|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1-1230 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 2134.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1 MSQEYTEDKEVTLSKLSSGRRLLEALLIVIALFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGVPGAWLADTLFFIFG 80
Cdd:PRK10263 1 MSQEYTEDKEVTLTKLSSGRRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 81 VMAYTIPVIIIGGCWFAWRHRQNDDYIDYFAVSLRLIGALALILTSCGLAAINADDIWYFASGGVIGSLLSSALQPMLHS 160
Cdd:PRK10263 81 VMAYTIPVIIVGGCWFAWRHQSSDEYIDYFAVSLRIIGVLALILTSCGLAAINADDIWYFASGGVIGSLLSTTLQPLLHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 161 SGGTLALLCIWAAGLTLFTGWSWVSIAEKIGSFILTILTFASNRTRRDDTWVDDDDYEEEEYEEEDeAPVPRRESRRARI 240
Cdd:PRK10263 161 SGGTIALLCVWAAGLTLFTGWSWVTIAEKLGGWILNILTFASNRTRRDDTWVDEDEYEDDEEYEDE-NHGKQHESRRARI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 241 LRGALARRQRVAEKFANPLGRKTDAALFSGKRMDEDEQVEYRAAGAAVDPDDVLFSGSRATPGEFDEYDPLLNGHSVTAP 320
Cdd:PRK10263 240 LRGALARRKRLAEKFINPMGRQTDAALFSGKRMDDDEEITYTARGVAADPDDVLFSGNRATQPEYDEYDPLLNGAPITEP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 321 VAAAAAATTAAQAYAAPVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIP----------------- 383
Cdd:PRK10263 320 VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQqsqyaqpavqyneplqq 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 384 -----------------------------------VQQEPWQQPYQPPQPEYEPQHYE-QPVAQPYQEYvPEPVEPAQPY 427
Cdd:PRK10263 400 pvqpqqpyyapaaeqpaqqpyyapapeqpaqqpyyAPAPEQPVAGNAWQAEEQQSTFApQSTYQTEQTY-QQPAAQEPLY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 428 AEPQPEPE--------VMEEVKPSRPPMYYFEEVEERRAREREQLAAWYQPVPEPAQEPVTKAPSV------SVPPVDAT 493
Cdd:PRK10263 479 QQPQPVEQqpvvepepVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSSLkapsvaAVPPVEAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 494 PAVAPVAESVKQATV----AAAAAAPVFSLATGGAPRPQVKEGIGPQLPRPNRVRVPTRRELASYGIKLPSQRMAEEKAR 569
Cdd:PRK10263 559 AAVSPLASGVKKATLatgaAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGIKLPSQRAAEEKAR 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 570 ESDY----------EDDADDMQQDELARQFAAQQNQRYGEEYQHDEPALDDED-EAAEAELARQFAATQQQRYSGEQPTG 638
Cdd:PRK10263 639 EAQRnqydsgdqynDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDAdAAAEAELARQFAQTQQQRYSGEQPAG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 639 ANPFSLSDFEFSPMKDLVDDGPSEPLFTPSVMPEAEPVR------------------------QQPAPQAYAQPQQPVQQ 694
Cdd:PRK10263 719 ANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQpvapqqqyqqpqqpvapqpqyqqpQQPVAPQPQYQQPQQPV 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 695 PYAQPQQPQHQPPQFQQPAPQPQ---------------------ESLIHPLLMRNGDSRPLQRPSTPLPSLDLLTPPPAE 753
Cdd:PRK10263 799 APQPQYQQPQQPVAPQPQYQQPQqpvapqpqyqqpqqpvapqpqDTLLHPLLMRNGDSRPLHKPTTPLPSLDLLTPPPSE 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 754 VEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKP 833
Cdd:PRK10263 879 VEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKP 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 834 YVGLELPNKKRQTVYLREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKA 913
Cdd:PRK10263 959 YVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKA 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 914 QPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAGYNEKIAQAMRMGRPI 993
Cdd:PRK10263 1039 QPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRMMRPI 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 994 PDPYWKPGDSMDAQHPVLEKLPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1073
Cdd:PRK10263 1119 PDPYWKPGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1074 PTRIAFTVSSKIDSRTILDQGGAESLLGMGDMLYSGPNSTSPVRVHGAFVRDEEVHAVVQDWKARGRPQYVDGITSDTES 1153
Cdd:PRK10263 1199 PTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSES 1278
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915228672 1154 EGGGGGFDGGEELDPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPPFD 1230
Cdd:PRK10263 1279 EGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPPFD 1355
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
739-1228 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 900.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 739 TPLPSLDLLTPPPAEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 818
Cdd:COG1674 135 AVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 819 STVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMPHLLVAGTTGSGK 898
Cdd:COG1674 215 AAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 899 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAG 978
Cdd:COG1674 295 SVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 979 YNEKIAQAMRMGRPipdpywkpgdsmdaqHPVLEKLPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQ 1058
Cdd:COG1674 375 YNEKVREAKAKGEE---------------EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1059 RPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQGGAESLLGMGDMLYSGPNSTSPVRVHGAFVRDEEVHAVVQDWKAR 1138
Cdd:COG1674 440 RPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQ 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1139 GRPQYVDGITSDtesEGGGGGFDGGEELDPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHN 1218
Cdd:COG1674 520 GEPEYIEEILEE---EEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGS 596
|
490
....*....|
gi 1915228672 1219 GNREVLAPPP 1228
Cdd:COG1674 597 KPREVLVSPE 606
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
849-1061 |
3.14e-89 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 287.35 E-value: 3.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 849 LREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMP-HLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKM 927
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 928 LELSVYEGIPHLLT-EVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAGYNEKIAQAMRMGRPIPDPYWKPGDSMDA 1006
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915228672 1007 QHPVLEKLPYIVVLVDEFADLMMTVGKK----VEELIARLAQKARAAGIHLVLATQRPS 1061
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1167-1226 |
2.16e-31 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 117.13 E-value: 2.16e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1167 DPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAP 1226
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
870-1091 |
4.10e-24 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 110.46 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 870 GKDiagDPVVADL---AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK---MLELsvYEGIPHLLTeV 943
Cdd:TIGR03928 454 GKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLLG-T 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 944 VTDMkDAANALRW--SVN-EMERRYKLMSALGVRNLAGYNEKiaqamrmgrpipdpYWkpgdsmdaQHPVLEKLPYIVVL 1020
Cdd:TIGR03928 528 ITNL-DGAQSMRAlaSIKaELKKRQRLFGENNVNHINQYQKL--------------YK--------QGKAKEPMPHLFLI 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915228672 1021 VDEFADLmmtvgkKVE--ELIARLAQKA---RAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTIL 1091
Cdd:TIGR03928 585 SDEFAEL------KSEqpEFMKELVSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
887-1079 |
8.55e-09 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 55.30 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 887 HLLVAGTTGSGKSVGVNAMILSMLykaqPEDVRFIMIDPKMlELSVyegiphllteVVTDMKDAANALRwsvnemerryK 966
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-ELFL----------VIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 967 LMSALgvrnLAGYNEKIAQAMRMGRPIPdpywkpgdsmdaqhpvleklpyIVVLVDEFADLMmtvgkKVEELIARLAqKA 1046
Cdd:cd01127 56 LFFNQ----LFRALTELASLSPGRLPRR----------------------VWFILDEFANLG-----RIPNLPNLLA-TG 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915228672 1047 RAAGIHLVLATQ------RPSVDVITGLIKANIPTRIAF 1079
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
337-504 |
7.16e-06 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 50.15 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIPVQQEPWQQPYQPPQPEYEPQHYE---QPvAQPY 413
Cdd:NF033839 317 PKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEvkpQP-EKPK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 414 QEYVPEPVEPaQPYAEPQPE---PEVM-------EEVKPSRPpmyyfeeveerrarereqlaawyQPVPEPAQEPVTKAP 483
Cdd:NF033839 396 PEVKPQPEKP-KPEVKPQPEkpkPEVKpqpekpkPEVKPQPE-----------------------KPKPEVKPQPEKPKP 451
|
170 180
....*....|....*....|.
gi 1915228672 484 SVSVPPVDATPAVAPVAESVK 504
Cdd:NF033839 452 EVKPQPETPKPEVKPQPEKPK 472
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
337-540 |
5.35e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 47.46 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIPVQQepwqqpyqppqpeyepqhyEQPvAQPYQEY 416
Cdd:NF033839 306 EKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK-------------------PQP-EKPKPEV 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 417 VPEPVEPaQPYAEPQPE---PEVMEEVKPSRPPMYyfeeveerrarereqlAAWYQPVPEPAQEPVTKAPSVSVPPVDAT 493
Cdd:NF033839 366 KPQPEKP-KPEVKPQPEtpkPEVKPQPEKPKPEVK----------------PQPEKPKPEVKPQPEKPKPEVKPQPEKPK 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915228672 494 PAVAPVAESVKQATVAAAAAAPVFSLATGGAPRPQVKEgiGPQLPRP 540
Cdd:NF033839 429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKP--QPEKPKP 473
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1-1230 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 2134.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1 MSQEYTEDKEVTLSKLSSGRRLLEALLIVIALFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGVPGAWLADTLFFIFG 80
Cdd:PRK10263 1 MSQEYTEDKEVTLTKLSSGRRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 81 VMAYTIPVIIIGGCWFAWRHRQNDDYIDYFAVSLRLIGALALILTSCGLAAINADDIWYFASGGVIGSLLSSALQPMLHS 160
Cdd:PRK10263 81 VMAYTIPVIIVGGCWFAWRHQSSDEYIDYFAVSLRIIGVLALILTSCGLAAINADDIWYFASGGVIGSLLSTTLQPLLHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 161 SGGTLALLCIWAAGLTLFTGWSWVSIAEKIGSFILTILTFASNRTRRDDTWVDDDDYEEEEYEEEDeAPVPRRESRRARI 240
Cdd:PRK10263 161 SGGTIALLCVWAAGLTLFTGWSWVTIAEKLGGWILNILTFASNRTRRDDTWVDEDEYEDDEEYEDE-NHGKQHESRRARI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 241 LRGALARRQRVAEKFANPLGRKTDAALFSGKRMDEDEQVEYRAAGAAVDPDDVLFSGSRATPGEFDEYDPLLNGHSVTAP 320
Cdd:PRK10263 240 LRGALARRKRLAEKFINPMGRQTDAALFSGKRMDDDEEITYTARGVAADPDDVLFSGNRATQPEYDEYDPLLNGAPITEP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 321 VAAAAAATTAAQAYAAPVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIP----------------- 383
Cdd:PRK10263 320 VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQqsqyaqpavqyneplqq 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 384 -----------------------------------VQQEPWQQPYQPPQPEYEPQHYE-QPVAQPYQEYvPEPVEPAQPY 427
Cdd:PRK10263 400 pvqpqqpyyapaaeqpaqqpyyapapeqpaqqpyyAPAPEQPVAGNAWQAEEQQSTFApQSTYQTEQTY-QQPAAQEPLY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 428 AEPQPEPE--------VMEEVKPSRPPMYYFEEVEERRAREREQLAAWYQPVPEPAQEPVTKAPSV------SVPPVDAT 493
Cdd:PRK10263 479 QQPQPVEQqpvvepepVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSSLkapsvaAVPPVEAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 494 PAVAPVAESVKQATV----AAAAAAPVFSLATGGAPRPQVKEGIGPQLPRPNRVRVPTRRELASYGIKLPSQRMAEEKAR 569
Cdd:PRK10263 559 AAVSPLASGVKKATLatgaAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGIKLPSQRAAEEKAR 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 570 ESDY----------EDDADDMQQDELARQFAAQQNQRYGEEYQHDEPALDDED-EAAEAELARQFAATQQQRYSGEQPTG 638
Cdd:PRK10263 639 EAQRnqydsgdqynDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDAdAAAEAELARQFAQTQQQRYSGEQPAG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 639 ANPFSLSDFEFSPMKDLVDDGPSEPLFTPSVMPEAEPVR------------------------QQPAPQAYAQPQQPVQQ 694
Cdd:PRK10263 719 ANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQpvapqqqyqqpqqpvapqpqyqqpQQPVAPQPQYQQPQQPV 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 695 PYAQPQQPQHQPPQFQQPAPQPQ---------------------ESLIHPLLMRNGDSRPLQRPSTPLPSLDLLTPPPAE 753
Cdd:PRK10263 799 APQPQYQQPQQPVAPQPQYQQPQqpvapqpqyqqpqqpvapqpqDTLLHPLLMRNGDSRPLHKPTTPLPSLDLLTPPPSE 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 754 VEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKP 833
Cdd:PRK10263 879 VEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKP 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 834 YVGLELPNKKRQTVYLREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKA 913
Cdd:PRK10263 959 YVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKA 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 914 QPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAGYNEKIAQAMRMGRPI 993
Cdd:PRK10263 1039 QPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRMMRPI 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 994 PDPYWKPGDSMDAQHPVLEKLPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1073
Cdd:PRK10263 1119 PDPYWKPGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1074 PTRIAFTVSSKIDSRTILDQGGAESLLGMGDMLYSGPNSTSPVRVHGAFVRDEEVHAVVQDWKARGRPQYVDGITSDTES 1153
Cdd:PRK10263 1199 PTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSES 1278
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915228672 1154 EGGGGGFDGGEELDPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPPFD 1230
Cdd:PRK10263 1279 EGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPPFD 1355
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
739-1228 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 900.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 739 TPLPSLDLLTPPPAEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 818
Cdd:COG1674 135 AVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 819 STVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMPHLLVAGTTGSGK 898
Cdd:COG1674 215 AAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 899 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAG 978
Cdd:COG1674 295 SVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 979 YNEKIAQAMRMGRPipdpywkpgdsmdaqHPVLEKLPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQ 1058
Cdd:COG1674 375 YNEKVREAKAKGEE---------------EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1059 RPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQGGAESLLGMGDMLYSGPNSTSPVRVHGAFVRDEEVHAVVQDWKAR 1138
Cdd:COG1674 440 RPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQ 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1139 GRPQYVDGITSDtesEGGGGGFDGGEELDPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHN 1218
Cdd:COG1674 520 GEPEYIEEILEE---EEEEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGS 596
|
490
....*....|
gi 1915228672 1219 GNREVLAPPP 1228
Cdd:COG1674 597 KPREVLVSPE 606
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
849-1061 |
3.14e-89 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 287.35 E-value: 3.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 849 LREVLDNTKFRDNPSPLTVVLGKDIAGDPVVADLAKMP-HLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKM 927
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 928 LELSVYEGIPHLLT-EVVTDMKDAANALRWSVNEMERRYKLMSALGVRNLAGYNEKIAQAMRMGRPIPDPYWKPGDSMDA 1006
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915228672 1007 QHPVLEKLPYIVVLVDEFADLMMTVGKK----VEELIARLAQKARAAGIHLVLATQRPS 1061
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
20-191 |
1.35e-56 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 193.57 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 20 RRLLEALLIVIALFAVWLMAALLSFNPSDPSWSQT-AWHEPIHNLGGVPGAWLADTLFFIFGVMAYTIPVIIIGGCWFAW 98
Cdd:pfam13491 2 RLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSgSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 99 RHRqnddyiDYFAVSLRLIGALALILTSCGLAAIN---ADDIWYFASGGVIGSLLSSALQPMLHSSGGTLALLCIWAAGL 175
Cdd:pfam13491 82 RRR------SLERRWLRLLGFLLLLLASSALFALRlpsLEFGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIGL 155
|
170
....*....|....*.
gi 1915228672 176 TLFTGWSWVSIAEKIG 191
Cdd:pfam13491 156 SLVTGFSWLALAERLG 171
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
741-841 |
1.06e-39 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 142.29 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 741 LPSLDLLTPPPAEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 820
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1915228672 821 VAVRVVEVIPGKPYVGLELPN 841
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
1167-1226 |
1.69e-31 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 117.47 E-value: 1.69e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1167 DPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAP 1226
Cdd:pfam09397 4 DELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1167-1226 |
2.16e-31 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 117.13 E-value: 2.16e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1167 DPLFDQAVNFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAP 1226
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
870-1091 |
4.10e-24 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 110.46 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 870 GKDiagDPVVADL---AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK---MLELsvYEGIPHLLTeV 943
Cdd:TIGR03928 454 GKD---DIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLLG-T 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 944 VTDMkDAANALRW--SVN-EMERRYKLMSALGVRNLAGYNEKiaqamrmgrpipdpYWkpgdsmdaQHPVLEKLPYIVVL 1020
Cdd:TIGR03928 528 ITNL-DGAQSMRAlaSIKaELKKRQRLFGENNVNHINQYQKL--------------YK--------QGKAKEPMPHLFLI 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915228672 1021 VDEFADLmmtvgkKVE--ELIARLAQKA---RAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTIL 1091
Cdd:TIGR03928 585 SDEFAEL------KSEqpEFMKELVSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
859-1123 |
1.48e-18 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 91.19 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 859 RDNPSPLTVVLGKDIAGDPVVADLAK-----M-PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK----ML 928
Cdd:TIGR03924 403 RPGRDRLRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 929 ELsvyEGIPHlLTEVVTDMKDAAN-------ALRwsvNEMERRYKLMSALG-VRNLAGYNEKIAQamrmGRPipdpywkp 1000
Cdd:TIGR03924 483 GL---EGLPH-VSAVITNLADEAPlvdrmqdALA---GEMNRRQELLRAAGnFANVAEYEKARAA----GAD-------- 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1001 gdsmdaqhpvLEKLPYIVVLVDEFADLMmtvGKKVE--ELIARLAQKARAAGIHLVLATQRPSVDVITGLiKANIPTRIA 1078
Cdd:TIGR03924 544 ----------LPPLPALFVVVDEFSELL---SQHPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIG 609
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1915228672 1079 FTVSSKIDSRTILDQGGA---ESLLGMGdmlYSGPNSTSPVRVHGAFV 1123
Cdd:TIGR03924 610 LKTFSASESRAVLGVPDAyhlPSTPGAG---YLKVDTAEPVRFRAAYV 654
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
839-1091 |
1.66e-14 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 78.88 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 839 LPNKkrqtVYLREvLDNTKFR----DNPSPLTVVLG-KDI----AGDPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSM 909
Cdd:TIGR03928 760 LEEK----IYLDD-LHAVEFDklwsKPKEPLQATIGlLDDpelqSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSL 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 910 LYKAQPEDVRFIMIDPKMLELSVYEGIPHlLTEVVT--DMKDAANALRWSVNEMERRYKLMSALGVRNLAGYNEKiaqam 987
Cdd:TIGR03928 835 ARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKA----- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 988 rmgrpipdpywkpgdsmdaqhpVLEKLPYIVVLVDEFadlmMTVGK-----KVEELIARLAQKARAAGIHLVL-ATQRPS 1061
Cdd:TIGR03928 909 ----------------------SGEKLPQIVIIIDNY----DAVKEepfyeDFEELLIQLAREGASLGIYLVMtAGRQNA 962
|
250 260 270
....*....|....*....|....*....|
gi 1915228672 1062 VDVItglIKANIPTRIAFTVSSKIDSRTIL 1091
Cdd:TIGR03928 963 VRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
866-1119 |
4.00e-09 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 60.01 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 866 TVVLGKDIAGD-PVVADLAKM--PHLLVAGTTGSGKSVGVnAMILSMLYKAqpeDVRFIMIDPK------------MLEL 930
Cdd:COG0433 25 GILIGKLLSPGvPVYLDLDKLlnRHILILGATGSGKSNTL-QVLLEELSRA---GVPVLVFDPHgeysglaepgaeRADV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 931 SVY---------------------------------EGIPHLLTEVVTDMKDAANALR---------WSVNEMERRYKLM 968
Cdd:COG0433 101 GVFdpgagrplpinpwdlfataselgplllsrldlnDTQRGVLREALRLADDKGLLLLdlkdliallEEGEELGEEYGNV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 969 SALGVRNLAGyneKIAQAMRMGRPIPDPYWKPGDSMDAQHPV----LEKLPY---------------------------- 1016
Cdd:COG0433 181 SAASAGALLR---RLESLESADGLFGEPGLDLEDLLRTDGRVtvidLSGLPEelqstfvlwllrelfearpevgdaddrk 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1017 --IVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSvDVITGlIKANIPTRIAFTVSSKIDSRTI---- 1090
Cdd:COG0433 258 lpLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKAVkaaa 335
|
330 340 350
....*....|....*....|....*....|...
gi 1915228672 1091 --LDQGGAESL--LGMGDMLYSGPNSTSPVRVH 1119
Cdd:COG0433 336 etLSEDLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
887-1079 |
8.55e-09 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 55.30 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 887 HLLVAGTTGSGKSVGVNAMILSMLykaqPEDVRFIMIDPKMlELSVyegiphllteVVTDMKDAANALRwsvnemerryK 966
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-ELFL----------VIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 967 LMSALgvrnLAGYNEKIAQAMRMGRPIPdpywkpgdsmdaqhpvleklpyIVVLVDEFADLMmtvgkKVEELIARLAqKA 1046
Cdd:cd01127 56 LFFNQ----LFRALTELASLSPGRLPRR----------------------VWFILDEFANLG-----RIPNLPNLLA-TG 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 1915228672 1047 RAAGIHLVLATQ------RPSVDVITGLIKANIPTRIAF 1079
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
769-949 |
1.02e-06 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 53.07 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 769 VEARLAD-------FRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLeLPn 841
Cdd:TIGR03925 248 IELRLGDpmdseidRRAAARVPAGRPGRGLTPDGLHMLIALPRLDGIASVDDLGTRGLVAVIRDVWGGPPAPPVRL-LP- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 842 kkrQTVYLREVLDntkfRDNPSPLTVVLGKDIAG-DPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRF 920
Cdd:TIGR03925 326 ---ARLPLSALPA----GGGAPRLRVPLGLGESDlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARL 398
|
170 180 190
....*....|....*....|....*....|....*..
gi 1915228672 921 IMIDPK--MLE------LSVYEGIPHLLTEVVTDMKD 949
Cdd:TIGR03925 399 VVVDYRrtLLGavpedyLAGYAATSAALTELIAALAA 435
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
876-1088 |
2.46e-06 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 51.92 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 876 DPVVADLAKMP-HLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLlTEVVTDMkdAANAL 954
Cdd:TIGR03925 69 DPLVVDLSGAAgHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHV-GGVAGRL--DPERV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 955 RWSVNEME----RRYKLMSALGVRNLAGYNEKIAqamrMGRPIPDPYwkpGDsmdaqhpvleklpyiVVLV--------D 1022
Cdd:TIGR03925 146 RRTVAEVEgllrRRERLFRTHGIDSMAQYRARRA----AGRLPEDPF---GD---------------VFLVidgwgtlrQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 1023 EFADLmmtvgkkvEELIARLAQKARAAGIHLVLATQRPSvdVITGLIKANIPTRIAF----TVSSKIDSR 1088
Cdd:TIGR03925 204 DFEDL--------EDKVTDLAARGLAYGVHVVLTASRWS--EIRPALRDLIGTRIELrlgdPMDSEIDRR 263
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
337-504 |
7.16e-06 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 50.15 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIPVQQEPWQQPYQPPQPEYEPQHYE---QPvAQPY 413
Cdd:NF033839 317 PKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEvkpQP-EKPK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 414 QEYVPEPVEPaQPYAEPQPE---PEVM-------EEVKPSRPpmyyfeeveerrarereqlaawyQPVPEPAQEPVTKAP 483
Cdd:NF033839 396 PEVKPQPEKP-KPEVKPQPEkpkPEVKpqpekpkPEVKPQPE-----------------------KPKPEVKPQPEKPKP 451
|
170 180
....*....|....*....|.
gi 1915228672 484 SVSVPPVDATPAVAPVAESVK 504
Cdd:NF033839 452 EVKPQPETPKPEVKPQPEKPK 472
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
867-925 |
9.23e-06 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 49.95 E-value: 9.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915228672 867 VVLGKDIAGDPVVADLAKM---PHLLVAGTTGSGKSVGVNAMILSMLYKaqpeDVRFIMIDP 925
Cdd:COG3451 183 IYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
877-1071 |
3.63e-05 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 48.45 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 877 PVVADLAKMPHLLVAGTTGSGKSvgvnAMILSML-YKAQPEDVRFIMIDPKMLELSVYEGIPHLLTeVVTDMKDAANALR 955
Cdd:TIGR03928 1088 PVYIDLTENPHLLIVGESDDGKT----NVLKSLLkTLAKQEKEKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILA 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 956 WSVNEMERRyklmsalgvrnlagyNEKIAQAMRMGRPIpdPYWKPgdsmdaqhpvleklpyIVVLVDEFADLMMTVGKKV 1035
Cdd:TIGR03928 1163 ELKEEIELR---------------EAAYKEALQNETGE--PAFKP----------------ILLIIDDLEDFIQRTDLEI 1209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1915228672 1036 EELIARLAQKARAAGIHLVLATQRPSV----DVITGLIKA 1071
Cdd:TIGR03928 1210 QDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ 1249
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
337-540 |
5.35e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 47.46 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIPVQQepwqqpyqppqpeyepqhyEQPvAQPYQEY 416
Cdd:NF033839 306 EKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK-------------------PQP-EKPKPEV 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 417 VPEPVEPaQPYAEPQPE---PEVMEEVKPSRPPMYyfeeveerrarereqlAAWYQPVPEPAQEPVTKAPSVSVPPVDAT 493
Cdd:NF033839 366 KPQPEKP-KPEVKPQPEtpkPEVKPQPEKPKPEVK----------------PQPEKPKPEVKPQPEKPKPEVKPQPEKPK 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1915228672 494 PAVAPVAESVKQATVAAAAAAPVFSLATGGAPRPQVKEgiGPQLPRP 540
Cdd:NF033839 429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKP--QPEKPKP 473
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
406-535 |
3.75e-04 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 43.52 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 406 EQPVA----QPYQEYVPEPVEPA-QPYAEPQPEPEVMEEVKPSRPpmyyfeeveerraREREQLAAWYQPVPEPAQEPVT 480
Cdd:PRK10819 45 AQPISvtmvAPADLEPPQAVQPPpEPVVEPEPEPEPIPEPPKEAP-------------VVIPKPEPKPKPKPKPKPKPVK 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1915228672 481 KAPSVSVPPVDatPAVAPVAESVKQATVAAaaaaPVFSLATGGAPRPQVKEGIGP 535
Cdd:PRK10819 112 KVEEQPKREVK--PVEPRPASPFENTAPAR----PTSSTATAAASKPVTSVSSGP 160
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
337-507 |
6.42e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 44.26 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESyipvqqepwqqpyqppqpeyepqhyEQPVAQPYQEY 416
Cdd:PRK10811 884 SAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQ-------------------------PQVITESDVAV 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 417 VPEPVEPAQPYAEPQPEPEVMEEVKPSRPPmyyfeeveerraREREQLAAWYQPVPEPAQEPVTKAPSVSVPPVDATPAV 496
Cdd:PRK10811 939 AQEVAEHAEPVVEPQDETADIEEAAETAEV------------VVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
|
170
....*....|.
gi 1915228672 497 APVAESVKQAT 507
Cdd:PRK10811 1007 PEATVEHNHAT 1017
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
366-593 |
1.54e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 366 GVHTPEPVIAPEPESYIPvQQEPWQQPYQPPQPEYEPQHYEQPVAQPYQEYVPEPVEPAQPYAEPQPEPEVMEEVK--PS 443
Cdd:PRK07764 580 GDWQVEAVVGPAPGAAGG-EGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPkhVA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 444 RPPMYYFEEVEERRAREREQLAAWYQPVPEPAQEPVTKAPSVSVPPVDATPAVAPVAESVKQATVAAAAAAPVFSLATGG 523
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915228672 524 APRPQVKE--GIGPQLPRPNRVRVPTRRELASYGIKLPSQR-----MAEEKARESDYED--DADDMQQDELARQFAAQQ 593
Cdd:PRK07764 739 VPLPPEPDdpPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPseeeeMAEDDAPSMDDEDrrDAEEVAMELLEEELGAKK 817
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
337-549 |
4.63e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 337 PVEAVMPSAPVPPPESVIQQPNVAWQTAPGVHTPEPVIAPEPESYIPVQQEPWQQPYQPPQPEYEPQHYEQPVAQPYQEY 416
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915228672 417 VPEP------VEPAQPYA-EPQPEPEVMEEVKPSRPPMYYFEEVEERRARERE---QLAAWYQPVPEPAQEPVTKAPsvs 486
Cdd:PHA03247 2846 PPPSlplggsVAPGGDVRrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFalpPDQPERPPQPQAPPPPQPQPQ--- 2922
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915228672 487 vPPVDATPAVAPVAESVKQATVAAAAAAPVFSLATGGAPRPQVKEGIGPQLPRPnRVRVPTRR 549
Cdd:PHA03247 2923 -PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP-RFRVPQPA 2983
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
887-926 |
6.30e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 40.35 E-value: 6.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1915228672 887 HLLVAGTTGSGKSVGVnamILSMLYKAQPEDvRFIMIDPK 926
Cdd:COG3505 1 HVLVIGPTGSGKTVGL---VIPNLTQLARGE-SVVVTDPK 36
|
|
| Trypan_PARP |
pfam05887 |
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ... |
370-446 |
7.77e-03 |
|
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.
Pssm-ID: 368653 Cd Length: 134 Bit Score: 38.23 E-value: 7.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915228672 370 PEPVIAPEPESyipvqqepwqqpyqppqpeyepqhyeQPVAQPYQEYVPEPVEPAQPYAEPQPEPEVMEEVKPSRPP 446
Cdd:pfam05887 61 PEPEPEPEPEP--------------------------EPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 111
|
|
| |
