|
Name |
Accession |
Description |
Interval |
E-value |
| hyperosmo_Ebh |
TIGR04264 |
hyperosmolarity resistance protein Ebh, N-terminal domain; Staphylococcal protein Ebh ... |
176-2527 |
0e+00 |
|
hyperosmolarity resistance protein Ebh, N-terminal domain; Staphylococcal protein Ebh (extracellular matrix-binding protein homolog) is a giant protein, sometimes over 10,000 amino acids long as reported. This model describes a non-repetitive amino-terminal domain of about 2400 amino acids.
Pssm-ID: 275090 [Multi-domain] Cd Length: 2354 Bit Score: 3612.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 176 DRNELQAFFDANYHDYRFIDRENADSGTFNYVKGIFDKINTLLGSNDPINNKDLQLAYKELEQAVALIRTMPQRQQTSRR 255
Cdd:TIGR04264 1 DKDKLQAFFDASYHDYRFIDRDKADNKEYNQVKATFDKVNTFLGNNDNPNSKSLQLLYKELEQAVALIRTLPQRQVRTRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 256 SSRIQtRSIESRAAEPRSVSDYQNANSSYYVENANDGSGYPVGTYINASSKGAPYNLPTTPWNTLKASDAKEFALITAKQ 335
Cdd:TIGR04264 81 NNREA-RSVRSRRAESRSVGSYNNAKTEYYVENENDGSGYPSGTYIHASNKGAPYYLPTTPWNTLSASDVKGIAYITAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 336 TGDGYQWVIKFNKGHAPHENMIFWFALPDGQTPVGRTEFVTVNADGTNVQWSNGAGAGANKPLPQMWEY-GVNDPHRSHD 414
Cdd:TIGR04264 160 VKDGYEWTINFNKGHIPHENMIFWFGLPKDQTPVGPVRFSITDPNGTNTSSSSGVGDGEGQPLPRMWDSaGGIDPSRAYN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 415 FKIRNRSGQVIYEWPTVNIKSLSDLARASDYLNEAGATPATKAFGRQIFDYINGQKPAESSGVPKVYTFIGQGDASYTIS 494
Cdd:TIGR04264 240 FRQGPRTGYEFYDWPTVHINNFGDFARAPEYFNREGAPNKARVYGDQNFRYLNGEVPDQIQGLDTIYAFIGKGNASYTIQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 495 FKTQGPTIDKLYYAAGARALEYNQLFMYSQLYVESTQDQQQRLNGLRQVVNRTYRIGTTKRV-EVSQGNVQTKKVLESTN 573
Cdd:TIGR04264 320 FKTQGPTTDRLYYAAGGRALEYNQLFNYNQLYVEPLEEYQDRIQSIVDVINRTYHLGNTKNVyDVPERRYVTKHILDSDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 574 LNIDDFVDDPLSYVKTPSNKVLGFYPTNANTNAFRQGGVNPLNDYQLSQLFSDQNFQEAARTKNPIRLMIGFDYPDAFGN 653
Cdd:TIGR04264 400 FNTHDYADDPLSYVRNPSNHVIGFFPYNAPTDRYRHGGVNPLNSYEIHQLFSEEKLKEAARTGNPIKLMIGFNVPDRYGN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 654 GETLVPVNLTVLPEIQHNIKFFKNDDGQNIAEKPASKQAGHPVFYVYAGNQGNASVNLGGSVTSIQPLRINLTSNENFTD 733
Cdd:TIGR04264 480 GETLKPVNLYVKPELQQNIGFFSNNETQNREESPESKAAGHPVFLVQAGNMGNTSTNGGNKDTYVQPIRIQLTSNEPFSD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 734 KDWQITGIPRTLHIENSTNRPNNARERNIELVGNLLPGDYFGTIRFGRKEQLFEIRVKPHTPRITTTAEELRGTALQKVP 813
Cdd:TIGR04264 560 NDWEISGIPPTLRIENAVGRTNNAREKNLELVGNLPPGDYFGTVRLGNREQIFEIRAKPNPPTISTTAAQLRGKGGQKPT 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 814 VTVTDIPLDPSALVYLVIPTSQTKDGGSEADQIPSGYTKIATGTPDGVHSTITIRPEDYVVFIPPVGhQIRALIFYNNVV 893
Cdd:TIGR04264 640 ITVTNVPQDTNAKVYLVAGGNGATDGTNDPGTIPSGYTILASATATGTGNTVTFNPSDYIQPLPNNG-VIRAITYYNKSV 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 894 ASNMSNAVTILPDDIPPTINNPVGLNAKYYRGDEVSFTMGVSDRH--SGLKSTTITTLPSGWTSNLTK-SDKKNGSLAIS 970
Cdd:TIGR04264 719 QSNFSNAVTILPDDTPPTISNPVGLQNKYYRGDQVNFTIPVSDNAygTGIKQVSVTGLPQGWTSNFVKnANGEAGTLTIT 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 971 GRVSMNQAYNSDITFKVSATDNVNNTTndsQSKHVTVHVGKISDDAHPIVLGNSEKVVVVNPTALTGDEKQRITTAFMNK 1050
Cdd:TIGR04264 799 GTISNSQTFNSDILVQVSATDNANNTT---QTKTIAIHIGKLSDDKPPIVLSNQEKIVVVNPTSISQDERNDIINALKAK 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1051 NQNIRGYLASSNPVTVDNHGNVTLQYRDGSSTTLDATNVMTYEPVVKPEYQTANAPKTATVTIAKGQSFNIGDIKQYFTL 1130
Cdd:TIGR04264 876 NTNISSYLATSNPYMVDNNGNVVLTYKDGSTRRIDPTNVITYEPIRKSIYAEGNNTKEATITIAKGQEFEIGDLKQYFSL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1131 SNGQAIPSSTFTNITSDRTIPTAQEVSQMNAGTQLYHITATNAYHKDTEDFYITLKIIDVKQPEGDQRVYRMSTYDITTD 1210
Cdd:TIGR04264 956 SNGQDIPNNSFTTITANDTIPTPQQISRLNAGTYTYHINASNAYNQDTERLTIKLKVVDVNQPSGDQRVYRTSTFNLTDD 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1211 EISKVKQAFINANRDAISFAEGDISVTNTPNGSNVSTITVNINKGRLTKSFTSNLANMNFLRWVNFPQDYTVTWTNAKIA 1290
Cdd:TIGR04264 1036 EINQVKQAFINANRGQLNLTDSDITVNNTPNSNHVSTVTVTITKGKLTKSFTSNFDHMNFLRWVNFPNDYTVTWTSQKIP 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1291 NRPTDGGLSWSDDHKSLIYRYDATLGTQITTNDILTLLKATTTVPGLRNNIAGNEKAQAEAGGRPNYKTTGYSQSNPTSD 1370
Cdd:TIGR04264 1116 GRGTDGGFEWSPDHKSLIYRYDATTGRQITLNDVLSLLTATTSIPGLRNNISGQEKALAEAGGTPGYKPVGYSKTNSISD 1195
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1371 GQRQFTLNGQVIQIMDIINPSNGFGGQPVTNSNVRANHSNSTVVSVNESAANGAGAFTIDHVVKNNSTHNAADAVYKAQL 1450
Cdd:TIGR04264 1196 GLRQYTYNGQVIQVLDLVQSSTGYGGQPVTYSNYRSNSSNSTVVNGNIPAANGAPAFTLDHVIKQNSGNGVMGAVYKAQL 1275
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1451 YLSPYGPKQYVEHLNQNTGNTTDAINIYFVPSDLVNPTVSVGNYTNHQVFSGETFTNTITANDNFGVQSVTVPNTSQLTG 1530
Cdd:TIGR04264 1276 YLTPYGAKQYIERLNQSTDNTTDVINVYFVPSDKVKPTISLGNYNNHVVFSGETFRNTITATDNYGLKSVTVPQTSQIAG 1355
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1531 TVDNNHQHVSATAPNVTSATNKTINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRIANISNNATVSQADQT 1610
Cdd:TIGR04264 1356 TVNNNNQIISGVAPNVTTPTTKTVKVIATDTSNNETTQSFNVTIKPLKDKYRVTTSSTEQNPIRIANIRNNATLSQADKQ 1435
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1611 AIINSLTFTSNAPNRNYATASASEITSKTVSNVSRTGNNAQVTVTVTYQDGTTSTVTVPVKHVIPEIVAHSHYTVQGQDF 1690
Cdd:TIGR04264 1436 AIINSLTITNNIPNRNYVTAGANEIRSKEVSNVSRTGNNANVTVTITYADGTTSQITVPVKHVIPEIVAIPRYTVQGQNF 1515
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1691 PTGNGASASDYFKLSNGSAIPDATITWVSGQAPNKNNTTIGQDINVTAHILIDGETTPITKTATYKVVSSVPKHVFETNR 1770
Cdd:TIGR04264 1516 PAGKGANPNDFFKLNNGSPVPDATITWVNGNGPNINSTRIGVDITVRANILFDGETTPIEKEASYMVVKSVPKRVFETTR 1595
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1771 GAVFPGISDVYDAKQYVKPVNDSWTQNAQRMNFQF-TNSYGPSKDVVGISTRDIRVTYDNHQTQIIKILAKVKPDPPRID 1849
Cdd:TIGR04264 1596 NGNFPGINNSYNPGSYVQPINNSWPQGAQAMNFDFgPNSGGPNSNVVGIFTRTIRVTYPNGQVENVKVLAKVKPDPPRID 1675
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1850 GNSVTYKAGLTNQQIKINNVLSSSSIKLFKADNTPLTITNTTYGSGNTAVVTVSDALPNGVIKARSSITMNNVTYTTQDE 1929
Cdd:TIGR04264 1676 SNSVTYKAGLTNQQIKVNNVLNNSPVKLYKSDGTELTNTTTTYGSNGSATVTVSGALPLGNIKAKSSITVNNVTYTTQNN 1755
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1930 HGRAIDVTRNESVDSNDSATVTVTPQLQATTEGAVFIKGGDGFDFGHVERFIQNPPHGATVAWHDSPDTWKNTVGNTHKT 2009
Cdd:TIGR04264 1756 SGQVVNVTRNESVESDDSAPVRVTPQLHATNGGAKFVKGGDNFDFNNAARYIDNLPDGATVEWEDNPDTWKNTVGNTTKT 1835
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2010 AVVTLPSGQGTRNVEVPVKVYPVANAKAPSRDVKGQNLTNGTDAINYITFDPNTNTNGITAAWANRQQPNNQQAGVQHLN 2089
Cdd:TIGR04264 1836 AVVTLPNGQGTRTVNIPVKVYPVATAKAPQRDVKGHQLTYGTDAMNYVTFEPNTNMNGITATWKNNNQPNNNQAGVQNLT 1915
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2090 VDVTYPGISAAKRVPVTVNVYQFEFPQTSYTTTVGGTLASGTQASGYAHIQNANGLPTDGFTYKWNRDTTGTNDANWAAM 2169
Cdd:TIGR04264 1916 ANVTYPGISTPYRVPVKVYVYKFDFAQSEYTTTVGTTFAGGTNVNNYVHLENANGLPTDGFHYVWNQATTGSNSEQWSAL 1995
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2170 NKPNAAKVINAKYDVIYNG-HTFATSLLAKFVVKDVQPAKPTVTETAAGAITIAPGANQTVNTHAGNVTTYADKLVIKRN 2248
Cdd:TIGR04264 1996 AKPNQAFVKNAKYDVLDNGnHVFATSQPAKFIVTNVQPNKATITESDVGDITITPGANKSVNTRTGNVTTYADRLVIKKN 2075
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2249 GNVVTTFTRHNNTSPWVKEASAATVAGIVGTNNGITVAAGTFNAADTIQVVATQGSGETISDEQLSDDFTVVAPQPNQAT 2328
Cdd:TIGR04264 2076 GQVITTFIRANNTSPWTKESSAINVPGVSGSPNGITINAGTFPPGDNIQVVATQGNGELISDEAISDTFTVVAPQPNQAT 2155
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2329 TKIWQNGHIDIMPNNPSGHLINPTQAMDIAYTEKVGNGAEHSKTLNAVRGQNNQWTIANKPDYVTLDAHTGKVTFNANTI 2408
Cdd:TIGR04264 2156 SKIWQNGTFEITPNNPNAHTTNPTDAVEITYTEKLGNSTEQSKTLTVTKGNNGQWSITNKPDYVTLDSATGKVTFNANTI 2235
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2409 KPNSAITITPKAGTGHSASSNPSTLTAPATHTVNTTEIVKDYGSNVTPAEINNAVQVANKRTATIKNGTAMPTNLAGGST 2488
Cdd:TIGR04264 2236 KPNSLITTISKAGSGNTESTNTNTITAPAAHTVTIHEIVKDYGSNVTNEEINNAVQVANKRHATIKQGTALPTNLAGGST 2315
|
2330 2340 2350
....*....|....*....|....*....|....*....
gi 616687517 2489 TTIPVTVTYNDSSTEEVQESIFTKADKRELITDKNHLDD 2527
Cdd:TIGR04264 2316 TTIPVTITYNDGSTEEVTETIRTKADKRELINARNHLDD 2354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9067-9904 |
3.86e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9067 TELDHAMETLKNKVDQVNTDKaqpnytEASTDKKDAVDQALQAAQSItdptngsnanKYAVEQALTKLQGKENELNG--- 9143
Cdd:TIGR02168 235 EELREELEELQEELKEAEEEL------EELTAELQELEEKLEELRLE----------VSELEEEIEELQKELYALANeis 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9144 --NERVAEAKTQAKQTIDQLTHLNADQIATAKQNIDQATKLqpiAELVDQATQLNQSMDQLQQAVNEHANVEQTVDYTQA 9221
Cdd:TIGR02168 299 rlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9222 DLDKQ-NAYKQAIAEAENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTNGKHDID----QLNALNNAQQDGFKG 9296
Cdd:TIGR02168 376 ELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9297 RIDQSNDLNQIQQIVDEAK----ALNRAMNQLSQEITGNE---GRTKGSTNYVNADTQVKRVYDEAVDKAKE-------- 9361
Cdd:TIGR02168 456 LERLEEALEELREELEEAEqaldAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSGLSGILGVLSElisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9362 --ALNKATGQNLTAEEVIKLNdavtAAKQALNGEERLNNRKSEALQrLDQLTHlnnaqRQLAIQQINNAETLNKASRAIN 9439
Cdd:TIGR02168 536 eaAIEAALGGRLQAVVVENLN----AAKKAIAFLKQNELGRVTFLP-LDSIKG-----TEIQGNDREILKNIEGFLGVAK 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9440 RAVQLDDAMGAVQQYIDEHhldVISSTNYINADDNLKA-NYDNAITNAAHELDKVQGSaIAKAEAEQlkqhiidAQKALN 9518
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGG---VLVVDDLDNALELAKKlRPGYRIVTLDGDLVRPGGV-ITGGSAKT-------NSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9519 GDQNLATAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIINDqidlnnaMETLKHLVDNEIPTAEQTVNyQNA 9598
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVE-QLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9599 DDVAKSNFDDAKrlANALINSDNTNVNDINGAIQAVKDVIQNLngEQRLQEAKDkAIQNVNKVLADKLKEIEASNATDQD 9678
Cdd:TIGR02168 747 ERIAQLSKELTE--LEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKE-ELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9679 KLIAKNKAEELANSI---INNINKATSNQDVSRVQTAGNQAIEQVHANEIpKAKIDANKDVDKQVQALIDEIDRNPNLTD 9755
Cdd:TIGR02168 822 LRERLESLERRIAATerrLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9756 KEKQALKDRINQILQQGHNginnamTKEEIEHAKAQLAQALQDIkdlvkakENAKQDVDKQVQALIDEIDRNPNLTDKEK 9835
Cdd:TIGR02168 901 EELRELESKRSELRRELEE------LREKLAQLELRLEGLEVRI-------DNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 9836 QALKDRINQILQQGHN-GINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKR-------DQINSN 9904
Cdd:TIGR02168 968 EEARRRLKRLENKIKElGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARerfkdtfDQVNEN 1044
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3623-5283 |
2.01e-13 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 79.04 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3623 TPAQKTNLTNQINSGTTVAGVHTVQSNANTLDQAMNTLRQSIANKDATKASEDYVDANNDKQTAYNNAVAAAETIINANS 3702
Cdd:COG3210 53 SNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3703 NPEMNPSTITQKADQVNSSKTALNGDENLAAAKQNAKTYLNSLTSITDAQKNNLISQITSATRVSGVDTVKQNAQHLDQA 3782
Cdd:COG3210 133 TTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3783 MANLQSGINNESQVkssekyRDADTNKQQEYDNAITAAKAILNKQHGPNTAQNAVEAALQRVNTAKNALNGDAKLIAAQN 3862
Cdd:COG3210 213 GGGTAGGVASANST------LTGGVVAAGTGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3863 AAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVKQSANSLDGAMGNLQTAINDKSGTLASQNFLDADEQKRNAYNQA 3942
Cdd:COG3210 287 TAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3943 VSNAETILNkQTGPNTAKTAVEQALNNVNSAKHALNGTQNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQ 4022
Cdd:COG3210 367 GNGGGLTTA-GAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGT 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4023 DVQRNATELNTAMGTLKHAIADKTTTLASSKYVNADSTKQNAYTTKVTNAEHIISGTPTVVTTPSEVTAAANQVNSAKQE 4102
Cdd:COG3210 446 IGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGG 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4103 LNGDERLREAKQNANTAIDALTQLNTPQKAKLKEQVGQANRLEDVQTVQTNGQALNNAMKGLRDSIANETTVKAGQNYTD 4182
Cdd:COG3210 526 NATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGT 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4183 ASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAATQVNNAKNGLNGAENLRNAQNTAKQNLNTLSHLTNNQKSAISS 4262
Cdd:COG3210 606 GSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGG 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4263 QIDRAGHVSEVTAAKNAATELNTQMGNLeQAIHDQNTVKQSVKFTDADKAKRDAYTNAVSRAETILNKTQGANTPKQDVE 4342
Cdd:COG3210 686 TTGTTLNAATGGTLNNAGNTLTISTGSI-TVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTAN 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4343 ASIQNVSSAKNALNGDQNVTNAKNAAKNALNNLTSINNAqkrdlttkidqaTTVAGVEAVSNTGTQLNTAMAKLQNGIND 4422
Cdd:COG3210 765 TTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGT------------ITAAGTTAINVTGSGGTITINTATTGLTG 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4423 KANTLASENYHDADSDKKTAYTQAVTNAENILNKNSGSNLDKAAVENALSQVTNAKGALNGNHNLEQAKSNANTTINGLQ 4502
Cdd:COG3210 833 TGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAV 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4503 HLTTAQKDKLKQQVQQAQNVAGVDTVKSSANTLNGAMGTLRNSIQDNAATKNGQNYLDATESNKTNYNNAVDSANSVINA 4582
Cdd:COG3210 913 LATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIA 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4583 TSNPNMDANAINQIATQVTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQRVANVTSIQQTANELN 4662
Cdd:COG3210 993 ATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGG 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4663 TAMGQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQVTSTKDALNGDAKLAEA 4742
Cdd:COG3210 1073 TAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVS 1152
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4743 KAAAKQNLSTLNHITNAQRTALEGQINQATTVDGVNTVKTNANTLDGAMNSLQGSINDKDATLRNQNYLDADESKRNAYT 4822
Cdd:COG3210 1153 AVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTA 1232
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4823 QAVTAAEGILNKQTGGNTSKADVDNALNAVTRAKTALNGAENLRNAKTTATNTINGLPHLTQLQKDNLKHQVEQAQNVAG 4902
Cdd:COG3210 1233 TGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGA 1312
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4903 VNGVKDKGNTLNTAMGALRTSIQNDNTTKTSQNYLDASDSNKNNYNTAVNNANGVINATNNPNIDANAINGMANQVNTTK 4982
Cdd:COG3210 1313 TVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTG 1392
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4983 AALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTATELNGAMTALKAAIADKERTKASGNY 5062
Cdd:COG3210 1393 AEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGST 1472
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5063 VNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAA---KTALNGDNNLRVAKEHANNTIDGLAQLNNAQK 5139
Cdd:COG3210 1473 AGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAevaKASLEGGEGTYGGSSVAEAGTGGGILGAVSGA 1552
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5140 AKLKEQVQSATTLDGVQTVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDASLNNRNEYDSAVTAAKAIINQTSNPTME 5219
Cdd:COG3210 1553 GSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNT 1632
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616687517 5220 ANTITQATSQVTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGVNQ 5283
Cdd:COG3210 1633 VVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDT 1696
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9649-10261 |
1.08e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9649 EAKDKAIQNVNKVLADKLKEIEASNATDQDKLIAKNKAEELANSIINNINKATSNQDVsRVQTAgnqaIEQVHAnEIPKA 9728
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKEK----IGELEA-EIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9729 K--IDAN----KDVDKQVQALIDEIDRnpnlTDKEKQALKDRInqilqqghnginnamtkEEIEHAKAQLAQALQDIKDL 9802
Cdd:TIGR02169 307 ErsIAEKerelEDAEERLAKLEAEIDK----LLAEIEELEREI-----------------EEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9803 VKAKENAKQDVDKQVQALIDEIDRnpnlTDKEKQALKDRINQILQQGHNGINNAMTK-EEIEQAKAQLAQALQDIKDLVK 9881
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQRLsEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9882 AKEDAKNAIKA--------------LANEKRDQINSNPDLTPEQKAKAlKEIDEAEKRA----LENIENAQTKDQLNKGL 9943
Cdd:TIGR02169 442 EKEDKALEIKKqewkleqlaadlskYEQELYDLKEEYDRVEKELSKLQ-RELAEAEAQAraseERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9944 ------------------------------NLGLDDirnthvwEVDAQPAV----------------NEI--FDATPEQI 9975
Cdd:TIGR02169 521 qgvhgtvaqlgsvgeryataievaagnrlnNVVVED-------DAVAKEAIellkrrkagratflplNKMrdERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9976 LVNG------ELI------------VHRDDIITEqDIHAHINLIDQ-----LTAEIIDtPSTATISDSLTAK---VEVTL 10029
Cdd:TIGR02169 594 SEDGvigfavDLVefdpkyepafkyVFGDTLVVE-DIEAARRLMGKyrmvtLEGELFE-KSGAMTGGSRAPRggiLFSRS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10030 LDGSKVIVSVPVKVVEKELTVVKQQaIESIENA----------AQQKINEINNHATLTPEQKEAAIAEVNKLK------Q 10093
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSE-LRRIENRldelsqelsdASRKIGEIEKEIEQLEQEEEKLKERLEELEedlsslE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10094 QAI-----EQINNAADVHTVEEVQHQEQAHIE----QFNPDQFTIDQAKSNAIKSISDAIQHMIDEINAS-------KDL 10157
Cdd:TIGR02169 751 QEIenvksELKELEARIEELEEDLHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlnrltleKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10158 TDKEKQEAISKLNQLKDQsIQAIQRAqsIDEIAQQLEQFKAQLKAANPFAKELENRKKSAISKIKDISTD------EINR 10231
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQ-IKSIEKE--IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrelerKIEE 907
|
730 740 750
....*....|....*....|....*....|
gi 616687517 10232 IrNSTIGTAEERQAAMNRINEIVLETIRDI 10261
Cdd:TIGR02169 908 L-EAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| aRib |
pfam18938 |
Atypical Rib domain; This entry contains atypical Rib (aRib) domains. These are found in a ... |
1023-1093 |
9.13e-11 |
|
Atypical Rib domain; This entry contains atypical Rib (aRib) domains. These are found in a variety of bacterial cell surface proteins. These proteins share a conserved motif with the Rib domain (YPDXXD). The structure of the aRib domain has been solved from two proteins, the SrpA adhesin and the GspB adhesin. In these proteins this domain has been termed the unique domain due to its lack of similarity to any other known structures at the time. The aRib domain from SrpA has been shown to mediate a dimer interaction. This family has been added to the E-set clan based on its similarity to the Rib domain, although it does not contain the Ig fold.
Pssm-ID: 465921 [Multi-domain] Cd Length: 71 Bit Score: 61.47 E-value: 9.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 1023 NSEKVVVVNPTALTGDEKQRITTAFMNKNQNIRgylaSSNPVTVDNHGNVTLQYRDGSSTTLDATNVMTYE 1093
Cdd:pfam18938 5 IPEKTEVKDPNKLTDEEKQEVKDAVKKANPDLP----EGTKVEVDDDGTVTVTYPDGSKDTIPAKDLVKEK 71
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
5481-7173 |
2.77e-10 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 68.64 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5481 TVTQANTALNGIQNLERAKQAANTAITNASDLNTKQKEALKAQVTSAGRVSVANGVEHTVTELNTAMTAlkrAIADKADT 5560
Cdd:COG3210 8 TTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSA---STGGIGAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5561 KASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPSDVTNAATQVTNAKTQLNGNHNLEVAKQNANTAIDGLTSLNG 5640
Cdd:COG3210 85 AANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5641 PQKAKLKEQVGQATTLPNVQTVRDNAQTLNTAMKGLRDSIANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQTTSP 5720
Cdd:COG3210 165 NNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5721 TMNAQEINQAKDQVTAKQQALNGQenlrTAQTNAKQHLNGLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMT 5800
Cdd:COG3210 245 GTDISSLSVAAGAGTGGAGGTGNA----GNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5801 NLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTQAEQILNKAQGPNTAKDGVETALQNVqRAKNDLNGNQNVANAKTTA 5880
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTV-ASTVGTATASTGNASSTTV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5881 KNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTASELNTAMSNLQNGINDEAATKAAQKYTDADSDKQTAYNDAVT 5960
Cdd:COG3210 400 LGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5961 AAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARLNEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGI 6040
Cdd:COG3210 480 TSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAAS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6041 QANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQNAYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSANSALN 6120
Cdd:COG3210 560 GSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6121 GDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKATSLNTAMGNLKHALAEKDNTKRSVNYTDAD 6200
Cdd:COG3210 640 GAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6201 QPKQQAYDTAVTQAEGITNAN--------------GSNANETQVQAALNQLNQAKNDLNGDNKVAQAKEAAKHALASYSN 6266
Cdd:COG3210 720 GALANANGDTVTFGNLGTGATltlnagvtitsgnaGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDIT 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6267 LNNAQSTAATSQIDNATTVAGVTTAQNTANELNTAMGQLQNGINDQNTVKQQVNFTDADQGKKDAYTNAVTNAQGILDKA 6346
Cdd:COG3210 800 ADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6347 NGQNMTKAQVEAALNQVTTAKNALNGDANVRQAKSDAKANLGTLTHLNNAQKQDLTSQIEGVTTVNGVNGVKTKAQDLDG 6426
Cdd:COG3210 880 GSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASA 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6427 AMQRLESAIANKDQTKASENYIDADPTNKTAFDNAITQAESYLNKDHGANKDKQAVEQAIQSVTSTENALNGDanlqrak 6506
Cdd:COG3210 960 SDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASAT------- 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6507 teATQAIDNLTHLNTPQKTALKQQVNAAQRVSGVTDLKNSATSLNSAMDQLKQAIADHDTIVAGGNYTNASPDKQGAYTD 6586
Cdd:COG3210 1033 --GTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTT 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6587 AYNAAKNIVNGSPNVITNAADVTAATQRVNNAETGLNGDTNLATAKQQAKDALRQMTHLSNAQKQSITGQIDSATQVTGV 6666
Cdd:COG3210 1111 TSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAAT 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6667 QSVKDNATNLDNAMNQLRNSIANKDEVKASQPYVDGDTDKQNAYNTAVTSAENIINATSQPTLDPSAVTQAANQVNTNKT 6746
Cdd:COG3210 1191 EGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGAT 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6747 ALNGAQNLANKKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQVKTKAEQLDQAMERLINGIQDKDQVKQSVNFT 6826
Cdd:COG3210 1271 STVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANT 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6827 DADPEKQTAYNNAVTAAENIINQANGTNENQSQVEAALSTVTTTKQALNGDRKVTDAKNNANQTLSTLDNLNNAQKGAVT 6906
Cdd:COG3210 1351 GLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSA 1430
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6907 GNINQAHTVAEVTQAIQTAQELNTAMGNLKNSLNDKDTTLGSQNFADADPEKKNAYNEAVRNAENILNKSTGTNVPKDQV 6986
Cdd:COG3210 1431 TTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGG 1510
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6987 EAAMNQVNTTKAALNGSQNLEKAKQHANTAIDGLSHLTNAQKDALKQLVQQSTTVAEAQGNEQKANNVDAAMDKLRQSIA 7066
Cdd:COG3210 1511 TAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPT 1590
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7067 DNATTKQNQNYTDASPNKKDAYNNAVTTAQGIIDQTTSPTLDPTVINQAAGQVSTTKNALNGNENLEAAKQQATQSLGSL 7146
Cdd:COG3210 1591 AGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAV 1670
|
1690 1700
....*....|....*....|....*..
gi 616687517 7147 DNLNNAQKQAVTNQINGAHTVDEANQI 7173
Cdd:COG3210 1671 DLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7119-7178 |
3.39e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 59.49 E-value: 3.39e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7119 VSTTKNALNGNENLEAAKQQATQSLGSLDNLNNAQKQAVTNQINGAHTVDEANQIKQNAQ 7178
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8882-8941 |
5.16e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 59.11 E-value: 5.16e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8882 VNQAKDNLHGDQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAK 8941
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8756-8815 |
5.86e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 58.72 E-value: 5.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8756 VNDAKNNLHGDQKLAQDKQRATETLNNLSNLNTPQRQALENQINNAATRGEVAQKLTEAQ 8815
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7245-7304 |
7.13e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 58.34 E-value: 7.13e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7245 VNTAKQALNGNANVQHAKDEATALINNSNDLNQAQKDALKQQVQNATTVAGVNNVKQTAQ 7304
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9149-9801 |
8.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9149 EAKTQAKQTIDQLTHLNA--DQIATAKQNIDQatkLQPIAELVDQATQLNQSMDQLQQAVN--EHANVEQTVDYTQADLD 9224
Cdd:COG4913 222 DTFEAADALVEHFDDLERahEALEDAREQIEL---LEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9225 KQNAYKQAIAEAENVLKQ--NANKQQVDQALQNILNA----KQALNGD---ERVALAKTNGKHDI--DQLNALN------ 9287
Cdd:COG4913 299 ELRAELARLEAELERLEArlDALREELDELEAQIRGNggdrLEQLEREierLERELEERERRRARleALLAALGlplpas 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9288 ----NAQQDGFKGRIDQSNDL-----NQIQQIVDEAKALNRAMNQLSQEITGNEGRtkgstnyvnadtqvKRVYDEAVDK 9358
Cdd:COG4913 379 aeefAALRAEAAALLEALEEElealeEALAEAEAALRDLRRELRELEAEIASLERR--------------KSNIPARLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9359 AKEALNKATGqnLTAEEV--------IKLNDAV--TAAKQALNG-------EERLNNRKSEALQRLDQLTHLN----NAQ 9417
Cdd:COG4913 445 LRDALAEALG--LDEAELpfvgelieVRPEEERwrGAIERVLGGfaltllvPPEHYAAALRWVNRLHLRGRLVyervRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9418 RQLAIQQINNAETLnkasrainrAVQLDDAMGAVQQYIDEHhldVISSTNYINADD--NLKaNYDNAIT--------NAA 9487
Cdd:COG4913 523 LPDPERPRLDPDSL---------AGKLDFKPHPFRAWLEAE---LGRRFDYVCVDSpeELR-RHPRAITragqvkgnGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9488 HELDK--------VQG-SAIAK-----AEAEQLKQHIIDAQKALngdQNLATAKDKANAFVDTLNGLNQQQQDLahqaIN 9553
Cdd:COG4913 590 HEKDDrrrirsryVLGfDNRAKlaaleAELAELEEELAEAEERL---EALEAELDALQERREALQRLAEYSWDE----ID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9554 NADTVTGIANIINDQIDLNNAMETLKHLvdneiptaEQTVnyqnadDVAKSNFDDAKRLANALinsdNTNVNDINGAIQA 9633
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAAL--------EEQL------EELEAELEELEEELDEL----KGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9634 VKDVIQNLngEQRLQEAKDKAIQNVNKVLADKLKEieasnatdqdkLIAKNKAEELANSIINNINKATsnqdvSRVQTAG 9713
Cdd:COG4913 725 AEEELDEL--QDRLEAAEDLARLELRALLEERFAA-----------ALGDAVERELRENLEERIDALR-----ARLNRAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9714 NQAIEQVHA--NEIPKAKIDANKDVDK--QVQALIDEIDRNpNLTDKEKQaLKDRINQilqqghnginnaMTKEEIEHAK 9789
Cdd:COG4913 787 EELERAMRAfnREWPAETADLDADLESlpEYLALLDRLEED-GLPEYEER-FKELLNE------------NSIEFVADLL 852
|
730
....*....|..
gi 616687517 9790 AQLAQALQDIKD 9801
Cdd:COG4913 853 SKLRRAIREIKE 864
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7497-7556 |
1.31e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 57.95 E-value: 1.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7497 VNDTNQALNGNQKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAPDIATVNNVKQNAQ 7556
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
4567-6253 |
1.50e-09 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 66.33 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4567 TNYNNAVDSANSVINATSNPNMDANAINQIATQVTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQ 4646
Cdd:COG3210 4 GLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4647 RVANVTSIQQTANELNTAMGQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQV 4726
Cdd:COG3210 84 AAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4727 TSTKDALNGDAKLAEAKAAAKQNLSTLNHITNAQRTALEGQINQA-----TTVDGVNTVKTNANTLDGAMNSLQGSINDK 4801
Cdd:COG3210 164 TNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVlanagGGTAGGVASANSTLTGGVVAAGTGAGVIST 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4802 DATLRNQNYLDADESKRNAYTQAVTAAEGILNKQTGGNTSKADVDNALNAVTRAKTALNGAENLRNAKTTATNTINGLPH 4881
Cdd:COG3210 244 GGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4882 LTQLQKDNLKHQVEQAQNVAGVNGVKDKGNTLNTAMGALRTSIQNDNTTKTSQNYLDASDSNKNNYNTAVNNANGVINAT 4961
Cdd:COG3210 324 NTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4962 NNPNIDANAINGMANQVNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTATELNG 5041
Cdd:COG3210 404 SLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSAT 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5042 AmTALKAAIADKERTKASGNYVNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAAKTALNGDNNLRVAK 5121
Cdd:COG3210 484 T-LAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5122 EHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDASLNNRNEYDS 5201
Cdd:COG3210 563 TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5202 AVTAAKAIINQTSNPTMEANTITQATSQVTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGV 5281
Cdd:COG3210 643 LSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGAL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5282 NQETAKATELNNAMHSLQNGINDE--TQTKQTQKYLDAEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQALQNVNST 5359
Cdd:COG3210 723 ANANGDTVTFGNLGTGATLTLNAGvtITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADG 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5360 KTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQQLDGAMGQLETSIRDKDTTLQSQN 5439
Cdd:COG3210 803 TITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSG 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5440 YQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVERAMQTVTQANTALNGIQNLERAKQAANTAITNASDLNTKQkeA 5519
Cdd:COG3210 883 GVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASA--S 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5520 LKAQVTSAGRVSVANGVEHTVTELNTAMTALKRAIADKADTKASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPS 5599
Cdd:COG3210 961 DGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5600 DVTNAATQVTNAKTQLNGNHNLEVAKQNANTAIDGLTSLNGPQKAKLKEQVGQATTLPNVQTVRDNAQTLNTAMKGLRDS 5679
Cdd:COG3210 1041 GGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASK 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5680 IANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQTTSPTMNAQEINQAKDQVTAKQQALNGQENLRTAQTNAKQHLN 5759
Cdd:COG3210 1121 VGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKG 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5760 GLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMTNLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTQAEQI 5839
Cdd:COG3210 1201 GDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGAT 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5840 LNKAQGPNTAKDGVETALQNVQRAKNDLNGNQNVANAKTTAKNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTAS 5919
Cdd:COG3210 1281 ATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATD 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5920 ELNTAMSNLQNGINDEAATKAAQKYTDADSDKQTAYNDAVTAAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARL 5999
Cdd:COG3210 1361 SAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNT 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6000 NEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGIQANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQN 6079
Cdd:COG3210 1441 TGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVA 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6080 AYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSANSALNGDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPN 6159
Cdd:COG3210 1521 KASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLS 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6160 LAAVTAAKNKATSLNTAMGNLKHALAEKDNTKRSVNYTDADQPKQQAYDTAVTQAEGITNANGSNANETQVQAALNQLNQ 6239
Cdd:COG3210 1601 LAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGL 1680
|
1690
....*....|....
gi 616687517 6240 AKNDLNGDNKVAQA 6253
Cdd:COG3210 1681 GGATTAAAGNVATG 1694
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8127-8186 |
1.65e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 57.57 E-value: 1.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8127 VNAAKQALNGNDNLANAKQQAKQQLANLTHLNDAQKQSFESQITQAPLVTDVTTINQKAQ 8186
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7623-7682 |
5.61e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 56.03 E-value: 5.61e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7623 VNAAKQALNGNDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDAAQTVANVNTNKQTAQ 7682
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7876-7934 |
1.29e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7876 NQAKDALNGDEKLAQAKQDALANLDTLRDLNQPQRDALRNQINQAQALATVEQTKQNAQ 7934
Cdd:smart00844 2 NTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8416-9242 |
1.39e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8416 ALKDQVTAATLVTAVHQIEQnantLNQAMHGLRESIqdnaatKANSKYINEDQPEQQNYDQAVQAANNIINEqtatlDNN 8495
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEE----LREELEELQEEL------KEAEEELEELTAELQELEEKLEELRLEVSE-----LEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8496 VINQAATTVNTTKAALHgdvKLQNDKDHAKQavsQLAHLNNAQKHMEDTLIDSETTRtavNHDLTEAQALDQLMDALQQS 8575
Cdd:TIGR02168 282 EIEELQKELYALANEIS---RLEQQKQILRE---RLANLERQLEELEAQLEELESKL---DELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8576 IADKDA--TRASSAYVNAEpNKKQAYDEAVQNAESIIAGLNNptinKGNVTSATQAVTSS-KNALDG-VERLAQDKQTag 8651
Cdd:TIGR02168 353 LESLEAelEELEAELEELE-SRLEELEEQLETLRSKVAQLEL----QIASLNNEIERLEArLERLEDrRERLQQEIEE-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8652 nslnHLDQLTPAQQQALENQInnattrDKVAEIIAQAQALNEAMKALKESIKDQpqteasskfinedqaqkdaytqavqh 8731
Cdd:TIGR02168 426 ----LLKKLEEAELKELQAEL------EELEEELEELQEELERLEEALEELREE-------------------------- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8732 akdlinkttdptlvksvIDQATQAVNDAKNNLHGdqklAQDKQRATETL-NNLSNLNTPQRQALENQINNAATRGEVAQK 8810
Cdd:TIGR02168 470 -----------------LEEAEQALDAAERELAQ----LQARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8811 LTEAQALNQAME-ALRNSIQD---------------QQQTEAGS------KFINEDKPQKDAYQAA------VQHAKDLI 8862
Cdd:TIGR02168 529 ISVDEGYEAAIEaALGGRLQAvvvenlnaakkaiafLKQNELGRvtflplDSIKGTEIQGNDREILkniegfLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8863 nqTSNPTLDKAQ---------VEQLTQAVNQAKDNLHG------DQKL---------ADDKQHAVTdLNQLNGLNNPQRQ 8918
Cdd:TIGR02168 609 --KFDPKLRKALsyllggvlvVDDLDNALELAKKLRPGyrivtlDGDLvrpggvitgGSAKTNSSI-LERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8919 ALESQINNAATRDEVAQKLAEAKALNQAMEALRNSIQD--QQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQTGNPTL 8996
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8997 DKSQVEQLTQAVATAKDNLHGDQKLVRDQQQAVTTVNAlpNLNHAQQQALTDAINAAPTRTEVAQHVQTATELDHAMETL 9076
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9077 KNKVDQVNTDKAQpnYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELNGNERVAEAKTQAKQ 9156
Cdd:TIGR02168 844 EEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9157 TidQLTHLNAdQIATAKQNIDQatklqpiaelvdqatqlnqsmdqLQQAVNEHANVEQTVD---YTQADLDKQNAYKQaI 9233
Cdd:TIGR02168 922 E--KLAQLEL-RLEGLEVRIDN-----------------------LQERLSEEYSLTLEEAealENKIEDDEEEARRR-L 974
|
....*....
gi 616687517 9234 AEAENVLKQ 9242
Cdd:TIGR02168 975 KRLENKIKE 983
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4978-5037 |
1.46e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4978 VNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTAT 5037
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
10051-10125 |
2.38e-08 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 54.90 E-value: 2.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 10051 VKQQAIESIENAAQQKINEINNHATLTPEQKEAAIAEVNKLKQQAIEQINNAADVHTVEEVQHQEQAHIEQFNPD 10125
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQPP 75
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
9805-9877 |
2.58e-08 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 54.52 E-value: 2.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687517 9805 AKENAKQDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIK 9877
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQ 73
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7750-7807 |
2.66e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 7750 TDAKNGLNGNHNLQVAKDNANTAIDQLPNLNQPQKTALKDQVTHAELVTGVNAIKQNA 7807
Cdd:smart00844 2 NTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5356-5415 |
2.96e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.96e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5356 VNSTKTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQ 5415
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7129-7183 |
3.04e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.70 E-value: 3.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7129 NENLEAAKQQATQSLGSLDNLNNAQKQAVTNQINGAHTVDEANQIKQNAQNLNTA 7183
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8892-8946 |
3.19e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.70 E-value: 3.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8892 DQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKALNQA 8946
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9649-10256 |
4.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9649 EAKDKAIQNVNKVLADKLKEIEA--SNATDQDKLIaKNKAEELAnSIINNINKATSNQDvsrvqtagnQAIEQVHANEIP 9726
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIEELI-KEKEKELE-EVLREINEISSELP---------ELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9727 KAKIDANKDvdkqvqaLIDEIDRNPNLTDKEKQALKDRINQIlqqghnginnamtKEEIEHAKAQLAQALQDIKDLVKAK 9806
Cdd:PRK03918 230 VKELEELKE-------EIEELEKELESLEGSKRKLEEKIREL-------------EERIEELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9807 ENAKQDVdkQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDA 9886
Cdd:PRK03918 290 EKAEEYI--KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9887 KnAIKALANEKRDQINsnpDLTPEqkaKALKEIDEAEKRALEnIENAQTKDQLNKGlnlGLDDIRNthvwevDAQPAVNE 9966
Cdd:PRK03918 368 K-AKKEELERLKKRLT---GLTPE---KLEKELEELEKAKEE-IEEEISKITARIG---ELKKEIK------ELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9967 IFDATPEQILVNGELIV-HRDDIITEqdIHAHINLIDQLTAEIIDtpstaTISDSLTAKVEVtlldgskvivsVPVKVVE 10045
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEeHRKELLEE--YTAELKRIEKELKEIEE-----KERKLRKELREL-----------EKVLKKE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10046 KELTVVKQQA--IESIENaaqqKINEINnhatltPEQKEAAIAEVNKLKQQAIE---QINNAAD---------------- 10104
Cdd:PRK03918 493 SELIKLKELAeqLKELEE----KLKKYN------LEELEKKAEEYEKLKEKLIKlkgEIKSLKKelekleelkkklaele 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10105 --VHTVEE----VQHQ-EQAHIEQFNPDQFTIDQAKS-----NAIKSISDAIQHM----------IDEINASKDLTDKEK 10162
Cdd:PRK03918 563 kkLDELEEelaeLLKElEELGFESVEELEERLKELEPfyneyLELKDAEKELEREekelkkleeeLDKAFEELAETEKRL 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10163 QEAISKLNQLKD-----------------QSIQAIQRAQ------SIDEIAQQLEQFKAQLKAANPFAKELENRKKsAIS 10219
Cdd:PRK03918 643 EELRKELEELEKkyseeeyeelreeylelSRELAGLRAEleelekRREEIKKTLEKLKEELEEREKAKKELEKLEK-ALE 721
|
650 660 670
....*....|....*....|....*....|....*..
gi 616687517 10220 KIKDIStDEINRIRNstigtaEERQAAMNRINEIVLE 10256
Cdd:PRK03918 722 RVEELR-EKVKKYKA------LLKERALSKVGEIASE 751
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8001-8060 |
4.43e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 4.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8001 VTDAKNGLNGEAKLATEKQNAKDAVNAMTHLNDAQKQALNGQIDQSPEIATVTQVKQTAT 8060
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8766-8820 |
4.77e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.31 E-value: 4.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8766 DQKLAQDKQRATETLNNLSNLNTPQRQALENQINNAATRGEVAQKLTEAQALNQA 8820
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8137-8191 |
4.87e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.31 E-value: 4.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8137 NDNLANAKQQAKQQLANLTHLNDAQKQSFESQITQAPLVTDVTTINQKAQALDHA 8191
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2785-4398 |
4.87e-08 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 61.32 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2785 INKSVTTDGMTQSSIQAYENAKRAGQTESTNAQNVINNGDATDQQIAAEKTKVEEKYNSLKQAIDGLTPDLAPLQTAKTQ 2864
Cdd:COG3210 78 TGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2865 LQNDIDQPTNTTGMTSASVATFNEKLSAARTKIQEIDRVLASHPDVATIRQNVTAANAakSALDQARNGLTVDKAPLENA 2944
Cdd:COG3210 158 AGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGG--TAGGVASANSTLTGGVVAAG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2945 KNQLQHSIDTQTSTTGMTQDSINAYNAKLTAARNKVQQINQVLAGSPTVDQINTNTSAANQAKSDLDHARQALTPDKAPL 3024
Cdd:COG3210 236 TGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3025 QNAKTQLEQSINQPTDTTGMTTASLNAYNQKLQAARQKLTEINQVLNGNPTVQKINDKVTEANQAKDQLNTARQGLTLDR 3104
Cdd:COG3210 316 TAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNAS 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3105 QPALSTLHGASNLNQAQQNNFTQQINAAQNHAALETIKSNITALNNAMTKLKESVADNNSIKSGQNYTDATQANKQAYDN 3184
Cdd:COG3210 396 STTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3185 AVNAAKGVIGETNNPTMDVNTVNQKASSVKSTQDALDGQQNLQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQAV 3264
Cdd:COG3210 476 AGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGT 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3265 NDIKQTTQSLNTAMTGLKRGVANHNQVVQSDNYVNADTNKKNDYNNAYNHANDIINGNAQHPVITPSDVNNALSNVTNKE 3344
Cdd:COG3210 556 TAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLT 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3345 HALNGEAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNATNLNSAMGNLRQAVADKDQVKRTEDY 3424
Cdd:COG3210 636 GSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITV 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3425 ADADTAKQNAYNSAVSSAETIINQTTNPTMSVNDVNSATSAVTTNKNALNGDEKLAQSKTDAASAIDALPHLNNAqKADV 3504
Cdd:COG3210 716 TGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNA-GAEI 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3505 KSKINVASNI--AGVNTVKQQGTDLN-TAMGNLQGAINDEQTTLNSQNYQDATPSKKTAYTNAVQAAKDILNKSNGQNKT 3581
Cdd:COG3210 795 SIDITADGTItaAGTTAINVTGSGGTiTINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATA 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3582 KDQVTEVMNQVDSAKTNLDGTRLLDQAKQTAKQQLNNMTHLTPAQKTNLTNQINSGTTVAGVHTVQSNANTLDQAMNTLR 3661
Cdd:COG3210 875 ASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGL 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3662 QSIANKDATKASEDYVDANNDKQTAYNNAVAAAETIINANSNPEMNPSTITQKADQVNSSKTALNGDENLAAAKQNAKTY 3741
Cdd:COG3210 955 SAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGT 1034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3742 LNSLTSITDAQKNNLISQITSATRVSG--VDTVKQNAQHLDQAMANLQSGINNESQVKSSEKYRDADTNKQQEYDNAITA 3819
Cdd:COG3210 1035 GTAATAGGQNGVGVNASGISGGNAAALtaSGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTG 1114
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3820 AKAILNKQHGPNTAQNAVEAALQRVNTAKNALNGDAKLIAAQNAAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVK 3899
Cdd:COG3210 1115 GVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTA 1194
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3900 QSANSLDGAMGNLQTAINDKSGTLASQNFLDADEQKRNAYNQAVSNAETILNKQTGPNTAKTAVEQALNNVNSAKHALNG 3979
Cdd:COG3210 1195 GTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVA 1274
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3980 TQNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQDVQRNATELNTAMGTLKHAIADKTTTLASSKYVNADS 4059
Cdd:COG3210 1275 GNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNG 1354
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4060 TKQNAYTTKVTNAEHIISGTPTVVTTPSEVTAAANQVNSAKQELNGDERLREAKQNANTAIDALTQLNTPQKAKLKEQVG 4139
Cdd:COG3210 1355 GNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGT 1434
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4140 QANRLEDVQTVQTNGQALNNAMKGLRDSIANETTVKAGQNYTDASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAA 4219
Cdd:COG3210 1435 GGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGG 1514
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4220 TQVNNAKNGLNGAENLRNAQNTAKQNLNTLSHLTNNQKSAISSQIDRAGHVSEVTAAKNAATELNTQMGNLEQAIHDQNT 4299
Cdd:COG3210 1515 TTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNT 1594
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4300 VKQSVKFTDADKAKRDAYTNAVSRAETILNKTQGANTPKQDVEASIQNVSSAKNALNGDQNVTNAKNAAKNALNNLTSIN 4379
Cdd:COG3210 1595 ATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTD 1674
|
1610
....*....|....*....
gi 616687517 4380 NAQKRDLTTKIDQATTVAG 4398
Cdd:COG3210 1675 ATLAGLGGATTAAAGNVAT 1693
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8379-8438 |
5.44e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 5.44e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8379 VQTTLQALNGDHNLQVAKTNATQAIDALTSLNDPQKTALKDQVTAATLVTAVHQIEQNAN 8438
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3340-3399 |
6.30e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.95 E-value: 6.30e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3340 VTNKEHALNGEAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNAT 3399
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8253-8312 |
7.22e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.95 E-value: 7.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8253 VNNTKVALDGDENLAAAKQQANNRLDQLDHLNNAQKQQLQSQITQSSDIAAVNGHKQTAE 8312
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9008-9067 |
1.16e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9008 VATAKDNLHGDQKLVRDQQQAVTTVNALPNLNHAQQQALTDAINAAPTRTEVAQHVQTAT 9067
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8745-9286 |
1.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8745 VKSVIDQATQAvndaknNLHgdQKLAQDKQRATETLNNLSNLNTPQRQAlenqinnAATRGEVAQKLTEAQALNQAMEAL 8824
Cdd:PRK02224 192 LKAQIEEKEEK------DLH--ERLNGLESELAELDEEIERYEEQREQA-------RETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8825 RNSIQDQQQTeagskfINEDKPQKDAYQAAVQHAKDLINQTS---NPTLDKAQVEQLTQ-AVNQAKDNLHG-DQKLADDK 8899
Cdd:PRK02224 257 EAEIEDLRET------IAETEREREELAEEVRDLRERLEELEeerDDLLAEAGLDDADAeAVEARREELEDrDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8900 QHAVTDLNQLNGlnnpqrQAlESQINNAATRDEVAQKLAE-AKALNQAMEALRNSIQDQQQTesgskfINEDKPQKDAYQ 8978
Cdd:PRK02224 331 EECRVAAQAHNE------EA-ESLREDADDLEERAEELREeAAELESELEEAREAVEDRREE------IEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8979 AAVqhakdlinqtGNPTLDKSQVEQLTQAVATAKDNLHGDQKLVRdqqqaVTTVNALPNLNHAQQ-----------QALT 9047
Cdd:PRK02224 398 ERF----------GDAPVDLGNAEDFLEELREERDELREREAELE-----ATLRTARERVEEAEAlleagkcpecgQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9048 DAINAAPT---RTEVAQHVQTATELDHAMETLKNKVDQVNTDKAQPNYTEASTDKKDAVDQALQAAQSITDPTNGSNANK 9124
Cdd:PRK02224 463 GSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9125 YAVEQAL-TKLQGKEnelngnERVAEAKTQAKQTIDQLTHLNADQiATAKQNIDQ----ATKLQPIAELVDQATQLNQSM 9199
Cdd:PRK02224 543 RERAAELeAEAEEKR------EAAAEAEEEAEEAREEVAELNSKL-AELKERIESleriRTLLAAIADAEDEIERLREKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9200 DQLQQaVNehanvEQTVDYtqadLDKQNAYKQAIAEA---ENVLKQNANKQQVDQALQNILNAKQALNgDERVALAKTNG 9276
Cdd:PRK02224 616 EALAE-LN-----DERRER----LAEKRERKRELEAEfdeARIEEAREDKERAEEYLEQVEEKLDELR-EERDDLQAEIG 684
|
570
....*....|..
gi 616687517 9277 --KHDIDQLNAL 9286
Cdd:PRK02224 685 avENELEELEEL 696
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8389-8443 |
2.07e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8389 DHNLQVAKTNATQAIDALTSLNDPQKTALKDQVTAATLVTAVHQIEQNANTLNQA 8443
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7507-7561 |
2.20e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7507 NQKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAPDIATVNNVKQNAQNLNNA 7561
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7759-7813 |
2.31e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7759 NHNLQVAKDNANTAIDQLPNLNQPQKTALKDQVTHAELVTGVNAIKQNADALNNA 7813
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7255-7309 |
3.59e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 50.62 E-value: 3.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7255 NANVQHAKDEATALINNSNDLNQAQKDALKQQVQNATTVAGVNNVKQTAQELNNA 7309
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9645-10224 |
3.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9645 QRLQ-EAKDKAIQnvnkVLADKLKEIEASNATDQDKLIAKNKAEELANSIINNINKATSNQDVSrvQTAGNQAIEQVHAN 9723
Cdd:COG1196 216 RELKeELKELEAE----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9724 EIpkakiDANKDVDKQVQALIDEIDRNPNLTDkEKQALKDRINQILQQghnginNAMTKEEIEHAKAQLAQALQDIKDLV 9803
Cdd:COG1196 290 EY-----ELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEE------LEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9804 KAKENAKQDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAK 9883
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9884 EDAKNAIKALANEKRDQinsnpdltpEQKAKALKEIDEAEKRALENIENAQTKDQLNKGLNLGLDDIRNTHVWEVDAQPA 9963
Cdd:COG1196 438 EEEEEALEEAAEEEAEL---------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9964 VNEIFDATPEQILVNGELIVHRDDIiTEQDIHAHINLIDQLTAEIIDTPSTAT--ISDSLTAKVE-VTLLDGSKVIVSVP 10040
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVE-AAYEAALEAALAAALQNIVVEDDEVAAaaIEYLKAAKAGrATFLPLDKIRARAA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10041 VKVVEKELTVvkQQAIESIE------NAAQQKINEINNHATLTPEQKEAAIAEVNKLKQQAIEqinnaadVHTVEEVQHQ 10114
Cdd:COG1196 588 LAAALARGAI--GAAVDLVAsdlreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-------VTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10115 EQAHIEQFNPDQFTIDQAKSNAIKSISDAIQHMIDEINASKDLTDKEKQEAISKLNQLKDQSIQAIQRAQSIDEIAQQLE 10194
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 616687517 10195 QFKAQLKAANPFA-----------KELENRKKSAISKIKDI 10224
Cdd:COG1196 739 EELLEEEELLEEEaleelpeppdlEELERELERLEREIEAL 779
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7371-7430 |
4.38e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 50.63 E-value: 4.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7371 VTQAKNDLNGNTNLATAKQNVQHAIDQLPNLNQAQRDEYSKQITQATLVPNVNAIQQAAT 7430
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8522-9203 |
5.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8522 DHAKQAVSQLAHLNNAQKHMEDtlidsetTRTAVNHdLTEAQALDQLMDALQQSIADKDATRASSAYVNAEpNKKQAYDE 8601
Cdd:COG4913 225 EAADALVEHFDDLERAHEALED-------AREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWFAQ-RRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8602 AVQNAESIIAGLnnptinKGNVTSATQAVTSSKNALDGVERlaqdkQTAGNSLNHLDQltpaqqqaLENQINNAttRDKV 8681
Cdd:COG4913 296 ELEELRAELARL------EAELERLEARLDALREELDELEA-----QIRGNGGDRLEQ--------LEREIERL--EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8682 AEIIAQAQALNEAMKALKESIkdqPQTEasskfinedqaqkDAYTQAVQHAKDLINKttdptlVKSVIDQATQAVNDAKN 8761
Cdd:COG4913 355 EERERRRARLEALLAALGLPL---PASA-------------EEFAALRAEAAALLEA------LEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8762 NLhgdQKLAQDKQRATETLNNLSN--LNTPQ-----RQALENQINNAATR----GEVAQKLTEAQALNQAME-ALRNS-- 8827
Cdd:COG4913 413 AL---RDLRRELRELEAEIASLERrkSNIPArllalRDALAEALGLDEAElpfvGELIEVRPEEERWRGAIErVLGGFal 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8828 --IQDQQQTEAGSKFINE-DKPQKDAYQAAVQHAKDLINQTSNP-TLdkaqVEQLTQAVNQAKDNLhgDQKLADDKQHA- 8902
Cdd:COG4913 490 tlLVPPEHYAAALRWVNRlHLRGRLVYERVRTGLPDPERPRLDPdSL----AGKLDFKPHPFRAWL--EAELGRRFDYVc 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8903 VTDLNQLN---------------------------------GLNN-PQRQALESQInnaatrDEVAQKLAEAKALNQAME 8948
Cdd:COG4913 564 VDSPEELRrhpraitragqvkgngtrhekddrrrirsryvlGFDNrAKLAALEAEL------AELEEELAEAEERLEALE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8949 ALRNSIQDQQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQ--TGNPTLD--KSQVEQLTQAVATAKDNLHGDQKLVRD 9024
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldASSDDLAalEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9025 QQQAVTTVNalpnlnhAQQQALTDAINAAPTRTEVAQHVQTATELDHAM-ETLKNKVDQVNTDKAQPNYTEASTDKKDAV 9103
Cdd:COG4913 718 LEKELEQAE-------EELDELQDRLEAAEDLARLELRALLEERFAAALgDAVERELRENLEERIDALRARLNRAEEELE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9104 DQALQAAQSITDPTNGSNANKYAVEQALTKLQG-KENELngNERVAEAKTQ-AKQTIDQLTHLNA---DQIATAKQNIDq 9178
Cdd:COG4913 791 RAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGL--PEYEERFKELlNENSIEFVADLLSklrRAIREIKERID- 867
|
730 740
....*....|....*....|....*
gi 616687517 9179 atklqpiaelvdqatQLNQSMDQLQ 9203
Cdd:COG4913 868 ---------------PLNDSLKRIP 877
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3728-3782 |
6.59e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.85 E-value: 6.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3728 DENLAAAKQNAKTYLNSLTSITDAQKNNLISQITSATRVSGVDTVKQNAQHLDQA 3782
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7185-7253 |
8.24e-07 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 50.01 E-value: 8.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7185 GNLKQAIADKDATKATVNFTDADQAKQQAYNTAVTNDENIISKANGGNATQTEVEQAIQQVNTAKQALN 7253
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3350-3404 |
9.01e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.46 E-value: 9.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3350 EAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNATNLNSA 3404
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7437-7505 |
1.80e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 49.24 E-value: 1.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7437 TQLKQGIANKAQIKGSENYHDADTDKQTAYDNAVTKAEELLKQTTNPTMDPNTIQQALTKVNDTNQALN 7505
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9383-9441 |
2.02e-06 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 48.71 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 9383 VTAAKQALNGEERLNNRKSEALQRLDQLTHLNNAQRQLAIQQINNAETLNKASRAINRA 9441
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8011-8065 |
2.36e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8011 EAKLATEKQNAKDAVNAMTHLNDAQKQALNGQIDQSPEIATVTQVKQTATSLDQA 8065
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5366-5420 |
2.52e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5366 DAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQQLDGA 5420
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7633-7687 |
3.77e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.92 E-value: 3.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7633 NDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDAAQTVANVNTNKQTAQDLNQA 7687
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2557-3293 |
3.96e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2557 KTEAQQVINNERATPQQVSDALTKVRAAQTKID-QAKALLQNKEDNSQLvtSKNNLQSSVNQVPSTtgmtQQSIDNYNAK 2635
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLErQAEKAERYKELKAEL--RELELALLVLRLEEL----REELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2636 KRDAESEITAAQRVIDNGDATAQQISDEKRRVDNALTALNQAKHDLTADTHALEQ-----------AVQQLNRTGITTGK 2704
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqkqilrerlanLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2705 KPASITAYNNSIRALQSDLTSAKN----------SANAIIQKPIRSVQEVQTALTNVNRVNERLTQAINQLvpladNSAL 2774
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEelesleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-----NNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2775 RTAKTKLdEEINKSV--TTDGMTQSSIQAYENAKRAGQTESTNAQNVINNGDATDQQIAAEKTKVEEKYNSLKQAIDGLT 2852
Cdd:TIGR02168 403 ERLEARL-ERLEDRRerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2853 PDLAPLQTAKTQLQNDID-----------------QPTNTTGMTSASVaTFNEKLSAArtkiqeIDRVLASHPDVATIRq 2915
Cdd:TIGR02168 482 RELAQLQARLDSLERLQEnlegfsegvkallknqsGLSGILGVLSELI-SVDEGYEAA------IEAALGGRLQAVVVE- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2916 NVTAANAAKSALDQARNG------LTVDKAPLENAKNQLqhSIDTQTSTTGMTQDSINaYNAKLTAArnkvqqINQVLAG 2989
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDRE--ILKNIEGFLGVAKDLVK-FDPKLRKA------LSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2990 SPTVDQIntnTSAANQAKS------------DLDHARQALTPDKAPLQNAKTQLEQSINQPTDTTGMTTASLNAYNQKLQ 3057
Cdd:TIGR02168 625 VLVVDDL---DNALELAKKlrpgyrivtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3058 AARQKLTEINQVLngnptvqkiNDKVTEANQAKDQLNTARQGLTLDRQPAlSTLHGASNLNQAQQNNFTQQINA-----A 3132
Cdd:TIGR02168 702 ELRKELEELEEEL---------EQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLSKELTELEAEIEEleerlE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3133 QNHAALETIKSNITALNNAMTKLKESVADNNSIKSGQNytDATQANKQAYDNAVNAAKGVIGETNNPTMDVNTVNQKASS 3212
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3213 VKSTQDALDGQQN-LQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQA-VNDIKQTTQSLNTAMTGLKRGVANHNQ 3290
Cdd:TIGR02168 850 LSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELSEeLRELESKRSELRRELEELREKLAQLEL 929
|
...
gi 616687517 3291 VVQ 3293
Cdd:TIGR02168 930 RLE 932
|
|
| YSIRK_signal |
pfam04650 |
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ... |
5-30 |
4.07e-06 |
|
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 428049 [Multi-domain] Cd Length: 26 Bit Score: 46.99 E-value: 4.07e-06
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7885-7939 |
4.73e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.53 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7885 DEKLAQAKQDALANLDTLRDLNQPQRDALRNQINQAQALATVEQTKQNAQNVNTA 7939
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| YSIRK_signal |
TIGR01168 |
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ... |
2-42 |
5.91e-06 |
|
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 273479 [Multi-domain] Cd Length: 39 Bit Score: 46.71 E-value: 5.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 616687517 2 NYRDKIQKFSIRKYTVGTFSTVIATLVFLGlntsQAQAAET 42
Cdd:TIGR01168 3 KFNEKQQKYSIRKLSVGVASVLVASLFFGG----GVAAAES 39
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7941-8009 |
6.08e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.70 E-value: 6.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7941 SNLKQGIANKDTVKASENYHDADADKQTAYTNAVSQAEGIINQTTNPTLNPDDITRVLTQVTDAKNGLN 8009
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8263-8317 |
8.19e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.76 E-value: 8.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8263 DENLAAAKQQANNRLDQLDHLNNAQKQQLQSQITQSSDIAAVNGHKQTAESLNTA 8317
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7563-7631 |
8.91e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 8.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7563 TNLSNALQDKTETLNSINFTDADKAKKDAYTNAVAQAEGILSKANGSNASQTEVEQAMQRVNAAKQALN 7631
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8067-8135 |
9.08e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 9.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8067 NQLSQAINDKTQTLADGNYLNADPDKQNAYKQAVAKAEALLNKQSGTNEVQAQVESITNEVNAAKQALN 8135
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8696-8764 |
1.05e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.93 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8696 KALKESIKDQPQTEASSKFINEDQAQKDAYTQAVQHAKDLINKTTDPTLVKSVIDQATQAVNDAKNNLH 8764
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7381-7435 |
1.07e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.38 E-value: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7381 NTNLATAKQNVQHAIDQLPNLNQAQRDEYSKQITQATLVPNVNAIQQAATTLNDA 7435
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5298-5364 |
1.17e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.93 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 5298 LQNGINDETQTKQTQKYLDAEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQALQNVNSTKTALN 5364
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7311-7379 |
1.68e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.54 E-value: 1.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7311 TQLKQGIADKEQTKADGNFVNADPDKQNAYKQAVAKAEALISGTPDVVVTPSEITAALNKVTQAKNDLN 7379
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
9090-9371 |
2.77e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9090 PNYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKEnelngneRVAEAKTQAKQTIDQLThlnaDQI 9169
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKID-------RQKEETEQLKQQLAQAP----AKL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9170 ATAKQNIDqatKLQPIAELVDQATQLNQSMDQLQQAVNEHANVEQTVdytQADLDKQNAykQAIA------EAENVLKQN 9243
Cdd:PRK11281 97 RQAQAELE---ALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNA---QNDLAEYNS--QLVSlqtqpeRAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9244 -ANKQQVDQALQNILNAKQALNGDERVAL----AKTNGKHD--------IDQLNALNNAQQDGFKGRIDQSNDLNQIQQI 9310
Cdd:PRK11281 169 sQRLQQIRNLLKGGKVGGKALRPSQRVLLqaeqALLNAQNDlqrkslegNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 9311 VDEAKALNRAMNQLSQEITGNEGRTKGSTNYVNADTQVKRVYDEAVDKAKEALNKATGQNL 9371
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNL 309
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8319-8387 |
3.45e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.77 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8319 GNLINAIADHQAVEQRGNFINADTDKQTAYTTAVNEAEAMINKQTGQNANQTEVEQAITKVQTTLQALN 8387
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5422-5490 |
1.11e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.23 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5422 GQLETSIRDKDTTLQSQNYQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVERAMQTVTQANTALN 5490
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8195-8261 |
1.43e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.85 E-value: 1.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 8195 LRNSIADNQATLASEDYHDAAAQRQNDYNQAVTAANNIINQTTSPTMNPDDVNRATTQVNNTKVALD 8261
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7815-7883 |
4.04e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 42.69 E-value: 4.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7815 GTLKQQIQANSQVPQSVDFTQADQDKQQAYNNAANQAQQIANGTPTPVLTPDAVTQAVTTMNQAKDALN 7883
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
5720-6009 |
1.75e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5720 PTMNAQEINQAKDqVTAKQQALNGQENLRTAQTNAKQHLN---GLSDLTDAQK---DAVKRQIEGAThvNEVTQAQNNad 5793
Cdd:PRK11281 28 RAASNGDLPTEAD-VQAQLDALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKeetEQLKQQLAQAP--AKLRQAQAE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5794 alntaMTNLKNgiqdqntikqgvnftDADEAKRNAYTNA-VTQAEQILNKAQgpntakdgveTALQNVQRAKNDLNGnqN 5872
Cdd:PRK11281 103 -----LEALKD---------------DNDEETRETLSTLsLRQLESRLAQTL----------DQLQNAQNDLAEYNS--Q 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5873 VANAKTTAKNALNNLTSiNNAQKEALKSQIDSATTvagvNQVSTTASELNTamsnLQngindeaatkAAQKYTDAdsdkQ 5952
Cdd:PRK11281 151 LVSLQTQPERAQAALYA-NSQRLQQIRNLLKGGKV----GGKALRPSQRVL----LQ----------AEQALLNA----Q 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5953 TAYNDAVTAAKTLLdKTAGTN--DNKAAVEQALQR-VNTAKTALNgDARLNEAKNTAKQQ 6009
Cdd:PRK11281 208 NDLQRKSLEGNTQL-QDLLQKqrDYLTARIQRLEHqLQLLQEAIN-SKRLTLSEKTVQEA 265
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7689-7757 |
3.68e-03 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 40.00 E-value: 3.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7689 TQLKQGVADKDQTKANGNFVNADTEKQNAYNNAVAHAEQIISGTPNANVDPQQVAQALQQVTDAKNGLN 7757
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2503-2752 |
4.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2503 EEVQESIFTKADKRE-LITDKNHLDdpvstdgkkpGTITQYNNAIHNAQQQINAAKTE-AQQVINNERATPQQVSDALTK 2580
Cdd:TIGR02169 740 EELEEDLSSLEQEIEnVKSELKELE----------ARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2581 VRAAQTKIDQA-KALLQNKEdnsQLVTSKNNLQSSVNQVPSTTGMTQQSIDNYNAKKRDAESEITAAQRVIDNGDATAQQ 2659
Cdd:TIGR02169 810 IEARLREIEQKlNRLTLEKE---YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2660 ISDEKRRVDNALTALNQAKHDLTADthaLEQAVQQLNRTGITTGKKPASITAYNNSIRALQSDltSAKNSANAIIQKPIR 2739
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI--PEEELSLEDVQAELQ 961
|
250
....*....|...
gi 616687517 2740 SVQEVQTALTNVN 2752
Cdd:TIGR02169 962 RVEEEIRALEPVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5723-6001 |
4.71e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5723 NAQEINQAKDQVTAKQQALNGqenLRTAQTNAKQHLNGL-SDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMTN 5801
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5802 LKNGIQDQNTiKQGVNFTDADEAKRNAYTNAvTQAEQILNKAQGPNTAKDGVETALQN----VQRAKNDLNGNQNVANAK 5877
Cdd:TIGR02168 759 LEAEIEELEE-RLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLlneeAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5878 TTAKNALNNLTSINNAQKEALKSQIDSATTvagvnQVSTTASELNtAMSNLQNGIndEAATKAAQKYTDADSDKQTAYND 5957
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELE-ALLNERASL--EEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 616687517 5958 AVTAAKTLLDKTAGT-NDNKAAVEQALQRVNTAKTALNGDARLNE 6001
Cdd:TIGR02168 909 KRSELRRELEELREKlAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3715-3953 |
7.84e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3715 ADQVNSSKTALNGDENL----AAAKQNAKTYLNSLTSITDAQKNNlisqitsatrvsgvDTVKQNAQHLDQAMANLQSGI 3790
Cdd:PRK11281 38 EADVQAQLDALNKQKLLeaedKLVQQDLEQTLALLDKIDRQKEET--------------EQLKQQLAQAPAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3791 NNESQVKSSEKYRDADT--------------NKQQEYDNAITAAKAIL-NKQHGPNTAQNAVEAALQRV----------- 3844
Cdd:PRK11281 104 EALKDDNDEETRETLSTlslrqlesrlaqtlDQLQNAQNDLAEYNSQLvSLQTQPERAQAALYANSQRLqqirnllkggk 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3845 -------NTAKNALNGDAKLIAAQNAAKQHL----GTLTHITTAQHNDLTNQISQatnlagvesvkqsansLDGAMGNLQ 3913
Cdd:PRK11281 184 vggkalrPSQRVLLQAEQALLNAQNDLQRKSlegnTQLQDLLQKQRDYLTARIQR----------------LEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 616687517 3914 TAINDKSGTLASQNFLDADEQKRNayNQAVSN----AETILNKQ 3953
Cdd:PRK11281 248 EAINSKRLTLSEKTVQEAQSQDEA--ARIQANplvaQELEINLQ 289
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
1540-1700 |
8.79e-03 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.88 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1540 SATAPNVTSATNKTINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRiANISNNATVSQADQTAIINSLTFT 1619
Cdd:NF038112 1242 SFTAPEVTADTVLTFQLVVSDGTKTSAPDTVTVLVRNVNRAPVAVAGAPATVDER-STVTLDGSGTDADGDALTYAWTQT 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1620 SNAP----NRNYATAS--ASEITSktvsnvsrtgnNAQVTVTVTYQDGTTS---TVTVPVKHV--IPEIVAHSHYTVQGQ 1688
Cdd:NF038112 1321 SGPAvtltGATTATATftAPEVTA-----------DTQLTFTLTVSDGTASatdTVTVTVRNVnrAPVANAGADQTVDER 1389
|
170
....*....|..
gi 616687517 1689 DFPTGNGaSASD 1700
Cdd:NF038112 1390 STVTLSG-SATD 1400
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| hyperosmo_Ebh |
TIGR04264 |
hyperosmolarity resistance protein Ebh, N-terminal domain; Staphylococcal protein Ebh ... |
176-2527 |
0e+00 |
|
hyperosmolarity resistance protein Ebh, N-terminal domain; Staphylococcal protein Ebh (extracellular matrix-binding protein homolog) is a giant protein, sometimes over 10,000 amino acids long as reported. This model describes a non-repetitive amino-terminal domain of about 2400 amino acids.
Pssm-ID: 275090 [Multi-domain] Cd Length: 2354 Bit Score: 3612.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 176 DRNELQAFFDANYHDYRFIDRENADSGTFNYVKGIFDKINTLLGSNDPINNKDLQLAYKELEQAVALIRTMPQRQQTSRR 255
Cdd:TIGR04264 1 DKDKLQAFFDASYHDYRFIDRDKADNKEYNQVKATFDKVNTFLGNNDNPNSKSLQLLYKELEQAVALIRTLPQRQVRTRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 256 SSRIQtRSIESRAAEPRSVSDYQNANSSYYVENANDGSGYPVGTYINASSKGAPYNLPTTPWNTLKASDAKEFALITAKQ 335
Cdd:TIGR04264 81 NNREA-RSVRSRRAESRSVGSYNNAKTEYYVENENDGSGYPSGTYIHASNKGAPYYLPTTPWNTLSASDVKGIAYITAKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 336 TGDGYQWVIKFNKGHAPHENMIFWFALPDGQTPVGRTEFVTVNADGTNVQWSNGAGAGANKPLPQMWEY-GVNDPHRSHD 414
Cdd:TIGR04264 160 VKDGYEWTINFNKGHIPHENMIFWFGLPKDQTPVGPVRFSITDPNGTNTSSSSGVGDGEGQPLPRMWDSaGGIDPSRAYN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 415 FKIRNRSGQVIYEWPTVNIKSLSDLARASDYLNEAGATPATKAFGRQIFDYINGQKPAESSGVPKVYTFIGQGDASYTIS 494
Cdd:TIGR04264 240 FRQGPRTGYEFYDWPTVHINNFGDFARAPEYFNREGAPNKARVYGDQNFRYLNGEVPDQIQGLDTIYAFIGKGNASYTIQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 495 FKTQGPTIDKLYYAAGARALEYNQLFMYSQLYVESTQDQQQRLNGLRQVVNRTYRIGTTKRV-EVSQGNVQTKKVLESTN 573
Cdd:TIGR04264 320 FKTQGPTTDRLYYAAGGRALEYNQLFNYNQLYVEPLEEYQDRIQSIVDVINRTYHLGNTKNVyDVPERRYVTKHILDSDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 574 LNIDDFVDDPLSYVKTPSNKVLGFYPTNANTNAFRQGGVNPLNDYQLSQLFSDQNFQEAARTKNPIRLMIGFDYPDAFGN 653
Cdd:TIGR04264 400 FNTHDYADDPLSYVRNPSNHVIGFFPYNAPTDRYRHGGVNPLNSYEIHQLFSEEKLKEAARTGNPIKLMIGFNVPDRYGN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 654 GETLVPVNLTVLPEIQHNIKFFKNDDGQNIAEKPASKQAGHPVFYVYAGNQGNASVNLGGSVTSIQPLRINLTSNENFTD 733
Cdd:TIGR04264 480 GETLKPVNLYVKPELQQNIGFFSNNETQNREESPESKAAGHPVFLVQAGNMGNTSTNGGNKDTYVQPIRIQLTSNEPFSD 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 734 KDWQITGIPRTLHIENSTNRPNNARERNIELVGNLLPGDYFGTIRFGRKEQLFEIRVKPHTPRITTTAEELRGTALQKVP 813
Cdd:TIGR04264 560 NDWEISGIPPTLRIENAVGRTNNAREKNLELVGNLPPGDYFGTVRLGNREQIFEIRAKPNPPTISTTAAQLRGKGGQKPT 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 814 VTVTDIPLDPSALVYLVIPTSQTKDGGSEADQIPSGYTKIATGTPDGVHSTITIRPEDYVVFIPPVGhQIRALIFYNNVV 893
Cdd:TIGR04264 640 ITVTNVPQDTNAKVYLVAGGNGATDGTNDPGTIPSGYTILASATATGTGNTVTFNPSDYIQPLPNNG-VIRAITYYNKSV 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 894 ASNMSNAVTILPDDIPPTINNPVGLNAKYYRGDEVSFTMGVSDRH--SGLKSTTITTLPSGWTSNLTK-SDKKNGSLAIS 970
Cdd:TIGR04264 719 QSNFSNAVTILPDDTPPTISNPVGLQNKYYRGDQVNFTIPVSDNAygTGIKQVSVTGLPQGWTSNFVKnANGEAGTLTIT 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 971 GRVSMNQAYNSDITFKVSATDNVNNTTndsQSKHVTVHVGKISDDAHPIVLGNSEKVVVVNPTALTGDEKQRITTAFMNK 1050
Cdd:TIGR04264 799 GTISNSQTFNSDILVQVSATDNANNTT---QTKTIAIHIGKLSDDKPPIVLSNQEKIVVVNPTSISQDERNDIINALKAK 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1051 NQNIRGYLASSNPVTVDNHGNVTLQYRDGSSTTLDATNVMTYEPVVKPEYQTANAPKTATVTIAKGQSFNIGDIKQYFTL 1130
Cdd:TIGR04264 876 NTNISSYLATSNPYMVDNNGNVVLTYKDGSTRRIDPTNVITYEPIRKSIYAEGNNTKEATITIAKGQEFEIGDLKQYFSL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1131 SNGQAIPSSTFTNITSDRTIPTAQEVSQMNAGTQLYHITATNAYHKDTEDFYITLKIIDVKQPEGDQRVYRMSTYDITTD 1210
Cdd:TIGR04264 956 SNGQDIPNNSFTTITANDTIPTPQQISRLNAGTYTYHINASNAYNQDTERLTIKLKVVDVNQPSGDQRVYRTSTFNLTDD 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1211 EISKVKQAFINANRDAISFAEGDISVTNTPNGSNVSTITVNINKGRLTKSFTSNLANMNFLRWVNFPQDYTVTWTNAKIA 1290
Cdd:TIGR04264 1036 EINQVKQAFINANRGQLNLTDSDITVNNTPNSNHVSTVTVTITKGKLTKSFTSNFDHMNFLRWVNFPNDYTVTWTSQKIP 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1291 NRPTDGGLSWSDDHKSLIYRYDATLGTQITTNDILTLLKATTTVPGLRNNIAGNEKAQAEAGGRPNYKTTGYSQSNPTSD 1370
Cdd:TIGR04264 1116 GRGTDGGFEWSPDHKSLIYRYDATTGRQITLNDVLSLLTATTSIPGLRNNISGQEKALAEAGGTPGYKPVGYSKTNSISD 1195
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1371 GQRQFTLNGQVIQIMDIINPSNGFGGQPVTNSNVRANHSNSTVVSVNESAANGAGAFTIDHVVKNNSTHNAADAVYKAQL 1450
Cdd:TIGR04264 1196 GLRQYTYNGQVIQVLDLVQSSTGYGGQPVTYSNYRSNSSNSTVVNGNIPAANGAPAFTLDHVIKQNSGNGVMGAVYKAQL 1275
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1451 YLSPYGPKQYVEHLNQNTGNTTDAINIYFVPSDLVNPTVSVGNYTNHQVFSGETFTNTITANDNFGVQSVTVPNTSQLTG 1530
Cdd:TIGR04264 1276 YLTPYGAKQYIERLNQSTDNTTDVINVYFVPSDKVKPTISLGNYNNHVVFSGETFRNTITATDNYGLKSVTVPQTSQIAG 1355
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1531 TVDNNHQHVSATAPNVTSATNKTINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRIANISNNATVSQADQT 1610
Cdd:TIGR04264 1356 TVNNNNQIISGVAPNVTTPTTKTVKVIATDTSNNETTQSFNVTIKPLKDKYRVTTSSTEQNPIRIANIRNNATLSQADKQ 1435
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1611 AIINSLTFTSNAPNRNYATASASEITSKTVSNVSRTGNNAQVTVTVTYQDGTTSTVTVPVKHVIPEIVAHSHYTVQGQDF 1690
Cdd:TIGR04264 1436 AIINSLTITNNIPNRNYVTAGANEIRSKEVSNVSRTGNNANVTVTITYADGTTSQITVPVKHVIPEIVAIPRYTVQGQNF 1515
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1691 PTGNGASASDYFKLSNGSAIPDATITWVSGQAPNKNNTTIGQDINVTAHILIDGETTPITKTATYKVVSSVPKHVFETNR 1770
Cdd:TIGR04264 1516 PAGKGANPNDFFKLNNGSPVPDATITWVNGNGPNINSTRIGVDITVRANILFDGETTPIEKEASYMVVKSVPKRVFETTR 1595
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1771 GAVFPGISDVYDAKQYVKPVNDSWTQNAQRMNFQF-TNSYGPSKDVVGISTRDIRVTYDNHQTQIIKILAKVKPDPPRID 1849
Cdd:TIGR04264 1596 NGNFPGINNSYNPGSYVQPINNSWPQGAQAMNFDFgPNSGGPNSNVVGIFTRTIRVTYPNGQVENVKVLAKVKPDPPRID 1675
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1850 GNSVTYKAGLTNQQIKINNVLSSSSIKLFKADNTPLTITNTTYGSGNTAVVTVSDALPNGVIKARSSITMNNVTYTTQDE 1929
Cdd:TIGR04264 1676 SNSVTYKAGLTNQQIKVNNVLNNSPVKLYKSDGTELTNTTTTYGSNGSATVTVSGALPLGNIKAKSSITVNNVTYTTQNN 1755
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1930 HGRAIDVTRNESVDSNDSATVTVTPQLQATTEGAVFIKGGDGFDFGHVERFIQNPPHGATVAWHDSPDTWKNTVGNTHKT 2009
Cdd:TIGR04264 1756 SGQVVNVTRNESVESDDSAPVRVTPQLHATNGGAKFVKGGDNFDFNNAARYIDNLPDGATVEWEDNPDTWKNTVGNTTKT 1835
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2010 AVVTLPSGQGTRNVEVPVKVYPVANAKAPSRDVKGQNLTNGTDAINYITFDPNTNTNGITAAWANRQQPNNQQAGVQHLN 2089
Cdd:TIGR04264 1836 AVVTLPNGQGTRTVNIPVKVYPVATAKAPQRDVKGHQLTYGTDAMNYVTFEPNTNMNGITATWKNNNQPNNNQAGVQNLT 1915
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2090 VDVTYPGISAAKRVPVTVNVYQFEFPQTSYTTTVGGTLASGTQASGYAHIQNANGLPTDGFTYKWNRDTTGTNDANWAAM 2169
Cdd:TIGR04264 1916 ANVTYPGISTPYRVPVKVYVYKFDFAQSEYTTTVGTTFAGGTNVNNYVHLENANGLPTDGFHYVWNQATTGSNSEQWSAL 1995
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2170 NKPNAAKVINAKYDVIYNG-HTFATSLLAKFVVKDVQPAKPTVTETAAGAITIAPGANQTVNTHAGNVTTYADKLVIKRN 2248
Cdd:TIGR04264 1996 AKPNQAFVKNAKYDVLDNGnHVFATSQPAKFIVTNVQPNKATITESDVGDITITPGANKSVNTRTGNVTTYADRLVIKKN 2075
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2249 GNVVTTFTRHNNTSPWVKEASAATVAGIVGTNNGITVAAGTFNAADTIQVVATQGSGETISDEQLSDDFTVVAPQPNQAT 2328
Cdd:TIGR04264 2076 GQVITTFIRANNTSPWTKESSAINVPGVSGSPNGITINAGTFPPGDNIQVVATQGNGELISDEAISDTFTVVAPQPNQAT 2155
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2329 TKIWQNGHIDIMPNNPSGHLINPTQAMDIAYTEKVGNGAEHSKTLNAVRGQNNQWTIANKPDYVTLDAHTGKVTFNANTI 2408
Cdd:TIGR04264 2156 SKIWQNGTFEITPNNPNAHTTNPTDAVEITYTEKLGNSTEQSKTLTVTKGNNGQWSITNKPDYVTLDSATGKVTFNANTI 2235
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2409 KPNSAITITPKAGTGHSASSNPSTLTAPATHTVNTTEIVKDYGSNVTPAEINNAVQVANKRTATIKNGTAMPTNLAGGST 2488
Cdd:TIGR04264 2236 KPNSLITTISKAGSGNTESTNTNTITAPAAHTVTIHEIVKDYGSNVTNEEINNAVQVANKRHATIKQGTALPTNLAGGST 2315
|
2330 2340 2350
....*....|....*....|....*....|....*....
gi 616687517 2489 TTIPVTVTYNDSSTEEVQESIFTKADKRELITDKNHLDD 2527
Cdd:TIGR04264 2316 TTIPVTITYNDGSTEEVTETIRTKADKRELINARNHLDD 2354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9067-9904 |
3.86e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.34 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9067 TELDHAMETLKNKVDQVNTDKaqpnytEASTDKKDAVDQALQAAQSItdptngsnanKYAVEQALTKLQGKENELNG--- 9143
Cdd:TIGR02168 235 EELREELEELQEELKEAEEEL------EELTAELQELEEKLEELRLE----------VSELEEEIEELQKELYALANeis 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9144 --NERVAEAKTQAKQTIDQLTHLNADQIATAKQNIDQATKLqpiAELVDQATQLNQSMDQLQQAVNEHANVEQTVDYTQA 9221
Cdd:TIGR02168 299 rlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9222 DLDKQ-NAYKQAIAEAENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTNGKHDID----QLNALNNAQQDGFKG 9296
Cdd:TIGR02168 376 ELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9297 RIDQSNDLNQIQQIVDEAK----ALNRAMNQLSQEITGNE---GRTKGSTNYVNADTQVKRVYDEAVDKAKE-------- 9361
Cdd:TIGR02168 456 LERLEEALEELREELEEAEqaldAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSGLSGILGVLSElisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9362 --ALNKATGQNLTAEEVIKLNdavtAAKQALNGEERLNNRKSEALQrLDQLTHlnnaqRQLAIQQINNAETLNKASRAIN 9439
Cdd:TIGR02168 536 eaAIEAALGGRLQAVVVENLN----AAKKAIAFLKQNELGRVTFLP-LDSIKG-----TEIQGNDREILKNIEGFLGVAK 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9440 RAVQLDDAMGAVQQYIDEHhldVISSTNYINADDNLKA-NYDNAITNAAHELDKVQGSaIAKAEAEQlkqhiidAQKALN 9518
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGG---VLVVDDLDNALELAKKlRPGYRIVTLDGDLVRPGGV-ITGGSAKT-------NSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9519 GDQNLATAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIINDqidlnnaMETLKHLVDNEIPTAEQTVNyQNA 9598
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVE-QLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9599 DDVAKSNFDDAKrlANALINSDNTNVNDINGAIQAVKDVIQNLngEQRLQEAKDkAIQNVNKVLADKLKEIEASNATDQD 9678
Cdd:TIGR02168 747 ERIAQLSKELTE--LEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKE-ELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9679 KLIAKNKAEELANSI---INNINKATSNQDVSRVQTAGNQAIEQVHANEIpKAKIDANKDVDKQVQALIDEIDRNPNLTD 9755
Cdd:TIGR02168 822 LRERLESLERRIAATerrLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9756 KEKQALKDRINQILQQGHNginnamTKEEIEHAKAQLAQALQDIkdlvkakENAKQDVDKQVQALIDEIDRNPNLTDKEK 9835
Cdd:TIGR02168 901 EELRELESKRSELRRELEE------LREKLAQLELRLEGLEVRI-------DNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 9836 QALKDRINQILQQGHN-GINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKR-------DQINSN 9904
Cdd:TIGR02168 968 EEARRRLKRLENKIKElGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARerfkdtfDQVNEN 1044
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
3623-5283 |
2.01e-13 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 79.04 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3623 TPAQKTNLTNQINSGTTVAGVHTVQSNANTLDQAMNTLRQSIANKDATKASEDYVDANNDKQTAYNNAVAAAETIINANS 3702
Cdd:COG3210 53 SNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3703 NPEMNPSTITQKADQVNSSKTALNGDENLAAAKQNAKTYLNSLTSITDAQKNNLISQITSATRVSGVDTVKQNAQHLDQA 3782
Cdd:COG3210 133 TTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3783 MANLQSGINNESQVkssekyRDADTNKQQEYDNAITAAKAILNKQHGPNTAQNAVEAALQRVNTAKNALNGDAKLIAAQN 3862
Cdd:COG3210 213 GGGTAGGVASANST------LTGGVVAAGTGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3863 AAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVKQSANSLDGAMGNLQTAINDKSGTLASQNFLDADEQKRNAYNQA 3942
Cdd:COG3210 287 TAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3943 VSNAETILNkQTGPNTAKTAVEQALNNVNSAKHALNGTQNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQ 4022
Cdd:COG3210 367 GNGGGLTTA-GAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGT 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4023 DVQRNATELNTAMGTLKHAIADKTTTLASSKYVNADSTKQNAYTTKVTNAEHIISGTPTVVTTPSEVTAAANQVNSAKQE 4102
Cdd:COG3210 446 IGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGG 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4103 LNGDERLREAKQNANTAIDALTQLNTPQKAKLKEQVGQANRLEDVQTVQTNGQALNNAMKGLRDSIANETTVKAGQNYTD 4182
Cdd:COG3210 526 NATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGT 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4183 ASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAATQVNNAKNGLNGAENLRNAQNTAKQNLNTLSHLTNNQKSAISS 4262
Cdd:COG3210 606 GSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGG 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4263 QIDRAGHVSEVTAAKNAATELNTQMGNLeQAIHDQNTVKQSVKFTDADKAKRDAYTNAVSRAETILNKTQGANTPKQDVE 4342
Cdd:COG3210 686 TTGTTLNAATGGTLNNAGNTLTISTGSI-TVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTAN 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4343 ASIQNVSSAKNALNGDQNVTNAKNAAKNALNNLTSINNAqkrdlttkidqaTTVAGVEAVSNTGTQLNTAMAKLQNGIND 4422
Cdd:COG3210 765 TTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGT------------ITAAGTTAINVTGSGGTITINTATTGLTG 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4423 KANTLASENYHDADSDKKTAYTQAVTNAENILNKNSGSNLDKAAVENALSQVTNAKGALNGNHNLEQAKSNANTTINGLQ 4502
Cdd:COG3210 833 TGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAV 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4503 HLTTAQKDKLKQQVQQAQNVAGVDTVKSSANTLNGAMGTLRNSIQDNAATKNGQNYLDATESNKTNYNNAVDSANSVINA 4582
Cdd:COG3210 913 LATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIA 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4583 TSNPNMDANAINQIATQVTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQRVANVTSIQQTANELN 4662
Cdd:COG3210 993 ATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGG 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4663 TAMGQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQVTSTKDALNGDAKLAEA 4742
Cdd:COG3210 1073 TAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVS 1152
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4743 KAAAKQNLSTLNHITNAQRTALEGQINQATTVDGVNTVKTNANTLDGAMNSLQGSINDKDATLRNQNYLDADESKRNAYT 4822
Cdd:COG3210 1153 AVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTA 1232
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4823 QAVTAAEGILNKQTGGNTSKADVDNALNAVTRAKTALNGAENLRNAKTTATNTINGLPHLTQLQKDNLKHQVEQAQNVAG 4902
Cdd:COG3210 1233 TGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGA 1312
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4903 VNGVKDKGNTLNTAMGALRTSIQNDNTTKTSQNYLDASDSNKNNYNTAVNNANGVINATNNPNIDANAINGMANQVNTTK 4982
Cdd:COG3210 1313 TVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTG 1392
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4983 AALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTATELNGAMTALKAAIADKERTKASGNY 5062
Cdd:COG3210 1393 AEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGST 1472
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5063 VNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAA---KTALNGDNNLRVAKEHANNTIDGLAQLNNAQK 5139
Cdd:COG3210 1473 AGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAevaKASLEGGEGTYGGSSVAEAGTGGGILGAVSGA 1552
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5140 AKLKEQVQSATTLDGVQTVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDASLNNRNEYDSAVTAAKAIINQTSNPTME 5219
Cdd:COG3210 1553 GSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNT 1632
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616687517 5220 ANTITQATSQVTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGVNQ 5283
Cdd:COG3210 1633 VVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDT 1696
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9121-9933 |
5.79e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9121 NANKYAVEQALTKLQGKENELNGNERVAEAKTQakQTIDQLTHLNaDQIATAKQNIDQATKLqpIAELVDQATQLNQSMD 9200
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLE--ELRLEVSELE-EEIEELQKELYALANE--ISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9201 QLQ----QAVNEHANVEQTVDYTQADLDKQNA-YKQAIAEAENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTN 9275
Cdd:TIGR02168 313 NLErqleELEAQLEELESKLDELAEELAELEEkLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9276 GkhdidQLNALNNaqqdgfkgridqsndlnQIQQIVDEAKALNRAMNQLSQEITGNEGRTKgstnyvnaDTQVKRVYDEA 9355
Cdd:TIGR02168 393 L-----QIASLNN-----------------EIERLEARLERLEDRRERLQQEIEELLKKLE--------EAELKELQAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9356 VDKAKEALNKATGQNLTAEEVIKLNDAVTAAKQALNGEERLNNRKSealQRLDQLthlnnaQRQLaiqqiNNAETLNKAS 9435
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ---ARLDSL------ERLQ-----ENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9436 RAI-NRAVQLDDAMGAVQQYIdehhldvisstnyinaddNLKANYDNAITNAAHE-LDK--VQGSAIAKAEAEQLKQHii 9511
Cdd:TIGR02168 509 KALlKNQSGLSGILGVLSELI------------------SVDEGYEAAIEAALGGrLQAvvVENLNAAKKAIAFLKQN-- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9512 daqkalngdqnlatAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIINDQIDLNNAMETL---KHLVDneipt 9588
Cdd:TIGR02168 569 --------------ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggVLVVD----- 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9589 aeqtvNYQNADDVAKS---------------------NFDDAKRLANALinSDNTNVNDINGAIQAVKDVIQNLngEQRL 9647
Cdd:TIGR02168 630 -----DLDNALELAKKlrpgyrivtldgdlvrpggviTGGSAKTNSSIL--ERRREIEELEEKIEELEEKIAEL--EKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9648 QEAKdKAIQNVNKVLADKLKEIE----ASNATDQDKLIAKNKAEELAnSIINNINKATSNQDVSRVQTAGNQAIEQVHAN 9723
Cdd:TIGR02168 701 AELR-KELEELEEELEQLRKELEelsrQISALRKDLARLEAEVEQLE-ERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9724 EIpKAKIDANKDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQiLQQGHNGINN--AMTKEEIEHAKAQLAQALQDIKD 9801
Cdd:TIGR02168 779 EA-EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN-LRERLESLERriAATERRLEDLEEQIEELSEDIES 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9802 LVKAKENAKQDVDKQVQALideidrnpnltdKEKQALKDRINQILQQGHNGINNAMTK-EEIEQAKAQLAQALQDIKDLV 9880
Cdd:TIGR02168 857 LAAEIEELEELIEELESEL------------EALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKL 924
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 9881 KAKEDAKNAIKALANEKRDQINS----NPDLTPEQKAKALKEIDEAEKRaLENIENA 9933
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRR-LKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9649-10261 |
1.08e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9649 EAKDKAIQNVNKVLADKLKEIEASNATDQDKLIAKNKAEELANSIINNINKATSNQDVsRVQTAgnqaIEQVHAnEIPKA 9728
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-RVKEK----IGELEA-EIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9729 K--IDAN----KDVDKQVQALIDEIDRnpnlTDKEKQALKDRInqilqqghnginnamtkEEIEHAKAQLAQALQDIKDL 9802
Cdd:TIGR02169 307 ErsIAEKerelEDAEERLAKLEAEIDK----LLAEIEELEREI-----------------EEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9803 VKAKENAKQDVDKQVQALIDEIDRnpnlTDKEKQALKDRINQILQQGHNGINNAMTK-EEIEQAKAQLAQALQDIKDLVK 9881
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQRLsEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9882 AKEDAKNAIKA--------------LANEKRDQINSNPDLTPEQKAKAlKEIDEAEKRA----LENIENAQTKDQLNKGL 9943
Cdd:TIGR02169 442 EKEDKALEIKKqewkleqlaadlskYEQELYDLKEEYDRVEKELSKLQ-RELAEAEAQAraseERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9944 ------------------------------NLGLDDirnthvwEVDAQPAV----------------NEI--FDATPEQI 9975
Cdd:TIGR02169 521 qgvhgtvaqlgsvgeryataievaagnrlnNVVVED-------DAVAKEAIellkrrkagratflplNKMrdERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9976 LVNG------ELI------------VHRDDIITEqDIHAHINLIDQ-----LTAEIIDtPSTATISDSLTAK---VEVTL 10029
Cdd:TIGR02169 594 SEDGvigfavDLVefdpkyepafkyVFGDTLVVE-DIEAARRLMGKyrmvtLEGELFE-KSGAMTGGSRAPRggiLFSRS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10030 LDGSKVIVSVPVKVVEKELTVVKQQaIESIENA----------AQQKINEINNHATLTPEQKEAAIAEVNKLK------Q 10093
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSE-LRRIENRldelsqelsdASRKIGEIEKEIEQLEQEEEKLKERLEELEedlsslE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10094 QAI-----EQINNAADVHTVEEVQHQEQAHIE----QFNPDQFTIDQAKSNAIKSISDAIQHMIDEINAS-------KDL 10157
Cdd:TIGR02169 751 QEIenvksELKELEARIEELEEDLHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKlnrltleKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10158 TDKEKQEAISKLNQLKDQsIQAIQRAqsIDEIAQQLEQFKAQLKAANPFAKELENRKKSAISKIKDISTD------EINR 10231
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQ-IKSIEKE--IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrelerKIEE 907
|
730 740 750
....*....|....*....|....*....|
gi 616687517 10232 IrNSTIGTAEERQAAMNRINEIVLETIRDI 10261
Cdd:TIGR02169 908 L-EAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| aRib |
pfam18938 |
Atypical Rib domain; This entry contains atypical Rib (aRib) domains. These are found in a ... |
1023-1093 |
9.13e-11 |
|
Atypical Rib domain; This entry contains atypical Rib (aRib) domains. These are found in a variety of bacterial cell surface proteins. These proteins share a conserved motif with the Rib domain (YPDXXD). The structure of the aRib domain has been solved from two proteins, the SrpA adhesin and the GspB adhesin. In these proteins this domain has been termed the unique domain due to its lack of similarity to any other known structures at the time. The aRib domain from SrpA has been shown to mediate a dimer interaction. This family has been added to the E-set clan based on its similarity to the Rib domain, although it does not contain the Ig fold.
Pssm-ID: 465921 [Multi-domain] Cd Length: 71 Bit Score: 61.47 E-value: 9.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 1023 NSEKVVVVNPTALTGDEKQRITTAFMNKNQNIRgylaSSNPVTVDNHGNVTLQYRDGSSTTLDATNVMTYE 1093
Cdd:pfam18938 5 IPEKTEVKDPNKLTDEEKQEVKDAVKKANPDLP----EGTKVEVDDDGTVTVTYPDGSKDTIPAKDLVKEK 71
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
5481-7173 |
2.77e-10 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 68.64 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5481 TVTQANTALNGIQNLERAKQAANTAITNASDLNTKQKEALKAQVTSAGRVSVANGVEHTVTELNTAMTAlkrAIADKADT 5560
Cdd:COG3210 8 TTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSA---STGGIGAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5561 KASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPSDVTNAATQVTNAKTQLNGNHNLEVAKQNANTAIDGLTSLNG 5640
Cdd:COG3210 85 AANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5641 PQKAKLKEQVGQATTLPNVQTVRDNAQTLNTAMKGLRDSIANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQTTSP 5720
Cdd:COG3210 165 NNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5721 TMNAQEINQAKDQVTAKQQALNGQenlrTAQTNAKQHLNGLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMT 5800
Cdd:COG3210 245 GTDISSLSVAAGAGTGGAGGTGNA----GNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5801 NLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTQAEQILNKAQGPNTAKDGVETALQNVqRAKNDLNGNQNVANAKTTA 5880
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTV-ASTVGTATASTGNASSTTV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5881 KNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTASELNTAMSNLQNGINDEAATKAAQKYTDADSDKQTAYNDAVT 5960
Cdd:COG3210 400 LGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNT 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5961 AAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARLNEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGI 6040
Cdd:COG3210 480 TSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAAS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6041 QANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQNAYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSANSALN 6120
Cdd:COG3210 560 GSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6121 GDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKATSLNTAMGNLKHALAEKDNTKRSVNYTDAD 6200
Cdd:COG3210 640 GAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6201 QPKQQAYDTAVTQAEGITNAN--------------GSNANETQVQAALNQLNQAKNDLNGDNKVAQAKEAAKHALASYSN 6266
Cdd:COG3210 720 GALANANGDTVTFGNLGTGATltlnagvtitsgnaGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDIT 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6267 LNNAQSTAATSQIDNATTVAGVTTAQNTANELNTAMGQLQNGINDQNTVKQQVNFTDADQGKKDAYTNAVTNAQGILDKA 6346
Cdd:COG3210 800 ADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6347 NGQNMTKAQVEAALNQVTTAKNALNGDANVRQAKSDAKANLGTLTHLNNAQKQDLTSQIEGVTTVNGVNGVKTKAQDLDG 6426
Cdd:COG3210 880 GSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASA 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6427 AMQRLESAIANKDQTKASENYIDADPTNKTAFDNAITQAESYLNKDHGANKDKQAVEQAIQSVTSTENALNGDanlqrak 6506
Cdd:COG3210 960 SDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASAT------- 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6507 teATQAIDNLTHLNTPQKTALKQQVNAAQRVSGVTDLKNSATSLNSAMDQLKQAIADHDTIVAGGNYTNASPDKQGAYTD 6586
Cdd:COG3210 1033 --GTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTT 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6587 AYNAAKNIVNGSPNVITNAADVTAATQRVNNAETGLNGDTNLATAKQQAKDALRQMTHLSNAQKQSITGQIDSATQVTGV 6666
Cdd:COG3210 1111 TSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAAT 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6667 QSVKDNATNLDNAMNQLRNSIANKDEVKASQPYVDGDTDKQNAYNTAVTSAENIINATSQPTLDPSAVTQAANQVNTNKT 6746
Cdd:COG3210 1191 EGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGAT 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6747 ALNGAQNLANKKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQVKTKAEQLDQAMERLINGIQDKDQVKQSVNFT 6826
Cdd:COG3210 1271 STVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANT 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6827 DADPEKQTAYNNAVTAAENIINQANGTNENQSQVEAALSTVTTTKQALNGDRKVTDAKNNANQTLSTLDNLNNAQKGAVT 6906
Cdd:COG3210 1351 GLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSA 1430
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6907 GNINQAHTVAEVTQAIQTAQELNTAMGNLKNSLNDKDTTLGSQNFADADPEKKNAYNEAVRNAENILNKSTGTNVPKDQV 6986
Cdd:COG3210 1431 TTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGG 1510
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6987 EAAMNQVNTTKAALNGSQNLEKAKQHANTAIDGLSHLTNAQKDALKQLVQQSTTVAEAQGNEQKANNVDAAMDKLRQSIA 7066
Cdd:COG3210 1511 TAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPT 1590
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7067 DNATTKQNQNYTDASPNKKDAYNNAVTTAQGIIDQTTSPTLDPTVINQAAGQVSTTKNALNGNENLEAAKQQATQSLGSL 7146
Cdd:COG3210 1591 AGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAV 1670
|
1690 1700
....*....|....*....|....*..
gi 616687517 7147 DNLNNAQKQAVTNQINGAHTVDEANQI 7173
Cdd:COG3210 1671 DLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7119-7178 |
3.39e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 59.49 E-value: 3.39e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7119 VSTTKNALNGNENLEAAKQQATQSLGSLDNLNNAQKQAVTNQINGAHTVDEANQIKQNAQ 7178
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8882-8941 |
5.16e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 59.11 E-value: 5.16e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8882 VNQAKDNLHGDQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAK 8941
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8756-8815 |
5.86e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 58.72 E-value: 5.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8756 VNDAKNNLHGDQKLAQDKQRATETLNNLSNLNTPQRQALENQINNAATRGEVAQKLTEAQ 8815
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7245-7304 |
7.13e-10 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 58.34 E-value: 7.13e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7245 VNTAKQALNGNANVQHAKDEATALINNSNDLNQAQKDALKQQVQNATTVAGVNNVKQTAQ 7304
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9149-9801 |
8.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9149 EAKTQAKQTIDQLTHLNA--DQIATAKQNIDQatkLQPIAELVDQATQLNQSMDQLQQAVN--EHANVEQTVDYTQADLD 9224
Cdd:COG4913 222 DTFEAADALVEHFDDLERahEALEDAREQIEL---LEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9225 KQNAYKQAIAEAENVLKQ--NANKQQVDQALQNILNA----KQALNGD---ERVALAKTNGKHDI--DQLNALN------ 9287
Cdd:COG4913 299 ELRAELARLEAELERLEArlDALREELDELEAQIRGNggdrLEQLEREierLERELEERERRRARleALLAALGlplpas 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9288 ----NAQQDGFKGRIDQSNDL-----NQIQQIVDEAKALNRAMNQLSQEITGNEGRtkgstnyvnadtqvKRVYDEAVDK 9358
Cdd:COG4913 379 aeefAALRAEAAALLEALEEElealeEALAEAEAALRDLRRELRELEAEIASLERR--------------KSNIPARLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9359 AKEALNKATGqnLTAEEV--------IKLNDAV--TAAKQALNG-------EERLNNRKSEALQRLDQLTHLN----NAQ 9417
Cdd:COG4913 445 LRDALAEALG--LDEAELpfvgelieVRPEEERwrGAIERVLGGfaltllvPPEHYAAALRWVNRLHLRGRLVyervRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9418 RQLAIQQINNAETLnkasrainrAVQLDDAMGAVQQYIDEHhldVISSTNYINADD--NLKaNYDNAIT--------NAA 9487
Cdd:COG4913 523 LPDPERPRLDPDSL---------AGKLDFKPHPFRAWLEAE---LGRRFDYVCVDSpeELR-RHPRAITragqvkgnGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9488 HELDK--------VQG-SAIAK-----AEAEQLKQHIIDAQKALngdQNLATAKDKANAFVDTLNGLNQQQQDLahqaIN 9553
Cdd:COG4913 590 HEKDDrrrirsryVLGfDNRAKlaaleAELAELEEELAEAEERL---EALEAELDALQERREALQRLAEYSWDE----ID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9554 NADTVTGIANIINDQIDLNNAMETLKHLvdneiptaEQTVnyqnadDVAKSNFDDAKRLANALinsdNTNVNDINGAIQA 9633
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAAL--------EEQL------EELEAELEELEEELDEL----KGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9634 VKDVIQNLngEQRLQEAKDKAIQNVNKVLADKLKEieasnatdqdkLIAKNKAEELANSIINNINKATsnqdvSRVQTAG 9713
Cdd:COG4913 725 AEEELDEL--QDRLEAAEDLARLELRALLEERFAA-----------ALGDAVERELRENLEERIDALR-----ARLNRAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9714 NQAIEQVHA--NEIPKAKIDANKDVDK--QVQALIDEIDRNpNLTDKEKQaLKDRINQilqqghnginnaMTKEEIEHAK 9789
Cdd:COG4913 787 EELERAMRAfnREWPAETADLDADLESlpEYLALLDRLEED-GLPEYEER-FKELLNE------------NSIEFVADLL 852
|
730
....*....|..
gi 616687517 9790 AQLAQALQDIKD 9801
Cdd:COG4913 853 SKLRRAIREIKE 864
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7497-7556 |
1.31e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 57.95 E-value: 1.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7497 VNDTNQALNGNQKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAPDIATVNNVKQNAQ 7556
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
5077-6795 |
1.41e-09 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 66.33 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5077 VTNAENIINGTPNATLTVNDVNSATSQVNAAKTALNGDNNLRVAKEHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQ 5156
Cdd:COG3210 13 TIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5157 TVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDASLNNRNEYDSAVTAAKAIINQTSNPTMEANTITQATSQVTTKEQA 5236
Cdd:COG3210 93 ETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5237 LNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGVNQETAKATELNNAMHSLQNGINDETQTKQTQkyLD 5316
Cdd:COG3210 173 IGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDI--SS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5317 AEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQALQNVNSTKTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDN 5396
Cdd:COG3210 251 LSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5397 EITQATNVEGVNTVKAKAQQLDGAMGQLETSIRDKDTTLQSQNYQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVE 5476
Cdd:COG3210 331 DGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5477 RAMQTVTQANTALNGIQNLERAKQAANTAITNASDLNTKQKEALKAQVTSAGRVSVANGVEHTVTELNTAMTALKRAIAD 5556
Cdd:COG3210 411 GTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGI 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5557 KADTKASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPSDVTNAATQVTNAKTQLNGNHNLEVAKQNANTAIDGLT 5636
Cdd:COG3210 491 GTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5637 SLNGpqkaklkeqvGQATTLPNVQTVRDNAQTLNTAMKGLRDSIANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQ 5716
Cdd:COG3210 571 AATG----------GTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5717 TTSPTMNAQEINQAKDQVTAKQQALNGQENLRTAQTNAKQHLNGLSDLTDAQkdavkrqiegATHVNEVTQAQNNADALN 5796
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLN----------AATGGTLNNAGNTLTIST 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5797 TAMTNLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTqaeqILNKAQGPNTAKDGVETALQNVQRAKNDLNGNQNVANA 5876
Cdd:COG3210 711 GSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVT----ITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGAT 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5877 KTTAKNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTASELNTAMSNLQNGINDEAATKAAQKYTDADSDKQTAYN 5956
Cdd:COG3210 787 LDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGAN 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5957 DAVTAAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARLNEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAG 6036
Cdd:COG3210 867 SGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALS 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6037 VQGIQANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQNAYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSAN 6116
Cdd:COG3210 947 GTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTT 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6117 SALNGDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKATSLNTAMGNLKHALAEKDNTKRSVNY 6196
Cdd:COG3210 1027 GTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTS 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6197 TDADQPKQQAYDTAVTQAEGITNANGSNANETQVQAALNQLNQAKNDLNGDNKVAQAKEAAKHALASYSNLNNAQSTAAT 6276
Cdd:COG3210 1107 GGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGAD 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6277 SQIDNATTVAGVTTAQNTANELNTAMGQLQNGINDQNTVKQQVNFTDADQGKKDAYTNAVTNAQGILDKANGQNMTKAQV 6356
Cdd:COG3210 1187 SAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVS 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6357 EAALNQVTTAKNALNGDANVRQAKSDAKANLGTLTHLNNAQKQDLTSQIEGVTTVNGVNGVKTKAQDLDGAMQRLESAIA 6436
Cdd:COG3210 1267 NGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTT 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6437 NKDQTKASENYIDADPTNKTAFDNAITQAESYLNKDHGANKDKQAVEQAIQSVTSTENALNGDANLQRAKTEATQAIDNL 6516
Cdd:COG3210 1347 AANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTT 1426
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6517 THLNTPQKTALKQQVNAAQRVSGVTDLKNSATSLNSAmdqlkqaiADHDTIVAGGNYTNASPDKQGAYTDAYNAAKNIVN 6596
Cdd:COG3210 1427 GSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNA--------SSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGAT 1498
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6597 GSPNVITNAADVTAATQRVNNAETGLNGDTNLATAKQQAKDALRQMTHLSNAQKQSITGQIDSATQVTGVQSVKDNATNL 6676
Cdd:COG3210 1499 ASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDT 1578
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6677 DNAMNQLRNSIANKDEVKASQPYVDGDTDKQNAYNTAVTSAENIINATSQPTLDPSAVTQAANQVNTNKTALNGAQNLAN 6756
Cdd:COG3210 1579 GGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLS 1658
|
1690 1700 1710
....*....|....*....|....*....|....*....
gi 616687517 6757 KKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQV 6795
Cdd:COG3210 1659 GAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTA 1697
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
4567-6253 |
1.50e-09 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 66.33 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4567 TNYNNAVDSANSVINATSNPNMDANAINQIATQVTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQ 4646
Cdd:COG3210 4 GLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4647 RVANVTSIQQTANELNTAMGQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQV 4726
Cdd:COG3210 84 AAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4727 TSTKDALNGDAKLAEAKAAAKQNLSTLNHITNAQRTALEGQINQA-----TTVDGVNTVKTNANTLDGAMNSLQGSINDK 4801
Cdd:COG3210 164 TNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVlanagGGTAGGVASANSTLTGGVVAAGTGAGVIST 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4802 DATLRNQNYLDADESKRNAYTQAVTAAEGILNKQTGGNTSKADVDNALNAVTRAKTALNGAENLRNAKTTATNTINGLPH 4881
Cdd:COG3210 244 GGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4882 LTQLQKDNLKHQVEQAQNVAGVNGVKDKGNTLNTAMGALRTSIQNDNTTKTSQNYLDASDSNKNNYNTAVNNANGVINAT 4961
Cdd:COG3210 324 NTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4962 NNPNIDANAINGMANQVNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTATELNG 5041
Cdd:COG3210 404 SLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSAT 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5042 AmTALKAAIADKERTKASGNYVNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAAKTALNGDNNLRVAK 5121
Cdd:COG3210 484 T-LAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5122 EHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDASLNNRNEYDS 5201
Cdd:COG3210 563 TANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5202 AVTAAKAIINQTSNPTMEANTITQATSQVTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGV 5281
Cdd:COG3210 643 LSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGAL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5282 NQETAKATELNNAMHSLQNGINDE--TQTKQTQKYLDAEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQALQNVNST 5359
Cdd:COG3210 723 ANANGDTVTFGNLGTGATLTLNAGvtITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADG 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5360 KTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQQLDGAMGQLETSIRDKDTTLQSQN 5439
Cdd:COG3210 803 TITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSG 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5440 YQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVERAMQTVTQANTALNGIQNLERAKQAANTAITNASDLNTKQkeA 5519
Cdd:COG3210 883 GVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASA--S 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5520 LKAQVTSAGRVSVANGVEHTVTELNTAMTALKRAIADKADTKASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPS 5599
Cdd:COG3210 961 DGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5600 DVTNAATQVTNAKTQLNGNHNLEVAKQNANTAIDGLTSLNGPQKAKLKEQVGQATTLPNVQTVRDNAQTLNTAMKGLRDS 5679
Cdd:COG3210 1041 GGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASK 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5680 IANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQTTSPTMNAQEINQAKDQVTAKQQALNGQENLRTAQTNAKQHLN 5759
Cdd:COG3210 1121 VGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKG 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5760 GLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMTNLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTQAEQI 5839
Cdd:COG3210 1201 GDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGAT 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5840 LNKAQGPNTAKDGVETALQNVQRAKNDLNGNQNVANAKTTAKNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTAS 5919
Cdd:COG3210 1281 ATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATD 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5920 ELNTAMSNLQNGINDEAATKAAQKYTDADSDKQTAYNDAVTAAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARL 5999
Cdd:COG3210 1361 SAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNT 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6000 NEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGIQANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQN 6079
Cdd:COG3210 1441 TGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVA 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6080 AYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSANSALNGDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPN 6159
Cdd:COG3210 1521 KASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLS 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6160 LAAVTAAKNKATSLNTAMGNLKHALAEKDNTKRSVNYTDADQPKQQAYDTAVTQAEGITNANGSNANETQVQAALNQLNQ 6239
Cdd:COG3210 1601 LAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGL 1680
|
1690
....*....|....
gi 616687517 6240 AKNDLNGDNKVAQA 6253
Cdd:COG3210 1681 GGATTAAAGNVATG 1694
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8127-8186 |
1.65e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 57.57 E-value: 1.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8127 VNAAKQALNGNDNLANAKQQAKQQLANLTHLNDAQKQSFESQITQAPLVTDVTTINQKAQ 8186
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8773-9523 |
2.67e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8773 KQRATETLNNL------------------SNLNTPQRQA--------LENQINNAatrgEVAQKLTEAQALNQAMEALRN 8826
Cdd:TIGR02168 171 KERRKETERKLertrenldrledilneleRQLKSLERQAekaerykeLKAELREL----ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8827 SIQDQQQTEagskfiNEDKPQKDAYQAAVQHAKDLINQtsnptlDKAQVEQLTQAVNQAKDNLHgdqKLADDKQHAVtdl 8906
Cdd:TIGR02168 247 ELKEAEEEL------EELTAELQELEEKLEELRLEVSE------LEEEIEELQKELYALANEIS---RLEQQKQILR--- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8907 NQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKALNQAMEALRNSIQDQQQTESGSKFinEDKPQKDAYQAAVQHAKD 8986
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE--ELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8987 LINQTgnptldKSQVEQLTQAVATAKDNLHGDQKLVRDQQQAVTTVNA---LPNLNHAQQQALTDAINAAPTRTEVAQHV 9063
Cdd:TIGR02168 387 KVAQL------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9064 QTATELDHAMETLKNKVDQVNTDKAQPNYTEAST--------DKKDAVDQALQAAQSITDPTNG-----SNANKY--AVE 9128
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLerlqenleGFSEGVKALLKNQSGLSGILGVlseliSVDEGYeaAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9129 QALtklqgkenELNGNERVAEAKTQAKQTIDQL--------THLNADQIATAKQNIDQATKLQPIAELVDQATQLNQSMD 9200
Cdd:TIGR02168 541 AAL--------GGRLQAVVVENLNAAKKAIAFLkqnelgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9201 QLQQAVNEH-ANVEQTVDYTQA-DLDKQNAYKQAI------------------AEAENVLKQNANK-----QQVDQALQN 9255
Cdd:TIGR02168 613 KLRKALSYLlGGVLVVDDLDNAlELAKKLRPGYRIvtldgdlvrpggvitggsAKTNSSILERRREieeleEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9256 ILNAKQALNGDERVALAKTNGKHDIDQlnALNNAQQDGFKGRIDQSNDLNQIQQIVDEAKALNRAMNQLSQEITGNEGRt 9335
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER- 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9336 KGSTNYVNADTQVKRVYDEA-VDKAKEALnKATGQNLTA--EEVIKLNDAVTAAKQALNGEERLNNRKSEALQRLDQLTH 9412
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAqIEQLKEEL-KALREALDElrAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9413 LNNAQRQLAIQQINNAET-LNKASRAINravQLDDAMGAVQQYIDEHhldvisSTNYINADDNLKaNYDNAITNAAHELD 9491
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEElIEELESELE---ALLNERASLEEALALL------RSELEELSEELR-ELESKRSELRRELE 918
|
810 820 830
....*....|....*....|....*....|...
gi 616687517 9492 KVQGS-AIAKAEAEQLKQHIIDAQKALNGDQNL 9523
Cdd:TIGR02168 919 ELREKlAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9614-10256 |
4.20e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9614 NALINSDNTNVNDINGAIQAVKDVIQNLNGEQRLQEAKDKAIQNVNKVLADKLKEIEASNATDQDKLIA-KNKAEELANS 9692
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEELKEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9693 IINNINKATSNQDVSRVQTAGNQAIEQVH-----------------ANEIPKAKIDANkDVDKQVQALIDEI-DRNPNLT 9754
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLetlrskvaqlelqiaslNNEIERLEARLE-RLEDRRERLQQEIeELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9755 DKEKQALKDRINQILQQghnginnamtKEEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALIDEID-------RN 9827
Cdd:TIGR02168 432 EAELKELQAELEELEEE----------LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqeNL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9828 PNLTDKEKQALK--DRINQILQQGHNGINnamTKEEIEQAK-AQLAQALQDIkdLVKAKEDAKNAIKALANEKRDQIN-- 9902
Cdd:TIGR02168 502 EGFSEGVKALLKnqSGLSGILGVLSELIS---VDEGYEAAIeAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTfl 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9903 ----SNPDLTPEQKAKALKEIDEAEKRALENIEnaqTKDQLNKGLNLGLDDIRnthvWEVDAQPAVNEIFDATPEQILV- 9977
Cdd:TIGR02168 577 pldsIKGTEIQGNDREILKNIEGFLGVAKDLVK---FDPKLRKALSYLLGGVL----VVDDLDNALELAKKLRPGYRIVt 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9978 -NGELIvHRDDIITEQDIHAHINL------IDQLTAEIIDTPSTATISDSLTAKVEVTLLDGSKVIVSVPVKVVEKELTV 10050
Cdd:TIGR02168 650 lDGDLV-RPGGVITGGSAKTNSSIlerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10051 VKQQAIESIENAAQQKINEINNHATLTPEQKEAAIAEVNKLKQQAIEQInnaadvHTVEEVQHQEQAHIEQFNPDQFTID 10130
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL------AEAEAEIEELEAQIEQLKEELKALR 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10131 Q---AKSNAIKSISDAIQHMIDEINASKDLTDKEKQEAISKLNQLKDQSIQAIQRAQSI-------DEIAQQLEQFKAQL 10200
Cdd:TIGR02168 803 EaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeleeliEELESELEALLNER 882
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 616687517 10201 KAANPFAKELENRKKSAISKIKDIStDEINRIRnstigtaEERQAAMNRINEIVLE 10256
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELE-SKRSELR-------RELEELREKLAQLELR 930
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5860-5918 |
4.66e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 56.03 E-value: 4.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5860 VQRAKNDLNGNQNVANAKTTAKNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTA 5918
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7623-7682 |
5.61e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 56.03 E-value: 5.61e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7623 VNAAKQALNGNDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDAAQTVANVNTNKQTAQ 7682
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6867-6926 |
5.72e-09 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 56.03 E-value: 5.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6867 VTTTKQALNGDRKVTDAKNNANQTLSTLDNLNNAQKGAVTGNINQAHTVAEVTQAIQTAQ 6926
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8872-9451 |
1.24e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8872 KAQVEQLTQAVNQAK--DNLHGDQKLADdKQHAVTDLNQLNGlnnpQRQALESQINNAATRDEVAQklAEAKALNQAMEA 8949
Cdd:COG1196 199 ERQLEPLERQAEKAEryRELKEELKELE-AELLLLKLRELEA----ELEELEAELEELEAELEELE--AELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8950 LRNSIQDQQQ--TESGSKFINEDKpQKDAYQAAVQHAKDLINQTGNpTLD--KSQVEQLTQAVATAKDNLHGDQKLVRDQ 9025
Cdd:COG1196 272 LRLELEELELelEEAQAEEYELLA-ELARLEQDIARLEERRRELEE-RLEelEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9026 QQAVTTVNAlpNLNHAQQQALTDAINAAPTRTEVAQHVQTATELDHAMETLKNKVDQVntdkaqpnyTEASTDKKDAVDQ 9105
Cdd:COG1196 350 EEELEEAEA--ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL---------EEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9106 ALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELNGNERVAEAKTQAKQtidQLTHLNADQIATAKQNIDQATKLQPI 9185
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9186 AELVDQATQLNQSMDQLQQAVNEHANVEQTVDytqADLDKQNAYKQAIAEAENVLKQNANKQQVDQALQNILNAKQALNG 9265
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVA---VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9266 DERVALAKTNGKHDIDQLNALNNAQQDGFKG----RIDQSNDLNQIQQIVDEAKALNRAMNQLSQEITGNEGRTKGSTNY 9341
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9342 VNADTQVKRVYDEAVDKAKEALNKAtgQNLTAEEVIKLNDAVTAAKQALNGEERLNNRKSEALQRLDQLTHLNNAQRQLA 9421
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEA--EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 616687517 9422 IQQINNAETLNKASRAINRAVQLD----------------------DAMGAV 9451
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEelpeppdleelerelerlereiEALGPV 782
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6741-6800 |
1.29e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6741 VNTNKTALNGAQNLANKKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQVKTKAE 6800
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7876-7934 |
1.29e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7876 NQAKDALNGDEKLAQAKQDALANLDTLRDLNQPQRDALRNQINQAQALATVEQTKQNAQ 7934
Cdd:smart00844 2 NTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6489-6548 |
1.30e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.30e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6489 VTSTENALNGDANLQRAKTEATQAIDNLTHLNTPQKTALKQQVNAAQRVSGVTDLKNSAT 6548
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8416-9242 |
1.39e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8416 ALKDQVTAATLVTAVHQIEQnantLNQAMHGLRESIqdnaatKANSKYINEDQPEQQNYDQAVQAANNIINEqtatlDNN 8495
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEE----LREELEELQEEL------KEAEEELEELTAELQELEEKLEELRLEVSE-----LEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8496 VINQAATTVNTTKAALHgdvKLQNDKDHAKQavsQLAHLNNAQKHMEDTLIDSETTRtavNHDLTEAQALDQLMDALQQS 8575
Cdd:TIGR02168 282 EIEELQKELYALANEIS---RLEQQKQILRE---RLANLERQLEELEAQLEELESKL---DELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8576 IADKDA--TRASSAYVNAEpNKKQAYDEAVQNAESIIAGLNNptinKGNVTSATQAVTSS-KNALDG-VERLAQDKQTag 8651
Cdd:TIGR02168 353 LESLEAelEELEAELEELE-SRLEELEEQLETLRSKVAQLEL----QIASLNNEIERLEArLERLEDrRERLQQEIEE-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8652 nslnHLDQLTPAQQQALENQInnattrDKVAEIIAQAQALNEAMKALKESIKDQpqteasskfinedqaqkdaytqavqh 8731
Cdd:TIGR02168 426 ----LLKKLEEAELKELQAEL------EELEEELEELQEELERLEEALEELREE-------------------------- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8732 akdlinkttdptlvksvIDQATQAVNDAKNNLHGdqklAQDKQRATETL-NNLSNLNTPQRQALENQINNAATRGEVAQK 8810
Cdd:TIGR02168 470 -----------------LEEAEQALDAAERELAQ----LQARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8811 LTEAQALNQAME-ALRNSIQD---------------QQQTEAGS------KFINEDKPQKDAYQAA------VQHAKDLI 8862
Cdd:TIGR02168 529 ISVDEGYEAAIEaALGGRLQAvvvenlnaakkaiafLKQNELGRvtflplDSIKGTEIQGNDREILkniegfLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8863 nqTSNPTLDKAQ---------VEQLTQAVNQAKDNLHG------DQKL---------ADDKQHAVTdLNQLNGLNNPQRQ 8918
Cdd:TIGR02168 609 --KFDPKLRKALsyllggvlvVDDLDNALELAKKLRPGyrivtlDGDLvrpggvitgGSAKTNSSI-LERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8919 ALESQINNAATRDEVAQKLAEAKALNQAMEALRNSIQD--QQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQTGNPTL 8996
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8997 DKSQVEQLTQAVATAKDNLHGDQKLVRDQQQAVTTVNAlpNLNHAQQQALTDAINAAPTRTEVAQHVQTATELDHAMETL 9076
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9077 KNKVDQVNTDKAQpnYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELNGNERVAEAKTQAKQ 9156
Cdd:TIGR02168 844 EEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9157 TidQLTHLNAdQIATAKQNIDQatklqpiaelvdqatqlnqsmdqLQQAVNEHANVEQTVD---YTQADLDKQNAYKQaI 9233
Cdd:TIGR02168 922 E--KLAQLEL-RLEGLEVRIDN-----------------------LQERLSEEYSLTLEEAealENKIEDDEEEARRR-L 974
|
....*....
gi 616687517 9234 AEAENVLKQ 9242
Cdd:TIGR02168 975 KRLENKIKE 983
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4978-5037 |
1.46e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4978 VNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTAT 5037
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5104-5163 |
1.60e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.87 E-value: 1.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5104 VNAAKTALNGDNNLRVAKEHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQ 5163
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
10051-10125 |
2.38e-08 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 54.90 E-value: 2.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 10051 VKQQAIESIENAAQQKINEINNHATLTPEQKEAAIAEVNKLKQQAIEQINNAADVHTVEEVQHQEQAHIEQFNPD 10125
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQPP 75
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3718-3777 |
2.51e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3718 VNSSKTALNGDENLAAAKQNAKTYLNSLTSITDAQKNNLISQITSATRVSGVDTVKQNAQ 3777
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
9805-9877 |
2.58e-08 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 54.52 E-value: 2.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687517 9805 AKENAKQDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIK 9877
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQ 73
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7750-7807 |
2.66e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 7750 TDAKNGLNGNHNLQVAKDNANTAIDQLPNLNQPQKTALKDQVTHAELVTGVNAIKQNA 7807
Cdd:smart00844 2 NTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5230-5289 |
2.71e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.71e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5230 VTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGVNQETAKAT 5289
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5356-5415 |
2.96e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 54.10 E-value: 2.96e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5356 VNSTKTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQ 5415
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7129-7183 |
3.04e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.70 E-value: 3.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7129 NENLEAAKQQATQSLGSLDNLNNAQKQAVTNQINGAHTVDEANQIKQNAQNLNTA 7183
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8892-8946 |
3.19e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.70 E-value: 3.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8892 DQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKALNQA 8946
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9649-10256 |
4.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9649 EAKDKAIQNVNKVLADKLKEIEA--SNATDQDKLIaKNKAEELAnSIINNINKATSNQDvsrvqtagnQAIEQVHANEIP 9726
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIEELI-KEKEKELE-EVLREINEISSELP---------ELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9727 KAKIDANKDvdkqvqaLIDEIDRNPNLTDKEKQALKDRINQIlqqghnginnamtKEEIEHAKAQLAQALQDIKDLVKAK 9806
Cdd:PRK03918 230 VKELEELKE-------EIEELEKELESLEGSKRKLEEKIREL-------------EERIEELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9807 ENAKQDVdkQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDA 9886
Cdd:PRK03918 290 EKAEEYI--KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9887 KnAIKALANEKRDQINsnpDLTPEqkaKALKEIDEAEKRALEnIENAQTKDQLNKGlnlGLDDIRNthvwevDAQPAVNE 9966
Cdd:PRK03918 368 K-AKKEELERLKKRLT---GLTPE---KLEKELEELEKAKEE-IEEEISKITARIG---ELKKEIK------ELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9967 IFDATPEQILVNGELIV-HRDDIITEqdIHAHINLIDQLTAEIIDtpstaTISDSLTAKVEVtlldgskvivsVPVKVVE 10045
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEeHRKELLEE--YTAELKRIEKELKEIEE-----KERKLRKELREL-----------EKVLKKE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10046 KELTVVKQQA--IESIENaaqqKINEINnhatltPEQKEAAIAEVNKLKQQAIE---QINNAAD---------------- 10104
Cdd:PRK03918 493 SELIKLKELAeqLKELEE----KLKKYN------LEELEKKAEEYEKLKEKLIKlkgEIKSLKKelekleelkkklaele 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10105 --VHTVEE----VQHQ-EQAHIEQFNPDQFTIDQAKS-----NAIKSISDAIQHM----------IDEINASKDLTDKEK 10162
Cdd:PRK03918 563 kkLDELEEelaeLLKElEELGFESVEELEERLKELEPfyneyLELKDAEKELEREekelkkleeeLDKAFEELAETEKRL 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10163 QEAISKLNQLKD-----------------QSIQAIQRAQ------SIDEIAQQLEQFKAQLKAANPFAKELENRKKsAIS 10219
Cdd:PRK03918 643 EELRKELEELEKkyseeeyeelreeylelSRELAGLRAEleelekRREEIKKTLEKLKEELEEREKAKKELEKLEK-ALE 721
|
650 660 670
....*....|....*....|....*....|....*..
gi 616687517 10220 KIKDIStDEINRIRNstigtaEERQAAMNRINEIVLE 10256
Cdd:PRK03918 722 RVEELR-EKVKKYKA------LLKERALSKVGEIASE 751
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8001-8060 |
4.43e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 4.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8001 VTDAKNGLNGEAKLATEKQNAKDAVNAMTHLNDAQKQALNGQIDQSPEIATVTQVKQTAT 8060
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6363-6422 |
4.56e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 4.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6363 VTTAKNALNGDANVRQAKSDAKANLGTLTHLNNAQKQDLTSQIEGVTTVNGVNGVKTKAQ 6422
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8766-8820 |
4.77e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.31 E-value: 4.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8766 DQKLAQDKQRATETLNNLSNLNTPQRQALENQINNAATRGEVAQKLTEAQALNQA 8820
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8137-8191 |
4.87e-08 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 53.31 E-value: 4.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8137 NDNLANAKQQAKQQLANLTHLNDAQKQSFESQITQAPLVTDVTTINQKAQALDHA 8191
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
2785-4398 |
4.87e-08 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 61.32 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2785 INKSVTTDGMTQSSIQAYENAKRAGQTESTNAQNVINNGDATDQQIAAEKTKVEEKYNSLKQAIDGLTPDLAPLQTAKTQ 2864
Cdd:COG3210 78 TGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2865 LQNDIDQPTNTTGMTSASVATFNEKLSAARTKIQEIDRVLASHPDVATIRQNVTAANAakSALDQARNGLTVDKAPLENA 2944
Cdd:COG3210 158 AGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGG--TAGGVASANSTLTGGVVAAG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2945 KNQLQHSIDTQTSTTGMTQDSINAYNAKLTAARNKVQQINQVLAGSPTVDQINTNTSAANQAKSDLDHARQALTPDKAPL 3024
Cdd:COG3210 236 TGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3025 QNAKTQLEQSINQPTDTTGMTTASLNAYNQKLQAARQKLTEINQVLNGNPTVQKINDKVTEANQAKDQLNTARQGLTLDR 3104
Cdd:COG3210 316 TAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNAS 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3105 QPALSTLHGASNLNQAQQNNFTQQINAAQNHAALETIKSNITALNNAMTKLKESVADNNSIKSGQNYTDATQANKQAYDN 3184
Cdd:COG3210 396 STTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNS 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3185 AVNAAKGVIGETNNPTMDVNTVNQKASSVKSTQDALDGQQNLQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQAV 3264
Cdd:COG3210 476 AGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGT 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3265 NDIKQTTQSLNTAMTGLKRGVANHNQVVQSDNYVNADTNKKNDYNNAYNHANDIINGNAQHPVITPSDVNNALSNVTNKE 3344
Cdd:COG3210 556 TAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLT 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3345 HALNGEAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNATNLNSAMGNLRQAVADKDQVKRTEDY 3424
Cdd:COG3210 636 GSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITV 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3425 ADADTAKQNAYNSAVSSAETIINQTTNPTMSVNDVNSATSAVTTNKNALNGDEKLAQSKTDAASAIDALPHLNNAqKADV 3504
Cdd:COG3210 716 TGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNA-GAEI 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3505 KSKINVASNI--AGVNTVKQQGTDLN-TAMGNLQGAINDEQTTLNSQNYQDATPSKKTAYTNAVQAAKDILNKSNGQNKT 3581
Cdd:COG3210 795 SIDITADGTItaAGTTAINVTGSGGTiTINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATA 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3582 KDQVTEVMNQVDSAKTNLDGTRLLDQAKQTAKQQLNNMTHLTPAQKTNLTNQINSGTTVAGVHTVQSNANTLDQAMNTLR 3661
Cdd:COG3210 875 ASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGL 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3662 QSIANKDATKASEDYVDANNDKQTAYNNAVAAAETIINANSNPEMNPSTITQKADQVNSSKTALNGDENLAAAKQNAKTY 3741
Cdd:COG3210 955 SAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGT 1034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3742 LNSLTSITDAQKNNLISQITSATRVSG--VDTVKQNAQHLDQAMANLQSGINNESQVKSSEKYRDADTNKQQEYDNAITA 3819
Cdd:COG3210 1035 GTAATAGGQNGVGVNASGISGGNAAALtaSGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTG 1114
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3820 AKAILNKQHGPNTAQNAVEAALQRVNTAKNALNGDAKLIAAQNAAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVK 3899
Cdd:COG3210 1115 GVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTA 1194
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3900 QSANSLDGAMGNLQTAINDKSGTLASQNFLDADEQKRNAYNQAVSNAETILNKQTGPNTAKTAVEQALNNVNSAKHALNG 3979
Cdd:COG3210 1195 GTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVA 1274
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3980 TQNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQDVQRNATELNTAMGTLKHAIADKTTTLASSKYVNADS 4059
Cdd:COG3210 1275 GNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNG 1354
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4060 TKQNAYTTKVTNAEHIISGTPTVVTTPSEVTAAANQVNSAKQELNGDERLREAKQNANTAIDALTQLNTPQKAKLKEQVG 4139
Cdd:COG3210 1355 GNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGT 1434
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4140 QANRLEDVQTVQTNGQALNNAMKGLRDSIANETTVKAGQNYTDASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAA 4219
Cdd:COG3210 1435 GGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGG 1514
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4220 TQVNNAKNGLNGAENLRNAQNTAKQNLNTLSHLTNNQKSAISSQIDRAGHVSEVTAAKNAATELNTQMGNLEQAIHDQNT 4299
Cdd:COG3210 1515 TTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNT 1594
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4300 VKQSVKFTDADKAKRDAYTNAVSRAETILNKTQGANTPKQDVEASIQNVSSAKNALNGDQNVTNAKNAAKNALNNLTSIN 4379
Cdd:COG3210 1595 ATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTD 1674
|
1610
....*....|....*....
gi 616687517 4380 NAQKRDLTTKIDQATTVAG 4398
Cdd:COG3210 1675 ATLAGLGGATTAAAGNVAT 1693
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5608-5667 |
5.13e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 5.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5608 VTNAKTQLNGNHNLEVAKQNANTAIDGLTSLNGPQKAKLKEQVGQATTLPNVQTVRDNAQ 5667
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8379-8438 |
5.44e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 5.44e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8379 VQTTLQALNGDHNLQVAKTNATQAIDALTSLNDPQKTALKDQVTAATLVTAVHQIEQNAN 8438
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6993-7052 |
5.49e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 53.33 E-value: 5.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6993 VNTTKAALNGSQNLEKAKQHANTAIDGLSHLTNAQKDALKQLVQQSTTVAEAQGNEQKAN 7052
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
9635-10264 |
5.79e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9635 KDVIQNLNGEQRLQEAKDKAIQNVNKVLADKLKEIEAsnatdqdKLIAKNKAEELANSIINNINKATSNQDvsrvQTAGN 9714
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE-------YLLYLDYLKLNEERIDLLQELLRDEQE----EIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9715 QAIEQVHANEIpkAKIDANKDVDKQVQALIDEIDrnpNLTDKEKQALKdRINQILQQGHNGINNAMTKEEIEHAKAQLAQ 9794
Cdd:pfam02463 257 KQEIEKEEEKL--AQVLKENKEEEKEKKLQEEEL---KLLAKEEEELK-SELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9795 ALQdiKDLVKAKENAKQDVDKQVQALIDEIDrnpNLTDKEKQALKDRINQI--LQQGHNGINNAM-TKEEIEQAKAQLAQ 9871
Cdd:pfam02463 331 KKE--KEEIEELEKELKELEIKREAEEEEEE---ELEKLQEKLEQLEEELLakKKLESERLSSAAkLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9872 ALQDIKDLVKAKEDAKNAIKA-------------LANEKRDQINSNPDLTPEQKAKALKEIDEAEKRALENIENAQTKDQ 9938
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKeeleileeeeesiELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9939 LNKGLNLGLDDIRNTHVWEVDAQPAVNEIFDATPEQILVNGELIVHRDDIITEQDIHAHINLIDqltaeiiDTPSTATIS 10018
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV-------IVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10019 DSLTAKVEVTLLDGSKVIVSVPVKVVEKELTVVKQQAIESIENA-----AQQKINEINNHATLTPE-QKEAAIAEVNKLK 10092
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlnlaqLDKATLEADEDDKRAKVvEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10093 QQAIEQI--------NNAADVHTVEEVQHQEQAHIEQFNPDQFTIDQAKSNAIKSISDAIQHMIDEINASKDLTDKEKQE 10164
Cdd:pfam02463 639 ESAKAKEsglrkgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10165 AISKLNQLKdqSIQAIQRAQSIDEIAQQLEQFKAQLKAANPFAKELENRKKSAISKIKDISTDEINRIRNSTIGTAEERQ 10244
Cdd:pfam02463 719 AEELLADRV--QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660
....*....|....*....|
gi 616687517 10245 AAMNRINEIVLETIRDINNA 10264
Cdd:pfam02463 797 KAQEEELRALEEELKEEAEL 816
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3340-3399 |
6.30e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.95 E-value: 6.30e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3340 VTNKEHALNGEAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNAT 3399
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
9735-9921 |
6.73e-08 |
|
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: 57.63 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9735 DVDKQVQALIDEIDRNPnltdKEKQALKDRINQILQQghngINNAmtKEEIEHAKAQLAQALQDIKDLVKAKENAKQDVD 9814
Cdd:COG1579 14 ELDSELDRLEHRLKELP----AELAELEDELAALEAR----LEAA--KTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9815 -----KQVQALIDEIDrnpnLTDKEKQALKDRINQILqqghnginnamtkEEIEQAKAQLAQALQDIKDLVKAKEDAKNA 9889
Cdd:COG1579 84 nvrnnKEYEALQKEIE----SLKRRISDLEDEILELM-------------ERIEELEEELAELEAELAELEAELEEKKAE 146
|
170 180 190
....*....|....*....|....*....|..
gi 616687517 9890 IKALANEKRDQINsnpDLTpEQKAKALKEIDE 9921
Cdd:COG1579 147 LDEELAELEAELE---ELE-AEREELAAKIPP 174
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4348-4407 |
7.08e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.95 E-value: 7.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4348 VSSAKNALNGDQNVTNAKNAAKNALNNLTSINNAQKRDLTTKIDQATTVAGVEAVSNTGT 4407
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8253-8312 |
7.22e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.95 E-value: 7.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8253 VNNTKVALDGDENLAAAKQQANNRLDQLDHLNNAQKQQLQSQITQSSDIAAVNGHKQTAE 8312
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6615-6674 |
8.53e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.56 E-value: 8.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6615 VNNAETGLNGDTNLATAKQQAKDALRQMTHLSNAQKQSITGQIDSATQVTGVQSVKDNAT 6674
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4600-4659 |
9.31e-08 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.56 E-value: 9.31e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4600 VTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQRVANVTSIQQTAN 4659
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3213-3272 |
1.04e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.56 E-value: 1.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3213 VKSTQDALDGQQNLQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQAVNDIKQTTQ 3272
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6237-6296 |
1.11e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6237 LNQAKNDLNGDNKVAQAKEAAKHALASYSNLNNAQSTAATSQIDNATTVAGVTTAQNTAN 6296
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9008-9067 |
1.16e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9008 VATAKDNLHGDQKLVRDQQQAVTTVNALPNLNHAQQQALTDAINAAPTRTEVAQHVQTAT 9067
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4096-4155 |
1.29e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4096 VNSAKQELNGDERLREAKQNANTAIDALTQLNTPQKAKLKEQVGQANRLEDVQTVQTNGQ 4155
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8745-9286 |
1.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8745 VKSVIDQATQAvndaknNLHgdQKLAQDKQRATETLNNLSNLNTPQRQAlenqinnAATRGEVAQKLTEAQALNQAMEAL 8824
Cdd:PRK02224 192 LKAQIEEKEEK------DLH--ERLNGLESELAELDEEIERYEEQREQA-------RETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8825 RNSIQDQQQTeagskfINEDKPQKDAYQAAVQHAKDLINQTS---NPTLDKAQVEQLTQ-AVNQAKDNLHG-DQKLADDK 8899
Cdd:PRK02224 257 EAEIEDLRET------IAETEREREELAEEVRDLRERLEELEeerDDLLAEAGLDDADAeAVEARREELEDrDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8900 QHAVTDLNQLNGlnnpqrQAlESQINNAATRDEVAQKLAE-AKALNQAMEALRNSIQDQQQTesgskfINEDKPQKDAYQ 8978
Cdd:PRK02224 331 EECRVAAQAHNE------EA-ESLREDADDLEERAEELREeAAELESELEEAREAVEDRREE------IEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8979 AAVqhakdlinqtGNPTLDKSQVEQLTQAVATAKDNLHGDQKLVRdqqqaVTTVNALPNLNHAQQ-----------QALT 9047
Cdd:PRK02224 398 ERF----------GDAPVDLGNAEDFLEELREERDELREREAELE-----ATLRTARERVEEAEAlleagkcpecgQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9048 DAINAAPT---RTEVAQHVQTATELDHAMETLKNKVDQVNTDKAQPNYTEASTDKKDAVDQALQAAQSITDPTNGSNANK 9124
Cdd:PRK02224 463 GSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9125 YAVEQAL-TKLQGKEnelngnERVAEAKTQAKQTIDQLTHLNADQiATAKQNIDQ----ATKLQPIAELVDQATQLNQSM 9199
Cdd:PRK02224 543 RERAAELeAEAEEKR------EAAAEAEEEAEEAREEVAELNSKL-AELKERIESleriRTLLAAIADAEDEIERLREKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9200 DQLQQaVNehanvEQTVDYtqadLDKQNAYKQAIAEA---ENVLKQNANKQQVDQALQNILNAKQALNgDERVALAKTNG 9276
Cdd:PRK02224 616 EALAE-LN-----DERRER----LAEKRERKRELEAEfdeARIEEAREDKERAEEYLEQVEEKLDELR-EERDDLQAEIG 684
|
570
....*....|..
gi 616687517 9277 --KHDIDQLNAL 9286
Cdd:PRK02224 685 avENELEELEEL 696
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5734-5792 |
1.34e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5734 VTAKQQALNGQENLRTAQTNAKQHLNGLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNA 5792
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4852-4911 |
1.35e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 52.18 E-value: 1.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4852 VTRAKTALNGAENLRNAKTTATNTINGLPHLTQLQKDNLKHQVEQAQNVAGVNGVKDKGN 4911
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8630-8689 |
1.76e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 51.79 E-value: 1.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8630 VTSSKNALDGVERLAQDKQTAGNSLNHLDQLTPAQQQALENQINNATTRDKVAEIIAQAQ 8689
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8389-8443 |
2.07e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8389 DHNLQVAKTNATQAIDALTSLNDPQKTALKDQVTAATLVTAVHQIEQNANTLNQA 8443
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7507-7561 |
2.20e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7507 NQKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAPDIATVNNVKQNAQNLNNA 7561
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7759-7813 |
2.31e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 51.39 E-value: 2.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7759 NHNLQVAKDNANTAIDQLPNLNQPQKTALKDQVTHAELVTGVNAIKQNADALNNA 7813
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
9728-9800 |
3.44e-07 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 51.43 E-value: 3.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687517 9728 AKIDANKDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEHAKAQLAQALQDIK 9800
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQ 73
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7255-7309 |
3.59e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 50.62 E-value: 3.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7255 NANVQHAKDEATALINNSNDLNQAQKDALKQQVQNATTVAGVNNVKQTAQELNNA 7309
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9645-10224 |
3.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9645 QRLQ-EAKDKAIQnvnkVLADKLKEIEASNATDQDKLIAKNKAEELANSIINNINKATSNQDVSrvQTAGNQAIEQVHAN 9723
Cdd:COG1196 216 RELKeELKELEAE----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9724 EIpkakiDANKDVDKQVQALIDEIDRNPNLTDkEKQALKDRINQILQQghnginNAMTKEEIEHAKAQLAQALQDIKDLV 9803
Cdd:COG1196 290 EY-----ELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEE------LEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9804 KAKENAKQDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAK 9883
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9884 EDAKNAIKALANEKRDQinsnpdltpEQKAKALKEIDEAEKRALENIENAQTKDQLNKGLNLGLDDIRNTHVWEVDAQPA 9963
Cdd:COG1196 438 EEEEEALEEAAEEEAEL---------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9964 VNEIFDATPEQILVNGELIVHRDDIiTEQDIHAHINLIDQLTAEIIDTPSTAT--ISDSLTAKVE-VTLLDGSKVIVSVP 10040
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVE-AAYEAALEAALAAALQNIVVEDDEVAAaaIEYLKAAKAGrATFLPLDKIRARAA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10041 VKVVEKELTVvkQQAIESIE------NAAQQKINEINNHATLTPEQKEAAIAEVNKLKQQAIEqinnaadVHTVEEVQHQ 10114
Cdd:COG1196 588 LAAALARGAI--GAAVDLVAsdlreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-------VTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10115 EQAHIEQFNPDQFTIDQAKSNAIKSISDAIQHMIDEINASKDLTDKEKQEAISKLNQLKDQSIQAIQRAQSIDEIAQQLE 10194
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 616687517 10195 QFKAQLKAANPFA-----------KELENRKKSAISKIKDI 10224
Cdd:COG1196 739 EELLEEEELLEEEaleelpeppdlEELERELERLEREIEAL 779
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
8504-8563 |
3.93e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 50.63 E-value: 3.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8504 VNTTKAALHGDVKLQNDKDHAKQAVSQLAHLNNAQKHMEDTLIDSETTRTAVNHDLTEAQ 8563
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
7371-7430 |
4.38e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 50.63 E-value: 4.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7371 VTQAKNDLNGNTNLATAKQNVQHAIDQLPNLNQAQRDEYSKQITQATLVPNVNAIQQAAT 7430
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5870-5924 |
4.67e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 50.23 E-value: 4.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5870 NQNVANAKTTAKNALNNLTSINNAQKEALKSQIDSATTVAGVNQVSTTASELNTA 5924
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5986-6044 |
5.22e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 50.25 E-value: 5.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5986 VNTAKTALNGDARLNEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGIQANA 6044
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8522-9203 |
5.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8522 DHAKQAVSQLAHLNNAQKHMEDtlidsetTRTAVNHdLTEAQALDQLMDALQQSIADKDATRASSAYVNAEpNKKQAYDE 8601
Cdd:COG4913 225 EAADALVEHFDDLERAHEALED-------AREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWFAQ-RRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8602 AVQNAESIIAGLnnptinKGNVTSATQAVTSSKNALDGVERlaqdkQTAGNSLNHLDQltpaqqqaLENQINNAttRDKV 8681
Cdd:COG4913 296 ELEELRAELARL------EAELERLEARLDALREELDELEA-----QIRGNGGDRLEQ--------LEREIERL--EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8682 AEIIAQAQALNEAMKALKESIkdqPQTEasskfinedqaqkDAYTQAVQHAKDLINKttdptlVKSVIDQATQAVNDAKN 8761
Cdd:COG4913 355 EERERRRARLEALLAALGLPL---PASA-------------EEFAALRAEAAALLEA------LEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8762 NLhgdQKLAQDKQRATETLNNLSN--LNTPQ-----RQALENQINNAATR----GEVAQKLTEAQALNQAME-ALRNS-- 8827
Cdd:COG4913 413 AL---RDLRRELRELEAEIASLERrkSNIPArllalRDALAEALGLDEAElpfvGELIEVRPEEERWRGAIErVLGGFal 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8828 --IQDQQQTEAGSKFINE-DKPQKDAYQAAVQHAKDLINQTSNP-TLdkaqVEQLTQAVNQAKDNLhgDQKLADDKQHA- 8902
Cdd:COG4913 490 tlLVPPEHYAAALRWVNRlHLRGRLVYERVRTGLPDPERPRLDPdSL----AGKLDFKPHPFRAWL--EAELGRRFDYVc 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8903 VTDLNQLN---------------------------------GLNN-PQRQALESQInnaatrDEVAQKLAEAKALNQAME 8948
Cdd:COG4913 564 VDSPEELRrhpraitragqvkgngtrhekddrrrirsryvlGFDNrAKLAALEAEL------AELEEELAEAEERLEALE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8949 ALRNSIQDQQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQ--TGNPTLD--KSQVEQLTQAVATAKDNLHGDQKLVRD 9024
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldASSDDLAalEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9025 QQQAVTTVNalpnlnhAQQQALTDAINAAPTRTEVAQHVQTATELDHAM-ETLKNKVDQVNTDKAQPNYTEASTDKKDAV 9103
Cdd:COG4913 718 LEKELEQAE-------EELDELQDRLEAAEDLARLELRALLEERFAAALgDAVERELRENLEERIDALRARLNRAEEELE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9104 DQALQAAQSITDPTNGSNANKYAVEQALTKLQG-KENELngNERVAEAKTQ-AKQTIDQLTHLNA---DQIATAKQNIDq 9178
Cdd:COG4913 791 RAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGL--PEYEERFKELlNENSIEFVADLLSklrRAIREIKERID- 867
|
730 740
....*....|....*....|....*
gi 616687517 9179 atklqpiaelvdqatQLNQSMDQLQ 9203
Cdd:COG4913 868 ---------------PLNDSLKRIP 877
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
9882-9955 |
5.44e-07 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 51.05 E-value: 5.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616687517 9882 AKEDAKNAIKALANEKRDQINSNPDLTPEQKAKALKEIDEAEKRALENIENAQTKDQLNKGLNLGLDDIRNTHV 9955
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQP 74
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8641-8694 |
5.86e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 50.23 E-value: 5.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 8641 ERLAQDKQTAGNSLNHLDQLTPAQQQALENQINNATTRDKVAEIIAQAQALNEA 8694
Cdd:pfam01468 2 QKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6499-6553 |
6.27e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.85 E-value: 6.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6499 DANLQRAKTEATQAIDNLTHLNTPQKTALKQQVNAAQRVSGVTDLKNSATSLNSA 6553
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
10213-10288 |
6.43e-07 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 50.66 E-value: 6.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616687517 10213 RKKSAISKIKDISTDEINRIRNSTIGTAEERQAAMNRINEIVLETIRDINNAHTPQQVEAALNNGIARILAVQIVT 10288
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQPPT 76
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3728-3782 |
6.59e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.85 E-value: 6.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3728 DENLAAAKQNAKTYLNSLTSITDAQKNNLISQITSATRVSGVDTVKQNAQHLDQA 3782
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3466-3525 |
7.07e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.86 E-value: 7.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3466 VTTNKNALNGDEKLAQSKTDAASAIDALPHLNNAQKADVKSKINVASNIAGVNTVKQQGT 3525
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6303-6371 |
7.11e-07 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 50.40 E-value: 7.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6303 GQLQNGINDQNTVKQQVNFTDADQGKKDAYTNAVTNAQGILDKANGQNMTKAQVEAALNQVTTAKNALN 6371
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
6112-6171 |
7.58e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.86 E-value: 7.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6112 VNSANSALNGDEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKAT 6171
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5240-5294 |
8.09e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.85 E-value: 8.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5240 AQNLAQAKTTAKNNLNNLTSINNAQKDALTRSIDGATTVAGVNQETAKATELNNA 5294
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7185-7253 |
8.24e-07 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 50.01 E-value: 8.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7185 GNLKQAIADKDATKATVNFTDADQAKQQAYNTAVTNDENIISKANGGNATQTEVEQAIQQVNTAKQALN 7253
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3970-4029 |
8.27e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.86 E-value: 8.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3970 VNSAKHALNGTQNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQDVQRNAT 4029
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4222-4281 |
8.69e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.86 E-value: 8.69e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4222 VNNAKNGLNGAENLRNAQNTAKQNLNTLSHLTNNQKSAISSQIDRAGHVSEVTAAKNAAT 4281
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3350-3404 |
9.01e-07 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.46 E-value: 9.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3350 EAKLNAAKQEANTALGHLNNLNNAQRQNLQSQINGAHQIETVNTIKQNATNLNSA 3404
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
10132-10205 |
9.32e-07 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 50.28 E-value: 9.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616687517 10132 AKSNAIKSISDAIQHMIDEINASKDLTDKEKQEAISKLNQLKDQSIQAIQRAQSIDEIAQQLEQFKAQLKAANP 10205
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNPDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQP 74
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3592-3651 |
9.58e-07 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.48 E-value: 9.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3592 VDSAKTNLDGTRLLDQAKQTAKQQLNNMTHLTPAQKTNLTNQINSGTTVAGVHTVQSNAN 3651
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| DUF1542 |
pfam07564 |
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, ... |
9650-9723 |
9.79e-07 |
|
Domain of Unknown Function (DUF1542); This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh. Some members are involved in antibiotic resistance (e.g Swiss:Q9RL69 and Swiss:Q9LCJ9) and/or cellular adhesion. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface.
Pssm-ID: 429541 [Multi-domain] Cd Length: 77 Bit Score: 50.28 E-value: 9.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9650 AKDKAIQNVNKVLADKLKEIEAS-NATDQDKLIAKNKAEELANSIINNINKATSNQDVSRVQTAGNQAIEQVHAN 9723
Cdd:pfam07564 1 KKPDAKAAIDQAANEKKNEINNNpDATDEEKQEAINQVNQAKNQAINNINNATTNQDVDQAKNNGINAINNIQPP 75
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6751-6805 |
1.26e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.08 E-value: 1.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6751 AQNLANKKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQVKTKAEQLDQA 6805
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
3844-3903 |
1.31e-06 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 49.09 E-value: 1.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3844 VNTAKNALNGDAKLIAAQNAAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVKQSAN 3903
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5618-5672 |
1.40e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 49.08 E-value: 1.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5618 NHNLEVAKQNANTAIDGLTSLNGPQKAKLKEQVGQATTLPNVQTVRDNAQTLNTA 5672
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3785-3852 |
1.50e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 49.63 E-value: 1.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 3785 NLQSGINNESQVKSSEKYRDADTNKQQEYDNAITAAKAILNKQHGPNTAQNAVEAALQRVNTAKNALN 3852
Cdd:pfam07554 2 ALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5744-5798 |
1.76e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.69 E-value: 1.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5744 QENLRTAQTNAKQHLNGLSDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTA 5798
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7437-7505 |
1.80e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 49.24 E-value: 1.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7437 TQLKQGIANKAQIKGSENYHDADTDKQTAYDNAVTKAEELLKQTTNPTMDPNTIQQALTKVNDTNQALN 7505
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4988-5042 |
1.88e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.69 E-value: 1.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4988 AQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNVQHTATELNGA 5042
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9383-9441 |
2.02e-06 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 48.71 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 9383 VTAAKQALNGEERLNNRKSEALQRLDQLTHLNNAQRQLAIQQINNAETLNKASRAINRA 9441
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKA 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9133-9932 |
2.03e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9133 KLQGKENELNGNERVAEAKTQAKQtIDQLTHlnadQIATAKQNIDQATKLqpIAELVDQATQLNQSMDQLQQAVN----- 9207
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQ-KEAIER----QLASLEEELEKLTEE--ISELEKRLEEIEQLLEELNKKIKdlgee 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9208 EHANVEQTVDYTQADLDKqnaYKQAIAEAENVLKQNANKQQVDQALQNilnakqalngdeRVALAKTNGKHDIDQLNALN 9287
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAKLEAEID------------KLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9288 NAQQDGFKGRIDQSNDL-NQIQQIVDEAKALNRAMNQLSQEITGNEGRTKGSTNYVNADTQVKRVYDEAVDKAKEALNKA 9366
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLrAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9367 TGQNLTAEEVIK-LNDAVTAAKQALNG--------EERLNNRKSEaLQRLDQltHLNNAQRQLAIqqinnAETLNKASR- 9436
Cdd:TIGR02169 433 EAKINELEEEKEdKALEIKKQEWKLEQlaadlskyEQELYDLKEE-YDRVEK--ELSKLQRELAE-----AEAQARASEe 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9437 --AINRAVQ--LDDAMGAVQQYIDehhlDVISstnyinaddnLKANYDNAITNAA-HELDK--VQGSAIAKAEAEQLKQH 9509
Cdd:TIGR02169 505 rvRGGRAVEevLKASIQGVHGTVA----QLGS----------VGERYATAIEVAAgNRLNNvvVEDDAVAKEAIELLKRR 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9510 iidaqkalngdqNLATAkdkanafvdTLNGLNQQQQDLAHQAINNADTVTGIAniindqIDLnnametlkhlVDNEiPTA 9589
Cdd:TIGR02169 571 ------------KAGRA---------TFLPLNKMRDERRDLSILSEDGVIGFA------VDL----------VEFD-PKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9590 EQTVNYQNADDVAKSNFDDAKRL-ANALINSDNTNVNDINGAIQAVKDVIQNLNGEQRLQEAKDKAiqnvnkvLADKLKE 9668
Cdd:TIGR02169 613 EPAFKYVFGDTLVVEDIEAARRLmGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR-------LRERLEG 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9669 IEASNATDQDKLiakNKAEELANSIINNINKATsnQDVSRVQTAGNQAieqvhaneipKAKIDANKDVDKQVQALIDEID 9748
Cdd:TIGR02169 686 LKRELSSLQSEL---RRIENRLDELSQELSDAS--RKIGEIEKEIEQL----------EQEEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9749 RNPNLTDKEKQALKDRInqilqqghnginnamtkEEIEHAKAQLAQALQDIKD-----LVKAKENAKQDVDKQVQ---AL 9820
Cdd:TIGR02169 751 QEIENVKSELKELEARI-----------------EELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSrieAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9821 IDEIDRNPNLTDKEKQ--------------ALKDRINQILQQGHNGINN-AMTKEEIEQAKAQLAQALQDIKDLVKAKED 9885
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEylekeiqelqeqriDLKEQIKSIEKEIENLNGKkEELEEELEELEAALRDLESRLGDLKKERDE 893
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 616687517 9886 AKNAIKALANEKRD---QINSNPDLTPEQKAKA------LKEIDEAEKRALENIEN 9932
Cdd:TIGR02169 894 LEAQLRELERKIEEleaQIEKKRKRLSELKAKLealeeeLSEIEDPKGEDEEIPEE 949
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8893-9844 |
2.19e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8893 QKLADDKQHAVTDL----NQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKA-----LNQAMEALRNSIQDQQQTESG 8963
Cdd:pfam15921 77 ERVLEEYSHQVKDLqrrlNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAdirrrESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8964 SKFINEdkpqkdayqaavqhakDLINQTgnptldKSQVEQLTQAVATAKDNLHGDQKLVRDQQQAvttvnalpnlnHAQQ 9043
Cdd:pfam15921 157 AKCLKE----------------DMLEDS------NTQIEQLRKMMLSHEGVLQEIRSILVDFEEA-----------SGKK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9044 QALTDAINAAPTRTEVAQHVQTATELDHAMETLKNKV----DQVNTDKAQP-NYTEASTDK-KDAVDQALQAAQ----SI 9113
Cdd:pfam15921 204 IYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIfpveDQLEALKSESqNKIELLLQQhQDRIEQLISEHEveitGL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9114 TDPTNGSNANKYAVEQALTKLQgkENELNGNERVAEAKTQAKQTIDQLTHLNADQIATAKQNIDQATKlqpiaELVDQAT 9193
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQ--EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK-----QLVLANS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9194 QLNQSMDQLQQAVNEHANVEQTVDYTQADLDKQnaykqaiaEAENVLKQNANKQQVDQALQNILNAKQAlngdeRVALAK 9273
Cdd:pfam15921 357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKR--------EKELSLEKEQNKRLWDRDTGNSITIDHL-----RRELDD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9274 TNgkHDIDQLNALNNAQQDGFKGRIDQ--------SNDLNQIQQIVDEAKALNRAMNQLSQEITGNEGRTKGSTNYVN-- 9343
Cdd:pfam15921 424 RN--MEVQRLEALLKAMKSECQGQMERqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdl 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9344 -ADTQVKrvydeavDKAKEALNKatgqnltaeEVIKLNDAVTAAKQAL----NGEERLNNRKSEALQRLDQLTHLNNAQR 9418
Cdd:pfam15921 502 tASLQEK-------ERAIEATNA---------EITKLRSRVDLKLQELqhlkNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9419 QLAiQQINNAETLNKASRAINRAVQLDDAMgaVQQYIDEHHLDVISSTNYINADDNLKANYDNAITNAahELDKVQgsaI 9498
Cdd:pfam15921 566 ILR-QQIENMTQLVGQHGRTAGAMQVEKAQ--LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVK---L 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9499 AKAEAEQLKQhIIDAQKalNGDQNLATAKDKANafvdTLNGLNQQQQDLAHQAINNADTVTGIANIINDQidLNNAMETL 9578
Cdd:pfam15921 638 VNAGSERLRA-VKDIKQ--ERDQLLNEVKTSRN----ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ--LKSAQSEL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9579 khlvdneiptaEQTVNYQNADDVAKSNfddAKRLANAL---INSDNTNVNDINGAIQAVKDVIQNLNGEQR-LQEAKDKA 9654
Cdd:pfam15921 709 -----------EQTRNTLKSMEGSDGH---AMKVAMGMqkqITAKRGQIDALQSKIQFLEEAMTNANKEKHfLKEEKNKL 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9655 IQNVNKVLADKLK---EIEASNATDQdKLIAKNKAEELAnsiinnINKATsnqdvsrVQTAGNQAIEQVHANEIPKAKID 9731
Cdd:pfam15921 775 SQELSTVATEKNKmagELEVLRSQER-RLKEKVANMEVA------LDKAS-------LQFAECQDIIQRQEQESVRLKLQ 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9732 ANKDVdKQVQAlideidrnPNLTdkEKQALKDRINQ--ILQQGHNGINNAMTKEEIEHAKAQLAQALqdikdlvkaKENA 9809
Cdd:pfam15921 841 HTLDV-KELQG--------PGYT--SNSSMKPRLLQpaSFTRTHSNVPSSQSTASFLSHHSRKTNAL---------KEDP 900
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 616687517 9810 KQDVDKQVQALIDEIDRNPNLTDKEKQ---------ALKDRINQ 9844
Cdd:pfam15921 901 TRDLKQLLQELRSVINEEPTVQLSKAEdkgrapslgALDDRVRD 944
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
9018-9072 |
2.20e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9018 DQKLVRDQQQAVTTVNALPNLNHAQQQALTDAINAAPTRTEVAQHVQTATELDHA 9072
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3223-3277 |
2.27e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3223 QQNLQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQAVNDIKQTTQSLNTA 3277
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9256-9315 |
2.34e-06 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 48.71 E-value: 2.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9256 ILNAKQALNGDERVALAKTNGKHDIDQLNALNNAQQDGFKGRIDQSNDLNQIQQIVDEAK 9315
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8011-8065 |
2.36e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8011 EAKLATEKQNAKDAVNAMTHLNDAQKQALNGQIDQSPEIATVTQVKQTATSLDQA 8065
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5044-5112 |
2.44e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 48.85 E-value: 2.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5044 TALKAAIADKERTKASGNYVNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAAKTALN 5112
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5366-5420 |
2.52e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.52e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5366 DAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQQLDGA 5420
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4611-4664 |
2.60e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 48.31 E-value: 2.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 4611 HNLTQAKQTATNAIDGAANLNKAQKDALKAQVTSAQRVANVTSIQQTANELNTA 4664
Cdd:pfam01468 2 QKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
8789-9084 |
2.65e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8789 PQRQALENQINNAATR--GEVAQKLTEaQALNQAMEALrNSIQDQQQ-TEAGSKFInEDKPQK-DAYQAAVQHAKDLINQ 8864
Cdd:PRK11281 36 PTEADVQAQLDALNKQklLEAEDKLVQ-QDLEQTLALL-DKIDRQKEeTEQLKQQL-AQAPAKlRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8865 TSNPTLDKAQVEQLTQAVNQAKDNLHGDQKladdkqhavtDLNQLNGL----------------NNPQR-QALESQINN- 8926
Cdd:PRK11281 113 ETRETLSTLSLRQLESRLAQTLDQLQNAQN----------DLAEYNSQlvslqtqperaqaalyANSQRlQQIRNLLKGg 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8927 ----AATRDEVAQKL-AEAKALNQAMEALRNSIQDQQQ-TESGSKFINEDKPQKDAYQAAVQHAKDLINQTgnpTLDKSQ 9000
Cdd:PRK11281 183 kvggKALRPSQRVLLqAEQALLNAQNDLQRKSLEGNTQlQDLLQKQRDYLTARIQRLEHQLQLLQEAINSK---RLTLSE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9001 vEQLTQAVATAKDNLHGDQKLVRDQQQAvttvnalpnlNHAQQQALTDAINAAPTRTEvaQHVQTATELDHAMETLKNKV 9080
Cdd:PRK11281 260 -KTVQEAQSQDEAARIQANPLVAQELEI----------NLQLSQRLLKATEKLNTLTQ--QNLRVKNWLDRLTQSERNIK 326
|
....
gi 616687517 9081 DQVN 9084
Cdd:PRK11281 327 EQIS 330
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6877-6931 |
3.01e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.92 E-value: 3.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6877 DRKVTDAKNNANQTLSTLDNLNNAQKGAVTGNINQAHTVAEVTQAIQTAQELNTA 6931
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4162-4230 |
3.09e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 48.47 E-value: 3.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4162 KGLRDSIANETTVKAGQNYTDASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAATQVNNAKNGLN 4230
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4415-4482 |
3.25e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 48.47 E-value: 3.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 4415 KLQNGINDKANTLASENYHDADSDKKTAYTQAVTNAENILNKNSGSNLDKAAVENALSQVTNAKGALN 4482
Cdd:pfam07554 2 ALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
9714-9952 |
3.67e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9714 NQAIEQVHAneiPKAKIDAnkdVDKQVQALIDEIdrnpnltdKEKQALKDRINQILQQghnginnamTKEEIEHAKAQLA 9793
Cdd:COG1340 32 DELNEELKE---LAEKRDE---LNAQVKELREEA--------QELREKRDELNEKVKE---------LKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9794 QALQDIKDL---VKAKENAKQDVD---KQVQALIDEIDRNPNLTDKEKQaLKDRINQILQQGHnginnamTKEEIEQAKA 9867
Cdd:COG1340 89 ELREELDELrkeLAELNKAGGSIDklrKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKELE-------KAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9868 QLAQALQDIKDLVKAKEDAKNAIKALANE---KRDQINSNpdltpEQKAKAL-KEIDEAEKRALENIENAqtkDQLNKGL 9943
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEaqeLHEEMIEL-----YKEADELrKEADELHKEIVEAQEKA---DELHEEI 232
|
....*....
gi 616687517 9944 NLGLDDIRN 9952
Cdd:COG1340 233 IELQKELRE 241
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7633-7687 |
3.77e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.92 E-value: 3.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7633 NDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDAAQTVANVNTNKQTAQDLNQA 7687
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2557-3293 |
3.96e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2557 KTEAQQVINNERATPQQVSDALTKVRAAQTKID-QAKALLQNKEDNSQLvtSKNNLQSSVNQVPSTtgmtQQSIDNYNAK 2635
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLErQAEKAERYKELKAEL--RELELALLVLRLEEL----REELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2636 KRDAESEITAAQRVIDNGDATAQQISDEKRRVDNALTALNQAKHDLTADTHALEQ-----------AVQQLNRTGITTGK 2704
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqkqilrerlanLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2705 KPASITAYNNSIRALQSDLTSAKN----------SANAIIQKPIRSVQEVQTALTNVNRVNERLTQAINQLvpladNSAL 2774
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEelesleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-----NNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2775 RTAKTKLdEEINKSV--TTDGMTQSSIQAYENAKRAGQTESTNAQNVINNGDATDQQIAAEKTKVEEKYNSLKQAIDGLT 2852
Cdd:TIGR02168 403 ERLEARL-ERLEDRRerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2853 PDLAPLQTAKTQLQNDID-----------------QPTNTTGMTSASVaTFNEKLSAArtkiqeIDRVLASHPDVATIRq 2915
Cdd:TIGR02168 482 RELAQLQARLDSLERLQEnlegfsegvkallknqsGLSGILGVLSELI-SVDEGYEAA------IEAALGGRLQAVVVE- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2916 NVTAANAAKSALDQARNG------LTVDKAPLENAKNQLqhSIDTQTSTTGMTQDSINaYNAKLTAArnkvqqINQVLAG 2989
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDRE--ILKNIEGFLGVAKDLVK-FDPKLRKA------LSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2990 SPTVDQIntnTSAANQAKS------------DLDHARQALTPDKAPLQNAKTQLEQSINQPTDTTGMTTASLNAYNQKLQ 3057
Cdd:TIGR02168 625 VLVVDDL---DNALELAKKlrpgyrivtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3058 AARQKLTEINQVLngnptvqkiNDKVTEANQAKDQLNTARQGLTLDRQPAlSTLHGASNLNQAQQNNFTQQINA-----A 3132
Cdd:TIGR02168 702 ELRKELEELEEEL---------EQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLSKELTELEAEIEEleerlE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3133 QNHAALETIKSNITALNNAMTKLKESVADNNSIKSGQNytDATQANKQAYDNAVNAAKGVIGETNNPTMDVNTVNQKASS 3212
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3213 VKSTQDALDGQQN-LQRAKTEATNAITHASDLNQAQKNALTQQVNSAQNVQA-VNDIKQTTQSLNTAMTGLKRGVANHNQ 3290
Cdd:TIGR02168 850 LSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELSEeLRELESKRSELRRELEELREKLAQLEL 929
|
...
gi 616687517 3291 VVQ 3293
Cdd:TIGR02168 930 RLE 932
|
|
| YSIRK_signal |
pfam04650 |
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ... |
5-30 |
4.07e-06 |
|
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 428049 [Multi-domain] Cd Length: 26 Bit Score: 46.99 E-value: 4.07e-06
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5926-5994 |
4.15e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 48.08 E-value: 4.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5926 SNLQNGINDEAATKAAQKYTDADSDKQTAYNDAVTAAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALN 5994
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4106-4160 |
4.33e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.53 E-value: 4.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4106 DERLREAKQNANTAIDALTQLNTPQKAKLKEQVGQANRLEDVQTVQTNGQALNNA 4160
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3605-3656 |
4.63e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.53 E-value: 4.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 616687517 3605 LDQAKQTAKQQLNNMTHLTPAQKTNLTNQINSGTTVAGVHTVQSNANTLDQA 3656
Cdd:pfam01468 4 LAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7885-7939 |
4.73e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.53 E-value: 4.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7885 DEKLAQAKQDALANLDTLRDLNQPQRDALRNQINQAQALATVEQTKQNAQNVNTA 7939
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4862-4916 |
5.16e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.53 E-value: 5.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4862 AENLRNAKTTATNTINGLPHLTQLQKDNLKHQVEQAQNVAGVNGVKDKGNTLNTA 4916
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8275-9161 |
5.40e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8275 NRLDQLdhlnNAQKQQLQSQITQSSDIaavngHKQTAESLNTAMGNLINAIADHQAVEQRgnfINADTDKQTAYTTAVNE 8354
Cdd:TIGR02168 232 LRLEEL----REELEELQEELKEAEEE-----LEELTAELQELEEKLEELRLEVSELEEE---IEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8355 AEAMINKQtgqNANQTEVEQAITKVQTTLQALngDHNLQVAKTNATQAIDALTSLNdPQKTALKDQVTAAT-----LVTA 8429
Cdd:TIGR02168 300 LEQQKQIL---RERLANLERQLEELEAQLEEL--ESKLDELAEELAELEEKLEELK-EELESLEAELEELEaeleeLESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8430 VHQIEQNANTLNQAMHGLRESIQDNAATKANskyiNEDQPEQQNydQAVQAANNIINEQTATLDNNVINQAATTVNTTKA 8509
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIER----LEARLERLE--DRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8510 ALHGDV-----------KLQNDKDHAKQAV----SQLAHLNNAQKHMEDTLIDSETTRTAVNHDLTEAQALDQLMDALQQ 8574
Cdd:TIGR02168 448 ELEELQeelerleealeELREELEEAEQALdaaeRELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8575 SIadkdatrassayvNAEPNKKQAYDEAVQnaesiiAGLNNPTINkgNVTSATQAVTSSKNALDG-----VERLAQDKQT 8649
Cdd:TIGR02168 528 LI-------------SVDEGYEAAIEAALG------GRLQAVVVE--NLNAAKKAIAFLKQNELGrvtflPLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8650 AGNSLNHLDQLTPAQQQA---------LENQINNATTRDKVAEIIAQAQALNEAMKALKESIKDQPQTEASSKFINEDQA 8720
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAkdlvkfdpkLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8721 QKDAYTQAVQhaKDLINKTTDPTLVKSVIDQATQAVNDAKNNLHGDQKLAQDKQRATETLNNLSNLNTPQRQALENQINN 8800
Cdd:TIGR02168 667 KTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8801 aatrgeVAQKLTEAQALNQAMEALRNSIQDQqqteagskfINEDKPQKDAyqaavqhakdlinqtsnptlDKAQVEQLTQ 8880
Cdd:TIGR02168 745 ------LEERIAQLSKELTELEAEIEELEER---------LEEAEEELAE--------------------AEAEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8881 AVNQAKDNLHGDQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKlaEAKALNQAMEALRNSIQDQQQt 8960
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIEELEE- 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8961 esgskfinedkpQKDAYQAAVQHAKDlinqtgnptldksQVEQLTQAVATAKDNLhgdQKLVRDQQQAVTTVNALPNLNH 9040
Cdd:TIGR02168 867 ------------LIEELESELEALLN-------------ERASLEEALALLRSEL---EELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9041 AQQQALTDAINA-APTRTEVAQHVQTATEldHAMETLKNKVDQVNTDKAQPNYTEASTDK-KDAVDQ-------ALQAAQ 9111
Cdd:TIGR02168 919 ELREKLAQLELRlEGLEVRIDNLQERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRlENKIKElgpvnlaAIEEYE 996
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 616687517 9112 SITDPTNGSNANKYAVEQALTKLQGKENELNgnervAEAKTQAKQTIDQL 9161
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEID-----REARERFKDTFDQV 1041
|
|
| YSIRK_signal |
TIGR01168 |
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ... |
2-42 |
5.91e-06 |
|
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 273479 [Multi-domain] Cd Length: 39 Bit Score: 46.71 E-value: 5.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 616687517 2 NYRDKIQKFSIRKYTVGTFSTVIATLVFLGlntsQAQAAET 42
Cdd:TIGR01168 3 KFNEKQQKYSIRKLSVGVASVLVASLFFGG----GVAAAES 39
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7941-8009 |
6.08e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.70 E-value: 6.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7941 SNLKQGIANKDTVKASENYHDADADKQTAYTNAVSQAEGIINQTTNPTLNPDDITRVLTQVTDAKNGLN 8009
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3910-3978 |
6.26e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.70 E-value: 6.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 3910 GNLQTAINDKSGTLASQNFLDADEQKRNAYNQAVSNAETILNKQTGPNTAKTAVEQALNNVNSAKHALN 3978
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7004-7057 |
6.66e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 47.15 E-value: 6.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 7004 QNLEKAKQHANTAIDGLSHLTNAQKDALKQLVQQSTTVAEAQGNEQKANNVDAA 7057
Cdd:pfam01468 2 QKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5114-5167 |
7.87e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.76 E-value: 7.87e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 5114 DNNLRVAKEHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQTLNT 5167
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNN 54
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
9579-9936 |
7.88e-06 |
|
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: 53.32 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9579 KHLVDNEIPTAEQTVnYQNADDVAKSNFDDAKRLANALinsdNTNVNDINGAIQAVKDVIQNLNG---EQRL--QEAKDK 9653
Cdd:pfam06160 55 DDIVTKSLPDIEELL-FEAEELNDKYRFKKAKKALDEI----EELLDDIEEDIKQILEELDELLEseeKNREevEELKDK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9654 aIQNVNKVLADK-------LKEIEASNATDQDKLiakNKAEELANSiiNNINKATSNQDVSRVQTagnQAIEQVhANEIP 9726
Cdd:pfam06160 130 -YRELRKTLLANrfsygpaIDELEKQLAEIEEEF---SQFEELTES--GDYLEAREVLEKLEEET---DALEEL-MEDIP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9727 KAKIDANKDVDKQVQALIDEIDR----NPNLT----DKEKQALKDRINQILQQGHNGinnamtkeEIEHAKAQLAQALQD 9798
Cdd:pfam06160 200 PLYEELKTELPDQLEELKEGYREmeeeGYALEhlnvDKEIQQLEEQLEENLALLENL--------ELDEAEEALEEIEER 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9799 IKDLVKAKE---NAKQDVDKQVQALIDEIDRnpnlTDKEKQALK---DRINQILQQGHNGINNAM-TKEEIEQAKAQLAQ 9871
Cdd:pfam06160 272 IDQLYDLLEkevDAKKYVEKNLPEIEDYLEH----AEEQNKELKeelERVQQSYTLNENELERVRgLEKQLEELEKRYDE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 9872 ALQDIKDLVKA----KEDAKNAIKALANEKRDQINSNpdltpeqkaKALKEIDEAEKRALENIENAQTK 9936
Cdd:pfam06160 348 IVERLEEKEVAyselQEELEEILEQLEEIEEEQEEFK---------ESLQSLRKDELEAREKLDEFKLE 407
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6807-6875 |
8.16e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 8.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6807 ERLINGIQDKDQVKQSVNFTDADPEKQTAYNNAVTAAENIINQANGTNENQSQVEAALSTVTTTKQALN 6875
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8263-8317 |
8.19e-06 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.76 E-value: 8.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 8263 DENLAAAKQQANNRLDQLDHLNNAQKQQLQSQITQSSDIAAVNGHKQTAESLNTA 8317
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9510-9566 |
8.70e-06 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 46.78 E-value: 8.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 9510 IIDAQKALNGDQNLATAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIIN 9566
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQ 57
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7563-7631 |
8.91e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 8.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7563 TNLSNALQDKTETLNSINFTDADKAKKDAYTNAVAQAEGILSKANGSNASQTEVEQAMQRVNAAKQALN 7631
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6916-7682 |
8.95e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6916 AEVTQAIQTAQELNTAMGNLKNSLNDKDTTLGSQNFADADPEKKNAYNEAVRnaENILNKstgtnvpKDQVEAAMNQVNT 6995
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL--EELESK-------LDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6996 TKAALNGSQNLEKAKQhaNTAIDGLSHLTNAQKDALKQLVQQSTTVAEAQGNEQKANNVDAAMDKLRQSIADNAtTKQNQ 7075
Cdd:TIGR02168 345 KLEELKEELESLEAEL--EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR-ERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7076 NYTDASPNKKDAYNNAVttaqgiidQTTSPTLDPtVINQAAGQVSTTKNALNGNENLEAAKQQATQSL-GSLDNLNNAQK 7154
Cdd:TIGR02168 422 EIEELLKKLEEAELKEL--------QAELEELEE-ELEELQEELERLEEALEELREELEEAEQALDAAeRELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7155 QAVTNQINGAHTVDEANQIKQNAQNLNTAMGNLKQAIadkdatkaTVnftdadqakQQAYNTAvtndeniISKANGGNAT 7234
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI--------SV---------DEGYEAA-------IEAALGGRLQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7235 QTEVEQAiqqvNTAKQALngNANVQHAKDEATALINNSNDLNQAQKDALkQQVQNATTVAGV-NNVKQTAQELNNAM--- 7310
Cdd:TIGR02168 549 AVVVENL----NAAKKAI--AFLKQNELGRVTFLPLDSIKGTEIQGNDR-EILKNIEGFLGVaKDLVKFDPKLRKALsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7311 -------TQLKQGIADKEQTKADGNFVNADPDkqnaykqaVAKAEALISGTPDVVVTpseitaalnkvtqakNDLNGNTN 7383
Cdd:TIGR02168 622 lggvlvvDDLDNALELAKKLRPGYRIVTLDGD--------LVRPGGVITGGSAKTNS---------------SILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7384 LATAKQNVQHAIDQLPNLnQAQRDEYSKQITQATlvpnvNAIQQAATTLNDAMTQLKQGianKAQIKGSENYHDADTDKQ 7463
Cdd:TIGR02168 679 IEELEEKIEELEEKIAEL-EKALAELRKELEELE-----EELEQLRKELEELSRQISAL---RKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7464 TAYDNAVTKAEEllkqttnptmdpnTIQQALTKVNdtnqalngnqKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAP 7543
Cdd:TIGR02168 750 AQLSKELTELEA-------------EIEELEERLE----------EAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7544 DI-ATVNNVKQNAQNLNNAMTNLSNALQDKTETLnsinfTDADKAKKDAYTNAVAQAEGILSKANGSNASQTEVEQAMQR 7622
Cdd:TIGR02168 807 ELrAELTLLNEEAANLRERLESLERRIAATERRL-----EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 7623 VNAAKQALngndnvHRAKDAAKQVITNANDLNQaQKDALKQQVDAAQT-VANVNTNKQTAQ 7682
Cdd:TIGR02168 882 RASLEEAL------ALLRSELEELSEELRELES-KRSELRRELEELREkLAQLELRLEGLE 935
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8067-8135 |
9.08e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 9.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8067 NQLSQAINDKTQTLADGNYLNADPDKQNAYKQAVAKAEALLNKQSGTNEVQAQVESITNEVNAAKQALN 8135
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3658-3726 |
9.63e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 9.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 3658 NTLRQSIANKDATKASEDYVDANNDKQTAYNNAVAAAETIINANSNPEMNPSTITQKADQVNSSKTALN 3726
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3406-3474 |
9.73e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 47.31 E-value: 9.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 3406 GNLRQAVADKDQVKRTEDYADADTAKQNAYNSAVSSAETIINQTTNPTMSVNDVNSATSAVTTNKNALN 3474
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8822-8890 |
9.92e-06 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.93 E-value: 9.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8822 EALRNSIQDQQQTEAGSKFINEDKPQKDAYQAAVQHAKDLINQTSNPTLDKAQVEQLTQAVNQAKDNLH 8890
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8696-8764 |
1.05e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.93 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8696 KALKESIKDQPQTEASSKFINEDQAQKDAYTQAVQHAKDLINKTTDPTLVKSVIDQATQAVNDAKNNLH 8764
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
7381-7435 |
1.07e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.38 E-value: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7381 NTNLATAKQNVQHAIDQLPNLNQAQRDEYSKQITQATLVPNVNAIQQAATTLNDA 7435
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5298-5364 |
1.17e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.93 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 5298 LQNGINDETQTKQTQKYLDAEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQALQNVNSTKTALN 5364
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6933-7001 |
1.40e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.54 E-value: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6933 GNLKNSLNDKDTTLGSQNFADADPEKKNAYNEAVRNAENILNKSTGTNVPKDQVEAAMNQVNTTKAALN 7001
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6625-6679 |
1.40e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 46.38 E-value: 1.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6625 DTNLATAKQQAKDALRQMTHLSNAQKQSITGQIDSATQVTGVQSVKDNATNLDNA 6679
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8596-9027 |
1.54e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8596 KQAYDEAVQNAESIIAgLNNPTINKGNvTSATQAVTSSKNALDGVERLAQDKQTAGNSLNhldqLTPAQQQAL-ENQINN 8674
Cdd:pfam15921 337 KRMYEDKIEELEKQLV-LANSELTEAR-TERDQFSQESGNLDDQLQKLLADLHKREKELS----LEKEQNKRLwDRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8675 ATTRDKVAEII----AQAQALNEAMKALKESIKDQPQTE-ASSKFINEDQAQKDAYTQAVQHAKDLINKTTDP-TLVKSV 8748
Cdd:pfam15921 411 SITIDHLRRELddrnMEVQRLEALLKAMKSECQGQMERQmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEElTAKKMT 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8749 IDQATQAVNDAKNNLhgdqklaQDKQRATETLN-------NLSNLNTPQRQALENQ---INNAATRGEvAQKLTEAQAlN 8818
Cdd:pfam15921 491 LESSERTVSDLTASL-------QEKERAIEATNaeitklrSRVDLKLQELQHLKNEgdhLRNVQTECE-ALKLQMAEK-D 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8819 QAMEALRNSIQDQQQ------TEAGS---------KFIN-------EDKPQKDAYQAAVqhaKDLINQTSNPTLDKAQVe 8876
Cdd:pfam15921 562 KVIEILRQQIENMTQlvgqhgRTAGAmqvekaqleKEINdrrlelqEFKILKDKKDAKI---RELEARVSDLELEKVKL- 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8877 qltqaVNQAKDNLHGDQKLADDKQHAVTDL----NQLNGLNNpQRQALESQINNAATRDEVA-QKLA-EAKALNQAMEAL 8950
Cdd:pfam15921 638 -----VNAGSERLRAVKDIKQERDQLLNEVktsrNELNSLSE-DYEVLKRNFRNKSEEMETTtNKLKmQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8951 RNSIQDQQQTESGS--------KFINEDKPQKDAYQAAVQHAKDLINQTGNPTL----DKSQVEQLTQAVATAKDNLHGD 9018
Cdd:pfam15921 712 RNTLKSMEGSDGHAmkvamgmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHflkeEKNKLSQELSTVATEKNKMAGE 791
|
....*....
gi 616687517 9019 QKLVRDQQQ 9027
Cdd:pfam15921 792 LEVLRSQER 800
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7311-7379 |
1.68e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.54 E-value: 1.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7311 TQLKQGIADKEQTKADGNFVNADPDKQNAYKQAVAKAEALISGTPDVVVTPSEITAALNKVTQAKNDLN 7379
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4358-4412 |
1.92e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 45.99 E-value: 1.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4358 DQNVTNAKNAAKNALNNLTSINNAQKRDLTTKIDQATTVAGVEAVSNTGTQLNTA 4412
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6373-6427 |
1.94e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 45.99 E-value: 1.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6373 DANVRQAKSDAKANLGTLTHLNNAQKQDLTSQIEGVTTVNGVNGVKTKAQDLDGA 6427
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8790-9408 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8790 QRQALEnQINNAATRgevAQKLTEAQALNQAMEALRNSIQDQQQTEAGSKFINEDKPQKDAYQAAVQHAKDLINQTsnpt 8869
Cdd:COG4913 250 QIELLE-PIRELAER---YAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL---- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8870 ldKAQVEQLTQAVNQAKdnlhGDQK--LADDKQHAVTDLNQLNGlnnpQRQALESQINNA-----ATRDEVAQKLAEAKA 8942
Cdd:COG4913 322 --REELDELEAQIRGNG----GDRLeqLEREIERLERELEERER----RRARLEALLAALglplpASAEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8943 LNQAMEALRNSIQD------------QQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQ-TGNPTLD----------KS 8999
Cdd:COG4913 392 LLEALEEELEALEEalaeaeaalrdlRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAElpfvgelievRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9000 QVEQLTQAVATAkdnLHGdQK---LVRDQQQAvttvnalpnlnhaqqqALTDAINAAPTRTEV-AQHVQTATELDHAME- 9074
Cdd:COG4913 472 EEERWRGAIERV---LGG-FAltlLVPPEHYA----------------AALRWVNRLHLRGRLvYERVRTGLPDPERPRl 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9075 ---TLKNKVDqVNTDKAQPnYTEASTDKK------DAVDQALQAAQSITDptngsnankyaveQALTKLQGKENELNGNE 9145
Cdd:COG4913 532 dpdSLAGKLD-FKPHPFRA-WLEAELGRRfdyvcvDSPEELRRHPRAITR-------------AGQVKGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9146 RVAEAKtqakqtidQLTHLNADQIATAKQNIDQATKLqpIAELVDQATQLNQSMDQLQQAVNEHANVEQtvdYTQADLDK 9225
Cdd:COG4913 597 RIRSRY--------VLGFDNRAKLAALEAELAELEEE--LAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9226 QnAYKQAIAEAENVLKQ-NANKQQVDQALQNILNAKQALNG--DERVALAKTNGKHDiDQLNALnNAQQDGFKGRIDQSN 9302
Cdd:COG4913 664 A-SAEREIAELEAELERlDASSDDLAALEEQLEELEAELEEleEELDELKGEIGRLE-KELEQA-EEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9303 DLNQIQQI---------VDEAKALNRAMNQLSQEITGNEGRTKGSTN-YVNADTQVKRVYD------------------- 9353
Cdd:COG4913 741 DLARLELRalleerfaaALGDAVERELRENLEERIDALRARLNRAEEeLERAMRAFNREWPaetadldadleslpeylal 820
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9354 ----------EAVDKAKEALNKATGQNLTaEEVIKLNDAVTAAKQALngeERLNnrksEALQRLD 9408
Cdd:COG4913 821 ldrleedglpEYEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI---DPLN----DSLKRIP 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9230-9904 |
2.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9230 KQA-IAEAENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTNGKHDIDQLNALNNAQQDGFKGRIDQSNDlnQIQ 9308
Cdd:COG1196 207 RQAeKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9309 QIVDEAKALNRAMNQLSQEITGNEGRTKgstnyvNADTQVKRVYDEAVDKAKEALNKATGQNLTAEEVIKLNDAVTAAKQ 9388
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRR------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9389 ALNG-EERLNNRKSEALQRLDQLTHLNNAQRQLAIQQINNAETLNKASRAINRAVQLDDAMGAVQQYIDEHHLDVISstn 9467
Cdd:COG1196 359 ELAEaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE--- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9468 yinADDNLKANYDNAITNAAHELDKVQGSAIAKAEAEQLKQHIIDAQKALNGDQNLATAKDKANAFVDTLNGLNQQQQDL 9547
Cdd:COG1196 436 ---EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9548 AHQAINNADTVTGIANIINDQIDLNNAMET-----LKHLVDNEIPTAEQTVNYQNADDVAKSNFDDAKRLANALINSDNT 9622
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9623 NVNDINGAIQAVKDviqnlngEQRLQEAKDKAIQNV----NKVLADKLKEIEASNATDQDKLIAKNKAEELANSiinnin 9698
Cdd:COG1196 593 ARGAIGAAVDLVAS-------DLREADARYYVLGDTllgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG------ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9699 katsnQDVSRVQTAGNQAIEQVHANEIPKAKIDANKDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQILQQghnginn 9778
Cdd:COG1196 660 -----GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE------- 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9779 amtkEEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALIDEIDRnpnltdkekqaLKDRINQIlqqghnG-IN-NA 9856
Cdd:COG1196 728 ----EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER-----------LEREIEAL------GpVNlLA 786
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9857 MtkEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKR-------DQINSN 9904
Cdd:COG1196 787 I--EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRerfletfDAVNEN 839
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7060-7127 |
2.22e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.16 E-value: 2.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 7060 KLRQSIADNATTKQNQNYTDASPNKKDAYNNAVTTAQGIIDQTTSPTLDPTVINQAAGQVSTTKNALN 7127
Cdd:pfam07554 2 ALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3476-3530 |
2.27e-05 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 45.61 E-value: 2.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3476 DEKLAQSKTDAASAIDALPHLNNAQKADVKSKINVASNIAGVNTVKQQGTDLNTA 3530
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
9129-9407 |
2.27e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9129 QALTKLQGKENELNgnERVAEAKTQAKQTIDQLTHLNAdQIATAKQNIDQatKLQPIAELVDQATQLNQSMDQLQQAVNE 9208
Cdd:COG1340 1 SKTDELSSSLEELE--EKIEELREEIEELKEKRDELNE-ELKELAEKRDE--LNAQVKELREEAQELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9209 HANVEQtvdytqadlDKQNAYKQAIAEAENVLKQNANKQQVDQALQNIlnaKQALNGDERVALAKTNGKHD-------ID 9281
Cdd:COG1340 76 LKEERD---------ELNEKLNELREELDELRKELAELNKAGGSIDKL---RKEIERLEWRQQTEVLSPEEekelvekIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9282 QLNALNNAQQDGFKGRIDQSNDLNQIQQIVDEAKALNRAMNQLSQEItgNEGRTKGSTNYVNADTQVKRV--YDEAVDKA 9359
Cdd:COG1340 144 ELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEA--QELHEEMIELYKEADELRKEAdeLHKEIVEA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9360 KEALNKATGQ-NLTAEEVIKLNDAVTAAKQALNGEER------LNNRKSEALQRL 9407
Cdd:COG1340 222 QEKADELHEEiIELQKELRELRKELKKLRKKQRALKRekekeeLEEKAEEIFEKL 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9727-9901 |
2.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9727 KAKIDAnkdVDKQVQALIDEIDRnpnlTDKEKQALKDRINQILQQGH----------NGINNAMTKEEIEHAKAQLAQAL 9796
Cdd:COG4913 609 RAKLAA---LEAELAELEEELAE----AEERLEALEAELDALQERREalqrlaeyswDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9797 QDIKDLVKAKENAKQdVDKQVQALIDEIDRnpnlTDKEKQALKDRINQI------LQQGHNGINNAMTKEEIEQAKAQLA 9870
Cdd:COG4913 682 ASSDDLAALEEQLEE-LEAELEELEEELDE----LKGEIGRLEKELEQAeeeldeLQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190
....*....|....*....|....*....|...
gi 616687517 9871 QALQD--IKDLVKAKEDAKNAIKALANEKRDQI 9901
Cdd:COG4913 757 AALGDavERELRENLEERIDALRARLNRAEEEL 789
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4666-4734 |
2.37e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 46.16 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4666 GQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQVTSTKDALN 4734
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
9090-9371 |
2.77e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9090 PNYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKEnelngneRVAEAKTQAKQTIDQLThlnaDQI 9169
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKID-------RQKEETEQLKQQLAQAP----AKL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9170 ATAKQNIDqatKLQPIAELVDQATQLNQSMDQLQQAVNEHANVEQTVdytQADLDKQNAykQAIA------EAENVLKQN 9243
Cdd:PRK11281 97 RQAQAELE---ALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNA---QNDLAEYNS--QLVSlqtqpeRAQAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9244 -ANKQQVDQALQNILNAKQALNGDERVAL----AKTNGKHD--------IDQLNALNNAQQDGFKGRIDQSNDLNQIQQI 9310
Cdd:PRK11281 169 sQRLQQIRNLLKGGKVGGKALRPSQRVLLqaeqALLNAQNDlqrkslegNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 9311 VDEAKALNRAMNQLSQEITGNEGRTKGSTNYVNADTQVKRVYDEAVDKAKEALNKATGQNL 9371
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNL 309
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
4166-4735 |
3.05e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 51.69 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4166 DSIANETTVKAGQNYTDASPNNQSTYNSAVSNAKGIINQTNNPTMDASAITQAATQVNNAKNGLNGAENLRNAQNTAKQN 4245
Cdd:COG5295 37 QSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASSVASGGASAATAASTGTGNTAGTAATVAGAASSGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4246 LNTLSHLTNNQKSAISSQIDRAGHVSEVTAAKNAATelnTQMGNLEQAIHDQNTVKQSVKFTDADKAKRDAYTNAVSRAE 4325
Cdd:COG5295 117 ATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAG---GSNTATATGSSTANAATAAAGATSTSASGSSSGASGAAAAS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4326 TILNKTQGANTPKQDVEASIQNVSSAKNALNGDQNVTNAKNAAKNALNNLTSINNAQKRDLTTKIDQATTVAGVEAVSNT 4405
Cdd:COG5295 194 AATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSASAGAASGNATTASASSVSGSAVAAGTASTATTAS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4406 GTQLN--TAMAKLQNGINDKANTLASENYHDADSDKKTAYTQAVTNAENILNKNSGSNLDKAAVENALSQVTNAKGALNG 4483
Cdd:COG5295 274 TTAASgaAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTASGASAAAATNDGTANGAG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4484 NHNLEQAKSNANTTINGLQHLTTAQKDKLKQQVQQAQNVAGVDTVKSSANTLNGAMGTLRNSIQDNAATKNGQNYLDATE 4563
Cdd:COG5295 354 TSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4564 SNKTNYNNAVDSANSVINATSNPNMDANAINQIATQVTSTKNALDGTHNLTQAKQTATNAIDGAANLNKAQKDALKAQVT 4643
Cdd:COG5295 434 GASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSA 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4644 SAQRVANVTSIQQTANELNTAMGQLQHGIDDENATKQTQKYRDAEQSKKTTYDQAVAAAKAILNKQTGSNSDKAAVDRAL 4723
Cdd:COG5295 514 AAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANSVALGAGSVASGANSVSVGAAGAENV 593
|
570
....*....|..
gi 616687517 4724 QQVTSTKDALNG 4735
Cdd:COG5295 594 AAGATDTDAVNG 605
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3532-3600 |
3.12e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.77 E-value: 3.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 3532 GNLQGAINDEQTTLNSQNYQDATPSKKTAYTNAVQAAKDILNKSNGQNKTKDQVTEVMNQVDSAKTNLD 3600
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6681-6749 |
3.15e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.77 E-value: 3.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6681 NQLRNSIANKDEVKASQPYVDGDTDKQNAYNTAVTSAENIINATSQPTLDPSAVTQAANQVNTNKTALN 6749
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5800-5868 |
3.45e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.77 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5800 TNLKNGIQDQNTIKQGVNFTDADEAKRNAYTNAVTQAEQILNKAQGPNTAKDGVETALQNVQRAKNDLN 5868
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8319-8387 |
3.45e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.77 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8319 GNLINAIADHQAVEQRGNFINADTDKQTAYTTAVNEAEAMINKQTGQNANQTEVEQAITKVQTTLQALN 8387
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4792-4860 |
3.69e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.39 E-value: 3.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4792 NSLQGSINDKDATLRNQNYLDADESKRNAYTQAVTAAEGILNKQTGGNTSKADVDNALNAVTRAKTALN 4860
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4540-4608 |
4.03e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.39 E-value: 4.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4540 GTLRNSIQDNAATKNGQNYLDATESNKTNYNNAVDSANSVINATSNPNMDANAINQIATQVTSTKNALD 4608
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
7125-7404 |
4.65e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 50.93 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7125 ALNGNENLEAA-KQQATQSLGSLDNL--NNAQKQAVTNQING-AHTVDEANQIKQNAQNLNTAMG----NLKQAIADkda 7196
Cdd:pfam18971 526 ATNGVSHLEAGfNKVAVFNLPDLNNLaiTSFVRRNLENKLTAkGLSLQEANKLIKDFLSSNKELAgkalNFNKAVAE--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7197 TKATVNFTDADQAkQQAYNTAVTNDENIiskanggnatQTEVEQAIQQVNTAKQALNGNANVQHAKDEATALINnsndln 7276
Cdd:pfam18971 603 AKSTGNYDEVKKA-QKDLEKSLRKREHL----------EKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALIN------ 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7277 qaqkdalKQQVQNATTVAGVNNVKQTAQELNNAMTQLKQGIadKEQTKADGNFVNAdpdKQNAYKQAVAKAEALISGTPD 7356
Cdd:pfam18971 666 -------KEANRDARAIAYTQNLKGIKRELSDKLEKISKDL--KDFSKSFDEFKNG---KNKDFSKAEETLKALKGSVKD 733
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 7357 VVVTPSEIT------AALN-----------KVTQAKNDLNGNTNLATAKQNVQHAIDqlpNLNQA 7404
Cdd:pfam18971 734 LGINPEWISkvenlnAALNefkngknkdfsKVTQAKSDLENSVKDVIINQKVTDKVD---NLNQA 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9345-10166 |
4.80e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9345 DTQVKRVYDEAVDKAKEALNKATGQnltAEEVIKLNDAVTAAKQALNGEERlnnRKSEALQRLDQLTHLNNAQRQLAIQQ 9424
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARKAEEA---RKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9425 INNAETLNKASRAiNRAVQLDDAMGAVQQYIDEhhlDVISSTNYINADDNLKANYDNAITNAAHELDKVQGSAIAKAE-A 9503
Cdd:PTZ00121 1160 AEDARKAEEARKA-EDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEeA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9504 EQLKQHIIDAQKALNGDQNLATAKDKANAFVDTLNGLNQQQQDLAHQA-----------------INNADTVTGIANIIN 9566
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkkaeekkkadeakkaeeKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9567 DQIDLNNAMETLKHLVDNEIPTAEQTvnyQNADDVAKSNFDDAKRLANALINSDNTNVNDINGAIQAVKDVIQNLNGEQR 9646
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9647 LQEAKDKAIQNVNKvlADKLKEIEASNATDQDkliAKNKAEEL-----ANSIINNINKA----TSNQDVSRVQTAGNQAI 9717
Cdd:PTZ00121 1393 ADEAKKKAEEDKKK--ADELKKAAAAKKKADE---AKKKAEEKkkadeAKKKAEEAKKAdeakKKAEEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9718 EQVHANEIPKAKIDANKDVDKQVQAliDEIDRNPNLTDKEKQALKDRINQILQQGHNGINNAMTKEEIEHA-KAQLAQAL 9796
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKA--EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9797 QDIKDLVKAKENAK-QDVDKQVQALIDEIDRNPNLTDKE--KQALKDRINQILQQGHNGIN---NAMTKEEIEQAKAQLA 9870
Cdd:PTZ00121 1546 KKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKmkaEEAKKAEEAKIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9871 QALQDIKDLV-----KAKEDAKNAIKALANEKRDQINSNPDLTPEQ----KAKALKEIDEAEKRALENI----ENAQTKD 9937
Cdd:PTZ00121 1626 KKAEEEKKKVeqlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkKAEEAKKAEEDEKKAAEALkkeaEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9938 QLNKGLNLGLDDIRNTHVWEVDAQPAVNEIFDATPEQILVNGELIVHRDdiitEQDIHAHINLIDQLTAEIIDTPSTATI 10017
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10018 SDSLTAKVEV-----------------TLLDGSKVIVSVPVKVVEKELTVVKQQAIESieNAAQQKINEINNHA-TLTPE 10079
Cdd:PTZ00121 1782 EEELDEEDEKrrmevdkkikdifdnfaNIIEGGKEGNLVINDSKEMEDSAIKEVADSK--NMQLEEADAFEKHKfNKNNE 1859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10080 QKEAAIAEVNKLKqqaiEQINNAADVHTVEEVQhqeqaHIEQFNPDQFTIDQAKSNAIKSISDAIQHMIDEINASKDLTD 10159
Cdd:PTZ00121 1860 NGEDGNKEADFNK----EKDLKEDDEEEIEEAD-----EIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAE 1930
|
....*..
gi 616687517 10160 KEKQEAI 10166
Cdd:PTZ00121 1931 ETREEII 1937
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
6319-7995 |
4.85e-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: 51.31 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6319 VNFTDADQGKKDAYTNAVTNAQGILDKANGQNMTKAQVEAALNQVTTAKNALNGDANVRQAKSDAKAN-LGTLTHLNNAQ 6397
Cdd:COG3210 8 TTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSaSTGGIGAAAAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6398 KQDLTSQIEGVTTVNGVNGVKTKAQDLDGAMQRLESAIANKDQTKASENYIDADPTNKTAFDNAITQAESYLNKDHGANK 6477
Cdd:COG3210 88 TAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6478 DKQAVEQAIQSVTSTENALNGDANLQRAKTEATQAIDNLTHLNTPQKTALKQQVNAAQRVSGVTDLKNSATSLNSAMDQL 6557
Cdd:COG3210 168 SSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6558 KQAIADHDTIVAGGNYTNASPDKQGAYTDAYNAAKNIVNGSPNVITNAADVTAATQRVNNAETGLNGDTNLATAKQQAKD 6637
Cdd:COG3210 248 ISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6638 ALRQMTHLSNAQKQSITGQIDSATQVTGVQSVKDNATNLDNAMNQLRNSIANKDEVKASQPYVDGDTDKQNAYNTAVTSA 6717
Cdd:COG3210 328 GNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLAT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6718 ENIINATSQPTLDPSAVTQAANQVNTNKTALNGAQNLANKKQESTANINQLSHLNNAQKQDLNTQVTNAPNISTVNQVKT 6797
Cdd:COG3210 408 GNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6798 KAEQLDQAMERLINGIQDKDQVKQSVNFTDADPEKQTAYNNAVTAAENIINQANGTNENQSQVEAALSTVTTTKQALNGD 6877
Cdd:COG3210 488 GGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6878 RKVTDAKNNANQTLSTLDNLNNAQKGAVTGNINQAHTVAEVTQAIQTAQELNTAMGNLKNSLNDKDTTLGSQNFADADPE 6957
Cdd:COG3210 568 GVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTG 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6958 KKNAYNEAVRNAEN-ILNKSTGTNVPKDQVEAAMNQVNTTKAALNGSQNLEKAKQHANTAIDGLSHLTNAQKDALKQLVQ 7036
Cdd:COG3210 648 SGTTGTASANGSNTtGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7037 QSTTVAEAQGNEQKANNVDAAMDKLRQSIADNATTKQNQNYTDASPNKKDAYNNAVTTAQGIIDQTTSPTLDPTVINQAA 7116
Cdd:COG3210 728 DTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAA 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7117 GQVSTTKNALNGNENLEAAKQQATQSLGSLDNLNNAQKQAVTNQINGAHTVDEANQIKQNAQNLNTAMGNLKQAIADKDA 7196
Cdd:COG3210 808 GTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATS 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7197 TKATVNFTDADQAKQQAYNTAVTNDENIISKANGGNATQTEVEQAIQQVNTAKQALNGNANVQHAKDEATALINNSNDLN 7276
Cdd:COG3210 888 TGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTG 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7277 QAQKDALKQQVQNATTVAGVNNVKQTAQELNNAMTQLKQ-------GIADKEQTKADGNFVNADPDKQNAYKQAVAKAEA 7349
Cdd:COG3210 968 ASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTAsttggsgAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVG 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7350 LISGTPDVVVTPSEITAALNKVTQAKNDLNGNTNLATAKQNVQHAIDQLPNLNQAQRDEYSKQITQATLVPNVNAIQQAA 7429
Cdd:COG3210 1048 VNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTV 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7430 TTLNDAMTQLKQGIANKAQI--KGSENYHDADTDKQTAYDNAVTKAEELLKQTTNPTMDPNTIQQALTKVNDTNQALNGN 7507
Cdd:COG3210 1128 GATGTSTASTEAAGAGTLTGlvAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGS 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7508 QKLADAKQAAKTNLGTLDHLNDAQKQALTTQVEQAPDIATVNNVKQNAQNLNNAMTNLSNALQDKTETLNSINFTDADKA 7587
Cdd:COG3210 1208 TTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVD 1287
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7588 KKDAYTNAVAQAEGILSKANGSNASQTEVEQAMQRVNAAKQALNGNDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDA 7667
Cdd:COG3210 1288 IGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGS 1367
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7668 AQTVANVNTNKQTAQDLNQAMTQLKQGVADKDQTKANGNFVNADTEKQNAYNNAVAHAEQIISGTPNANVDPQQVAQALQ 7747
Cdd:COG3210 1368 GGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAG 1447
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7748 QVTDAKNGLNGNHNLQVAKDNANTAIDQLPNLNQPQKTALKDQVTHAELVTGVNAIKQNADALNNAMGTLKQQIQANSQV 7827
Cdd:COG3210 1448 AGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGG 1527
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7828 PQSVDFTQADQDKQQAYNNAANQAQQIANGTPTPVLTPDAVTQAVTTMNQAKDALNGDEKLAQAKQDALANLDTLRDLNQ 7907
Cdd:COG3210 1528 EGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNA 1607
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7908 PQRDALRNQINQAQALATVEQTKQNAQNVNTAMSNLKQGIANKDTVKASENYHDADADKQTAYTNAVSQAEGIINQTTNP 7987
Cdd:COG3210 1608 EYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAA 1687
|
....*...
gi 616687517 7988 TLNPDDIT 7995
Cdd:COG3210 1688 AGNVATGD 1695
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3153-3221 |
5.05e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 45.00 E-value: 5.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 3153 TKLKESVADNNSIKSGQNYTDATQANKQAYDNAVNAAKGVIGETNNPTMDVNTVNQKASSVKSTQDALD 3221
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5548-5616 |
6.91e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.62 E-value: 6.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5548 TALKRAIADKADTKASGNYVNADANKRQAYDEKVTAAENIVSGTPTPTLTPSDVTNAATQVTNAKTQLN 5616
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8571-8638 |
7.12e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.62 E-value: 7.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 8571 ALQQSIADKDATRASSAYVNAEPNKKQAYDEAVQNAESIIAGLNNPTINKGNVTSATQAVTSSKNALD 8638
Cdd:pfam07554 2 ALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4918-4986 |
7.19e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.62 E-value: 7.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4918 GALRTSIQNDNTTKTSQNYLDASDSNKNNYNTAVNNANGVINATNNPNIDANAINGMANQVNTTKAALN 4986
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2625-3042 |
8.04e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2625 TQQSIDNYNAKKRDAESEITAAQRVIDNGDATAQQISDEKRRVDNALTALNQAKHDLTADTHALEQAVQQLNRTgittgk 2704
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER------ 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2705 kpasitaynnsIRALQSDLTSAKNSANAIIQKPIRSVQEVQTALTNVNRVNERLTQAINQLvpladnSALRTAKTKLDEE 2784
Cdd:TIGR02168 749 -----------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------KALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2785 inksvttdgmtqssiqaYENAKRAGQTESTNAQNVINNGDATDQQIaaekTKVEEKYNSLKQAIDGLTPDLAPLQTAKTQ 2864
Cdd:TIGR02168 812 -----------------LTLLNEEAANLRERLESLERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2865 LQNDIDQPTNTTGMTSASVATFNEKLSAARTKIQEIDRvlashpDVATIRQNVTAANAAKSALDQARNGLTVDKAPL-EN 2943
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELES------KRSELRRELEELREKLAQLELRLEGLEVRIDNLqER 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2944 AKNQLQHSIDTQTSTTGMTQDSINAYNAKLTAARNKVQQINQVlagsptvdqintNTSAANQAKsDLDHARQALTPDKAP 3023
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV------------NLAAIEEYE-ELKERYDFLTAQKED 1011
|
410
....*....|....*....
gi 616687517 3024 LQNAKTQLEQSINQPTDTT 3042
Cdd:TIGR02168 1012 LTEAKETLEEAIEEIDREA 1030
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9775-10008 |
8.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9775 GINNAMTKEEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALI-------DEIDRNPnlTDKEKQALKDRINQiLQ 9847
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVAS--AEREIAELEAELER-LD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9848 QGHNGINNAmtKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALA---NEKRDQINSNPDLTPEQKAKALKE------ 9918
Cdd:COG4913 682 ASSDDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEErfaaal 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9919 IDEAEKRALENIENAQtkDQLNKGLNLGLDDIRNT-----HVWEVDAQPavneiFDATPEQI---------LVNGELIVH 9984
Cdd:COG4913 760 GDAVERELRENLEERI--DALRARLNRAEEELERAmrafnREWPAETAD-----LDADLESLpeylalldrLEEDGLPEY 832
|
250 260
....*....|....*....|....*..
gi 616687517 9985 RDDI---ITEQDIHAHINLIDQLTAEI 10008
Cdd:COG4913 833 EERFkelLNENSIEFVADLLSKLRRAI 859
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
9137-9193 |
8.56e-05 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 44.09 E-value: 8.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 9137 KENELNGNERVAEAKTQAKQTIDQLTHLNADQIATAKQNIDQATKLQPIAELVDQAT 9193
Cdd:smart00844 4 AKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8948-9016 |
9.19e-05 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.23 E-value: 9.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 8948 EALRNSIQDQQQTESGSKFINEDKPQKDAYQAAVQHAKDLINQTGNPTLDKSQVEQLTQAVATAKDNLH 9016
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8615-9027 |
9.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8615 NPTINKGNVTSATQAVtssKNALDGVERLAQDKQTagnslnhLDQLTpAQQQALENQINNATTRDKVAEIIAQAQALNEA 8694
Cdd:COG4717 65 KPELNLKELKELEEEL---KEAEEKEEEYAELQEE-------LEELE-EELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8695 MKALKESIKDQP----QTEASSKFINEDQAQKDAYTQAVQHAKDLINKTTDPTLVksvidQATQAVNDAKNNLhgdQKLA 8770
Cdd:COG4717 134 LEALEAELAELPerleELEERLEELRELEEELEELEAELAELQEELEELLEQLSL-----ATEEELQDLAEEL---EELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8771 QDKQRATETLNNLSNLNTPQRQALEnQINNAATRGEVAQKLTEAQALNQAM------EALRNSIQDQQQTEAGSKFI--- 8841
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8842 -----------NEDKPQKDAYQAAVQHAKDLINQTS----------NPTLDKAQVEQLTQAVNQAKDNLhgdQKLADDKQ 8900
Cdd:COG4717 285 llallflllarEKASLGKEAEELQALPALEELEEEEleellaalglPPDLSPEELLELLDRIEELQELL---REAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8901 HAvtdlnQLNGLNNPQRQALESqiNNAATRDEVAQKLAEAKALNQAMEALrNSIQDQQQTESGSKFINEDKPQKDAYQAA 8980
Cdd:COG4717 362 EL-----QLEELEQEIAALLAE--AGVEDEEELRAALEQAEEYQELKEEL-EELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 616687517 8981 VQHAKDLINQTgnptldKSQVEQLTQAVATAK---DNLHGDQKLVRDQQQ 9027
Cdd:COG4717 434 LEELEEELEEL------EEELEELREELAELEaelEQLEEDGELAELLQE 477
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4726-4785 |
1.09e-04 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 43.70 E-value: 1.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4726 VTSTKDALNGDAKLAEAKAAAKQNLSTLNHITNAQRTALEGQINQATTVDGVNTVKTNAN 4785
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5422-5490 |
1.11e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.23 E-value: 1.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5422 GQLETSIRDKDTTLQSQNYQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVERAMQTVTQANTALN 5490
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5170-5238 |
1.19e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 44.23 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5170 KGLRDSIANEATIKAGQNYTDASLNNRNEYDSAVTAAKAIINQTSNPTMEANTITQATSQVTTKEQALN 5238
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
9266-9320 |
1.24e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 43.68 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9266 DERVALAKTNGKHDIDQLNALNNAQQDGFKGRIDQSNDLNQIQQIVDEAKALNRA 9320
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
4474-4533 |
1.33e-04 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 43.70 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4474 VTNAKGALNGNHNLEQAKSNANTTINGLQHLTTAQKDKLKQQVQQAQNVAGVDTVKSSAN 4533
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQILQKAK 60
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3981-4034 |
1.41e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 43.30 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 3981 QNLNNAKQAAITAINGSSDLNQHQKEALKAQANGAQRVSNAQDVQRNATELNTA 4034
Cdd:pfam01468 2 QKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8195-8261 |
1.43e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.85 E-value: 1.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 8195 LRNSIADNQATLASEDYHDAAAQRQNDYNQAVTAANNIINQTTSPTMNPDDVNRATTQVNNTKVALD 8261
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6052-6120 |
1.52e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.85 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6052 NQLRQSIVSKDATKASEDYHDANTDLQNAYNHAVSEAEGIISASNNPEMNPDTINQKASQVNSANSALN 6120
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6122-6176 |
1.53e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 43.30 E-value: 1.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6122 DEKLAEAKQTAKSDIGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKATSLNTA 6176
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8669-9406 |
1.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8669 ENQINNaTTRDKVAEIIAQAQALNEAMKALKESIKDQPQTEAsskfinEDQAQKDAYTQAVQHAKDLINKTTDPTLVKSV 8748
Cdd:PTZ00121 1044 EKDIID-EDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAK------EDNRADEATEEAFGKAEEAKKTETGKAEEARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8749 IDQATQAVNDAKNNlhGDQKLAQDKQRATETlnnlsnlntpqRQALENQINNAATRGEVAQKLTEAQALNQA--MEALRN 8826
Cdd:PTZ00121 1117 AEEAKKKAEDARKA--EEARKAEDARKAEEA-----------RKAEDAKRVEIARKAEDARKAEEARKAEDAkkAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8827 SIQDQQQTEAgskfinedKPQKDAYQAavQHAKDLINQTSNPTLDKAQVEQLTQAVNQAKDNlhgdQKLADDKQHAVTDL 8906
Cdd:PTZ00121 1184 AEEVRKAEEL--------RKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEEA----KKDAEEAKKAEEER 1249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8907 NQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKALNQAMEA--LRNSIQDQQQTESGSKfiNEDKPQKDAYQAAVQHA 8984
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEA 1327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8985 KDLINQTGNPTLDKSQVEQLTQAVATAKDNlhgdqKLVRDQQQAvttvnalpnlnHAQQQALTDAINAAPTRTEVAQHVQ 9064
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----EAEAAEEKA-----------EAAEKKKEEAKKKADAAKKKAEEKK 1391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9065 TATELDHAMETLKNKVDQVNTDKAQPNYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELNGN 9144
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9145 ERVAEAKTQAKQTIDQLTHlnadqiaTAKQNIDQATKLQPIAELVDQATQLNQSMDQLQQAVNEHANVEQTVDYTQADLD 9224
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKK-------KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9225 KQNAYKQAIAE----AENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTNGKHDIDQLNALNNAQQDGFKGRIDQ 9300
Cdd:PTZ00121 1545 KKKADELKKAEelkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9301 SNDLNQIQQIVDEAKALN----RAMNQLSQEITGNEGRTKGSTNYVNAD---TQVKRVYDEAVDKAKEALNKATGQNLTA 9373
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEaeekKKAEELKKAEEENKIKAAEEAKKAEEDkkkAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
730 740 750
....*....|....*....|....*....|...
gi 616687517 9374 EEVIKLNDAVTAAKQALNGEERLNNRKSEALQR 9406
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4036-4104 |
1.62e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.85 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4036 GTLKHAIADKTTTLASSKYVNADSTKQNAYTTKVTNAEHIISGTPTVVTTPSEVTAAANQVNSAKQELN 4104
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
964-2496 |
1.62e-04 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 49.38 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 964 NGSLAISGRVSMNQAYNSDITFKVSATDNVNNTTNDSQSKHVTVHVGKISDDAHPIVLGNSEKVVVVNPTALTGDEKQRI 1043
Cdd:COG3210 63 GGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1044 TTAFMNKNQNIRGYLASSNPVTVDNHGNVTLQYRDGSSTTLDATNVMTYEPVVKPEYQTANAPkTATVTIAKGQSFNIGD 1123
Cdd:COG3210 143 LGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINAT-AGVLANAGGGTAGGVA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1124 IKQYFTLSNGQAIPSSTFTNITSDRTIPTAQEVSQMNAGTQLYHITATNAYHKDTEDFYITLKIIDVKQPEGDQRVYRMS 1203
Cdd:COG3210 222 SANSTLTGGVVAAGTGAGVISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1204 TYDITTDEISKVKQAFINANRDAISFAEGDISVTNTPNGSNVSTITVNINKGRLTKSFTSNLANMNFLRWVNFPQDYTVT 1283
Cdd:COG3210 302 SVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1284 WTNAKIANRPTDGGLSWSDDHKSLIYRYDATLGTQITTNDILTLLKATTTVPGLRNNIAGNEKAQAEAGGRPNYKTTGYS 1363
Cdd:COG3210 382 STVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1364 QSNPTSDGQRQFTLNGQVIQIMDIINPSNGFGGQPVTNSNVRANHSNSTVVSVNESAANGAGAFTIDHVVKNNSTHNAAD 1443
Cdd:COG3210 462 GNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSG 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1444 AVYKAQLYLSPYGPKQYVEHLNQNTGNTTDAINIYFVPSDLVNPTVSVGNYTNHqvfSGETFTNTITANDNFGVQSVTVP 1523
Cdd:COG3210 542 SGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTN---SGGTVLSIGTGSAGATGTITLGA 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1524 NTSQLTGTVDNNHQHVSATAPNVTSATNKTINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRIANISNNAT 1603
Cdd:COG3210 619 GTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGT 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1604 VSQADQTAIINSLTFTSNAPNRNYATASASEITSKTVSNVSRTGNNAQVTVTVTYQDGTTSTVTVPVKHVIPEI-VAHSH 1682
Cdd:COG3210 699 LNNAGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLtLANAN 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1683 YTVQGQDFPTGNGASASDYFKLSNGSAIPDATITWVSGQAPN--KNNTTIGQDINVTAHILIDGETTPITKTATYKVVSS 1760
Cdd:COG3210 779 GNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTitINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGAS 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1761 VPKHVFETNRGAVFPGISDVYDAKQYVKPVNDSWTQNAQRMNFQFTNSYGPSKDVVGISTRDIRVTYDNHQTQIIKILAK 1840
Cdd:COG3210 859 GGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGA 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1841 VKPDPPRIDGNSVTYKAGLTNQQIKINNVLSSSSIKLFKADNTPLTITNTTYGSGNTAVVTVSDALPNGVIKARSSITMN 1920
Cdd:COG3210 939 GNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAG 1018
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1921 NVTYTTQDEHGRAIDVTRNESVDSNDSATVTVTPQLQATTEGAVFIKGGDGFDFGHVERFIQNPPHGATVAWHDSPDTWK 2000
Cdd:COG3210 1019 GNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGIT 1098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2001 NTVGNTHKTAVVTLPSGQGTRNVEVPVKVYPVANAKAPSRDVKGQNLTNGTDAINYITFDPNTNTNGITAAWANRQQPNN 2080
Cdd:COG3210 1099 NGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTG 1178
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2081 QQAGVQHLNVDVTYPGISAAKRVPVTVNVYQFEFPQTSYTTTVGGTLASGTQASGYAH-IQNANGLPTDGFTYKWNRDTT 2159
Cdd:COG3210 1179 SAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSsAGQTGSFVAAGSASGTGDATT 1258
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2160 GTNDANWAAMNKPNAAKVINAKYDVIYNGHTFATSLLAKFVVKDVQPAKPTVTETAAGAITIAPGANQTVNTHAGNVTTY 2239
Cdd:COG3210 1259 GATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNA 1338
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2240 ADKLVIKRNGNVVTTFTRHNNTSPWVKEASAATVAGIVGTNNGITVAAGTFNAADTIQVVATQGSGETISDEQLSDDFTV 2319
Cdd:COG3210 1339 GGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVS 1418
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2320 VAPQPNQATTKIWQNGHIDIMPNNPSGHLINPTQAMDIAYTEKVGNGAEHSKTLNAVRGQNNQWTIANKPDYVTLDAHTG 2399
Cdd:COG3210 1419 GTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGAT 1498
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2400 KVTFNANTIKPNSAITITPKAGTGHSASSNPSTLTAPATHTVNTTEIVKDYGSNVTPAEINNAVQVANKRTATIKNGTAM 2479
Cdd:COG3210 1499 ASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDT 1578
|
1530
....*....|....*..
gi 616687517 2480 PTNLAGGSTTTIPVTVT 2496
Cdd:COG3210 1579 GGADDTGAQAPTAGNTA 1595
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6431-6497 |
1.67e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.46 E-value: 1.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 6431 LESAIANKDQTKASENYIDADPTNKTAFDNAITQAESYLNKDHGANKDKQAVEQAIQSVTSTENALN 6497
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
5674-5742 |
1.70e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.46 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 5674 KGLRDSIANEATIKAGQNYTDASPNNRSEYDSAVTAAKAIIGQTTSPTMNAQEINQAKDQVTAKQQALN 5742
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
1313-1747 |
1.74e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 49.17 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1313 ATLGTQITTNDILTLLKATTTVPGLRNNIAGNEKAQAEAGGRPNYKTTGYSQSNPTSDGQRQFTLNGQVIQIMDIINPSN 1392
Cdd:COG3468 19 GGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNSGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1393 GFGGQPVTNSNVRANHSNSTVVSVNESAANGAGAFTIDHVVKNNSTHNAADAVYKAQLYLSPYGPKQYVEHLNQNTGNTT 1472
Cdd:COG3468 99 GGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1473 DAINIYFVPSDLVNPTVSVGNYTNhqVFSGETFTNTITANDNFGVQSVTVPNTSQLTGTVDNNHQHVSATAPNVTSATNK 1552
Cdd:COG3468 179 GGGAGGSGGAGSTGSGAGGGGGGS--GGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1553 TINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRIANISNNATVSQADQTAIINSLTFTSNAPNR----NYA 1628
Cdd:COG3468 257 GAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGggggGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1629 TASASEITSKTVSNVSRTGNNAQVTVTVTYQDGTTSTVTVPVKHVIPEIVAHSHYTVQGQDFPTGNGASASDYFKLSNGS 1708
Cdd:COG3468 337 GGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGL 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 616687517 1709 AIPDATITwVSGQAPNKN-----NTTIGQDINVTAHILIDGETT 1747
Cdd:COG3468 417 TLTGGTLT-VNGNYTGNNgtlvlNTVLGDDNSPTDRLVVNGNTS 459
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
5996-6050 |
2.01e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.91 E-value: 2.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5996 DARLNEAKNTAKQQLATMSHLTDAQKGNLTEQIERGTTVAGVQGIQANAGTLDQA 6050
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
6247-6301 |
2.09e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.91 E-value: 2.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 6247 DNKVAQAKEAAKHALASYSNLNNAQSTAATSQIDNATTVAGVTTAQNTANELNTA 6301
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
8514-8567 |
2.15e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.91 E-value: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 8514 DVKLQNDKDHAKQAVSQLAHLNNAQKHMEDTLIDSETTRTAVNHDLTEAQALDQ 8567
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNN 54
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
4288-4356 |
2.27e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 43.46 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 4288 GNLEQAIHDQNTVKQSVKFTDADKAKRDAYTNAVSRAETILNKTQGANTPKQDVEASIQNVSSAKNALN 4356
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
smart00844 |
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha ... |
5482-5536 |
2.40e-04 |
|
GA module; The protein G-related albumin-binding (GA) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from the Peptostreptococcus magnus albumin-binding protein (PAB) shows a strong affinity for albumin.
Pssm-ID: 197912 [Multi-domain] Cd Length: 60 Bit Score: 42.93 E-value: 2.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 5482 VTQANTALNGIQNLERAKQAANTAITNASDLNTKQKEALKAQVTSAGRVSVANGV 5536
Cdd:smart00844 1 VNTAKNALNGDQKLAQAKQNAKQAINNLTHLNNAQKQALKNQINQATTRAEVNQI 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7491-8340 |
2.52e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7491 QQALTKVNDTNQALngnQKLADAKQAAKTNLGTL--------------DHLNDAQKQALTTQVEQAPD-IATVNNVKQNA 7555
Cdd:TIGR02168 175 KETERKLERTRENL---DRLEDILNELERQLKSLerqaekaerykelkAELRELELALLVLRLEELREeLEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7556 QNLNNAMTNLSNALQDKTETLNSINFTDADK-----AKKDAYTNAVAQAEG--ILSKANGSNASQTEVEQAMQRVNAAKQ 7628
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEieelqKELYALANEISRLEQqkQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7629 ALNGNDNVHRAKDAAKQVITNANDLNQAQKDALKQQVDAaqtvanvntnKQTAQDLNQAMTQLKQGVAD--KDQTKANGN 7706
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEEL----------ESRLEELEEQLETLRSKVAQleLQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7707 FVNADTEKQNAyNNAVAHAEQIISGTPNANVDPQQVAQALQQVTDAKNGLNGNHNLQVAKDNANTAIDQLPNLNQPQKTA 7786
Cdd:TIGR02168 402 IERLEARLERL-EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7787 LKDQVTHAELVTGVNAIKQNADALNNAMGTLKQ-QIQANSQVPQSVDFTQADQDKQQAYNNAanqaqqiangtptpvLTP 7865
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKnQSGLSGILGVLSELISVDEGYEAAIEAA---------------LGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7866 DAVTQAVTTMNQAKDALNGDEKLAQAKQDALAnLDTLRD--LNQPQRDALRNQINQAQALATVEQTKQNAQNvntAMSNL 7943
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQNELGRVTFLP-LDSIKGteIQGNDREILKNIEGFLGVAKDLVKFDPKLRK---ALSYL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 7944 KQGIANKDTVKASenyhDADADKQTAYTNAVSQ------AEGII----NQTTNPTLNPD--------DITRVLTQVTDAK 8005
Cdd:TIGR02168 622 LGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdlvrPGGVItggsAKTNSSILERRreieeleeKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8006 NGLNGEAKLATEKQNAKDAVNAMTH-----LNDAQKQALNGQIDQSPEIATVTQVKQTATSLDQAMNQLSQAINDKTQTL 8080
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEelsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8081 ADG----NYLNADPDKQN----AYKQAVAKAEALLNKQSGT-NEVQAQVESITNEVNAAKQALngnDNLANAKQQAKQQL 8151
Cdd:TIGR02168 778 AEAeaeiEELEAQIEQLKeelkALREALDELRAELTLLNEEaANLRERLESLERRIAATERRL---EDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8152 ANLTH-LNDAQKQSFESQITQAPLVTDVTTINQKAQALDHAMELLRNSIAD-NQATLASEDYHDAAAQRQNDYNQAVTAA 8229
Cdd:TIGR02168 855 ESLAAeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8230 NNIINQttsptmnpddvnrattqvNNTKVALDGDENLAAAKQQANNRLDQLDHLNNAQKQqLQSQITQssdIAAVNghkq 8309
Cdd:TIGR02168 935 EVRIDN------------------LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKE---LGPVN---- 988
|
890 900 910
....*....|....*....|....*....|.
gi 616687517 8310 taeslntamgnlINAIADHQAVEQRGNFINA 8340
Cdd:TIGR02168 989 ------------LAAIEEYEELKERYDFLTA 1007
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
9144-9198 |
2.92e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.53 E-value: 2.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9144 NERVAEAKTQAKQTIDQLTHLNADQIATAKQNIDQATKLQPIAELVDQATQLNQS 9198
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
9520-9574 |
3.41e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.14 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9520 DQNLATAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIINDQIDLNNA 9574
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10080-10283 |
3.72e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10080 QKEAAIAEVNKLKQQAIEQINNAADVHTVEEVQHQEQAHIEQfnpdqfTIDQAKSnAIKSISDAIQHMIDEINASKDLTD 10159
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA------ELEELRL-ELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10160 KEKQEAISKLNQLKDQSIQAIQRAQSIDEIAQQLEQFKAQLKAANPFAKELENRKKSAISKIKDiSTDEINRIRNSTIGT 10239
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEA 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616687517 10240 AEERQAAMNRINEIVLETIRDINNAHTPQQVEAALNNGIARILA 10283
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
9752-9933 |
3.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9752 NLTDKEKQALKDRINQILQQGHNGINnAMTKEEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALIDEIDRNPNLT 9831
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAE-AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9832 DKEKQALKDRINQILQQgHNGINNamTKEEIEQAKAQLAQALQDIKDLvkAKEDAKNAI-KALANEKRdqinsnpdltpE 9910
Cdd:PRK12704 106 EKREEELEKKEKELEQK-QQELEK--KEEELEELIEEQLQELERISGL--TAEEAKEILlEKVEEEAR-----------H 169
|
170 180
....*....|....*....|....*...
gi 616687517 9911 QKAKALKEI-----DEAEKRALENIENA 9933
Cdd:PRK12704 170 EAAVLIKEIeeeakEEADKKAKEILAQA 197
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7815-7883 |
4.04e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 42.69 E-value: 4.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7815 GTLKQQIQANSQVPQSVDFTQADQDKQQAYNNAANQAQQIANGTPTPVLTPDAVTQAVTTMNQAKDALN 7883
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
9393-9447 |
4.45e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 42.14 E-value: 4.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9393 EERLNNRKSEALQRLDQLTHLNNAQRQLAIQQINNAETLNKASRAINRAVQLDDA 9447
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
8863-9692 |
4.62e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8863 NQTSNPTLDKAQVEQLTQAVNQAKDNLHgDQKLADDKQHAVTDLNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAK- 8941
Cdd:pfam02463 184 NLAELIIDLEELKLQELKLKEQAKKALE-YYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEk 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8942 -----ALNQAMEALRNSIQDQQQTESGSKFINEDKPQKDAYQAAVQHaKDLINQTGNPTLDKSQVEQLTQAVATAKDNLH 9016
Cdd:pfam02463 263 eeeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK-VDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9017 GDQKLVRDQQQAVTTVNAlpNLNHAQQQALTDAINAAPTRTEVAQHVQTATELDHAMETLKNKvdQVNTDKAQpnyTEAS 9096
Cdd:pfam02463 342 KELKELEIKREAEEEEEE--ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE--EEKEAQLL---LELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9097 TDKKDAVDQALQAAQSITDptngsnankyAVEQALTKLQGKENELNGNERVAEAKTQAKQTIDQLTHLNADQIATAKQNI 9176
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILE----------EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9177 DQATKLQpiaelvdqaTQLNQSMDQLQQAVNEHANVEQ-------TVDYTQADLDKqnAYKQAIAEAENVLKQNANKQQV 9249
Cdd:pfam02463 485 QLELLLS---------RQKLEERSQKESKARSGLKVLLalikdgvGGRIISAHGRL--GDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9250 DQALQNILNAKQALNGDERVALAKTNGKHDIDQLNALNNAQQDGFKGRIDQSNDLNQIQQIVDEAK--ALNRAMNQLSQE 9327
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDkrAKVVEGILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9328 ITGNEGRTKGSTNYVNADTQVKRVYDEAVDKAKEALNKATGQNLTAEEVIKLNDAVTAAKQALNGEERLNN---RKSEAL 9404
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKeqrEKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9405 QRLDQLTHLNNAQRQLAIQQINNAETLNKASRAINRA-------------------VQLDDAMGAVQQYIDEHHLDVISS 9465
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeeeksrlkkeekeeekselSLKEKELAEEREKTEKLKVEEEKE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9466 TNYINADDNLKANY----DNAITNAAHELDKVQGSAIAKAEAEQLKQHIIDAQKALNGDQNLAT---AKDKANAFVDTLN 9538
Cdd:pfam02463 794 EKLKAQEEELRALEeelkEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleEEITKEELLQELL 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9539 GLNQQQQDLAH-QAINNADTVTGIANIINDQIDLNNAMETLKHLVDNEIPTAEQTVNYQNADDVAKSNFDDAKRLANALI 9617
Cdd:pfam02463 874 LKEEELEEQKLkDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9618 NSDN---------------TNVNDINGAIQAVKDVIQN--LNGEQRLQEAKDKAIQNVNKVLADKLKE-IEASNATDQDK 9679
Cdd:pfam02463 954 NKEEeeernkrlllakeelGKVNLMAIEEFEEKEERYNkdELEKERLEEEKKKLIRAIIEETCQRLKEfLELFVSINKGW 1033
|
890
....*....|...
gi 616687517 9680 LIAKNKAEELANS 9692
Cdd:pfam02463 1034 NKVFFYLELGGSA 1046
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6556-6623 |
4.78e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 42.31 E-value: 4.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 6556 QLKQAIADHDTIVAGGNYTNASPDKQGAYTDAYNAAKNIVNGSPNVITNAADVTAATQRVNNAETGLN 6623
Cdd:pfam07554 2 ALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
6178-6245 |
5.07e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 42.31 E-value: 5.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 6178 GNLKHALAEKDNTKRSVNYTDADQPKQQAYDTAVTQAEGITN-ANGSNANETQVQAALNQLNQAKNDLN 6245
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNkTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9482-9936 |
5.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9482 AITNAAHELDKVQGS--AIAKAEAEQLKQHIIDAQKALNGDQNLATAKDKANAFVDTL-NGLNQQQQDLAH--QAINNAD 9556
Cdd:COG4717 50 RLEKEADELFKPQGRkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9557 TVTGIANIindQIDLNNAMETLKHLVDNEIPTAEQTVNYQNADDVAKSNfddAKRLANALINSDNTNVNDINGAIQAVKD 9636
Cdd:COG4717 130 LYQELEAL---EAELAELPERLEELEERLEELRELEEELEELEAELAEL---QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9637 VIQNLngeQRLQEAKDKAIQNVNKvLADKLKEIEASNATDQD-KLIAKNKAEELANSIINNINKATSNQDVSRVQTAGNQ 9715
Cdd:COG4717 204 LQQRL---AELEEELEEAQEELEE-LEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9716 AI---------------EQVHANEIPKAKIDANKDV--DKQVQALIDEIDRNPNLTDKEKQALKDRINQILQqghnginn 9778
Cdd:COG4717 280 FLvlgllallflllareKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEELQE-------- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9779 AMTKEEIEHAKAQLAQALQDIKDLVkakENAKQDVDKQVQALIDEIDRNPNLTdKEKQALKDRINQIL---QQGHNGINN 9855
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIAALL---AEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLgelEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9856 AMTKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKR-DQINsnpdltpEQKAKALKEIDEAEKR------ALE 9928
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElAELL-------QELEELKAELRELAEEwaalklALE 500
|
....*...
gi 616687517 9929 NIENAQTK 9936
Cdd:COG4717 501 LLEEAREE 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2787-3057 |
5.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2787 KSVTTDGMTQSSIQAYENAKRAGQTEstnaQNVInnGDATDQQIAAEKTKVEEkynsLKQAIDGLTPDLAPLQTAKTQLQ 2866
Cdd:COG4913 575 RAITRAGQVKGNGTRHEKDDRRRIRS----RYVL--GFDNRAKLAALEAELAE----LEEELAEAEERLEALEAELDALQ 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2867 NDIDQPTNTTGMTSASVatfneKLSAARTKI----QEIDRVLASHPDVATIRQNVTAANAAKSALDQARNGLTVDKAPLE 2942
Cdd:COG4913 645 ERREALQRLAEYSWDEI-----DVASAEREIaeleAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2943 NAKNQLQHSIDT-QTSTTGMTQDSINAYNAKLTAARNKVQQINqvlagsptvdqintntsAANQAKSDLDHARQALtpdK 3021
Cdd:COG4913 720 KELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAALGDA-----------------VERELRENLEERIDAL---R 779
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 616687517 3022 APLQNAKTQLEQSINQ-----PTDTTGMTT--ASLNAYNQKLQ 3057
Cdd:COG4913 780 ARLNRAEEELERAMRAfnrewPAETADLDAdlESLPEYLALLD 822
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8742-9211 |
5.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8742 PTLVKSVIDQATQAVNDAKNNLHGDQKLAQDKQRATEtlnnlsnlntpQRQALENQINNAATRGEVAQKLTEAQALNQAM 8821
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEE-----------ELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8822 EALRNSIQD-QQQTEAGSKFINEDKPQKDAYQAAVQHAKDL-------INQTSNPTLD-----KAQVEQLTQAVNQAKDN 8888
Cdd:COG4717 135 EALEAELAElPERLEELEERLEELRELEEELEELEAELAELqeeleelLEQLSLATEEelqdlAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8889 LHGDQKLADDKQHAVTDLNQLNGLNNPQRQ------------ALESQINNAATRDEVAQKLAEAKALNQAMEALRNSIQD 8956
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8957 QQQTESGSKF--INEDKPQKDAYQAAVQHAKDLINqtGNPTLDKSQVEQLTQAVATAKDNLHGDQKLVRDQQQAVttvna 9034
Cdd:COG4717 295 REKASLGKEAeeLQALPALEELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE----- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9035 lpnlNHAQQQALTDAINAApTRTEVAQHVQTATELDHAMETLKNKVDQVNtDKAQPNYTEASTDKKDAVDQALQAAqsit 9114
Cdd:COG4717 368 ----LEQEIAALLAEAGVE-DEEELRAALEQAEEYQELKEELEELEEQLE-ELLGELEELLEALDEEELEEELEEL---- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9115 dptngsnankyavEQALTKLQGKENELngNERVAEAKTQAKQ-----TIDQLTHLNADQIATAKQNIDQATKLQPIAELV 9189
Cdd:COG4717 438 -------------EEELEELEEELEEL--REELAELEAELEQleedgELAELLQELEELKAELRELAEEWAALKLALELL 502
|
490 500
....*....|....*....|..
gi 616687517 9190 DQATQlnQSMDQLQQAVNEHAN 9211
Cdd:COG4717 503 EEARE--EYREERLPPVLERAS 522
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4232-4286 |
5.81e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 41.76 E-value: 5.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4232 AENLRNAQNTAKQNLNTLSHLTNNQKSAISSQIDRAGHVSEVTAAKNAATELNTQ 4286
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9557-10263 |
6.21e-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: 47.32 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9557 TVTGIA-----NIINDQIDLNNAMETLKHLVDNEIPTAEQTVNyqnadDVAKSNFDDAKRL--ANALINSDNTNVNDING 9629
Cdd:TIGR04523 15 TATGFSyvgykNIANKQDTEEKQLEKKLKTIKNELKNKEKELK-----NLDKNLNKDEEKInnSNNKIKILEQQIKDLND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9630 AIQAVKDVIQNLNGEQRL---QEAKDKAIQNVNKVLADKLKEIEASNATDQDKLIA--KNKAEELA--NSIINNINKATS 9702
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKinsEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTeiKKKEKELEklNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9703 N---------QDVSRVQTAGNQAIEQVHANEIPKAKIDANKDVDKQVQALIDEIDRNPNLTDKEKQALKDRINQIlqqgh 9773
Cdd:TIGR04523 170 ElenelnlleKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9774 nginnamtKEEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALIDeidrnpnlTDKEKQALKDRINQILQQGHNGI 9853
Cdd:TIGR04523 245 --------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE--------LEKQLNQLKSEISDLNNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9854 NNAMtKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKRDQINSNPDLTPEQKAKaLKEIDEAEKraleniENA 9933
Cdd:TIGR04523 309 NKEL-KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK-QNEIEKLKK------ENQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9934 QTKDQLNKgLNLGLDDIRNthvwEVDAQPAVNEIFDATPEQILVNGELIVHRDDIITEQDIHAH---INLIDQLTAEIID 10010
Cdd:TIGR04523 381 SYKQEIKN-LESQINDLES----KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNseiKDLTNQDSVKELI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10011 TPSTATISDSLTAKVEVtlLDGSKVIVSVPVKVVEKELTVVKQQaiesIENAAQQKINEINNHATLTPEQKEaAIAEVNK 10090
Cdd:TIGR04523 456 IKNLDNTRESLETQLKV--LSRSINKIKQNLEQKQKELKSKEKE----LKKLNEEKKELEEKVKDLTKKISS-LKEKIEK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10091 LKQQaIEQINNaadvhtveEVQHQEqahiEQFNPDQFTIdqaKSNAIKSISDAIQHMIDEI---NASKDLTDKEKQEAIS 10167
Cdd:TIGR04523 529 LESE-KKEKES--------KISDLE----DELNKDDFEL---KKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10168 KLNQLKDQSIQAIQ-RAQSIDEIAQQLEQFKAQLKAANPFAKELENRKKSAISKIKDIStDEINRIRNSTIGTAEERQAA 10246
Cdd:TIGR04523 593 QKEKEKKDLIKEIEeKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK-ETIKEIRNKWPEIIKKIKES 671
|
730
....*....|....*..
gi 616687517 10247 MNRINEIVlETIRDINN 10263
Cdd:TIGR04523 672 KTKIDDII-ELMKDWLK 687
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
9785-9936 |
6.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9785 IEHAKAQLAQALQDIKDLVKAKENAKQDVD---KQVQALIDEidrnpnlTDKEKQALKDRINQIlqqghnginnamtKEE 9861
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEqkaEEAEALLKE-------AEKLKEELEEKKEKL-------------QEE 563
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 9862 IEQAKAQLAQALQDIkdLVKAKEDAKNAIKALANEKRDQInsnpdltPEQKAKALKEIDEAEKRALENIENAQTK 9936
Cdd:PRK00409 564 EDKLLEEAEKEAQQA--IKEAKKEADEIIKELRQLQKGGY-------ASVKAHELIEARKRLNKANEKKEKKKKK 629
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
8590-9028 |
6.62e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8590 NAEPNKKQAYDEAVQNAESIIAGLNNptiNKGNVTSATQavtsSKNALDGVERLAQDKQTAGNSLNHLDQLTPAQQ--QA 8667
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEE---RKGSLERAKQ----YQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8668 LENQINNATTRdkVAEIIAQAQALNEAMKALKESIKD--QPQTEAsskfinedqaqKDAYTQAVQHAKDLINKTTDPTLV 8745
Cdd:PRK10929 107 LEQEILQVSSQ--LLEKSRQAQQEQDRAREISDSLSQlpQQQTEA-----------RRQLNEIERRLQTLGTPNTPLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8746 KSVIDQATQAVNDAKNNlhgDQKLAQdkqratetlnnLSNLNtpqRQALenqinnAATRGEVAQKltEAQALNQAMEALR 8825
Cdd:PRK10929 174 QLTALQAESAALKALVD---ELELAQ-----------LSANN---RQEL------ARLRSELAKK--RSQQLDAYLQALR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8826 NSIQDQQQTEAgskfinedkpqkdayQAAVQHAKDLINQTSNptLDKAQVEQ------LTQAVNQAKDNLhgDQkLADDK 8899
Cdd:PRK10929 229 NQLNSQRQREA---------------ERALESTELLAEQSGD--LPKSIVAQfkinreLSQALNQQAQRM--DL-IASQQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8900 QHAVTDLNQLnglnnpqRQALesqinnaATRDEVAQKLAEAKALNqamEALRNSIqdqqqtesgSKFINEDKPQK---DA 8976
Cdd:PRK10929 289 RQAASQTLQV-------RQAL-------NTLREQSQWLGVSNALG---EALRAQV---------ARLPEMPKPQQldtEM 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 8977 YQAAVQ--HAKDLINQTGnptldksqveQLTQAVATAKDNLHGDQKLVRDQQQA 9028
Cdd:PRK10929 343 AQLRVQrlRYEDLLNKQP----------QLRQIRQADGQPLTAEQNRILDAQLR 386
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3854-3908 |
7.50e-04 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 41.37 E-value: 7.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 3854 DAKLIAAQNAAKQHLGTLTHITTAQHNDLTNQISQATNLAGVESVKQSANSLDGA 3908
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
9422-10259 |
1.01e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9422 IQQINNAETLNKASRAINRAVQLDDAMGAVQQYIdehHLDVISSTNYINAD-DNLKANYDNAITNAAHELDK--VQGSAI 9498
Cdd:TIGR01612 712 IQNMETATVELHLSNIENKKNELLDIIVEIKKHI---HGEINKDLNKILEDfKNKEKELSNKINDYAKEKDElnKYKSKI 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9499 AKAEAEQLKQHIIDAQKALNGDQNLATAKD-------KANAFVDTLNGLNQQQQDLahqaINNADTVTGIANIINDQIDL 9571
Cdd:TIGR01612 789 SEIKNHYNDQINIDNIKDEDAKQNYDKSKEyiktisiKEDEIFKIINEMKFMKDDF----LNKVDKFINFENNCKEKIDS 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9572 NNAMET-LKHLVDNEIpTAEQTVNYQNaddvaksNFDDAKRLANALINS---DNTNVN---DINGAIQAVKDVIQNL--- 9641
Cdd:TIGR01612 865 EHEQFAeLTNKIKAEI-SDDKLNDYEK-------KFNDSKSLINEINKSieeEYQNINtlkKVDEYIKICENTKESIekf 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9642 -NGEQRLQEAKDKAIQ------NVNKVLADKLKEIEASNATDQDKLIAK---NKAEELANSIINNINKATSNQDVSRVQT 9711
Cdd:TIGR01612 937 hNKQNILKEILNKNIDtikesnLIEKSYKDKFDNTLIDKINELDKAFKDaslNDYEAKNNELIKYFNDLKANLGKNKENM 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9712 AGNQAIEQVHA-NEIPKAKIDANKDVDK-------QVQALIDEIDrnpNLTDKEKQALKdriNQILQQGHNGINN-AMTK 9782
Cdd:TIGR01612 1017 LYHQFDEKEKAtNDIEQKIEDANKNIPNieiaihtSIYNIIDEIE---KEIGKNIELLN---KEILEEAEINITNfNEIK 1090
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9783 EEIEH---------AKAQLAQALQDIKDLVKakeNAKQDVDKQVQALIDEIDRNPNLTDKekqaLKDRINQILQQGHNGI 9853
Cdd:TIGR01612 1091 EKLKHynfddfgkeENIKYADEINKIKDDIK---NLDQKIDHHIKALEEIKKKSENYIDE----IKAQINDLEDVADKAI 1163
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9854 NNAMTKEeieqakaqLAQALQDIKDLVKAKEDAKNAIKALANEKrDQINSNPDLTPEQKAKALKEIDEAEKRALENIENA 9933
Cdd:TIGR01612 1164 SNDDPEE--------IEKKIENIVTKIDKKKNIYDEIKKLLNEI-AEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEE 1234
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9934 QTK-DQLNKGLNLGLDDIRNTHVWEVDAQPAVNEIFDATPEQILVNGELIVHRDDIITEQDIHAHINLIDQLTAEIIDTP 10012
Cdd:TIGR01612 1235 KKKsEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDF 1314
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10013 STATISDSLTAKVEVTLLDGSKVIVSVPVKVVE--KELTVVKQQAIESIENAAQQKINEI-----------NNHATLTPE 10079
Cdd:TIGR01612 1315 SEESDINDIKKELQKNLLDAQKHNSDINLYLNEiaNIYNILKLNKIKKIIDEVKEYTKEIeennknikdelDKSEKLIKK 1394
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10080 QKEAAIAEVNKLKqqaIEQINNAADVHTVEEVQHQEQAHI--EQFNPDQFTIDQAKSNAIKSISDAIQHMIDeiNASKDL 10157
Cdd:TIGR01612 1395 IKDDINLEECKSK---IESTLDDKDIDECIKKIKELKNHIlsEESNIDTYFKNADENNENVLLLFKNIEMAD--NKSQHI 1469
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10158 TDKEKQEAIS----KLNQLKDQSIQAIQRAQSIDEIAQQLEQFKAQLKAANPFAKELENRK-----KSAISKIKDISTDE 10228
Cdd:TIGR01612 1470 LKIKKDNATNdhdfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsalaiKNKFAKTKKDSEII 1549
|
890 900 910
....*....|....*....|....*....|.
gi 616687517 10229 INRIRNSTIGTAEERQAAMNRINEIVLETIR 10259
Cdd:TIGR01612 1550 IKEIKDAHKKFILEAEKSEQKIKEIKKEKFR 1580
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8766-9431 |
1.08e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8766 DQKLAQDKQRATETLNNLSNLNTPQRQALENQINNAATRGEVAQKLTEAQALNQAMEA------------------LRNS 8827
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCmpdtyherkqvlekelkhLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8828 IQDQQQTEAGSKFINEDKPQKDAYQAAVQHAKDLIN--QTSNPTLDKAQvEQLTQAVNQAKDNLHGdQKLADDKQHAVTD 8905
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEelRAQEAVLEETQ-ERINRARKAAPLAAHI-KAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8906 LNQLNGLNNPQRQALESQINNAATRDEVAQKLAEAKALNQAMEALRnsiqdqQQTESGSKFINEDKPQKDAYQAAVQHAK 8985
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR------DAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8986 DLINQTGNPTLDKSQVEQLTQAVATAkDNLHGDQKLVRdQQQAVTTVNALPNLNHAQQQALTDAINAAPTRTEVAQHVQT 9065
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATI-DTRTSAFRDLQ-GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9066 ATELDHAMETLKNKvdqvntdkaqPNYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELNGNE 9145
Cdd:TIGR00618 465 AQSLKEREQQLQTK----------EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9146 -RVAEAKTQAKQTIDQLTHLnadqiatakqnidqatkLQPIAELVDQATQLNQSMDQLQQAVNEHA----NVEQTVDYTQ 9220
Cdd:TIGR00618 535 qTYAQLETSEEDVYHQLTSE-----------------RKQRASLKEQMQEIQQSFSILTQCDNRSKedipNLQNITVRLQ 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9221 ADLDKQNAYKQAIAEAENVLKQNANKQQVDQALQNILNAKQALNGDERVALAKTngkhdidqlnALNNAQQD----GFKG 9296
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL----------QLTLTQERvrehALSI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9297 RIDQSNDLNQIQQIVDEAKALNRAMNQLSQEITGNEGRTKGSTNYVNADTQVKRVYDEAVDKAKEALNkatGQNLTAEEV 9376
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQS 744
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 9377 IK--LNDAVTAAKQALNGEERLNNRKSEALQRLDQLTHL----NNAQRQLAIQQINNAETL 9431
Cdd:TIGR00618 745 LKelMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLaaeiQFFNRLREEDTHLLKTLE 805
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
9074-9142 |
1.17e-03 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 41.15 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 9074 ETLKNKVDQVNTDKAQPNYTEASTDKKDAVDQALQAAQSITDPTNGSNANKYAVEQALTKLQGKENELN 9142
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
9715-9941 |
1.65e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9715 QAIEQVHANEIPKAKIDANKDVDKQvqaLIDEIDRNPNLTDKEKQALKDRINQILQQGHNGINnamtkEEIEHAKAQlaQ 9794
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQERE---QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFN-----EEQAEWKEL--E 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9795 ALQDIKDLVKAKENAKQdVDKQVQALIDEIDRNpnltDKEKQALKDRINQILQQGHNginnamTKEEIEQAKAQLAQALQ 9874
Cdd:pfam13868 147 KEEEREEDERILEYLKE-KAEREEEREAEREEI----EEEKEREIARLRAQQEKAQD------EKAERDELRAKLYQEEQ 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 9875 DIKDLVKAKEDAKNAIK---ALANEKRDQINSNpdltpEQKAKALKEIDEAEK-RALENIENAQTKDQLNK 9941
Cdd:pfam13868 216 ERKERQKEREEAEKKARqrqELQQAREEQIELK-----ERRLAEEAEREEEEFeRMLRKQAEDEEIEQEEA 281
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
8916-9285 |
1.74e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8916 QRQALESQINNAATRDEVAQKLAEAKALNQAMEA-------LRNSIQDQQQTESgskfinedkpqkdaYQAAVQHAK-DL 8987
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlVQTALRQQEKIER--------------YQEDLEELTeRL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 8988 INQTGnptldksQVEQLTQAVATAKDNLHGDQKLVR-------DQQQAVTT-----------VNAL---------PNLN- 9039
Cdd:COG3096 364 EEQEE-------VVEEAAEQLAEAEARLEAAEEEVDslksqlaDYQQALDVqqtraiqyqqaVQALekaralcglPDLTp 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9040 ----------HAQQQALTDAINAAPTRTEVAQhvQTATELDHAMETLKNKVDQVNTDKAQPNYTEASTDKKDAVDQALQA 9109
Cdd:COG3096 437 enaedylaafRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9110 AQsitdptngsnankyaVEQALTKLQGKENELNGNERVAE--AKTQAKQ--TIDQLTHLNADQIATAKQNIDQAtklqpi 9185
Cdd:COG3096 515 QQ---------------LRAQLAELEQRLRQQQNAERLLEefCQRIGQQldAAEELEELLAELEAQLEELEEQA------ 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9186 AELVDQATQLNQSMDQLQQAVNEHANVEqtvdytQADLDKQNAYKQAiaeAENVLKQNANKQQVDQALQNIL-NAKQALN 9264
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAARA------PAWLAAQDALERL---REQSGEALADSQEVTAAMQQLLeREREATV 644
|
410 420
....*....|....*....|.
gi 616687517 9265 GDERVALAKTNGKHDIDQLNA 9285
Cdd:COG3096 645 ERDELAARKQALESQIERLSQ 665
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
5720-6009 |
1.75e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5720 PTMNAQEINQAKDqVTAKQQALNGQENLRTAQTNAKQHLN---GLSDLTDAQK---DAVKRQIEGAThvNEVTQAQNNad 5793
Cdd:PRK11281 28 RAASNGDLPTEAD-VQAQLDALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKeetEQLKQQLAQAP--AKLRQAQAE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5794 alntaMTNLKNgiqdqntikqgvnftDADEAKRNAYTNA-VTQAEQILNKAQgpntakdgveTALQNVQRAKNDLNGnqN 5872
Cdd:PRK11281 103 -----LEALKD---------------DNDEETRETLSTLsLRQLESRLAQTL----------DQLQNAQNDLAEYNS--Q 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5873 VANAKTTAKNALNNLTSiNNAQKEALKSQIDSATTvagvNQVSTTASELNTamsnLQngindeaatkAAQKYTDAdsdkQ 5952
Cdd:PRK11281 151 LVSLQTQPERAQAALYA-NSQRLQQIRNLLKGGKV----GGKALRPSQRVL----LQ----------AEQALLNA----Q 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5953 TAYNDAVTAAKTLLdKTAGTN--DNKAAVEQALQR-VNTAKTALNgDARLNEAKNTAKQQ 6009
Cdd:PRK11281 208 NDLQRKSLEGNTQL-QDLLQKqrDYLTARIQRLEHqLQLLQEAIN-SKRLTLSEKTVQEA 265
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10045-10259 |
2.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10045 EKELTVVKQQAIESIENAAQQKINEINNHAtltpEQKEAAIAEVNKLKQQAIEQINNAADvhTVEEVQHQEQAHIEQfnp 10124
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAEL----EELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAE--- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 10125 dqftidqaksnaIKSISDAIQHMIDEINASKDLTDKEKQEAISKLNQLKDQSIQAIQRAQSIDEIAQQLEQFKAQLKAAn 10204
Cdd:COG1196 297 ------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA- 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 10205 pfAKELENRKKSAISKIKDIST--DEINRIRNSTIGTAEERQAAMNRINEIVLETIR 10259
Cdd:COG1196 364 --EEALLEAEAELAEAEEELEElaEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4484-4538 |
2.94e-03 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 39.83 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 4484 NHNLEQAKSNANTTINGLQHLTTAQKDKLKQQVQQAQNVAGVDTVKSSANTLNGA 4538
Cdd:pfam01468 1 DQKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9345-9930 |
3.03e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9345 DTQVKRVYDEAvDKAKEALN-KATGQNLTAEEVIKLNDAVTAAKQALNGEERLNNRKSEALQRldQLTHLNNAQRQLAIQ 9423
Cdd:COG1196 199 ERQLEPLERQA-EKAERYRElKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA--ELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9424 QINNAETLNKASRAINRAVQlddAMGAVQQYIDEHHLDVISSTNYINADDNLKANYDNAITNAAHELDKVQGSAI-AKAE 9502
Cdd:COG1196 276 LEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9503 AEQLKQHIIDAQKALNGD-----QNLATAKDKANAFVDTLNGLNQQQQDLAHQAINNADTVTGIANIINDQIDLNNAMET 9577
Cdd:COG1196 353 LEEAEAELAEAEEALLEAeaelaEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9578 LKHLVDNEIPTAEQTVNYQNADDVAKSNFDDAKRLANALINSDNTNVNDINGAIQAVKDVIQNLNGEQRLQEAKDKAIQN 9657
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9658 VNKVLADKLKEIEASNATDQDKLIAKNKAEELANSIINNINKATSN--QDVSRVQTAGNQAIEQVHANEIPKAKIDANKD 9735
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaaAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9736 VDKQVQALIDEIDRNPNLTDKEKQALKDRI---NQILQQGHNGINNAMTKEEIEHAKAQLAQALQDIKDLVKAKENAKQD 9812
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9813 VDKQVQALIDEidrnpnLTDKEKQALKDRINQILQQghngINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKA 9892
Cdd:COG1196 673 ALLEAEAELEE------LAERLAEEELELEEALLAE----EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 616687517 9893 LANEKRDQINSNPDLTPEQKAKALKEIDEAEKR--ALENI 9930
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREieALGPV 782
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
8447-8512 |
3.12e-03 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 40.00 E-value: 3.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616687517 8447 LRESIQDNAATKANSKYINEDQPEQQNYDQAVQAANNIINEQT-ATLDNNVINQAATTVNTTKAALH 8512
Cdd:pfam07554 3 LKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNnPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
3279-3348 |
3.54e-03 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 40.00 E-value: 3.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3279 TGLKRGVANHNQVVQSDNYVNADTNKKNDYNNAYNHANDIINGNaQHPVITPSDVNNALSNVTNKEHALN 3348
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKT-NNPNATQEEVNQALTKLNTAINALN 69
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
7689-7757 |
3.68e-03 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 40.00 E-value: 3.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687517 7689 TQLKQGVADKDQTKANGNFVNADTEKQNAYNNAVAHAEQIISGTPNANVDPQQVAQALQQVTDAKNGLN 7757
Cdd:pfam07554 1 KALKTSINDKNATKTSSNYINADNDKKAAYNNAITAAKAILNKTNNPNATQEEVNQALTKLNTAINALN 69
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
9186-9572 |
3.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9186 AELVDQATQLNQSMDQLQQAVN---EHANVEQTVDYTQADLDKQNAYKQAIAEaenvLKQNANK--QQVDQALQNILNAK 9260
Cdd:PRK11281 32 NGDLPTEADVQAQLDALNKQKLleaEDKLVQQDLEQTLALLDKIDRQKEETEQ----LKQQLAQapAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9261 QALNGDERVALAKTNGKHDIDQLNALNNAQQDGfkgridqSNDLNQIQ-QIVDEAKALNRAMNQLSQeitgNEGRTKGST 9339
Cdd:PRK11281 108 DDNDEETRETLSTLSLRQLESRLAQTLDQLQNA-------QNDLAEYNsQLVSLQTQPERAQAALYA----NSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9340 NYVNAdtqvkrvydeavdkakealNKATGQNLTAEEVIKLNdavtaAKQALNGEERLNNRKSeaLQRLDQLTHLNNAQRQ 9419
Cdd:PRK11281 177 NLLKG-------------------GKVGGKALRPSQRVLLQ-----AEQALLNAQNDLQRKS--LEGNTQLQDLLQKQRD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9420 LAIQQINNAEtlnkasrainRAVQLddamgaVQQYIDEHHLDVISST--NYINADDNLKAnydnaitnaaheldkvQGSA 9497
Cdd:PRK11281 231 YLTARIQRLE----------HQLQL------LQEAINSKRLTLSEKTvqEAQSQDEAARI----------------QANP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9498 IAKAEAE---QLKQHIIDAQKALNG--DQNLATAK--DKANAF-------VDTLNG-------LNQQQQDLAhQAINNAD 9556
Cdd:PRK11281 279 LVAQELEinlQLSQRLLKATEKLNTltQQNLRVKNwlDRLTQSernikeqISVLKGslllsriLYQQQQALP-SADLIEG 357
|
410
....*....|....*.
gi 616687517 9557 TVTGIANIINDQIDLN 9572
Cdd:PRK11281 358 LADRIADLRLEQFEIN 373
|
|
| Rib |
pfam08428 |
Rib domain; The region featured in this family is found repeated in a number of bacterial ... |
2443-2506 |
3.95e-03 |
|
Rib domain; The region featured in this family is found repeated in a number of bacterial surface proteins, such as Rib and alpha. These are expressed by group B streptococci, and Rib is thought to confer protective immunity.
Pssm-ID: 462474 [Multi-domain] Cd Length: 76 Bit Score: 39.90 E-value: 3.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687517 2443 TTEIVKDYGSNVTPAE-INNAVQVANKRTATIKngTAMPTNLAGgsTTTIPVTVTYNDSSTEEVQ 2506
Cdd:pfam08428 9 GKDITVEVGETPDAEDgIKNKDDLPEGTKYTWK--TPPDTTTPG--DKTGTVVVTYPDGSTDEVE 69
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9612-9952 |
4.09e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9612 LANALINSD--NTNVNDINGAIQAVKDVIQNLNGEQR-LQEAKDKAIQNVNKVLADKLKEIEASN-ATDQDKLIAKNKAE 9687
Cdd:PRK01156 397 LKIQEIDPDaiKKELNEINVKLQDISSKVSSLNQRIRaLRENLDELSRNMEMLNGQSVCPVCGTTlGEEKSNHIINHYNE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9688 ELA--NSIINNINKATSNQDVSRVQTagNQAIEQVHANEIPKAKIDANKDVDKQVQALIDEIDRNpNLTDKEK--QALKD 9763
Cdd:PRK01156 477 KKSrlEEKIREIEIEVKDIDEKIVDL--KKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDkyEEIKN 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9764 RIN----QILQQGHNGINNAMTK------EEIEHAKAQLAQALQDIKDLVKAKENAKQDVDKQVQALIDEIDRNPNLTD- 9832
Cdd:PRK01156 554 RYKslklEDLDSKRTSWLNALAVislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNn 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9833 --KEKQALKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDAKNAIKALANEKRDQINSNpdltpe 9910
Cdd:PRK01156 634 kyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL------ 707
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 616687517 9911 qkakaLKEIDEAEKRALENIENAQTKDQLNKGLNLgLDDIRN 9952
Cdd:PRK01156 708 -----RTRINELSDRINDINETLESMKKIKKAIGD-LKRLRE 743
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
4693-5263 |
4.49e-03 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 44.38 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4693 TTYDQAVAAAKAILNKQTGSNSDKAAVDRALQQVTSTKDALNGDAKLAEAKAAAKQNLSTLNHITNAQRTALEGQINQAT 4772
Cdd:COG5295 79 AASSVASGGASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAGGSNTAT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4773 TVDGVNTVKTNANTLDGAMNSLQGSINDKDATLrnqnyldadESKRNAYTQAVTAAEGILNKQTGGNTSKADVDNALNAV 4852
Cdd:COG5295 159 ATGSSTANAATAAAGATSTSASGSSSGASGAAA---------ASAATGASAGGTASAAASASSSATGTSASVGVNAGAAT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4853 TRAKTALNGAENLRNAKTTATNTINGLPHLTQLQKDNLKHQVEQAQNVAGVNGVKDKGNTLNTAMGALRTSIQNDNTTKT 4932
Cdd:COG5295 230 GSAASAGGSASAGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4933 SQNYLDASDSNKNNYNTAVNNANGVINATNNPNIDANAINGMANQVNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKq 5012
Cdd:COG5295 310 GGNAGSGGGGAAALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAA- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5013 kdalkaqvNNAQRVSDANNVQHTATELNGAMTALKAAIADKERTKASGNYVNADQEKRQAYDSKVTNAENIINGTPNATL 5092
Cdd:COG5295 389 --------GAAGAGSAGSGGSSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5093 TVNDVNSATSQVNAAKTALNGDNNLRVAKEHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQTLNTVmkGL 5172
Cdd:COG5295 461 GAANVGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGG--GA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5173 RDSIANEATIKAGQNYTDASLNNRNEYDSAVTAAKAIINQTSNPTMEANTITQATSQVTTKEQALNGAQNLAQAKTTAKN 5252
Cdd:COG5295 539 AAAAGGGSTTAATGTNSVAVGNNTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAV 618
|
570
....*....|.
gi 616687517 5253 NLNNLTSINNA 5263
Cdd:COG5295 619 GNNAQASGANS 629
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2503-2752 |
4.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2503 EEVQESIFTKADKRE-LITDKNHLDdpvstdgkkpGTITQYNNAIHNAQQQINAAKTE-AQQVINNERATPQQVSDALTK 2580
Cdd:TIGR02169 740 EELEEDLSSLEQEIEnVKSELKELE----------ARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2581 VRAAQTKIDQA-KALLQNKEdnsQLVTSKNNLQSSVNQVPSTTGMTQQSIDNYNAKKRDAESEITAAQRVIDNGDATAQQ 2659
Cdd:TIGR02169 810 IEARLREIEQKlNRLTLEKE---YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 2660 ISDEKRRVDNALTALNQAKHDLTADthaLEQAVQQLNRTGITTGKKPASITAYNNSIRALQSDltSAKNSANAIIQKPIR 2739
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI--PEEELSLEDVQAELQ 961
|
250
....*....|...
gi 616687517 2740 SVQEVQTALTNVN 2752
Cdd:TIGR02169 962 RVEEEIRALEPVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5723-6001 |
4.71e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5723 NAQEINQAKDQVTAKQQALNGqenLRTAQTNAKQHLNGL-SDLTDAQKDAVKRQIEGATHVNEVTQAQNNADALNTAMTN 5801
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5802 LKNGIQDQNTiKQGVNFTDADEAKRNAYTNAvTQAEQILNKAQGPNTAKDGVETALQN----VQRAKNDLNGNQNVANAK 5877
Cdd:TIGR02168 759 LEAEIEELEE-RLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLlneeAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5878 TTAKNALNNLTSINNAQKEALKSQIDSATTvagvnQVSTTASELNtAMSNLQNGIndEAATKAAQKYTDADSDKQTAYND 5957
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELE-ALLNERASL--EEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 616687517 5958 AVTAAKTLLDKTAGT-NDNKAAVEQALQRVNTAKTALNGDARLNE 6001
Cdd:TIGR02168 909 KRSELRRELEELREKlAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
3098-3151 |
5.36e-03 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 39.06 E-value: 5.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 616687517 3098 QGLTLDRQPALSTLHGASNLNQAQQNNFTQQINAAQNHAALETIKSNITALNNA 3151
Cdd:pfam01468 2 QKLAQAKQDAKQEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| COG5412 |
COG5412 |
Phage-related protein [Mobilome: prophages, transposons]; |
5939-6310 |
6.20e-03 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 444167 [Multi-domain] Cd Length: 704 Bit Score: 43.92 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5939 KAAQKYTDADSDKQTAYNDAVtAAKTLLDKTAGTNDNKAAVEQALQRVNTAKTALNGDARLNEAKNTAKQQLATmshltd 6018
Cdd:COG5412 2 AAADASAKEAASAALLLAQAK-AADSELTAASGGVVSAAAKAQGSIAQLGKIGAAAGAEAALADSSLAFATLAA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6019 aqkGNLTEQIERGTTVAGVQGIQANAGTLDQAMNQLRQSIVSKDATKASEDYHDANTDLQNAY-NHAVSEAEGIISASNN 6097
Cdd:COG5412 75 ---ALGATVAGASLLLAAGGARAKGSAAAAAALGAVAAAAKVLNGALAAAGAALAATQALAAAaTGAKGEANAAAKAGGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6098 PEMNPDTINQKASQVNSANSALNGDEKLAEAKQTAKSDiGRLSDLNNAQQTSATAEVDHAPNLAAVTAAKNKATSLNTAM 6177
Cdd:COG5412 152 AALASAGLAAAGAAAAASALAAAGAIAKAILSASKLSG-QALAGQSAAAGGALEAAAAAAAGAAAAGAAAAAATAASALL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 6178 GNLKHALAEKDNTKRSVNYTDADQPKQQAYDTA---VTQAEGITNANGSNANETQVQAALNQLNQAKNDLNGDNKVAQAK 6254
Cdd:COG5412 231 ALAALQGLAAGAATGAAAGAAGAAGLGAAGAGAgqaAALLGLVAGAEASGGTAGGAVAGLAAGLAAAAGASANLGAAAAA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 616687517 6255 EAAKHALASYSNLNNAQSTAATSQIDNATTVAGVTTAQNTANELNTAMGQLQNGIN 6310
Cdd:COG5412 311 SFGASLAASAGVDTAAAALAAAEAIADGSLVAGLGSAGTVLSTLSGAVGGLEGAIG 366
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
9128-9440 |
6.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9128 EQALTKLQGKENEL--------NGNERVAEAKTQAKQTIDQLTHLN-----------ADQIATAKQNIDQATKLQP-IAE 9187
Cdd:PRK04863 836 EAELRQLNRRRVELeraladheSQEQQQRSQLEQAKEGLSALNRLLprlnlladetlADRVEEIREQLDEAEEAKRfVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9188 LVDQATQLNQSMDQLQQAVNEHANVEQtvDYTQADLDKQNAYKQAIAEAEnvLKQNANKQQVDQAlQNILNAKQALNgde 9267
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQ--DYQQAQQTQRDAKQQAFALTE--VVQRRAHFSYEDA-AEMLAKNSDLN--- 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9268 rvalaktngkhdiDQLNAlnnaqqdgfkgridqsnDLNQIQQIVDEAK-ALNRAMNQLSQeitgnegrtkgsTNYVNADT 9346
Cdd:PRK04863 988 -------------EKLRQ-----------------RLEQAEQERTRAReQLRQAQAQLAQ------------YNQVLASL 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9347 QVK-RVYDEAVDKAKEALnKATGQNLTAEeviklndavtAAKQALNGEERLNNRKSEALQRLDQLthlnnaQRQLAIQQI 9425
Cdd:PRK04863 1026 KSSyDAKRQMLQELKQEL-QDLGVPADSG----------AEERARARRDELHARLSANRSRRNQL------EKQLTFCEA 1088
|
330
....*....|....*
gi 616687517 9426 nNAETLNKASRAINR 9440
Cdd:PRK04863 1089 -EMDNLTKKLRKLER 1102
|
|
| GA |
pfam01468 |
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha ... |
4748-4790 |
6.34e-03 |
|
GA module; The GA (protein G-related Albumin-binding) module is composed of three alpha helices. This module is found in a range of bacterial cell surface proteins. The GA module from Swiss:Q51911 shows a strong affinity for albumin.
Pssm-ID: 396173 [Multi-domain] Cd Length: 55 Bit Score: 38.68 E-value: 6.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 616687517 4748 QNLSTLNHITNAQRTALEGQINQATTVDGVNTVKTNANTLDGA 4790
Cdd:pfam01468 13 QEINGLTGLNDAQKQALKDQINQATTRTEVNQILQKAKALNNA 55
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
4953-5583 |
6.52e-03 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 43.99 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 4953 NANGVINATNNPNIDANAINGMANQVNTTKAALNGAQNLAQAKTNATNTINNAHDLNQKQKDALKAQVNNAQRVSDANNV 5032
Cdd:COG5295 1 SASNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5033 QHTATELNGAMTALKAAIADKERTKASGNYVNADQEKRQAYDSKVTNAENIINGTPNATLTVNDVNSATSQVNAAKTALN 5112
Cdd:COG5295 81 SSVASGGASAATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAGGSNTATAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5113 GDNNLRVAKEHANNTIDGLAQLNNAQKAKLKEQVQSATTLDGVQTVKNSSQTLNTVMKGLRDSIANEATIKAGQNYTDAS 5192
Cdd:COG5295 161 GSSTANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5193 LNNRNEYDSAVTAAKAIINQTSNPTMEANTITQATSQVTTKEQALNGAQNLAQAKTTAKNNLNNLTSINNAQKDALTRSI 5272
Cdd:COG5295 241 AGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5273 DGATTVAGVNQETAKATELNNAMHSLQNGINDETQTKQTQKYLDAEPSKKSAYDQAVNAAKAILTKASGQNVDKAAVEQA 5352
Cdd:COG5295 321 AALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5353 LQNVNSTKTALNGDAKLNEAKAAAKQTLGTLTHINNAQRTALDNEITQATNVEGVNTVKAKAQQLDGAMGQLETSIRDKD 5432
Cdd:COG5295 401 SSTGASAGGGASAAGGAAAGSAAAGTSSNTSAVGASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAAATAAA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 5433 TTLQSQNYQDADDAKRTAYSQAVNAAATILNKTSGGNTPKADVERAMQTVTQANTALNGIQNLERAKQAANTAITNASDL 5512
Cdd:COG5295 481 ATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGN 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616687517 5513 NTKQKEALKAQVTSAGRVSVANGVEHTVTELNTAMTALKRAIADKADTKASGNYVNADANKRQAYDEKVTA 5583
Cdd:COG5295 561 NTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDTDAVNGGGAVATGDNSVAVGNNAQASGANSVA 631
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3715-3953 |
7.84e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3715 ADQVNSSKTALNGDENL----AAAKQNAKTYLNSLTSITDAQKNNlisqitsatrvsgvDTVKQNAQHLDQAMANLQSGI 3790
Cdd:PRK11281 38 EADVQAQLDALNKQKLLeaedKLVQQDLEQTLALLDKIDRQKEET--------------EQLKQQLAQAPAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3791 NNESQVKSSEKYRDADT--------------NKQQEYDNAITAAKAIL-NKQHGPNTAQNAVEAALQRV----------- 3844
Cdd:PRK11281 104 EALKDDNDEETRETLSTlslrqlesrlaqtlDQLQNAQNDLAEYNSQLvSLQTQPERAQAALYANSQRLqqirnllkggk 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 3845 -------NTAKNALNGDAKLIAAQNAAKQHL----GTLTHITTAQHNDLTNQISQatnlagvesvkqsansLDGAMGNLQ 3913
Cdd:PRK11281 184 vggkalrPSQRVLLQAEQALLNAQNDLQRKSlegnTQLQDLLQKQRDYLTARIQR----------------LEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 616687517 3914 TAINDKSGTLASQNFLDADEQKRNayNQAVSN----AETILNKQ 3953
Cdd:PRK11281 248 EAINSKRLTLSEKTVQEAQSQDEA--ARIQANplvaQELEINLQ 289
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9782-9953 |
7.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9782 KEEIEHAKAQLAqaLQDIKDLVKAKENAKQDVDKQVQaLIDEIDRNPNLTDKEKQALKDRIN------QILQQGHNGINN 9855
Cdd:TIGR02168 219 KAELRELELALL--VLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSeleeeiEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9856 AMTK--EEIEQAKAQLAQALQDIKDL------VKAKEDAKNAIKALANEKRDQINSNPDLTPEQKAKALKEIDEAEKRAL 9927
Cdd:TIGR02168 296 EISRleQQKQILRERLANLERQLEELeaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180
....*....|....*....|....*.
gi 616687517 9928 ENIENAQTKDQLNKGLNLGLDDIRNT 9953
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
1540-1700 |
8.79e-03 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 43.88 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1540 SATAPNVTSATNKTINLVATDTSGNTATTSFNVTIKPLRDKYRVGTSSTAANPVRiANISNNATVSQADQTAIINSLTFT 1619
Cdd:NF038112 1242 SFTAPEVTADTVLTFQLVVSDGTKTSAPDTVTVLVRNVNRAPVAVAGAPATVDER-STVTLDGSGTDADGDALTYAWTQT 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 1620 SNAP----NRNYATAS--ASEITSktvsnvsrtgnNAQVTVTVTYQDGTTS---TVTVPVKHV--IPEIVAHSHYTVQGQ 1688
Cdd:NF038112 1321 SGPAvtltGATTATATftAPEVTA-----------DTQLTFTLTVSDGTASatdTVTVTVRNVnrAPVANAGADQTVDER 1389
|
170
....*....|..
gi 616687517 1689 DFPTGNGaSASD 1700
Cdd:NF038112 1390 STVTLSG-SATD 1400
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
9622-9886 |
9.91e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9622 TNVNDINGAIQAVKDVIQNLNGE--QRLQEAKDKAIQNVNKVlADKLKEIEASNATDQDK--LIAKNKAEELANSIINNI 9697
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAISKAESatAVAKEAKDDAIQAVKAH-TDSLKEASDTAEISREKatDSALQKAEALAEKLKEVI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9698 NKATSNQDVSRVQTAGNqaieqvhANEIPKAKIDANKDVDKQVQALIDEIDRNPNLTD-------KEKQALKDRINQILQ 9770
Cdd:pfam09731 200 NLAKQSEEEAAPPLLDA-------APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKElvaseriVFQQELVSIFPDIIP 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687517 9771 --QGHNGINNAMTKEEIEHAKA---QLAQALQDIKDLVKAK-----ENAKQDVDKQVQALIDEIDRNPNLTDKEKQA--- 9837
Cdd:pfam09731 273 vlKEDNLLSNDDLNSLIAHAHReidQLSKKLAELKKREEKHieralEKQKEELDKLAEELSARLEEVRAADEAQLRLefe 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 616687517 9838 ---------LKDRINQILQQGHNGINNAMTKEEIEQAKAQLAQALQDIKDLVKAKEDA 9886
Cdd:pfam09731 353 rereeiresYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAG 410
|
|
|