleELQKERQDLEQQRKQLEAQIAELQSEIAEreeELKELEEQLE--------SLQEELAALEQELQA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556195944 990 DVNDAAKQAADQLLSAKNELKTSIDSLSEvvtsgDENLARQISQIAAGTGEQFDSLKIWYFDQDAEGWTEDDN 1062
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAE-----AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1196-1378 |
4.17e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1196 LQEEQQARANADTA-EAQARSTLAAQIRGSSESGNLDDIRSGLiyQEKNARITADAAEASAR----ESLQTEFNRNKASV 1270
Cdd:pfam07888 36 LEECLQERAELLQAqEAANRQREKEKERYKRDREQWERQRREL--ESRVAELKEELRQSREKheelEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1271 AEELHTLSTEQASQASKITGLQ---TSLGQKADASAVQ--TISQKVEEQGNTLKSQGAALSTLDNRVGSVESGVSANSKA 1345
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEediKTLTQRVLERETEleRMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190
....*....|....*....|....*....|...
gi 556195944 1346 ITGLQSTVTQQDKTLSSQSESITTLNNSLSDIQ 1378
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3629-3771 |
6.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 3629 ITDAKEAQDSANANASA----LTSLTSRVTNVEGLVTSQASQLSSLTSQVNDASSKVDQmaqtitnnekTQSSLNTSLQS 3704
Cdd:COG4372 26 IAALSEQLRKALFELDKlqeeLEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----------LNEQLQAAQAE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 3705 QIDAQASANIKNQtELNNATTSLAAIKSTQQTQATTISALSQQQTNLTAQVGGQSAELQELKKTVVE 3771
Cdd:COG4372 96 LAQAQEELESLQE-EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
832-1022 |
1.06e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.69 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 832 ATTRDVLSFLKDKITSS----ELGKELLDEIDS--KATQEAVDNAigevqNSVNESIQQVENDLAQTSSEIKAQVDSVNQ 905
Cdd:pfam04108 3 SSAQDLCRWANELLTDArsllEELVVLLAKIAFlrRGLSVQLANL-----EKVREGLEKVLNELKKDFKQLLKDLDAALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 906 SLKEDIDTVNQTIVDNIDTVNQTINTNISN-VN-SQIEAAKQSIKDgdaaLSQEIKKAQSSLTTSLSQTSKDLTaAIQKE 983
Cdd:pfam04108 78 RLEETLDKLRNTPVEPALPPGEEKQKTLLDfIDeDSVEILRDALKE----LIDELQAAQESLDSDLKRFDDDLR-DLQKE 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 556195944 984 TNDriADVNDAAKQAADQLLSAKNELKTSIDSLSEVVTS 1022
Cdd:pfam04108 153 LES--LSSPSESISLIPTLLKELESLEEEMASLLESLTN 189
|
|
| CBM_4_9 |
pfam02018 |
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains. |
1389-1507 |
1.18e-03 |
|
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
Pssm-ID: 396553 Cd Length: 134 Bit Score: 42.05 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 1389 SNLLVNASFE-RDLAGWSAGNSVSSIIKASAPHSGSKILVCAAGT-----VQITQSVSVVEGRTYKLSSFVRcttdavIS 1462
Cdd:pfam02018 1 GNLIKNGTFEdGGLDGWKARGGSGKATVDVTSYNGTYSLKVSGRTatwdgQIIDITIRLEKGTTYTVSFWVK------AS 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 556195944 1463 SPGNNKLRI-----GAATLLKEIPIRPENLPKDetWKEVSDTWKATLTGK 1507
Cdd:pfam02018 75 SGPPQTVSVtlqitDASGNYDTVADEKVVLTGE--WTKLEGTFTIPKTAS 122
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
856-997 |
1.35e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 856 DEIDSKATQEAVDNAIG-EVQNSVNESIQQVENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVN--QTINTN 932
Cdd:cd22656 154 DQTALETLEKALKDLLTdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIAdlTAADTD 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556195944 933 ISNVNSQIEAAKQSIkdgdaalsQEIKKAQSSLTTSLSQTSKDLTAAIQKETNDRIA--DVNDAAKQ 997
Cdd:cd22656 234 LDNLLALIGPAIPAL--------EKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAklELEKAIEK 292
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
841-1034 |
1.46e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 841 LKDKITSSELG-KELLDEIDSKATQ-EAVDNAIgevqNSVNESIQQVENDLAQTSSEIKaQVDSVNQSLKEDIDTVNQTI 918
Cdd:TIGR04523 445 LTNQDSVKELIiKNLDNTRESLETQlKVLSRSI----NKIKQNLEQKQKELKSKEKELK-KLNEEKKELEEKVKDLTKKI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 919 vdnidtvnQTINTNISNVNSQIEAAKQSIKDgdaaLSQEIKKAQSSLTTSLSQTSKD-LTAAIQ--KETNDRIADVNDAA 995
Cdd:TIGR04523 520 --------SSLKEKIEKLESEKKEKESKISD----LEDELNKDDFELKKENLEKEIDeKNKEIEelKQTQKSLKKKQEEK 587
|
170 180 190
....*....|....*....|....*....|....*....
gi 556195944 996 KQAADQLLSAKNELKTSIDSLSEVVtsgdENLARQISQI 1034
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKI----SSLEKELEKA 622
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
898-1036 |
1.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 898 AQVDSVNQSLKEDIDTVNQTIVDNIDTVnQTINTNISNVNSQIEAAKQSIKDGDAALSQE---IKKAQSSLTTSlsQTSK 974
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL-AALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNV--RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556195944 975 DLTAaIQKE----------TNDRIADVNDAAKQAADQLLSAKNELKTSIDSLSEVVTSGDENLARQISQIAA 1036
Cdd:COG1579 90 EYEA-LQKEieslkrrisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
770-1045 |
2.08e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.86 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 770 LAQINVYASKTNKLDTATLIAQAATTTFTHAGLGDNETWYYWIRAVNKRGMVGQPNSNLGTEATTRDVLSFLKDKITSSE 849
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 850 LGKELLDEIDSKATQEAVDNAIGEVQNSVNESIQQVENDLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVNQTI 929
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 930 NTNISNVNSQIEAAKQSIKDGDAA--LSQEIKKAQSSLTTSLSQTSK-DLTAAIQKETNDRIADVNDAAKQAADQLlsak 1006
Cdd:COG0840 176 AAALALALLAAALLALVALAIILAllLSRSITRPLRELLEVLERIAEgDLTVRIDVDSKDEIGQLADAFNRMIENL---- 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 556195944 1007 NELKTSIDSLSEVVTSGDENLARQISQIAAGTGEQFDSL 1045
Cdd:COG0840 252 RELVGQVRESAEQVASASEELAASAEELAAGAEEQAASL 290
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
869-1019 |
2.70e-03 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 43.02 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 869 NAIGEVQNSVnesiQQVENDLAQTSSEIKA---QVDSVNQSLKEDID-------TVNQTIV---DNIDTVNQTINTNISN 935
Cdd:cd22654 97 NGINKLQSQL----QTIQNSMEQTSSNLNRfktLLDADSKNFSTDAKkaidslsGSNGEIAqlrTQIKTINDEIQEELTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 936 -VNSQIEAAKQSIKDGDAALSqeikkaqssLTTSLSQTSKDLTAAIQKETNDRIADVNDAAKQAADQLLSAKNELKTSID 1014
Cdd:cd22654 173 iLNRPIEVGDGSINIGKQVFT---------ITITTATTKTVDVTSIGGLINGIGNASDDEVKEAANKIQQKQKELVDLIK 243
|
....*
gi 556195944 1015 SLSEV 1019
Cdd:cd22654 244 KLSDA 248
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
859-1022 |
2.84e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 42.40 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 859 DSKATQEAVDNAIGEVQNSVNESIQQVEN--DLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIVDNIDTVNQ---TINTNI 933
Cdd:cd21116 3 DLGAASALVQAYVTAILNQPNINLIPLDLlpSLNTHQALARAHALEWLNEIKPKLLSLPNDIIGYNNTFQSyypDLIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 934 SNVNSQIEAAKQSIKDGDAALSQEIKKAQSSLT---TSLSQTSKDLTAAIQKETNdriaDVNDAAKQAAdQLLSAKNELK 1010
Cdd:cd21116 83 DNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTsfiNELTTFKNDLDDDSRNLQT----DATKAQAQVA-VLNALKNQLN 157
|
170
....*....|..
gi 556195944 1011 TSIDSLSEVVTS 1022
Cdd:cd21116 158 SLAEQIDAAIDA 169
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
921-1041 |
3.60e-03 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 40.81 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 921 NIDTVNQTINTNISNVNSQIEAAKQSIKDgdaalsqEIKKAQSSLTTSLSQTSKDLTaaiqkETNDRIADVNDAAKQAAD 1000
Cdd:pfam07464 17 SQQEVVETIKENTENLVDQLKQVQKSLQE-------ELKKASGEAEEALKELNTKIV-----ETADKLSEANPEVVQKAN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 556195944 1001 QLlsaKNELKTSIDSLSEVVtsgdENLARQISQIAAGTGEQ 1041
Cdd:pfam07464 85 EL---QEKFQSGVQSLVTES----QKLAKSISENSQGATEK 118
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
841-1009 |
4.35e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 841 LKDKITSSElgkELLDEIDSKATQEAVDNAIGEVQNSVN------ESIQQVENDLAQTSSEIKaQVDSVNQSLKEDIDTV 914
Cdd:pfam06160 242 LEEQLEENL---ALLENLELDEAEEALEEIEERIDQLYDllekevDAKKYVEKNLPEIEDYLE-HAEEQNKELKEELERV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 915 NQT-IVDNIDTVN-QTINTNISNVNSQIEAAKQSIKDGDAALSqEIKKAQSSLTTSLSQTSKDltaaiQKETNDRIADVN 992
Cdd:pfam06160 318 QQSyTLNENELERvRGLEKQLEELEKRYDEIVERLEEKEVAYS-ELQEELEEILEQLEEIEEE-----QEEFKESLQSLR 391
|
170
....*....|....*..
gi 556195944 993 DAAKQAADQLLSAKNEL 1009
Cdd:pfam06160 392 KDELEAREKLDEFKLEL 408
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
865-1041 |
5.26e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.70 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 865 EAVDNAIGEVQNSVNESIQQVEN--DLAQTSSEIKAQVDSVNQSLKEDIDTVNQTI------VDNIDTVNQTIN-----T 931
Cdd:COG0840 298 EELSATVQEVAENAQQAAELAEEasELAEEGGEVVEEAVEGIEEIRESVEETAETIeelgesSQEIGEIVDVIDdiaeqT 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 932 NISNVNSQIEAAKQsikdGD-----AALSQEIKK-AQSSlTTSLSQTsKDLTAAIQKETNDRIADVNDAAKQAADQLLSA 1005
Cdd:COG0840 378 NLLALNAAIEAARA----GEagrgfAVVADEVRKlAERS-AEATKEI-EELIEEIQSETEEAVEAMEEGSEEVEEGVELV 451
|
170 180 190
....*....|....*....|....*....|....*.
gi 556195944 1006 kNELKTSIDSLSEVVtsgdENLARQISQIAAGTGEQ 1041
Cdd:COG0840 452 -EEAGEALEEIVEAV----EEVSDLIQEIAAASEEQ 482
|
|
| NTTRR-F1 |
NF033675 |
NTTRR-F1 domain; NTTRR-F1 (N-terminal To Repetitive Region - Firmicutes 1) is a homology ... |
3236-3277 |
7.09e-03 |
|
NTTRR-F1 domain; NTTRR-F1 (N-terminal To Repetitive Region - Firmicutes 1) is a homology domain found strictly as the N-terminal non-repetitive region of otherwise highly repetitive proteins of various Firmicutes. The repetitive region that follows typically is collagen-like, with every third residue a glycine.
Pssm-ID: 468135 Cd Length: 155 Bit Score: 40.23 E-value: 7.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556195944 3236 NLIVNPSFERGTegYTGWSGIATVVTLQVPHLGTKAAKLAAG 3277
Cdd:NF033675 4 NLIVNGGFETGS--LTPWSGVNASITSQFSHSGFYSARLLGG 43
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
834-1020 |
8.94e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 834 TRDVLSFLKDKITSSE-LGKELLDEIDSKATQ-EAVDNAIGEVQNSVNESIQQVENDLAQTSSEIKAQVDSVNQSLKEDI 911
Cdd:COG5185 404 AQEILATLEDTLKAADrQIEELQRQIEQATSSnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 912 DTVNQTIVDNIDTVNQTINTNISNVNSQIEAAKQSIKDGdaalsqeikkaQSSLTTSLSQTSKDLTAAIQKETNDRIA-- 989
Cdd:COG5185 484 NEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV-----------AESLKDFMRARGYAHILALENLIPASELiq 552
|
170 180 190
....*....|....*....|....*....|.
gi 556195944 990 DVNDAAKQAADQLLSAKNELKTSIDSLSEVV 1020
Cdd:COG5185 553 ASNAKTDGQAANLRTAVIDELTQYLSTIESQ 583
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
861-965 |
9.65e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 41.77 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556195944 861 KATQEAVDNAIGEVQNSVN--ESIQQVendLAQTSSEIKAQVDSVNQSLKEDIDTVNQTIvDNIDTVNQTINTNISNVNS 938
Cdd:pfam03148 204 KFTQDNIERAEKERAASAQlrELIDSI---LEQTANDLRAQADAVNFALRKRIEETEDAK-NKLEWQLKKTLQEIAELEK 279
|
90 100
....*....|....*....|....*..
gi 556195944 939 QIEAAKQSIKDGDAALsqeiKKAQSSL 965
Cdd:pfam03148 280 NIEALEKAIRDKEAPL----KLAQTRL 302
|
|
| |
