|
Name |
Accession |
Description |
Interval |
E-value |
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
258-1424 |
2.98e-143 |
|
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: 471.78 E-value: 2.98e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 258 MYAMFAaLSPVMAVGSWYEQKSRRKQERKSEDKRFALALETLRRDLAKAASEEAARRRVECPDPATTLRVAAIPTTQLWQ 337
Cdd:TIGR03928 67 SIAMSL-VTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVNSRIWE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 338 RRFGAHDFLSLHAGVGAVPWDPPVERSG---AGRPDERVRKVIAA----SMIPCSPVEVNLSDaGVVGIVGDRDGALALA 410
Cdd:TIGR03928 146 KTPEHHDFLHVRLGTGNVPSSFEIKFPEeefSQRKDELLDEAQELkekyNTIENVPIVLDLSN-GPIGYVGKRSLVLEEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 411 RSLVCQAAVHSGPADVTIGVFCDQGRETDWEWTTWLPH-TRRLGNAsadRWFS-HARQRS------NEMLR----GLRDE 478
Cdd:TIGR03928 225 QNLVGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHfWLRDINV---RGFVyNERTRDqllnslYQILKerklALDDA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 479 IQSHPT----MSVLLVLDsdvltegrespaRSLL---GFGRHMNKQASSAremsrEVSGIVIAAAEDQLPAACTVVVTVA 551
Cdd:TIGR03928 302 NSKEKKrfspHYVFLITD------------RKLIldhVIMEYLNEDPSEL-----GISLIFVQDVMESLPENVKTVIDIK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 552 D-----------DAAATVTRPDDLKKVDDVVLAgvtleRAqrcaldLARFEdpELKTPGAALPSLVRLPPLIDLEAPTAG 620
Cdd:TIGR03928 365 NrnegeivleegELVEKSFTPDHLDNEDLEEYS-----RT------LAPLN--HLQNLKNSIPESVTFLEMYGVKKVEEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 621 KILHAW---ETSRGVSTPVGV-GENGVYSLDIVKD--GPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKG 694
Cdd:TIGR03928 432 NIQERWaknETYKSLAVPIGLrGKDDIVYLNLHEKahGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKG 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 695 GAAFAACERLPHTIGTISNLDEQLANRALRALEAEMEYRQRLFAAAGegVDNLDAYI----RAKPSEPLPRLLLVVDEFA 770
Cdd:TIGR03928 512 GGMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENN--VNHINQYQklykQGKAKEPMPHLFLISDEFA 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 771 MLAKDFPEVLSSLVRVATVGRTLGVHMILATQRPAGVVNDDILANTNLRVALRVQSREDSNNVIGVPDAAAIANAqkGRA 850
Cdd:TIGR03928 590 ELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVP--GRA 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 851 YVKLGQDDITPV-QTALvTGA---AQKDQDNAIEIQELRD--GVPIPNPPKPTRKDAK------SDLDLLIDAIVEANEK 918
Cdd:TIGR03928 668 YLQVGNNEVYELfQSAW-SGApydPDKDKKEEEDIYMINDlgQYELLNEDLSGLKRKKeikevpTELEAVIDEIQAYTEE 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 919 AG-YAPPRPvWPEALGERVDLAgfETGPIEGRPPLPTAGEVVgeQVNFAVSDDPDRQRQIPGGWDMA-GGNLMLVGIPGF 996
Cdd:TIGR03928 747 LNiEALPSP-WLPPLEEKIYLD--DLHAVEFDKLWSKPKEPL--QATIGLLDDPELQSQEPLTLDLSkDGHLAIFGSPGY 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 997 GTTTACATVALTLAQHYAPKDLDLIVLDMGARDLEPLEKLPHTSAYVGSGAGgrEKQMRLLRFLRQELETRR-------- 1068
Cdd:TIGR03928 822 GKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEE--EKIEKLIRRIKKEIDRRKklfseygv 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1069 ATSGPYRRM--------VVIIDGLAALRDE--YQDFEgmALLEGMYRayaDGPDLNMHFVITTSRARAI-PSAIDEVTTQ 1137
Cdd:TIGR03928 900 ASISMYNKAsgeklpqiVIIIDNYDAVKEEpfYEDFE--ELLIQLAR---EGASLGIYLVMTAGRQNAVrMPLMNNIKTK 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1138 KWMFrLADPYDYSTGGLKPAEAPSPVPGRCVPSVTKLQ-THVATPsVPLSDAVAVIVN----------RWGAPnKEQVVR 1206
Cdd:TIGR03928 975 IALY-LIDKSEYRSIVGRTKFTIEEIPGRGLIKKDEPTlFQTALP-VKGEDDLEVIENikaeiqkmneAWTGE-RPKPIP 1051
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1207 ELPDHVSVTELDA--VAHLGDEPWRIPIGLREADMAPQYLELYEGEHMLIAGPARSGKS----TLLMGLAESLRTS-AVA 1279
Cdd:TIGR03928 1052 MVPEELSLEEFREryEVRKILEEGSIPIGLDEETVEPVYIDLTENPHLLIVGESDDGKTnvlkSLLKTLAKQEKEKiGLI 1131
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1280 EGTDLAVWGIgSKRSPIAS--SDLDNVAVGPDEI--------PALVAAARMRT-----APLVLLIDDAERF----DDADQ 1340
Cdd:TIGR03928 1132 DSIDRGLLAY-RDLKEVATyiEEKEDLKEILAELkeeielreAAYKEALQNETgepafKPILLIIDDLEDFiqrtDLEIQ 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1341 SITDLVGSNLPH--VHVIAAGRSDDLRSLYSHWTKVVRKSRCGVLLVpnRDYDGELLGITVPRSAPvRISSGRGYACMGG 1418
Cdd:TIGR03928 1211 DILALIMKNGKKlgIHFIVAGTHSELSKSYDGVPKEIKQLRTGILGM--RKSDQSFFKLPFTRSEK-ELEPGEGYFVVNG 1287
|
....*.
gi 550741601 1419 QGALIQ 1424
Cdd:TIGR03928 1288 KYQKIK 1293
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
626-805 |
4.57e-32 |
|
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: 125.18 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 626 WETSRGvSTPVGVGENGV---YSLDIVKDGPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKGGaAFAACE 702
Cdd:pfam01580 10 FDTDYS-RLPIALGKDISgnpEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG-ELSAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 703 RLPHTIGTISNLDEQLANRALRALEAEMEYRQRLFAAAG--------EGVDNLDAYIRAKP----------------SEP 758
Cdd:pfam01580 88 DIPHLLSVPVATDPKRALRALEWLVDEMERRYALFRALGvrsiagynGEIAEDPLDGFGDVflviygvhvmctagrwLEI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 550741601 759 LPRLLLVVDEFAMLAKDFPE-----VLSSLVRVATVGRTLGVHMILATQRPA 805
Cdd:pfam01580 168 LPYLVVIVDERAELRLAAPKdsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
653-830 |
4.76e-26 |
|
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: 115.41 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 653 PHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILID--------FKGgaafaacerLPHTIG---TisnlDEQLANR 721
Cdd:COG1674 282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDpkmvelsvYNG---------IPHLLTpvvT----DPKKAAN 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 722 ALRALEAEMEYRQRLFAAAgeGVDNLDAY-----------IRAKPSEPLPRLLLVVDEFA---MLAKDfpEVLSSLVRVA 787
Cdd:COG1674 349 ALKWAVREMERRYKLFAKA--GVRNIAGYnekvreakakgEEEEGLEPLPYIVVIIDELAdlmMVAGK--EVEEAIARLA 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 550741601 788 TVGRTLGVHMILATQRPA-----GVvnddILANTNLRVALRVQSREDS 830
Cdd:COG1674 425 QKARAAGIHLILATQRPSvdvitGL----IKANIPSRIAFAVSSKIDS 468
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
653-883 |
6.83e-19 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 93.61 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 653 PHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKgGAAFAACERLPHTIGTISNlDEQLANRALRALEAEMEY 732
Cdd:PRK10263 1011 PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHLLTEVVT-DMKDAANALRWCVNEMER 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 733 RQRLFAAAgeGVDNLDAYIRA----------------KPS----------EPLPRLLLVVDEFAMLAKDFPEVLSSLV-R 785
Cdd:PRK10263 1089 RYKLMSAL--GVRNLAGYNEKiaeadrmmrpipdpywKPGdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIaR 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 786 VATVGRTLGVHMILATQRPA-GVVNDDILANTNLRVALRVQSREDSNNVIgvpdaaaianaQKGRAYVKLGQDDI----- 859
Cdd:PRK10263 1167 LAQKARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTIL-----------DQAGAESLLGMGDMlysgp 1235
|
250 260
....*....|....*....|....*..
gi 550741601 860 ---TPVQtalVTGAAQKDQDNAIEIQE 883
Cdd:PRK10263 1236 nstLPVR---VHGAFVRDQEVHAVVQD 1259
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
100-183 |
1.07e-13 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 68.06 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 100 DRPLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTgqSVAVDTTLAVGGSTLL 179
Cdd:COG1716 20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTF-----VNGQRVTEPA--PLRDGDVIRLGKTELR 92
|
....
gi 550741601 180 LRES 183
Cdd:COG1716 93 FRLS 96
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
654-824 |
2.04e-12 |
|
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: 66.09 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 654 HGLVGGTTGSGKSEFLRSMVAGLAACNAPtkltFILIDFKGGaafaacerlphtiGTISNLDEQLANRALRALeaemeYR 733
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGGS----VIITDPKGE-------------LFLVIPDRDDSFAALRAL-----FF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 734 QRLFAAAGEGVDNldayiraKPSEPLPRLLLVVDEFAMLAKdfpevLSSLVRVATVGRTLGVHMILATQRPA-------G 806
Cdd:cd01127 59 NQLFRALTELASL-------SPGRLPRRVWFILDEFANLGR-----IPNLPNLLATGRKRGISVVLILQSLAqleavygK 126
|
170
....*....|....*...
gi 550741601 807 VVNDDILANTNLRVALRV 824
Cdd:cd01127 127 DGAQTILGNCNTKLYLGT 144
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
105-181 |
2.95e-10 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 58.06 E-value: 2.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTgqSVAVDTTLAVGGSTLLLR 181
Cdd:cd00060 23 IGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTF-----VNGKRITPPV--PLQDGDVIRLGDTTFRFE 92
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
105-159 |
1.60e-07 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 49.50 E-value: 1.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVG-LRVIDQGSTNGTFaysseVDGLKVDS 159
Cdd:pfam00498 3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGGrFYLEDLGSTNGTF-----VNGQRLGP 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1249-1342 |
6.35e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1249 GEHMLIAGPARSGKSTLLMGLAESLR----------TSAVAEGTDLAVWGIGSKRSPIASSDLDNVAVgpdeipaLVAAA 1318
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGppgggviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRL-------ALALA 74
|
90 100
....*....|....*....|....
gi 550741601 1319 RmRTAPLVLLIDDAERFDDADQSI 1342
Cdd:smart00382 75 R-KLKPDVLILDEITSLLDAEQEA 97
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
105-157 |
4.55e-03 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 36.77 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 550741601 105 IGRSP-QADLSIASASVSWDHVHIQRD-DVGLRVIDQGSTNGTFaysseVDGLKV 157
Cdd:smart00240 3 IGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTF-----VNGKRI 52
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
258-1424 |
2.98e-143 |
|
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: 471.78 E-value: 2.98e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 258 MYAMFAaLSPVMAVGSWYEQKSRRKQERKSEDKRFALALETLRRDLAKAASEEAARRRVECPDPATTLRVAAIPTTQLWQ 337
Cdd:TIGR03928 67 SIAMSL-VTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVNSRIWE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 338 RRFGAHDFLSLHAGVGAVPWDPPVERSG---AGRPDERVRKVIAA----SMIPCSPVEVNLSDaGVVGIVGDRDGALALA 410
Cdd:TIGR03928 146 KTPEHHDFLHVRLGTGNVPSSFEIKFPEeefSQRKDELLDEAQELkekyNTIENVPIVLDLSN-GPIGYVGKRSLVLEEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 411 RSLVCQAAVHSGPADVTIGVFCDQGRETDWEWTTWLPH-TRRLGNAsadRWFS-HARQRS------NEMLR----GLRDE 478
Cdd:TIGR03928 225 QNLVGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHfWLRDINV---RGFVyNERTRDqllnslYQILKerklALDDA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 479 IQSHPT----MSVLLVLDsdvltegrespaRSLL---GFGRHMNKQASSAremsrEVSGIVIAAAEDQLPAACTVVVTVA 551
Cdd:TIGR03928 302 NSKEKKrfspHYVFLITD------------RKLIldhVIMEYLNEDPSEL-----GISLIFVQDVMESLPENVKTVIDIK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 552 D-----------DAAATVTRPDDLKKVDDVVLAgvtleRAqrcaldLARFEdpELKTPGAALPSLVRLPPLIDLEAPTAG 620
Cdd:TIGR03928 365 NrnegeivleegELVEKSFTPDHLDNEDLEEYS-----RT------LAPLN--HLQNLKNSIPESVTFLEMYGVKKVEEL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 621 KILHAW---ETSRGVSTPVGV-GENGVYSLDIVKD--GPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKG 694
Cdd:TIGR03928 432 NIQERWaknETYKSLAVPIGLrGKDDIVYLNLHEKahGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKG 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 695 GAAFAACERLPHTIGTISNLDEQLANRALRALEAEMEYRQRLFAAAGegVDNLDAYI----RAKPSEPLPRLLLVVDEFA 770
Cdd:TIGR03928 512 GGMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENN--VNHINQYQklykQGKAKEPMPHLFLISDEFA 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 771 MLAKDFPEVLSSLVRVATVGRTLGVHMILATQRPAGVVNDDILANTNLRVALRVQSREDSNNVIGVPDAAAIANAqkGRA 850
Cdd:TIGR03928 590 ELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVP--GRA 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 851 YVKLGQDDITPV-QTALvTGA---AQKDQDNAIEIQELRD--GVPIPNPPKPTRKDAK------SDLDLLIDAIVEANEK 918
Cdd:TIGR03928 668 YLQVGNNEVYELfQSAW-SGApydPDKDKKEEEDIYMINDlgQYELLNEDLSGLKRKKeikevpTELEAVIDEIQAYTEE 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 919 AG-YAPPRPvWPEALGERVDLAgfETGPIEGRPPLPTAGEVVgeQVNFAVSDDPDRQRQIPGGWDMA-GGNLMLVGIPGF 996
Cdd:TIGR03928 747 LNiEALPSP-WLPPLEEKIYLD--DLHAVEFDKLWSKPKEPL--QATIGLLDDPELQSQEPLTLDLSkDGHLAIFGSPGY 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 997 GTTTACATVALTLAQHYAPKDLDLIVLDMGARDLEPLEKLPHTSAYVGSGAGgrEKQMRLLRFLRQELETRR-------- 1068
Cdd:TIGR03928 822 GKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEE--EKIEKLIRRIKKEIDRRKklfseygv 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1069 ATSGPYRRM--------VVIIDGLAALRDE--YQDFEgmALLEGMYRayaDGPDLNMHFVITTSRARAI-PSAIDEVTTQ 1137
Cdd:TIGR03928 900 ASISMYNKAsgeklpqiVIIIDNYDAVKEEpfYEDFE--ELLIQLAR---EGASLGIYLVMTAGRQNAVrMPLMNNIKTK 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1138 KWMFrLADPYDYSTGGLKPAEAPSPVPGRCVPSVTKLQ-THVATPsVPLSDAVAVIVN----------RWGAPnKEQVVR 1206
Cdd:TIGR03928 975 IALY-LIDKSEYRSIVGRTKFTIEEIPGRGLIKKDEPTlFQTALP-VKGEDDLEVIENikaeiqkmneAWTGE-RPKPIP 1051
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1207 ELPDHVSVTELDA--VAHLGDEPWRIPIGLREADMAPQYLELYEGEHMLIAGPARSGKS----TLLMGLAESLRTS-AVA 1279
Cdd:TIGR03928 1052 MVPEELSLEEFREryEVRKILEEGSIPIGLDEETVEPVYIDLTENPHLLIVGESDDGKTnvlkSLLKTLAKQEKEKiGLI 1131
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1280 EGTDLAVWGIgSKRSPIAS--SDLDNVAVGPDEI--------PALVAAARMRT-----APLVLLIDDAERF----DDADQ 1340
Cdd:TIGR03928 1132 DSIDRGLLAY-RDLKEVATyiEEKEDLKEILAELkeeielreAAYKEALQNETgepafKPILLIIDDLEDFiqrtDLEIQ 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1341 SITDLVGSNLPH--VHVIAAGRSDDLRSLYSHWTKVVRKSRCGVLLVpnRDYDGELLGITVPRSAPvRISSGRGYACMGG 1418
Cdd:TIGR03928 1211 DILALIMKNGKKlgIHFIVAGTHSELSKSYDGVPKEIKQLRTGILGM--RKSDQSFFKLPFTRSEK-ELEPGEGYFVVNG 1287
|
....*.
gi 550741601 1419 QGALIQ 1424
Cdd:TIGR03928 1288 KYQKIK 1293
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
256-869 |
2.55e-100 |
|
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: 335.79 E-value: 2.55e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 256 NPMYAMFAAL---SPVMAVGSWYEQKSRRKQERKSEDKRFALALETLRRDLAKAASEEAARRRVECPDPATTlrVAAIPT 332
Cdd:TIGR03924 32 NPMFLIFPLMmlvSMLGMLAGGRGGGGKKTPELDEDRRDYLRYLDQLRREVRETAAAQRAALEWRHPDPDTL--WALVGT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 333 TQLWQRRFGAHDFLSLHAGVGAVPWDPPVERSGAGRPDER-------VRKVIAA-SMIPCSPVEVNLSDAGVVGIVGDRD 404
Cdd:TIGR03924 110 PRMWERRPGDPDFLEVRVGVGVQPLATRLVVPETGPVEDLepvtavaLRRFLRAhSTVPDLPVAVSLRGFARISLVGDRD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 405 GALALARSLVCQAAVHSGPADVTIGVFCDqGRETDWEWTTWLPH----TRRLGNASADRWFSHARQRSN----EMLRGLR 476
Cdd:TIGR03924 190 QARALARAMLCQLAVFHGPDDVGIAVVTS-DPDRDWDWLKWLPHnqhpTRFDAAGPARLVYTSLAELEAalaeLLADRGR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 477 DEIQSHPTMSVLLVLDSDVLTEGRESPARSllgfgrhmnkqassarEMSREVSGIVIAAAEDQLPAACTVVVTVADDAAA 556
Cdd:TIGR03924 269 FSPDDAASLPHLVVVVDGGDLPGWEDLIGE----------------SGLDGVTVIDLGGSLPGLPDRRGLRLVVEADRLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 557 TVTRPDDLKKVddVVLAGVTLERAQRCALDLARFEDPELKTPGAALPSLVRLPPLIDLEAPTAGKILHAWETSRG---VS 633
Cdd:TIGR03924 333 ARTADGVEEFG--VAPDQLSIAEAEALARRLARWRAATAGTVDAPLTGARDLLELLGIGDPATLDVDRLWRPRPGrdrLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 634 TPVGVGENG-VYSLDIvKD------GPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKGGAAFAACERLPH 706
Cdd:TIGR03924 411 VPIGVGDDGePVELDL-KEsaeggmGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLPH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 707 TIGTISNLDEQ--LANRALRALEAEMEYRQRLFAAAGeGVDNLDAYIRA----KPSEPLPRLLLVVDEFAMLAKDFPEVL 780
Cdd:TIGR03924 490 VSAVITNLADEapLVDRMQDALAGEMNRRQELLRAAG-NFANVAEYEKAraagADLPPLPALFVVVDEFSELLSQHPDFA 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 781 SSLVRVATVGRTLGVHMILATQRPAGVVNDDILANTNLRVALRVQSREDSNNVIGVPDAAAIANaQKGRAYVKLGQDDIT 860
Cdd:TIGR03924 569 DLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYHLPS-TPGAGYLKVDTAEPV 647
|
....*....
gi 550741601 861 PVQTALVTG 869
Cdd:TIGR03924 648 RFRAAYVSG 656
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
908-1425 |
8.69e-43 |
|
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: 165.94 E-value: 8.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 908 LIDAIVEANEKAGyAPPRPVWPEALGERVDLAGFeTGPIEGRPPLPTAGEVVGEQVNFAVSDDPDRQRQIPGGWDM--AG 985
Cdd:TIGR03925 2 VLDVVVDRLAGQG-PPAHQVWLPPLPEPPALDDL-LPRLDVDPWRVDYGQRGRLTVPVGIVDRPFEQRQDPLVVDLsgAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 986 GNLMLVGIPGFGTTTACATVALTLAQHYAPKDLDLIVLDMGARDLEPLEKLPHtsayVGSGAG--GREKQMRLLRFLRQE 1063
Cdd:TIGR03925 80 GHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH----VGGVAGrlDPERVRRTVAEVEGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1064 LETRRA--------TSGPYRRM--------------VVIIDGLAALRDEYQDFEG--MALLegmyrayADGPDLNMHFVI 1119
Cdd:TIGR03925 156 LRRRERlfrthgidSMAQYRARraagrlpedpfgdvFLVIDGWGTLRQDFEDLEDkvTDLA-------ARGLAYGVHVVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1120 TTSRARAIPSAIDEVTTQKWMFRLADPYDYSTGGLKPAEAPSPVPGRCVpSVTKLQTHVATPS---------VPLSDAVA 1190
Cdd:TIGR03925 229 TASRWSEIRPALRDLIGTRIELRLGDPMDSEIDRRAAARVPAGRPGRGL-TPDGLHMLIALPRldgiasvddLGTRGLVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1191 VIVNRWGAPnKEQVVRELPDHVSVTELdaVAHLGDEPWRIPIGLREADMAPQYLELYEGEHMLIAGPARSGKSTLLMGLA 1270
Cdd:TIGR03925 308 VIRDVWGGP-PAPPVRLLPARLPLSAL--PAGGGAPRLRVPLGLGESDLAPVYVDFAESPHLLIFGDSESGKTTLLRTIA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1271 ESLRTSAVAEGTDLAVwgIGSKRSP---IASSDLDNVAVGPDEIPALVAAA----RMRTAP------------------L 1325
Cdd:TIGR03925 385 RGIVRRYSPDQARLVV--VDYRRTLlgaVPEDYLAGYAATSAALTELIAALaallERRLPGpdvtpqqlrarswwsgpeI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1326 VLLIDDAERFDDADQSITDLVGSNLPH-----VHVIAAGRSDD-LRSLYSHWTKVVRKSRCGVLLVPNRDYDGELLGITV 1399
Cdd:TIGR03925 463 YVVVDDYDLVATGSGNPLAPLVELLPHardigLHVVVARRSGGaARALMDPVLARLKDLGAPGLLLSGDRDEGPLLGGVR 542
|
570 580
....*....|....*....|....*..
gi 550741601 1400 PRSAPvrisSGRGYACMGGQGA-LIQA 1425
Cdd:TIGR03925 543 PRPLP----PGRGVLVTRGGGPqLIQV 565
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
626-805 |
4.57e-32 |
|
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: 125.18 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 626 WETSRGvSTPVGVGENGV---YSLDIVKDGPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKGGaAFAACE 702
Cdd:pfam01580 10 FDTDYS-RLPIALGKDISgnpEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG-ELSAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 703 RLPHTIGTISNLDEQLANRALRALEAEMEYRQRLFAAAG--------EGVDNLDAYIRAKP----------------SEP 758
Cdd:pfam01580 88 DIPHLLSVPVATDPKRALRALEWLVDEMERRYALFRALGvrsiagynGEIAEDPLDGFGDVflviygvhvmctagrwLEI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 550741601 759 LPRLLLVVDEFAMLAKDFPE-----VLSSLVRVATVGRTLGVHMILATQRPA 805
Cdd:pfam01580 168 LPYLVVIVDERAELRLAAPKdsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
602-1120 |
2.83e-28 |
|
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: 121.64 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 602 LPSLVRLPPLIDLEAPTAGKILH-AWETSRGVSTPVGVGE------NGVYSLDIVKDGPHGLVGGTTGSGKSEFLRSMVA 674
Cdd:TIGR03925 22 LPPLPEPPALDDLLPRLDVDPWRvDYGQRGRLTVPVGIVDrpfeqrQDPLVVDLSGAAGHVAIVGAPQSGKSTALRTLIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 675 GLAACNAPTKLTFILIDFkGGAAFAACERLPHTIGTISNLDEQLANRALRALEAEMEYRQRLFAAAgeGVDNLDAYIRAK 754
Cdd:TIGR03925 102 ALALTHTPEEVQFYCLDF-GGGGLASLADLPHVGGVAGRLDPERVRRTVAEVEGLLRRRERLFRTH--GIDSMAQYRARR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 755 -----PSEPLPRLLLVVDEFAMLAKDFPEVLSSLVRVATVGRTLGVHMILATQRPAGvVNDDILANTNLRVALRVQSRED 829
Cdd:TIGR03925 179 aagrlPEDPFGDVFLVIDGWGTLRQDFEDLEDKVTDLAARGLAYGVHVVLTASRWSE-IRPALRDLIGTRIELRLGDPMD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 830 SnnVIGVPDAAAIANAQKGRAyvklgqddITPVQTALVTGAAQKDqdnaieiqelrdgvpipnppkptrkDAKSDLDLLI 909
Cdd:TIGR03925 258 S--EIDRRAAARVPAGRPGRG--------LTPDGLHMLIALPRLD-------------------------GIASVDDLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 910 DAIVEA-NEKAGYAPPRPVwpEALGERVDLAGFETGPIEGRPPLPTAgevVGEQVNFAVSDDPDRQRqipggwdmaggNL 988
Cdd:TIGR03925 303 RGLVAViRDVWGGPPAPPV--RLLPARLPLSALPAGGGAPRLRVPLG---LGESDLAPVYVDFAESP-----------HL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 989 MLVGIPGFGTTTACATVALTLAQHYAPKDLDLIVLD-----MGARDLEpleklpHTSAYVGSGAGGREKQMRLLRFLR-- 1061
Cdd:TIGR03925 367 LIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDyrrtlLGAVPED------YLAGYAATSAALTELIAALAALLErr 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550741601 1062 --------QELETRRATSGPyrRMVVIIdglaalrDEYQDFEG------MALLEGMYRAyadgPDLNMHFVIT 1120
Cdd:TIGR03925 441 lpgpdvtpQQLRARSWWSGP--EIYVVV-------DDYDLVATgsgnplAPLVELLPHA----RDIGLHVVVA 500
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
653-830 |
4.76e-26 |
|
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: 115.41 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 653 PHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILID--------FKGgaafaacerLPHTIG---TisnlDEQLANR 721
Cdd:COG1674 282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDpkmvelsvYNG---------IPHLLTpvvT----DPKKAAN 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 722 ALRALEAEMEYRQRLFAAAgeGVDNLDAY-----------IRAKPSEPLPRLLLVVDEFA---MLAKDfpEVLSSLVRVA 787
Cdd:COG1674 349 ALKWAVREMERRYKLFAKA--GVRNIAGYnekvreakakgEEEEGLEPLPYIVVIIDELAdlmMVAGK--EVEEAIARLA 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 550741601 788 TVGRTLGVHMILATQRPA-----GVvnddILANTNLRVALRVQSREDS 830
Cdd:COG1674 425 QKARAAGIHLILATQRPSvdvitGL----IKANIPSRIAFAVSSKIDS 468
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
653-883 |
6.83e-19 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 93.61 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 653 PHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKgGAAFAACERLPHTIGTISNlDEQLANRALRALEAEMEY 732
Cdd:PRK10263 1011 PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHLLTEVVT-DMKDAANALRWCVNEMER 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 733 RQRLFAAAgeGVDNLDAYIRA----------------KPS----------EPLPRLLLVVDEFAMLAKDFPEVLSSLV-R 785
Cdd:PRK10263 1089 RYKLMSAL--GVRNLAGYNEKiaeadrmmrpipdpywKPGdsmdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVEELIaR 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 786 VATVGRTLGVHMILATQRPA-GVVNDDILANTNLRVALRVQSREDSNNVIgvpdaaaianaQKGRAYVKLGQDDI----- 859
Cdd:PRK10263 1167 LAQKARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTIL-----------DQAGAESLLGMGDMlysgp 1235
|
250 260
....*....|....*....|....*..
gi 550741601 860 ---TPVQtalVTGAAQKDQDNAIEIQE 883
Cdd:PRK10263 1236 nstLPVR---VHGAFVRDQEVHAVVQD 1259
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
100-183 |
1.07e-13 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 68.06 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 100 DRPLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTgqSVAVDTTLAVGGSTLL 179
Cdd:COG1716 20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTF-----VNGQRVTEPA--PLRDGDVIRLGKTELR 92
|
....
gi 550741601 180 LRES 183
Cdd:COG1716 93 FRLS 96
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
654-824 |
2.04e-12 |
|
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: 66.09 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 654 HGLVGGTTGSGKSEFLRSMVAGLAACNAPtkltFILIDFKGGaafaacerlphtiGTISNLDEQLANRALRALeaemeYR 733
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGGS----VIITDPKGE-------------LFLVIPDRDDSFAALRAL-----FF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 734 QRLFAAAGEGVDNldayiraKPSEPLPRLLLVVDEFAMLAKdfpevLSSLVRVATVGRTLGVHMILATQRPA-------G 806
Cdd:cd01127 59 NQLFRALTELASL-------SPGRLPRRVWFILDEFANLGR-----IPNLPNLLATGRKRGISVVLILQSLAqleavygK 126
|
170
....*....|....*...
gi 550741601 807 VVNDDILANTNLRVALRV 824
Cdd:cd01127 127 DGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
652-862 |
1.80e-11 |
|
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: 67.71 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 652 GPHGLVGGTTGSGKSEFLRSMVAGLAACNAPtkltFILIDFKG---GAAFAACER--------------------LPHTI 708
Cdd:COG0433 47 NRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHGeysGLAEPGAERadvgvfdpgagrplpinpwdLFATA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 709 G-----------------------------------TISNLDEQL-----------------ANRALRALEAeMEYRQRL 736
Cdd:COG0433 123 SelgplllsrldlndtqrgvlrealrladdkgllllDLKDLIALLeegeelgeeygnvsaasAGALLRRLES-LESADGL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 737 FAAAGEGVDNL--------------------------------DAYIRAKPSEPLPR-LLLVVDEFAMLAKDFPEV-LSS 782
Cdd:COG0433 202 FGEPGLDLEDLlrtdgrvtvidlsglpeelqstfvlwllrelfEARPEVGDADDRKLpLVLVIDEAHLLAPAAPSAlLEI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 783 LVRVATVGRTLGVHMILATQRPAGvVNDDILANTNLRVALRVQSREDSNNV------IGVPDAAAIANAQKGRAYVkLGQ 856
Cdd:COG0433 282 LERIAREGRKFGVGLILATQRPSD-IDEDVLSQLGTQIILRLFNPRDQKAVkaaaetLSEDLLERLPSLGTGEALV-LGE 359
|
....*.
gi 550741601 857 DDITPV 862
Cdd:COG0433 360 GIPLPV 365
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
105-181 |
2.95e-10 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 58.06 E-value: 2.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTgqSVAVDTTLAVGGSTLLLR 181
Cdd:cd00060 23 IGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTF-----VNGKRITPPV--PLQDGDVIRLGDTTFRFE 92
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
558-800 |
7.73e-09 |
|
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: 60.01 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 558 VTRPDDLKKVDDVVLAGVTLERAQRcaldlarfedpelkTPGAALPSLVRLPPLIDLEAptagkiLHAWETSRGVSTPVG 637
Cdd:TIGR03925 288 LPRLDGIASVDDLGTRGLVAVIRDV--------------WGGPPAPPVRLLPARLPLSA------LPAGGGAPRLRVPLG 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 638 VGEN--GVYSLDIVKDgPHGLVGGTTGSGKSEFLRSMVAGLAACNAPTKLTFILIDFKGGAAFAACERlpHTIGTISNLD 715
Cdd:TIGR03925 348 LGESdlAPVYVDFAES-PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTLLGAVPED--YLAGYAATSA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 716 EqlANRALRALEAEMEYRqrlfaAAGEGVDNldAYIRAKPSEPLPRLLLVVDEFAMLAKDFPEVLSSLVRVATVGRTLGV 795
Cdd:TIGR03925 425 A--LTELIAALAALLERR-----LPGPDVTP--QQLRARSWWSGPEIYVVVDDYDLVATGSGNPLAPLVELLPHARDIGL 495
|
....*
gi 550741601 796 HMILA 800
Cdd:TIGR03925 496 HVVVA 500
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
92-161 |
1.46e-08 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 53.49 E-value: 1.46e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 92 GGVLQPPVDRPLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFAYSSEVDGLKVDSST 161
Cdd:cd22694 7 GGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGT 76
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
105-159 |
1.60e-07 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 49.50 E-value: 1.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVG-LRVIDQGSTNGTFaysseVDGLKVDS 159
Cdd:pfam00498 3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGGrFYLEDLGSTNGTF-----VNGQRLGP 53
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
105-168 |
8.22e-06 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 45.94 E-value: 8.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFAYSSEVDGLKVDSSTGQSVAVD 168
Cdd:cd22683 25 IGRSRSCDLVLSDPSISRFHAELRLEQNGINVIDNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
95-180 |
2.36e-05 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 44.66 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 95 LQPPVDRPLAIGRSPQADLSIASASVSWDHVHIQRDDVGLR--VIDQGSTNGTfayssEVDGLKVD-SSTGQSVAVDTTL 171
Cdd:cd22678 17 LQPGTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKweLVDLGSLNGT-----LVNGESISpNGRPVVLSSGDVI 91
|
....*....
gi 550741601 172 AVGGSTLLL 180
Cdd:cd22678 92 TLGSETKIL 100
|
|
| TraG-D_C |
pfam12696 |
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as ... |
761-828 |
2.88e-05 |
|
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as VirD4 proteins. TraG is essential for DNA transfer in bacterial conjugation. These proteins are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. This domain interacts with the relaxosome component TraM via the latter's tetramerization domain. TraD is a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore.
Pssm-ID: 432726 [Multi-domain] Cd Length: 125 Bit Score: 44.95 E-value: 2.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550741601 761 RLLLVVDEFAMLAK--DFPEVLSslvrvatVGRTLGVHMILATQRPAGVVN-------DDILANTNLRVALRVQSRE 828
Cdd:pfam12696 1 PVLFVLDEFANLGKipDLEKLIS-------TGRSRGISLMLILQSIAQLEElygkdgaETILGNCNTKVFLGGGDEE 70
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
105-148 |
5.28e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 43.48 E-value: 5.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFAY 148
Cdd:cd22680 25 IGRDPENVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVN 68
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
106-159 |
5.66e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 43.14 E-value: 5.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550741601 106 GRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDS 159
Cdd:cd22684 26 GRHPESDIFLDDVTVSRRHAEFRRAEGGFVVRDVGSLNGTY-----VNRERIDS 74
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1249-1342 |
6.35e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1249 GEHMLIAGPARSGKSTLLMGLAESLR----------TSAVAEGTDLAVWGIGSKRSPIASSDLDNVAVgpdeipaLVAAA 1318
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGppgggviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRL-------ALALA 74
|
90 100
....*....|....*....|....
gi 550741601 1319 RmRTAPLVLLIDDAERFDDADQSI 1342
Cdd:smart00382 75 R-KLKPDVLILDEITSLLDAEQEA 97
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
103-182 |
1.07e-04 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 42.63 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 103 LAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSStGQSVAVDTTLAVGGSTLLLRE 182
Cdd:pfam16697 19 YRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGSGNGTL-----VNGQRVTEL-GIALRPGDRIELGQTEFCLVP 92
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
986-1067 |
1.19e-04 |
|
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: 45.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 986 GNLMLVGIPGFGTTTACATVALTLAQHYAPKDLDLIVLDMGARDLEPLEKLPHTSAYvgSGAGGREKQMRLLRFLRQELE 1065
Cdd:pfam01580 39 VHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLSV--PVATDPKRALRALEWLVDEME 116
|
..
gi 550741601 1066 TR 1067
Cdd:pfam01580 117 RR 118
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
94-158 |
2.27e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 41.74 E-value: 2.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550741601 94 VLQPPVD--------RPLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVD 158
Cdd:cd22682 5 IIGPPGVgkqfpiteSTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVSIIDLGSTNGTI-----VNGKKIP 72
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1248-1356 |
2.39e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 43.26 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1248 EGEHMLIAGPARSGKSTLLMGLAESLRTSAV--------------------------------AEGTDLAVWG--IGSKR 1293
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGyflrgkcdenlpyspllealtregllrqlldeLESSLLEAWRaaLLEAL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550741601 1294 SPIASSDLDNVAVGPDEIPALVAAARMRTAPLVLLIDDAERFDDADQSITDLVGSNLPHVHVI 1356
Cdd:pfam13191 103 APVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEASLQLLAALLRLLESLPLL 165
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
102-181 |
4.20e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 40.75 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 102 PLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFAYSSEVDGLKVdsstgqsVAVDTTLAVGGSTLLLR 181
Cdd:cd22693 19 GITIGRADDNDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGNRVTQPVV-------VQPGDTIRIGATVFEVR 91
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
97-181 |
5.37e-04 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 41.25 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 97 PPVDRPLAIGRSPQADLSIASASVSWDH--VHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTGQSVAVDTTLAVG 174
Cdd:cd22691 25 SEEEDILVVGRHPDCDIVLDHPSISRFHleIRIIPSRRKITLTDLSSVHGTW-----VNGQRIEPGVPVELEEGDTVRLG 99
|
....*..
gi 550741601 175 GSTLLLR 181
Cdd:cd22691 100 ASTRVYR 106
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
105-171 |
1.63e-03 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 39.32 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVDSS---TGQSVAVDTTL 171
Cdd:cd22698 25 IGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTF-----LNGIRVGTHelkHGDRIQLGETI 89
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
105-157 |
1.77e-03 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 39.58 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550741601 105 IGRSPQADLSIASAS-VSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKV 157
Cdd:cd22672 25 IGRAKDCDLSFPGNKlVSGDHCKIIRDEKGQVWLEDTSTNGTL-----VNKVKV 73
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| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
105-158 |
2.07e-03 |
|
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 39.01 E-value: 2.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFaysseVDGLKVD 158
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTF-----VNGLRVD 73
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| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1242-1376 |
2.12e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 40.21 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 1242 QYLELYEGEHMLIAGPARSGKSTLLMGLAESLRTSavaeGTDLAVWGIGSKRSPIASSDLDNVavgpdEIPALVAAARMR 1321
Cdd:cd00009 12 EALELPPPKNLLLYGPPGTGKTTLARAIANELFRP----GAPFLYLNASDLLEGLVVAELFGH-----FLVRLLFELAEK 82
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550741601 1322 TAPLVLLIDDAERFDDADQSITDLV-------GSNLPHVHVIAAG----RSDDLRSLYSHWTKVVR 1376
Cdd:cd00009 83 AKPGVLFIDEIDSLSRGAQNALLRVletlndlRIDRENVRVIGATnrplLGDLDRALYDRLDIRIV 148
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| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
105-180 |
2.96e-03 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 38.69 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQ------RDDVGLRVIDQGSTNGTFaysseVDGLKVDSSTGQSVAVDTTLAVGGSTL 178
Cdd:cd22677 26 FGRLPGCDVVLEHPSISRYHAVLQyrgdadDHDGGFYLYDLGSTHGTF-----LNKQRIPPKQYYRLRVGHVLKFGGSTR 100
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..
gi 550741601 179 LL 180
Cdd:cd22677 101 LY 102
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
105-157 |
4.55e-03 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 36.77 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 550741601 105 IGRSP-QADLSIASASVSWDHVHIQRD-DVGLRVIDQGSTNGTFaysseVDGLKV 157
Cdd:smart00240 3 IGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTF-----VNGKRI 52
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
88-154 |
5.14e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 37.83 E-value: 5.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550741601 88 GLEAGGVLQPPVDR-PLAIGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTFAYSSEVDG 154
Cdd:cd22668 4 QLDDGSGRVYQLREgSNIIGRGSDADFRLPDTGVSRRHAEIRWDGQVAHLTDLGSTNGTTVNNAPVTP 71
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|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
105-146 |
9.57e-03 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 37.21 E-value: 9.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 550741601 105 IGRSPQADLSIASASVSWDHVHIQRDDVGLRVIDQGSTNGTF 146
Cdd:cd22665 25 IGRDPSCSVVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTR 66
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