|
Name |
Accession |
Description |
Interval |
E-value |
| McrB super family |
cl34253 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1852-2089 |
4.86e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms]; The actual alignment was detected with superfamily member COG1401:
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 51.69 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1852 PKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFIlskTGREVTDTNLATFNVDQKSSKDLRQYLSSLAEQ----- 1926
Cdd:COG1401 207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1927 -------CNTEECEIELPTVVILD-----NLHHIgsLSDIF------------NGFLNCKYHKCP-------YVIGTMNQ 1975
Cdd:COG1401 284 pgiflrfCLKAEKNPDKPYVLIIDeinraNVEKY--FGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1976 GVSSspnlelhhnfrwvlcanhtepvKGFLGRFLRRK--LIETEIDKNMRSNDLIKiidwipKIWQHLNSFLEahsSSDV 2053
Cdd:COG1401 362 DDRS----------------------LALSDKALRRRftFEFLDPDLDKLSNEEVV------DLLEELNEILE---KRDF 410
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207171731 2054 TIGPRLFLSCPMDADGSRVWFTDLWNYSLVPYLLEA 2089
Cdd:COG1401 411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
|
|
| TPR_MLP1_2 super family |
cl25510 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1355-1438 |
6.24e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity. The actual alignment was detected with superfamily member pfam07926:
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1355 HSEgqTVQnttQIRKLRRELDASQEKVATLTSQL-AANAHLVAAfEKSLAnmtcrlqsltmtaEQK---ESELAELRETI 1430
Cdd:pfam07926 52 HAE--DIK---ALQALREELNELKAEIAELKAEAeSAKAELEES-EESWE-------------EQKkelEKELSELEKRI 112
|
....*...
gi 1207171731 1431 EALKTQNT 1438
Cdd:pfam07926 113 EDLNEQNK 120
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
977-1300 |
1.23e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.22 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 977 AVGTPTSTKRRDTGKVGSGRSSPVTINQTDkekvAGSDQEGTGLPTSPKSSPTSTQSGLRQPGSKYPDIASPTfrrlfgs 1056
Cdd:pfam05109 409 ATNATTTTHKVIFSKAPESTTTSPTLNTTG----FAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT------- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1057 kaSSKPSSPGTPDSgkcPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQsggssplygKTPDLGTDSP-ASSPASGLSL 1135
Cdd:pfam05109 478 --PAGTTSGASPVT---PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS---------PTPAVTTPTPnATSPTLGKTS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1136 PSNARPWP-PNLSSSSAgskdtlschsmtslhtsseSIDLPLPHHHGPKVTRTGSVKSTLSegmPLDRNTLPKKGLRYPP 1214
Cdd:pfam05109 544 PTSAVTTPtPNATSPTP-------------------AVTTPTPNATIPTLGKTSPTSAVTT---PTPNATSPTVGETSPQ 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1215 SSRQtsheegkewlrSHSTGGLQDTGSPLSPP--GTTCANAGKYHYSN------LLSPTSMSQYNIPSTSMSRSNSIPaq 1286
Cdd:pfam05109 602 ANTT-----------NHTLGGTSSTPVVTSPPknATSAVTTGQHNITSsstssmSLRPSSISETLSPSTSDNSTSHMP-- 668
|
330
....*....|....
gi 1207171731 1287 dsfeLYGEGHPLGG 1300
Cdd:pfam05109 669 ----LLTSAHPTGG 678
|
|
| Herpes_pp85 super family |
cl27999 |
Herpesvirus phosphoprotein 85 (HHV6-7 U14/HCMV UL25); This family includes UL25 proteins from ... |
728-887 |
6.25e-03 |
|
Herpesvirus phosphoprotein 85 (HHV6-7 U14/HCMV UL25); This family includes UL25 proteins from HCMV, as well as U14 proteins from HHV 6 and HHV7. These 85 kD phosphoproteins appear to act as structural antigens, but their precise function is otherwise unknown. The actual alignment was detected with superfamily member PHA03249:
Pssm-ID: 355693 Cd Length: 653 Bit Score: 41.53 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 728 DASSWAGAEDLkkvdEEMEPGMDPSckwktSSPSSSCQGEDISQKTGLPmSQTGSWRRGMSAQVGIT----PPRTKGTST 803
Cdd:PHA03249 32 DPRPRAPTEDL----DRMEAGLSSY-----SSSSDNKSSFEVVSETDSG-SEAEAERGRRAGMGGRNkatkPSRRNKTTQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 804 SLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSG 883
Cdd:PHA03249 102 CRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEEDEGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFC 181
|
....
gi 1207171731 884 SATL 887
Cdd:PHA03249 182 DSDI 185
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1852-2089 |
4.86e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 51.69 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1852 PKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFIlskTGREVTDTNLATFNVDQKSSKDLRQYLSSLAEQ----- 1926
Cdd:COG1401 207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1927 -------CNTEECEIELPTVVILD-----NLHHIgsLSDIF------------NGFLNCKYHKCP-------YVIGTMNQ 1975
Cdd:COG1401 284 pgiflrfCLKAEKNPDKPYVLIIDeinraNVEKY--FGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1976 GVSSspnlelhhnfrwvlcanhtepvKGFLGRFLRRK--LIETEIDKNMRSNDLIKiidwipKIWQHLNSFLEahsSSDV 2053
Cdd:COG1401 362 DDRS----------------------LALSDKALRRRftFEFLDPDLDKLSNEEVV------DLLEELNEILE---KRDF 410
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207171731 2054 TIGPRLFLSCPMDADGSRVWFTDLWNYSLVPYLLEA 2089
Cdd:COG1401 411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1866-1986 |
5.58e-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: 45.44 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1866 HRRIILSGPSGTGKSYLATKLAYFILSKTGREV----TDTNLATFNVDQKSSKDLRQYLSSLAEQCN--TEECEIELPTV 1939
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRlaLALARKLKPDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171731 1940 VILDNLHHIGS---------LSDIFNGFLNCKYHKCPyVIGTMNQGVSSSPNLELH 1986
Cdd:smart00382 82 LILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1355-1438 |
6.24e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1355 HSEgqTVQnttQIRKLRRELDASQEKVATLTSQL-AANAHLVAAfEKSLAnmtcrlqsltmtaEQK---ESELAELRETI 1430
Cdd:pfam07926 52 HAE--DIK---ALQALREELNELKAEIAELKAEAeSAKAELEES-EESWE-------------EQKkelEKELSELEKRI 112
|
....*...
gi 1207171731 1431 EALKTQNT 1438
Cdd:pfam07926 113 EDLNEQNK 120
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
977-1300 |
1.23e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.22 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 977 AVGTPTSTKRRDTGKVGSGRSSPVTINQTDkekvAGSDQEGTGLPTSPKSSPTSTQSGLRQPGSKYPDIASPTfrrlfgs 1056
Cdd:pfam05109 409 ATNATTTTHKVIFSKAPESTTTSPTLNTTG----FAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT------- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1057 kaSSKPSSPGTPDSgkcPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQsggssplygKTPDLGTDSP-ASSPASGLSL 1135
Cdd:pfam05109 478 --PAGTTSGASPVT---PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS---------PTPAVTTPTPnATSPTLGKTS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1136 PSNARPWP-PNLSSSSAgskdtlschsmtslhtsseSIDLPLPHHHGPKVTRTGSVKSTLSegmPLDRNTLPKKGLRYPP 1214
Cdd:pfam05109 544 PTSAVTTPtPNATSPTP-------------------AVTTPTPNATIPTLGKTSPTSAVTT---PTPNATSPTVGETSPQ 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1215 SSRQtsheegkewlrSHSTGGLQDTGSPLSPP--GTTCANAGKYHYSN------LLSPTSMSQYNIPSTSMSRSNSIPaq 1286
Cdd:pfam05109 602 ANTT-----------NHTLGGTSSTPVVTSPPknATSAVTTGQHNITSsstssmSLRPSSISETLSPSTSDNSTSHMP-- 668
|
330
....*....|....
gi 1207171731 1287 dsfeLYGEGHPLGG 1300
Cdd:pfam05109 669 ----LLTSAHPTGG 678
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1348-1445 |
1.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1348 DKTEEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELR 1427
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90
....*....|....*...
gi 1207171731 1428 ETIEALKTQNTDAQTAIQ 1445
Cdd:COG4372 129 QQRKQLEAQIAELQSEIA 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1869-1960 |
1.10e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 41.04 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1869 IILSGPSGTGKSYLATKLAyfilSKTGREVTDTNLATFnVDQ---KSSKDLRQYLsslaeqcntEECEIELPTVVILDNL 1945
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVA----KELGAPFIEISGSEL-VSKyvgESEKRLRELF---------EAAKKLAPCVIFIDEI 66
|
90 100
....*....|....*....|....
gi 1207171731 1946 HHIGS---------LSDIFNGFLN 1960
Cdd:pfam00004 67 DALAGsrgsggdseSRRVVNQLLT 90
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1841-1961 |
1.28e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.50 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1841 SIDDLVFDTLIPKPIIQRYLNLlmeHRRIILSGPSGTGKSYLATKLAYFILSKTGReVTDTNLATFNVDQkSSKDLRQYL 1920
Cdd:cd19481 4 SLREAVEAPRRGSRLRRYGLGL---PKGILLYGPPGTGKTLLAKALAGELGLPLIV-VKLSSLLSKYVGE-SEKNLRKIF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1207171731 1921 SSLAEQCnteeceielPTVVILD----------NLHHIGSLSDIFNGFLNC 1961
Cdd:cd19481 79 ERARRLA---------PCILFIDeidaigrkrdSSGESGELRRVLNQLLTE 120
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
1842-1890 |
1.43e-03 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 43.54 E-value: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207171731 1842 IDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFI 1890
Cdd:PRK11331 170 LEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLL 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-1454 |
1.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1348 DKTEEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELR 1427
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100
....*....|....*....|....*..
gi 1207171731 1428 ETIEALKTQNTDAQTAIQVALNGPDHV 1454
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| PHA03249 |
PHA03249 |
DNA packaging tegument protein UL25; Provisional |
728-887 |
6.25e-03 |
|
DNA packaging tegument protein UL25; Provisional
Pssm-ID: 223023 Cd Length: 653 Bit Score: 41.53 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 728 DASSWAGAEDLkkvdEEMEPGMDPSckwktSSPSSSCQGEDISQKTGLPmSQTGSWRRGMSAQVGIT----PPRTKGTST 803
Cdd:PHA03249 32 DPRPRAPTEDL----DRMEAGLSSY-----SSSSDNKSSFEVVSETDSG-SEAEAERGRRAGMGGRNkatkPSRRNKTTQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 804 SLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSG 883
Cdd:PHA03249 102 CRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEEDEGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFC 181
|
....
gi 1207171731 884 SATL 887
Cdd:PHA03249 182 DSDI 185
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
1841-1888 |
8.68e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 40.15 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1207171731 1841 SIDDLVFDTL--IPKPIIQRYLNL--LMEHRRIILSGPSGTGKSYLATKLAY 1888
Cdd:NF038214 61 TLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGY 112
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1852-2089 |
4.86e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 51.69 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1852 PKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFIlskTGREVTDTNLATFNVDQKSSKDLRQYLSSLAEQ----- 1926
Cdd:COG1401 207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1927 -------CNTEECEIELPTVVILD-----NLHHIgsLSDIF------------NGFLNCKYHKCP-------YVIGTMNQ 1975
Cdd:COG1401 284 pgiflrfCLKAEKNPDKPYVLIIDeinraNVEKY--FGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1976 GVSSspnlelhhnfrwvlcanhtepvKGFLGRFLRRK--LIETEIDKNMRSNDLIKiidwipKIWQHLNSFLEahsSSDV 2053
Cdd:COG1401 362 DDRS----------------------LALSDKALRRRftFEFLDPDLDKLSNEEVV------DLLEELNEILE---KRDF 410
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207171731 2054 TIGPRLFLSCPMDADGSRVWFTDLWNYSLVPYLLEA 2089
Cdd:COG1401 411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1866-1986 |
5.58e-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: 45.44 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1866 HRRIILSGPSGTGKSYLATKLAYFILSKTGREV----TDTNLATFNVDQKSSKDLRQYLSSLAEQCN--TEECEIELPTV 1939
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRlaLALARKLKPDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171731 1940 VILDNLHHIGS---------LSDIFNGFLNCKYHKCPyVIGTMNQGVSSSPNLELH 1986
Cdd:smart00382 82 LILDEITSLLDaeqeallllLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1355-1438 |
6.24e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1355 HSEgqTVQnttQIRKLRRELDASQEKVATLTSQL-AANAHLVAAfEKSLAnmtcrlqsltmtaEQK---ESELAELRETI 1430
Cdd:pfam07926 52 HAE--DIK---ALQALREELNELKAEIAELKAEAeSAKAELEES-EESWE-------------EQKkelEKELSELEKRI 112
|
....*...
gi 1207171731 1431 EALKTQNT 1438
Cdd:pfam07926 113 EDLNEQNK 120
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
977-1300 |
1.23e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.22 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 977 AVGTPTSTKRRDTGKVGSGRSSPVTINQTDkekvAGSDQEGTGLPTSPKSSPTSTQSGLRQPGSKYPDIASPTfrrlfgs 1056
Cdd:pfam05109 409 ATNATTTTHKVIFSKAPESTTTSPTLNTTG----FAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT------- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1057 kaSSKPSSPGTPDSgkcPSALGSPHGTLARQASLDSPSSGTGSLGSMGGQsggssplygKTPDLGTDSP-ASSPASGLSL 1135
Cdd:pfam05109 478 --PAGTTSGASPVT---PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS---------PTPAVTTPTPnATSPTLGKTS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1136 PSNARPWP-PNLSSSSAgskdtlschsmtslhtsseSIDLPLPHHHGPKVTRTGSVKSTLSegmPLDRNTLPKKGLRYPP 1214
Cdd:pfam05109 544 PTSAVTTPtPNATSPTP-------------------AVTTPTPNATIPTLGKTSPTSAVTT---PTPNATSPTVGETSPQ 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1215 SSRQtsheegkewlrSHSTGGLQDTGSPLSPP--GTTCANAGKYHYSN------LLSPTSMSQYNIPSTSMSRSNSIPaq 1286
Cdd:pfam05109 602 ANTT-----------NHTLGGTSSTPVVTSPPknATSAVTTGQHNITSsstssmSLRPSSISETLSPSTSDNSTSHMP-- 668
|
330
....*....|....
gi 1207171731 1287 dsfeLYGEGHPLGG 1300
Cdd:pfam05109 669 ----LLTSAHPTGG 678
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1348-1445 |
1.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1348 DKTEEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELR 1427
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90
....*....|....*...
gi 1207171731 1428 ETIEALKTQNTDAQTAIQ 1445
Cdd:COG4372 129 QQRKQLEAQIAELQSEIA 146
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1344-1453 |
2.06e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1344 LAFLDKTE---EKAHSEGQTVQNTT-QIRKLRRELDASQEKVATLTSQLAANAHLvAAFEKSLANMTCRLQSLTMTAEQK 1419
Cdd:pfam12795 26 LSLLDKIDaskQRAAAYQKALDDAPaELRELRQELAALQAKAEAAPKEILASLSL-EELEQRLLQTSAQLQELQNQLAQL 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207171731 1420 ESELAELR---ETIEALKTQNTDAQTAIQVALNGPDH 1453
Cdd:pfam12795 105 NSQLIELQtrpERAQQQLSEARQRLQQIRNRLNGPAP 141
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1351-1460 |
3.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1351 EEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAF---------EKSLANMTCRLQSLtmtaEQKES 1421
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelealEAELAELPERLEEL----EERLE 156
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207171731 1422 ELAELRETIEALKTQNTDAQTAIQVALNGPDHVHRADLR 1460
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1869-1960 |
1.10e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 41.04 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1869 IILSGPSGTGKSYLATKLAyfilSKTGREVTDTNLATFnVDQ---KSSKDLRQYLsslaeqcntEECEIELPTVVILDNL 1945
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVA----KELGAPFIEISGSEL-VSKyvgESEKRLRELF---------EAAKKLAPCVIFIDEI 66
|
90 100
....*....|....*....|....
gi 1207171731 1946 HHIGS---------LSDIFNGFLN 1960
Cdd:pfam00004 67 DALAGsrgsggdseSRRVVNQLLT 90
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1841-1961 |
1.28e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.50 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1841 SIDDLVFDTLIPKPIIQRYLNLlmeHRRIILSGPSGTGKSYLATKLAYFILSKTGReVTDTNLATFNVDQkSSKDLRQYL 1920
Cdd:cd19481 4 SLREAVEAPRRGSRLRRYGLGL---PKGILLYGPPGTGKTLLAKALAGELGLPLIV-VKLSSLLSKYVGE-SEKNLRKIF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1207171731 1921 SSLAEQCnteeceielPTVVILD----------NLHHIGSLSDIFNGFLNC 1961
Cdd:cd19481 79 ERARRLA---------PCILFIDeidaigrkrdSSGESGELRRVLNQLLTE 120
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
1842-1890 |
1.43e-03 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 43.54 E-value: 1.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207171731 1842 IDDLVFDTLIPKPIIQRYLNLLMEHRRIILSGPSGTGKSYLATKLAYFI 1890
Cdd:PRK11331 170 LEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1362-1436 |
1.74e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207171731 1362 QNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELRETIEALKTQ 1436
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-1454 |
1.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1348 DKTEEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAANAHLVAAFEKSLANMTCRLQSLTMTAEQKESELAELR 1427
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100
....*....|....*....|....*..
gi 1207171731 1428 ETIEALKTQNTDAQTAIQVALNGPDHV 1454
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1350-1447 |
2.98e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1350 TEEKAHSEGQTVQNTTQIRKLRRELDASQEKVATLTSQLAAnahlvaaFEKSLANMTCRLQSLTMTAEQKESELAELRET 1429
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90
....*....|....*...
gi 1207171731 1430 IEALKTQNTDAQTAIQVA 1447
Cdd:COG1196 332 LEELEEELEELEEELEEA 349
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
1841-1888 |
3.42e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 41.30 E-value: 3.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1207171731 1841 SIDDLVFDTL--IPKPIIQRYLNL--LMEHRRIILSGPSGTGKSYLATKLAY 1888
Cdd:COG1484 70 TLEDFDFDAQpgLDRRQILELATLdfIERGENLILLGPPGTGKTHLAIALGH 121
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
1842-1905 |
3.75e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.83 E-value: 3.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171731 1842 IDDLVFDTLIPKPIIQRYL--NLLMEHRRIILSGPSGTGKSYLATKLAYFILskTGREVTDTNLAT 1905
Cdd:pfam13481 7 LLDVLADGLAAPPPPRRWLikGLLPAGGLGLLAGAPGTGKTTLALDLAAAVA--TGKPWLGGPRVP 70
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1869-1949 |
3.92e-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: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1869 IILSGPSGTGKSYLATKLAYfILSKTGREVTDTNLATFNVDQKSSKDLRQYlsslAEQCNTEECEIELPTVVILDNLHHI 1948
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIAN-ELFRPGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFELAEKAKPGVLFIDEIDSL 96
|
.
gi 1207171731 1949 G 1949
Cdd:cd00009 97 S 97
|
|
| PRK09183 |
PRK09183 |
transposase/IS protein; Provisional |
1844-1888 |
4.61e-03 |
|
transposase/IS protein; Provisional
Pssm-ID: 181681 Cd Length: 259 Bit Score: 41.23 E-value: 4.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1207171731 1844 DLVFDTLIPKPIIQ--RYLNLLMEHRRIILSGPSGTGKSYLATKLAY 1888
Cdd:PRK09183 78 DFTFATGAPQKQLQslRSLSFIERNENIVLLGPSGVGKTHLAIALGY 124
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
1863-1956 |
5.33e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 1863 LMEHRRII-LSGPSGTGKSYLATKLayfiLSKTGREVTDTNLATFNVDQKSSKDLRQYLSSLAEQCNTEECEIEL----- 1936
Cdd:pfam13401 1 IRFGAGILvLTGESGTGKTTLLRRL----LEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELlaalq 76
|
90 100 110
....*....|....*....|....*....|...
gi 1207171731 1937 --------PTVVILDNLHHIGS-----LSDIFN 1956
Cdd:pfam13401 77 qlllalavAVVLIIDEAQHLSLealeeLRDLLN 109
|
|
| PHA03249 |
PHA03249 |
DNA packaging tegument protein UL25; Provisional |
728-887 |
6.25e-03 |
|
DNA packaging tegument protein UL25; Provisional
Pssm-ID: 223023 Cd Length: 653 Bit Score: 41.53 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 728 DASSWAGAEDLkkvdEEMEPGMDPSckwktSSPSSSCQGEDISQKTGLPmSQTGSWRRGMSAQVGIT----PPRTKGTST 803
Cdd:PHA03249 32 DPRPRAPTEDL----DRMEAGLSSY-----SSSSDNKSSFEVVSETDSG-SEAEAERGRRAGMGGRNkatkPSRRNKTTQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171731 804 SLKTPGKTDDAKASEKGKGSPKSPSIQRSPSDAGKSSGDEGKKPPSGIARPPTTSSFGYKKIPGPAGALITASGATLTSG 883
Cdd:PHA03249 102 CRPTSLALATAATMPATPSSGKSPKVSSPPSIPSLSEEDEGAERNSGGDDSSHTDNESTQSQPEADDEPDLAEGHEFSFC 181
|
....
gi 1207171731 884 SATL 887
Cdd:PHA03249 182 DSDI 185
|
|
| IS21_help_AAA |
NF038214 |
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ... |
1841-1888 |
8.68e-03 |
|
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.
Pssm-ID: 439516 Cd Length: 232 Bit Score: 40.15 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1207171731 1841 SIDDLVFDTL--IPKPIIQRYLNL--LMEHRRIILSGPSGTGKSYLATKLAY 1888
Cdd:NF038214 61 TLEDFDFTAApgLDKAQIRELATLdfIERAENVLLLGPPGTGKTHLAIALGY 112
|
|
|