|
Name |
Accession |
Description |
Interval |
E-value |
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
35-280 |
4.62e-136 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 410.14 E-value: 4.62e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 35 DKPKDKWSNFDPTGLERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLN 114
Cdd:pfam12037 14 DKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 115 EETKQHQARAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMR-----KATIEHEMELRHKNELLRIEAESKA 189
Cdd:pfam12037 94 EETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 190 RARVERENADIIREQIRLKAAEHRQTVLESIKTAGAVFGEGFRAFVSDWDKVTATVAGLTLLAVGVYSARNATGVAGRYI 269
Cdd:pfam12037 174 RAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYI 253
|
250
....*....|.
gi 1712965699 270 EARLGKPSLVR 280
Cdd:pfam12037 254 EARLGKPSLVR 264
|
|
| RecA-like_ATAD3-like |
cd19512 |
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ... |
318-467 |
1.53e-107 |
|
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410920 [Multi-domain] Cd Length: 150 Bit Score: 330.64 E-value: 1.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 318 LEERVRDVAIATRNTRQNNGLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRDGVTAMHKVFDWANTSR 397
Cdd:cd19512 1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 398 RGLLLFVDEADAFLRKRSTEKISEDLRATLNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEIVNF 467
Cdd:cd19512 81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
318-467 |
1.21e-37 |
|
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: 138.57 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 318 LEERVRDVAIATRNTRQNNGLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-DGVTAMHKVFDWANTS 396
Cdd:cd19481 5 LREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFERARRL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 397 RRGLLLFvDEADAFLRKRSTEKISEDLRATLNAFLYRT--GEQSNKFMLVLASNQPEQFDWAIND--RIDEIVNF 467
Cdd:cd19481 85 APCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
309-563 |
1.67e-29 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 118.06 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 309 LEGVVLSPTLEERVRDVaiaTRNTRQNNGLY-------RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR- 380
Cdd:COG1223 1 LDDVVGQEEAKKKLKLI---IKELRRRENLRkfglwppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 381 --DGVTAMHKVFDWANtsRRGLLLFVDEADAFLRKRSTEKISEDLRATLNAFLYRTGEQSNKFMLVLASNQPEQFDWAIN 458
Cdd:COG1223 76 lgETARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 459 DRIDEIVNFALPGPDERDRLVRLYFDKYVLEpatggrqrmklaqFDYIAKcsEIAKRTEGMSGREISKLGVAWQAAAYSS 538
Cdd:COG1223 154 RRFDEVIEFPLPDKEERKEILELNLKKFPLP-------------FELDLK--KLAKKLEGLSGADIEKVLKTALKKAILE 218
|
250 260
....*....|....*....|....*
gi 1712965699 539 EDGVLTEAMIDArvddAVKQHRQKM 563
Cdd:COG1223 219 DREKVTKEDLEE----ALKQRKERK 239
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
154-558 |
1.11e-28 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 119.63 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 154 EESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENADIIREQIRLKAAEHRQTVLESIKTAGAVFGEGFRA 233
Cdd:COG0464 4 LLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 234 FVSDWDKVTATVAGLTLLAVGVYSARNATGVAGRYIEARLGKPSLVRETSRFTVGEAIKHPVKTVKRLKSkpqDALEGVV 313
Cdd:COG0464 84 ALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELRE---AILDDLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 314 LSPTLEERVRDVAIATRN---TRQNNGLY--RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGRD-GVTA-- 385
Cdd:COG0464 161 GLEEVKEELRELVALPLKrpeLREEYGLPppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKYvGETEkn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 386 MHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKiSEDLRATLNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEIV 465
Cdd:COG0464 239 LREVFDKARGLAPCVLFI-DEADALAGKRGEVG-DGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 466 NFALPGPDERDRLVRLYFDKYVLEPAtggrqrmklaqfdyiAKCSEIAKRTEGMSGREISKLGV-AWQAAAYSSEDGVLT 544
Cdd:COG0464 317 FFPLPDAEERLEIFRIHLRKRPLDED---------------VDLEELAEATEGLSGADIRNVVRrAALQALRLGREPVTT 381
|
410
....*....|....*.
gi 1712965699 545 EAMIDA--RVDDAVKQ 558
Cdd:COG0464 382 EDLLEAleREDIFLKR 397
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
342-467 |
4.67e-22 |
|
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: 92.66 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-DGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRSTEKIS 420
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1712965699 421 EDLRaTLNAFLYRT-GEQSN--KFMLVLASNQPEQFDWAINDRIDEIVNF 467
Cdd:pfam00004 80 ESRR-VVNQLLTELdGFTSSnsKVIVIAATNRPDKLDPALLGRFDRIIEF 128
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
342-564 |
3.98e-21 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 95.84 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrDGVTAMHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKI 419
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI-DEIDAIAARRTDDGT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 420 SEDLRATLNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEIVNFALPGPDERDRLVRLYfdkyvlepatggR 495
Cdd:COG1222 193 SGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEILKIH------------L 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 496 QRMKLA-QFDYiakcSEIAKRTEGMSGREISKlgVAWQAAAYSSEDGVLTEAMIDarVDDAVKQHRQKMD 564
Cdd:COG1222 261 RDMPLAdDVDL----DKLAKLTEGFSGADLKA--IVTEAGMFAIREGRDTVTMED--LEKAIEKVKKKTE 322
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
808-970 |
3.05e-16 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 83.94 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 808 PVVEVTPPPSEE-----AVAAAPLVQDVIAPVVeVTPPPSEEAAAPVAEDVIAPVVEVTP--PLAVEVEAPLAEDVAAPV 880
Cdd:PRK10811 846 PVVRPQDVQVEEqreaeEVQVQPVVAEVPVAAA-VEPVVSAPVVEAVAEVVEEPVVVAEPqpEEVVVVETTHPEVIAAPV 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 881 VEvtpPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVaAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDV 960
Cdd:PRK10811 925 TE---QPQVITESDVAVAQEVAEHAEPVVEPQDETADI-EEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPE 1000
|
170
....*....|
gi 1712965699 961 AAPVVEVTPP 970
Cdd:PRK10811 1001 VAPAQVPEAT 1010
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
825-974 |
3.79e-15 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 80.47 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 825 PLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPlaEDVAAPVVEVTPPPSAEAPLA----EDVAAP 900
Cdd:PRK10811 846 PVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVA--EVVEEPVVVAEPQPEEVVVVEtthpEVIAAP 923
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 901 VVEVTPP-PSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:PRK10811 924 VTEQPQViTESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
782-965 |
2.32e-14 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 77.77 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPsEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVaedVIAPVVEvT 861
Cdd:PRK10811 853 VQVEEQREAE-EVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEV---IAAPVTE-Q 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 862 PPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEV-TPPPSAEAPLAEDVA 940
Cdd:PRK10811 928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVeTVTAVEPEVAPAQVP 1007
|
170 180
....*....|....*....|....*..
gi 1712965699 941 APVVE--VTPPPSAEAPLAEDVAAPVV 965
Cdd:PRK10811 1008 EATVEhnHATAPMTRAPAPEYVPEAPR 1034
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
731-923 |
2.69e-13 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 74.31 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 731 PVVEVTPPPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVV 810
Cdd:PRK10811 846 PVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVT 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 811 EVTPPPSEEAVAAAPLVQDVIAPVVEvtPPPSEEAAAPVAEdvIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAE 890
Cdd:PRK10811 926 EQPQVITESDVAVAQEVAEHAEPVVE--PQDETADIEEAAE--TAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEV 1001
|
170 180 190
....*....|....*....|....*....|....*
gi 1712965699 891 APlaEDVAAPVVE--VTPPPSAEAPLAEDVAAPVV 923
Cdd:PRK10811 1002 AP--AQVPEATVEhnHATAPMTRAPAPEYVPEAPR 1034
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
848-1023 |
5.93e-13 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 73.54 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 848 PVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA----EDVAAPVV 923
Cdd:PRK10811 846 PVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVEtthpEVIAAPVT 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 924 EVTPP-PSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPsaevkctlsdgldsdntVKAEPASETEHLAQ 1002
Cdd:PRK10811 926 EQPQViTESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPE-----------------VVAQPAAPVVAEVA 988
|
170 180
....*....|....*....|.
gi 1712965699 1003 PAASAETEAKMKKEDKTVSPP 1023
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEA 1009
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
750-950 |
6.08e-13 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 73.15 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 750 PLVQDVIAPVVEVTPPPSEEAAAAAPLVQdVIAPVVEVAPPPSEEAVAAAPvaedvIAPVVEVTPPPSEEAVAAAPLVQD 829
Cdd:PRK10811 846 PVVRPQDVQVEEQREAEEVQVQPVVAEVP-VAAAVEPVVSAPVVEAVAEVV-----EEPVVVAEPQPEEVVVVETTHPEV 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 830 VIAPVVEvTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAplaedvaAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPS 909
Cdd:PRK10811 920 IAAPVTE-QPQVITESDVAVAQEVAEHAEPVVEPQDETADI-------EEAAETAEVVVAEPEVVAQPAAPVVAEVAAEV 991
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1712965699 910 AEAPLAEDVAAPVVEVTPPPS---AEAPLAEdvaAPVVEVTPPP 950
Cdd:PRK10811 992 ETVTAVEPEVAPAQVPEATVEhnhATAPMTR---APAPEYVPEA 1032
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
339-469 |
3.47e-11 |
|
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: 62.16 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 339 YRNILMYGPPGTGKTLFAKKLAMHSG--------MDYAIMTGGDVapMGRDGVTAMHKVFDWANTSRRGLLLFVDEADAF 410
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELFrpgapflyLNASDLLEGLV--VAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 411 lrkrsTEKISEDLRATLNAFLYRTGEQSNkFMLVLASNQPE--QFDWAINDRIDEIVNFAL 469
Cdd:cd00009 97 -----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
|
|
| PTZ00436 |
PTZ00436 |
60S ribosomal protein L19-like protein; Provisional |
818-973 |
9.60e-11 |
|
60S ribosomal protein L19-like protein; Provisional
Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 64.59 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 818 EEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPlaVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDV 897
Cdd:PTZ00436 191 EDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPP--AKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAA 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 898 AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSA 973
Cdd:PTZ00436 269 APPAKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKA 344
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
858-1029 |
3.11e-10 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 64.68 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 858 VEVTPPLAVEVEAPLAEDVAAPVVEVTPPpsaeapLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA- 936
Cdd:PRK10811 841 VWIRYPVVRPQDVQVEEQREAEEVQVQPV------VAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVEt 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 937 ---EDVAAPVVEVTPP-PSAEAPLAEDVAAPVVEVTPPPSAEVKCTlsdgldSDNTVKAEPASETEHLAQPAASAETEAK 1012
Cdd:PRK10811 915 thpEVIAAPVTEQPQViTESDVAVAQEVAEHAEPVVEPQDETADIE------EAAETAEVVVAEPEVVAQPAAPVVAEVA 988
|
170
....*....|....*..
gi 1712965699 1013 MKKEDKTVSPPKDGTPV 1029
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQ 1005
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
248-574 |
3.68e-10 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 63.90 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 248 LTLLAVGVYSARNATGVAGRyiearlGKPSLVRETSRFTVGEAIKHPVKTVKRLKSKPQDALEgvvlsptLEERVRDvai 327
Cdd:PRK10733 110 LLLIGVWIFFMRQMQGGGGK------GAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAE-------LVEYLRE--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 328 ATRNTRQNNGLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRD-GVTAMHKVFDWANTSRRgLLLFVDE 406
Cdd:PRK10733 174 PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 407 ADAFLRKRST--EKISEDLRATLNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEIVNFALPGPDERDRLVR 480
Cdd:PRK10733 253 IDAVGRQRGAglGGGHDEREQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 481 LYFDKYVLEPATggrqrmklaqfdyiaKCSEIAKRTEGMSGREISKLgvAWQAAAYSSEDGVLTEAMID---ARVDDAVK 557
Cdd:PRK10733 333 VHMRRVPLAPDI---------------DAAIIARGTPGFSGADLANL--VNEAALFAARGNKRVVSMVEfekAKDKIMMG 395
|
330
....*....|....*..
gi 1712965699 558 QHRQKMDWLHAEEEAQA 574
Cdd:PRK10733 396 AERRSMVMTEAQKESTA 412
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
340-457 |
4.15e-10 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410909 [Multi-domain] Cd Length: 171 Bit Score: 59.55 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMgRDGVTAmHKVFDWANTSRRG--LLLFVDEADAFLRKRSTE 417
Cdd:cd19501 38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQAKKNapCIVFIDEIDAVGRKRGAG 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1712965699 418 KI-SEDLR-ATLNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 457
Cdd:cd19501 116 LGgGHDEReQTLNQLLVEMdGFESNTGVIVIaATNRPDVLDPAL 159
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
337-460 |
1.44e-09 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 58.13 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 337 GLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVA--PMGrDGVTAMHKVFDWANtSRRGLLLFVDEADAFLRKR 414
Cdd:cd19509 30 GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLSER 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1712965699 415 STEKiSEDLRATLNAFLYR----TGEQSNKFMLVLASNQPEQFDWAINDR 460
Cdd:cd19509 108 GSGE-HEASRRVKTEFLVQmdgvLNKPEDRVLVLGATNRPWELDEAFLRR 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-470 |
5.61e-09 |
|
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: 55.84 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLA------------------MHSGMDYAIMTGGDVAPMGRDGVTAMHKVFDWANTSRRGlL 401
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALArelgppgggviyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 402 LFVDEADAFLRKRSTEKISEDLRATLNAFLyrtgEQSNKFMLVLASNQPEQFDWA-INDRIDEIVNFALP 470
Cdd:smart00382 82 LILDEITSLLDAEQEALLLLLEELRLLLLL----KSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
|
|
| PTZ00436 |
PTZ00436 |
60S ribosomal protein L19-like protein; Provisional |
807-964 |
6.55e-09 |
|
60S ribosomal protein L19-like protein; Provisional
Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 59.19 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPseEAAAPVAEDVIAPVVEVTPPlaveveaplAEDVAAPVVEVTPP 886
Cdd:PTZ00436 203 AAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPA--KAAAAPAKAAAAPAKAAAPP---------AKAAAPPAKAAAPP 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 887 PSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPV 964
Cdd:PTZ00436 272 AKAAAPPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAPV 349
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
788-960 |
8.52e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 59.86 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 788 APPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVE 867
Cdd:PRK07003 382 APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADS 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 868 VEAPL-AEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEV 946
Cdd:PRK07003 462 RCDERdAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAA 541
|
170
....*....|....
gi 1712965699 947 TPPPSAEAPLAEDV 960
Cdd:PRK07003 542 PAARAGGAAAALDV 555
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
832-1011 |
8.52e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 59.86 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 832 APVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEVTPPPSAE 911
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA-ATRAEAPPAAPAPPATAD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 912 ---------APLAEDVAAPvveVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEVKCTLSDG 982
Cdd:PRK07003 438 rgddaadgdAPVPAKANAR---ASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA 514
|
170 180
....*....|....*....|....*....
gi 1712965699 983 LDSDNTVKAEPASETEHLAQPAASAETEA 1011
Cdd:PRK07003 515 AASREDAPAAAAPPAPEARPPTPAAAAPA 543
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
808-956 |
1.28e-08 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 58.96 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 808 PVVEVTPPPSEEAVAAAPlvqdviapvvevtPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVeaplaedVAAPVVEVTPPP 887
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPAR-------------PEAAAPAAAPVAQAAAAPAPAAAPAAAASA-------PAAPPAAAPPAP 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 888 SAEAPLAEDVAAP---VVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEVTPPPSAEAPL 956
Cdd:PRK14951 426 VAAPAAAAPAAAPaaaPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASA-APAPAAAPAAARLTPTEEGDV 496
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
863-973 |
1.39e-08 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 58.96 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 863 PLAVEVEAPLAEdvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEdvAAP 942
Cdd:PRK14951 366 PAAAAEAAAPAE--KKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAP--AAA 441
|
90 100 110
....*....|....*....|....*....|.
gi 1712965699 943 VVEVTPPPSAEAPLAEDVAAPVVEVTPPPSA 973
Cdd:PRK14951 442 PAAVALAPAPPAQAAPETVAIPVRVAPEPAV 472
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
788-973 |
1.42e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 58.73 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 788 APPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPvvevtPPPSEEAAAPVAEDVIAPVVEVTPPLAVE 867
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR-----AVAAAPARRSPAPEALAAARQASARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 868 VEAPLAEDVAAPVVevTPPPSAEAPLAEDVAAPVVEVTPPPSAeAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVT 947
Cdd:PRK12323 447 APAPAPAPAAAPAA--AARPAAAGPRPVAAAAAAAPARAAPAA-APAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
|
170 180
....*....|....*....|....*.
gi 1712965699 948 PPPSAEAPLAEDVAAPVVEVTPPPSA 973
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAP 549
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
342-457 |
1.84e-08 |
|
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410938 [Multi-domain] Cd Length: 161 Bit Score: 54.80 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMG-RDGVTAMHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 420
Cdd:cd19530 33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYvGESERAVRQVFQRARASAPCVIFF-DEVDALVPKRGDGGSW 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 1712965699 421 EDLRaTLNAFLYRT--GEQSNKFMLVLASNQPEQFDWAI 457
Cdd:cd19530 112 ASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAM 149
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
833-974 |
2.47e-08 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 57.80 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 833 PVVEVTPPPSEEAAAPvaedviapvveVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEA 912
Cdd:PRK14951 366 PAAAAEAAAPAEKKTP-----------ARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAP 434
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 913 PLAEdvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEVTPPPSAE 974
Cdd:PRK14951 435 AAAP--AAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASA-APAPAAAPAAARLTPTEE 493
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
782-963 |
2.60e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 57.94 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDviapvvEVT 861
Cdd:PRK07003 367 APGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD------RGD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 862 PPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPlaedvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAA 941
Cdd:PRK07003 441 DAADGDAPVPAKANARASADSRCDERDAQPP-----ADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAA 515
|
170 180
....*....|....*....|..
gi 1712965699 942 PVVEVTPPPSAEAPLAEDVAAP 963
Cdd:PRK07003 516 ASREDAPAAAAPPAPEARPPTP 537
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
674-1028 |
2.68e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 674 PDVIAPIVEVTPPPSEEAVAAAPLVQDVitPVVEVTP-----PPSEEAVAAAAAPLVQDVIAPvvevTPPPSEEAVAAAA 748
Cdd:PHA03247 2564 PDRSVPPPRPAPRPSEPAVTSRARRPDA--PPQSARPrapvdDRGDPRGPAPPSPLPPDTHAP----DPPPPSPSPAANE 2637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 749 APLVQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQ 828
Cdd:PHA03247 2638 PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS 2717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 829 DVIAPVVevtpPPSEEAAAPVAedviaPVVEVTPPLAVEVEAPlaedvAAPVVEVTPPPSAEAPLAedvAAPVVEVTPPP 908
Cdd:PHA03247 2718 ATPLPPG----PAAARQASPAL-----PAAPAPPAVPAGPATP-----GGPARPARPPTTAGPPAP---APPAAPAAGPP 2780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 909 SAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAA-PVVEVTPPPSAEVKCTLSDGLDSDN 987
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAqPTAPPPPPGPPPPSLPLGGSVAPGG 2860
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 988 TVK---------AEPASET----EHLAQPAASAETEAKMKKEDKTVSPPKDGTP 1028
Cdd:PHA03247 2861 DVRrrppsrspaAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
340-457 |
2.76e-08 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410919 [Multi-domain] Cd Length: 159 Bit Score: 54.21 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrDGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRSTE 417
Cdd:cd19511 28 KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQS 105
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1712965699 418 KISEDLRATLNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 457
Cdd:cd19511 106 DSSGVTDRVVSQLLTELDgiESLKGVVVIAATNRPDMIDPAL 147
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
339-463 |
3.09e-08 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 54.22 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 339 YRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRDGVTAMHK-VFDWANTSRRGlLLFVDEADAFLRKRSTE 417
Cdd:cd19522 33 WKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRlLFEMARFYAPT-TIFIDEIDSICSRRGTS 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 418 KISEDLRATLNAFLYR--------TGEQSNKFMLVL-ASNQPEQFDWAINDRIDE 463
Cdd:cd19522 112 EEHEASRRVKSELLVQmdgvggasENDDPSKMVMVLaATNFPWDIDEALRRRLEK 166
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
342-525 |
3.63e-08 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 56.76 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTG--------GDVAPMGRDgvtamhkVFDWANtSRRGLLLFVDEADAFLRK 413
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 414 RSTEKISED---------LRATLNAFlyrtgEQSNKFMLVLASNQPEQFDWAI-----NDRIDEIvnfalPGPDERDRLV 479
Cdd:PRK03992 240 RTDSGTSGDrevqrtlmqLLAEMDGF-----DPRGNVKIIAATNRIDILDPAIlrpgrFDRIIEV-----PLPDEEGRLE 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1712965699 480 rlyfdkyVLEPATggrQRMKLAQ-FDYiakcSEIAKRTEGMSGREIS 525
Cdd:PRK03992 310 -------ILKIHT---RKMNLADdVDL----EELAELTEGASGADLK 342
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-271 |
4.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDK 129
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 130 LARQRYEDQLRQQQI-LNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENADIIREQIRLK 208
Cdd:COG1196 431 AELEEEEEEEEEALEeAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 209 AAEHRQTVLESIKTAGAVfgegfrafVSDWDKVTATVAGLTLLAVGVYSARNATGVAGRYIEA 271
Cdd:COG1196 511 KAALLLAGLRGLAGAVAV--------LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
780-974 |
5.10e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 57.19 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 780 VIAPVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTP---PPSEEAVAAAPlvQDVIAPVVEVTPPPSEEAAAPVAedviap 856
Cdd:PRK12323 389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAParrSPAPEALAAAR--QASARGPGGAPAPAPAPAAAPAA------ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 857 vveVTPPLAVEVEAPLAEDVAAPVvevtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA 936
Cdd:PRK12323 461 ---AARPAAAGPRPVAAAAAAAPA----RAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170 180 190
....*....|....*....|....*....|....*...
gi 1712965699 937 EDVAAPVVEVtPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:PRK12323 534 PDDAFETLAP-APAAAPAPRAAAATEPVVAPRPPRASA 570
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-219 |
5.32e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDK 129
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 130 LARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENaDIIREQIRLKA 209
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEA 411
|
170
....*....|
gi 1712965699 210 AEHRQTVLES 219
Cdd:COG1196 412 LLERLERLEE 421
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
340-467 |
5.66e-08 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 53.50 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGD-VAPMGRDGVTAMHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK 418
Cdd:cd19502 38 KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRELFEMARE-KAPSIIFIDEIDAIGAKRFDSG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 419 ISED---------LRATLNAFlyrtgEQSNKFMLVLASNQPEQFDWAI--NDRIDEIVNF 467
Cdd:cd19502 117 TGGDrevqrtmleLLNQLDGF-----DPRGNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
339-463 |
5.73e-08 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410929 [Multi-domain] Cd Length: 170 Bit Score: 53.71 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 339 YRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP--MGrDGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRSt 416
Cdd:cd19521 40 WSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCGTRG- 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1712965699 417 EKISEDLRATLNAFLYR---TGEQSNKFMLVLASNQPEQFDWAINDRIDE 463
Cdd:cd19521 117 EGESEASRRIKTELLVQmngVGNDSQGVLVLGATNIPWQLDSAIRRRFEK 166
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
782-1003 |
5.74e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 57.17 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVT 861
Cdd:PRK07003 400 TAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASA 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 862 PplAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDV-- 939
Cdd:PRK07003 480 P--ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVlr 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 940 --------------AAPVVEVTPPPSAEAPLAEDVAAPVvevtPPPSAEVKCTLSDGldsDNTVKAEPASETEHLAQP 1003
Cdd:PRK07003 558 nagmrvssdrgaraAAAAKPAAAPAAAPKPAAPRVAVQV----PTPRARAATGDAPP---NGAARAEQAAESRGAPPP 628
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
340-527 |
7.37e-08 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 56.45 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGRDGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRSTEK 418
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 419 ISEDLRATLNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEIVnfALPGPDERDRlvrlyFDKYVLEPatgg 494
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLI--LVPPPDEEAR-----KEIFKIHT---- 635
|
170 180 190
....*....|....*....|....*....|...
gi 1712965699 495 rQRMKLAQfdyIAKCSEIAKRTEGMSGREISKL 527
Cdd:TIGR01243 636 -RSMPLAE---DVDLEELAEMTEGYTGADIEAV 664
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-214 |
7.41e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEH-QSKIKEYEAAVEQLKG--DQIRIQGEERRKTLNEETKQhQARAQY 126
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEElEAELAELEAELEELRLelEELELELEEAQAEEYELLAE-LARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 QDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNEL-LRIEAESKARARVERENADIIREQI 205
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeAELAEAEEALLEAEAELAEAEEELE 382
|
....*....
gi 1712965699 206 RLKAAEHRQ 214
Cdd:COG1196 383 ELAEELLEA 391
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
678-963 |
1.09e-07 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 56.25 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 678 APIVEVTPPPSEEAVAAAPLvqdviTPVVEVTPPPSEEAVaaaaaplvQDVIAPVVEVTPPPSE--EAVAAAAAPLVQdv 755
Cdd:PRK10263 335 APVEPVTQTPPVASVDVPPA-----QPTVAWQPVPGPQTG--------EPVIAPAPEGYPQQSQyaQPAVQYNEPLQQ-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 756 iaPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVV 835
Cdd:PRK10263 400 --PVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 836 EVTPPPSEEAAAPVAEDVIAPVVEVTPPLAV--EVEAPLA---EDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSA 910
Cdd:PRK10263 478 YQQPQPVEQQPVVEPEPVVEETKPARPPLYYfeEVEEKRArerEQLAAWYQPIPEPVKEPEPIKSSLKAPSVAAVPPVEA 557
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 911 EAPLAEdVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAP 963
Cdd:PRK10263 558 AAAVSP-LASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRP 609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-221 |
1.43e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLK--GDQIRIQGEERRKTLNEETKQHQARAQYQ 127
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKkkAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 128 DKLARQ-------RYEDQLRQ-QQILNEENLRKQEEsVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENAD 199
Cdd:PTZ00121 1521 AKKADEakkaeeaKKADEAKKaEEKKKADELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
170 180
....*....|....*....|..
gi 1712965699 200 IIREQIRLKAAEHRQTVLESIK 221
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIK 1621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-223 |
1.65e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAK-------DLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQ-H 120
Cdd:COG1196 205 LERQAEKAEryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 121 QARAQYQDKLAR--------QRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARAR 192
Cdd:COG1196 285 EAQAEEYELLAElarleqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190
....*....|....*....|....*....|.
gi 1712965699 193 VERENADIIREQIRLKAAEHRQTVLESIKTA 223
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAA 395
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
807-1028 |
1.70e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 55.27 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPvvevTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPvvevTPP 886
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAAAPAAAAPAP----AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASA----RGP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 887 PSAEAPLAEDVAAPVVEVTPPPSAEAPlaedvaaPVVEVTPPPSAEAPLAEDVAAPvveVTPPPSAEAPLAEDVAAPVVE 966
Cdd:PRK12323 445 GGAPAPAPAPAAAPAAAARPAAAGPRP-------VAAAAAAAPARAAPAAAPAPAD---DDPPPWEELPPEFASPAPAQP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 967 VTPPPSAEVKCTLSDGldsdnTVKAEPASETEHLAQPAASAETEAKMKKEDKTVSPPKDGTP 1028
Cdd:PRK12323 515 DAAPAGWVAESIPDPA-----TADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASAS 571
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
340-461 |
1.71e-07 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410928 [Multi-domain] Cd Length: 166 Bit Score: 52.04 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDY-----AIMTG---GDvapmGRDGVTAmhkVFDWANTSRRGlLLFVDEADAFL 411
Cdd:cd19520 36 KGVLLYGPPGCGKTMLAKATAKEAGARFinlqvSSLTDkwyGE----SQKLVAA---VFSLASKLQPS-IIFIDEIDSFL 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 412 RKRStekiSEDLRATL---NAFL-----YRTGEQSnKFMLVLASNQPEQFDWAINDRI 461
Cdd:cd19520 108 RQRS----STDHEATAmmkAEFMslwdgLSTDGNC-RVIVMGATNRPQDLDEAILRRM 160
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
678-846 |
2.02e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 55.43 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 678 APIVEVTPPPSEEAVAAAPLVQDVITPVVEVTPPPSEEAVAAAaaplvqdvIAPVVEVTPPPSEEAVAAAAAPLVqdVIA 757
Cdd:PRK10811 853 VQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVV--------EEPVVVAEPQPEEVVVVETTHPEV--IAA 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 758 PVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEV 837
Cdd:PRK10811 923 PVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVA 1002
|
....*....
gi 1712965699 838 TPPPSEEAA 846
Cdd:PRK10811 1003 PAQVPEATV 1011
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
61-218 |
2.40e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 61 KSRHAKEALDLARMQEQSTQlEHQSKIKEYEAAVEQLKGDQ-------IRIQGEERRKTLnEETKQHQARAQYQDKLARQ 133
Cdd:pfam17380 390 KNERVRQELEAARKVKILEE-ERQRKIQQQKVEMEQIRAEQeearqreVRRLEEERAREM-ERVRLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 134 RYEDQLRQQQilneeNLRKQEESVQKQEAMRKATIEHEMELRHKnellRIEAESKARARVERENAD----IIREQIRLKA 209
Cdd:pfam17380 468 QEEERKRKKL-----ELEKEKRDRKRAEEQRRKILEKELEERKQ----AMIEEERKRKLLEKEMEErqkaIYEEERRREA 538
|
....*....
gi 1712965699 210 AEHRQTVLE 218
Cdd:pfam17380 539 EEERRKQQE 547
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-218 |
2.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLD--KSRHAKEALDLARMQEQSTQLE-----HQSKIKEYEAAVEQLKGDQIRIQgEERRKTLNEETKQHQ 121
Cdd:COG1196 294 LAELARLEQDIArlEERRRELEERLEELEEELAELEeeleeLEEELEELEEELEEAEEELEEAE-AELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 122 ARAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENADII 201
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
170
....*....|....*..
gi 1712965699 202 REQIRLKAAEHRQTVLE 218
Cdd:COG1196 453 ELEEEEEALLELLAELL 469
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
810-974 |
2.49e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 54.87 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 810 VEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEdviAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSA 889
Cdd:PRK07994 364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPAS---APQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 890 EAPLAEDVAAPVvevtppPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP--PSAEAPLAEDVAAPvvEV 967
Cdd:PRK07994 441 SEPAAASRARPV------NSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVatPKALKKALEHEKTP--EL 512
|
....*..
gi 1712965699 968 TPPPSAE 974
Cdd:PRK07994 513 AAKLAAE 519
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
830-974 |
2.52e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 54.86 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 830 VIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEdvaAPVVEVTPPPSAEA---PLAEDVAAPVVEVTP 906
Cdd:PRK07003 380 VPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAE---APPAAPAPPATADRgddAADGDAPVPAKANAR 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 907 --PPSAEAPL-AEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:PRK07003 457 asADSRCDERdAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAP 527
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
342-527 |
3.37e-07 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 54.29 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMgRDGVTA--MHKVFDWANtSRRGLLLFVDEADAFLRKRSTE-K 418
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAarVRDLFKKAK-ENSPCIVFIDEIDAVGRQRGAGiG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 419 ISEDLR-ATLNAFL-YRTGEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEIVNFALPGPDERDRLVRLYFDKYVLEPATG 493
Cdd:CHL00176 297 GGNDEReQTLNQLLtEMDGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376
|
170 180 190
....*....|....*....|....*....|....
gi 1712965699 494 GRQrmklaqfdyiakcseIAKRTEGMSGREISKL 527
Cdd:CHL00176 377 LEL---------------IARRTPGFSGADLANL 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-214 |
5.18e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 51 RAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVE--------QLKGDQIRIQGEERRKTlnEETKQHQA 122
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkaeedKKKADELKKAAAAKKKA--DEAKKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 123 RAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATiehemELRHKNELLRIEAESKARARVERENADIIR 202
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-----EAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
170
....*....|....
gi 1712965699 203 --EQIRLKAAEHRQ 214
Cdd:PTZ00121 1504 kaAEAKKKADEAKK 1517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-214 |
5.31e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 52 AAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQskIKEYEAAVEQLKGDQIRIQGE--ERRKTLNEETKQHQARAQYQDK 129
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEEleELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 130 LARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENADIIREQIRLKA 209
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
....*
gi 1712965699 210 AEHRQ 214
Cdd:COG1196 443 ALEEA 447
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
807-962 |
5.47e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 53.72 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPP---PSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEV 883
Cdd:PRK07994 370 VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPasaPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 884 TPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP--PSAEAPLAEDVAAPvvEVTPPPSAEAPLAEDVA 961
Cdd:PRK07994 450 RPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVatPKALKKALEHEKTP--ELAAKLAAEAIERDPWA 527
|
.
gi 1712965699 962 A 962
Cdd:PRK07994 528 A 528
|
|
| PTZ00454 |
PTZ00454 |
26S protease regulatory subunit 6B-like protein; Provisional |
340-483 |
5.87e-07 |
|
26S protease regulatory subunit 6B-like protein; Provisional
Pssm-ID: 240423 [Multi-domain] Cd Length: 398 Bit Score: 53.23 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGD-VAPMGRDGVTAMHKVFDWANTSRRGlLLFVDEADAFLRK----- 413
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKrfdaq 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 414 ----RSTEKISEDLRATLNAFlyrtgEQSNKFMLVLASNQPEQFDWAI--NDRIDEIVNFalPGPDERDRlvRLYF 483
Cdd:PTZ00454 259 tgadREVQRILLELLNQMDGF-----DQTTNVKVIMATNRADTLDPALlrPGRLDRKIEF--PLPDRRQK--RLIF 325
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
639-1022 |
7.08e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 639 PPPSVEAAAPQAQDVATPIAEVTPPPSVEVEPPLVPDVIAPIVEVTPPPSEEAVAAAPlvqdvitpvvEVTPPPseeavA 718
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA----------QASSPP-----Q 2681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 719 AAAAPLVQDVIAPVVEVT-PPPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEaaaaaplvqdviAPVVEVAPPPSEEAVA 797
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLAdPPPPPPTPEPAPHALVSATPLPPGPAAARQASP------------ALPAAPAPPAVPAGPA 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 798 AAPVAEDVIAPVVEVTPPPSeeAVAAAPlvqdvIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVA 877
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAP--APPAAP-----AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA 2822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 878 APVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlaedvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPla 957
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST-- 2895
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 958 EDVAAPVVEVTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQPAASAETEAKMKKEDKTVSP 1022
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
833-973 |
7.31e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 53.33 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 833 PVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVEVTPPPSAEA 912
Cdd:PRK07994 361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQA--PAVPLPETTSQLLAARQQLQRAQGATKA 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 913 PLAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP--PSA 973
Cdd:PRK07994 439 KKSEPAAASRAR--PVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVatPKA 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-223 |
9.27e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYE---AAVEQLKGDQIRiQGEERRKTLNEETKQHQARAQY 126
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADE 1538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 QDKLARQRYEDQLRQQqilneENLRKQEEsVQKQEAMRKATIEHEMELRHKNELLRIE------------------AESK 188
Cdd:PTZ00121 1539 AKKAEEKKKADELKKA-----EELKKAEE-KKKAEEAKKAEEDKNMALRKAEEAKKAEearieevmklyeeekkmkAEEA 1612
|
170 180 190
....*....|....*....|....*....|....*..
gi 1712965699 189 ARARVERENADIIR--EQIRLKAAEHRQTVLESIKTA 223
Cdd:PTZ00121 1613 KKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKA 1649
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
886-1010 |
1.03e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 52.79 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 886 PPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVV 965
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712965699 966 EVTPPPSAEVKctlSDGLDSDNTVKAEPASETEHLAQPAASAETE 1010
Cdd:PRK14951 446 ALAPAPPAQAA---PETVAIPVRVAPEPAVASAAPAPAAAPAAAR 487
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
60-221 |
1.04e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 60 DKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQyQDKLARQRYEDQL 139
Cdd:pfam15709 359 EQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ-QEEFRRKLQELQR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 140 RQQQilnEENLRKQ-EESVQKQEAMRKATiEH----EMELRHKNELLRIEAESKARARVErenadiiREQIRLKAAEHRQ 214
Cdd:pfam15709 438 KKQQ---EEAERAEaEKQRQKELEMQLAE-EQkrlmEMAEEERLEYQRQKQEAEEKARLE-------AEERRQKEEEAAR 506
|
....*..
gi 1712965699 215 TVLESIK 221
Cdd:pfam15709 507 LALEEAM 513
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
340-457 |
1.04e-06 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410937 [Multi-domain] Cd Length: 159 Bit Score: 49.42 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGRDGVTAMHKVFDWANTSRRgLLLFVDEADAFLRKRS--- 415
Cdd:cd19529 28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELlSKWVGESEKAIREIFRKARQVAP-CVIFFDEIDSIAPRRGttg 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1712965699 416 ----TEKISEDLRATLNAFlyrtgEQSNKFMLVLASNQPEQFDWAI 457
Cdd:cd19529 107 dsgvTERVVNQLLTELDGL-----EEMNGVVVIAATNRPDIIDPAL 147
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-223 |
1.48e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 36 KPKDKWSNFDPTGLERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERR----K 111
Cdd:PTZ00121 1073 KPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKaedaK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 112 TLNEETKQHQARAQYQDKLAR--QRYEDQLRQQQILNEENLRKQE-----------ESVQKQEAMRKATIEHEMELRHKN 178
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEdaKKAEAARKAEEVRKAEELRKAEdarkaeaarkaEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 179 ELLRIEAESKARARVERENADI-----------IREQIRLKAAEHRQTvlESIKTA 223
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIrkfeearmahfARRQAAIKAEEARKA--DELKKA 1286
|
|
| RecA-like_CDC48_r2-like |
cd19528 |
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ... |
340-465 |
1.68e-06 |
|
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410936 [Multi-domain] Cd Length: 161 Bit Score: 49.05 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMG-RDGVTAMHKVFDWANTSRRgLLLFVDEADAFLRKRSTeK 418
Cdd:cd19528 28 KGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWfGESEANVRDIFDKARAAAP-CVLFFDELDSIAKARGG-N 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 419 ISEDLRAT---LNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEIV 465
Cdd:cd19528 106 IGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLI 159
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-232 |
2.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEaavEQLKGDQIRIQGEE--------RRKTLNEETKQHQ 121
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE---EKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 122 ARAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKAtiehEMELRHKNELLRIEAESKAR----ARVEREN 197
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA----EEENKIKAEEAKKEAEEDKKkaeeAKKDEEE 1755
|
170 180 190
....*....|....*....|....*....|....*
gi 1712965699 198 adiiREQIRLKAAEHRQTVLESIKTAGAVFGEGFR 232
Cdd:PTZ00121 1756 ----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
340-457 |
2.30e-06 |
|
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410927 [Multi-domain] Cd Length: 166 Bit Score: 48.59 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGRDGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRSTEK 418
Cdd:cd19519 35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKREKTH 113
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1712965699 419 ISEDLRATLNAFLYRTGEQSNKFMLVL-ASNQPEQFDWAI 457
Cdd:cd19519 114 GEVERRIVSQLLTLMDGLKQRAHVIVMaATNRPNSIDPAL 153
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
807-935 |
2.51e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 51.64 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAedvaapvvevtPP 886
Cdd:PRK14951 380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVA-----------LA 448
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1712965699 887 PSAEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEVTPPPSAEAPL 935
Cdd:PRK14951 449 PAPPAQAAPETVAIPVRVAPEPAVASA-APAPAAAPAAARLTPTEEGDV 496
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
340-457 |
2.64e-06 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 48.44 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---DGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRST 416
Cdd:cd19503 35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712965699 417 --EKISEDLRATLNAfLYRTGEQSNKFMLVLASNQPEQFDWAI 457
Cdd:cd19503 112 dqREVERRVVAQLLT-LMDGMSSRGKVVVIAATNRPDAIDPAL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-200 |
3.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 51 RAAQAAKDLDKSRhaKEALDLARMQEQSTQLEHQSKIKEYEAAveqlKGDQIRIQGEERRKTLNEETKQHQARAQYQDKL 130
Cdd:PTZ00121 1662 KAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 131 ARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELlrIEAESKARARVERENADI 200
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL--DEEDEKRRMEVDKKIKDI 1803
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
49-221 |
3.28e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKsrhAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQiriqgEERRKTLNEETKQHQAR--AQY 126
Cdd:pfam13868 122 LEKQRQLREEIDE---FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER-----EAEREEIEEEKEREIARlrAQQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 QDKLARQRYEDQLRQQQILnEENLRKQEEsVQKQEAMRKATIEHEM------ELRHKNELLRIEA--ESKARARVERENA 198
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQ-EEQERKERQ-KEREEAEKKARQRQELqqareeQIELKERRLAEEAerEEEEFERMLRKQA 271
|
170 180
....*....|....*....|....*....
gi 1712965699 199 DIIR------EQIRLKAAEHRQTVLESIK 221
Cdd:pfam13868 272 EDEEieqeeaEKRRMKRLEHRRELEKQIE 300
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
340-461 |
3.41e-06 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 48.83 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM----GRDGVTAMHKVFDWANTSrrglLLFVDEADAFLRKRS 415
Cdd:cd19525 56 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKwvgeGEKMVRALFSVARCKQPA----VIFIDEIDSLLSQRG 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1712965699 416 tEKISEDLRATLNAFLYR----TGEQSNKFMLVLASNQPEQFDWAINDRI 461
Cdd:cd19525 132 -EGEHESSRRIKTEFLVQldgaTTSSEDRILVVGATNRPQEIDEAARRRL 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
49-255 |
3.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKSRHAKEALD--LARMQEQSTQLEHqsKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQY 126
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEeeLEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 QDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEM----ELRHKNELLRIEAEskaRARVERENADIIR 202
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqrLAELEEELEEAQEE---LEELEEELEQLEN 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 203 EQIRLKAAEHRQTVLESIKTAGAVFgeGFRAFVSDWDKVTATVAGLTLLAVGV 255
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGVLFLVLGL 285
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
63-218 |
3.49e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 63 RHAKEALDLARMQ-EQSTQLEHQSKIKeYEAAVEQLKGDQIRIqgEERRKTLNEETKQHQARAQyqdklARQRYEDQLrQ 141
Cdd:pfam13868 9 RELNSKLLAAKCNkERDAQIAEKKRIK-AEEKEEERRLDEMME--EERERALEEEEEKEEERKE-----ERKRYRQEL-E 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 142 QQILNEENLRKQEESVQKQEA-MRKATIEHEMELRHKNELLRIEAESKARarveRENADIIREQIRLKAAEHRQTVLE 218
Cdd:pfam13868 80 EQIEEREQKRQEEYEEKLQEReQMDEIVERIQEEDQAEAEEKLEKQRQLR----EEIDEFNEEQAEWKELEKEEEREE 153
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
813-1022 |
4.27e-06 |
|
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: 51.07 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 813 TPPPSEEAVAAAPlvqdviapvVEVTPPPSEEAAAPVAEDVIAPVVEVTPPlaveveaplAEDVAAPVVEVTPP-PSAEA 891
Cdd:pfam05109 475 SPTPAGTTSGASP---------VTPSPSPRDNGTESKAPDMTSPTSAVTTP---------TPNATSPTPAVTTPtPNATS 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 892 PLAEDVAAPVVEVTPPPSAEAPlaedvaAPVVeVTPPPSAeaplaedvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPP 971
Cdd:pfam05109 537 PTLGKTSPTSAVTTPTPNATSP------TPAV-TTPTPNA--------TIPTLGKTSPTSAVTTPTPNATSPTVGETSPQ 601
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712965699 972 SAEVKCTLSdGLDSDNTVKAEPASET------EHLAQPAASAETEAKMKKEDKTVSP 1022
Cdd:pfam05109 602 ANTTNHTLG-GTSSTPVVTSPPKNATsavttgQHNITSSSTSSMSLRPSSISETLSP 657
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-214 |
4.58e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 51 RAAQAAKDLDKSRHAKEAldlaRMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKtLNEETKQHQARAQYQDKL 130
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEA----RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK-FEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 131 ARQRYEDQLRQ-QQILNEENLRKQEESVQKQEAMRKATIEHEM-ELRHKNELLRIEAESKARARVERENADIIREQ---- 204
Cdd:PTZ00121 1275 EEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeaea 1354
|
170
....*....|..
gi 1712965699 205 --IRLKAAEHRQ 214
Cdd:PTZ00121 1355 aaDEAEAAEEKA 1366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-221 |
5.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 51 RAAQAAKDLDKSRHAKE---ALDL-----ARMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRiQGEERRKTLNEETKQHQA 122
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEvrkAEELrkaedARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 123 RAQYQ-DKLARQRYEDQLRQQQILNEEN------LRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVER 195
Cdd:PTZ00121 1249 RNNEEiRKFEEARMAHFARRQAAIKAEEarkadeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
170 180
....*....|....*....|....*.
gi 1712965699 196 ENADIIReqirlKAAEHRQTVLESIK 221
Cdd:PTZ00121 1329 KKADAAK-----KKAEEAKKAAEAAK 1349
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
50-211 |
5.62e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAkdlDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLK------GDQIRIQGEERRKTLNEETKQHQAR 123
Cdd:pfam13868 23 ERDAQIA---EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKeerkryRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 124 AQYQDKLARQRYEDQLRQQQILNEENLRKQEEsVQKQEAMRKATIEhEMELRHKNELLRIEAESKARARVERENADIIRE 203
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREE-IDEFNEEQAEWKE-LEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
....*...
gi 1712965699 204 QIRLKAAE 211
Cdd:pfam13868 178 IEEEKERE 185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-221 |
6.00e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 51 RAAQAAKDLDKSRHAKEALDLaRMQEQSTQLEHQSKIKEYE----AAVEQLKGDQIRIQGEERRKTlNEETKQHQARAQY 126
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAEeakkAEEDKKKAEEAKKAEEDEKKA-AEALKKEAEEAKK 1703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 QDKLARQRYEDQLRQQQILNEENLR--KQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARA-RVERENADIIRE 203
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAeEIRKEKEAVIEE 1783
|
170
....*....|....*...
gi 1712965699 204 QIRLKAAEHRQTVLESIK 221
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-223 |
9.44e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 55 AAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKG-------DQIRIQGE-----ERRKTLNEETKQHQA 122
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseleeEIEELQKElyalaNEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 123 RAQY--QDKLARQRYEDQLRQQQILNEENL---RKQEESVQKQ-EAMRKATIEHEM---ELRHKNELLRIEAESKARARV 193
Cdd:TIGR02168 310 RLANleRQLEELEAQLEELESKLDELAEELaelEEKLEELKEElESLEAELEELEAeleELESRLEELEEQLETLRSKVA 389
|
170 180 190
....*....|....*....|....*....|....*.
gi 1712965699 194 ERE------NADIIREQIRLKAAEHRQTVLESIKTA 223
Cdd:TIGR02168 390 QLElqiaslNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
50-221 |
1.00e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEA----LDLARMQEQSTQLEHQSKIKEYEAAVEQLKGD--QIRIQGEERRKTLNEETKQHQAR 123
Cdd:pfam13868 155 ERILEYLKEKAEREEEREAereeIEEEKEREIARLRAQQEKAQDEKAERDELRAKlyQEEQERKERQKEREEAEKKARQR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 124 A------QYQDKLARQRYEDQLRQQQILNEENLRKQEEsvQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVEREN 197
Cdd:pfam13868 235 QelqqarEEQIELKERRLAEEAEREEEEFERMLRKQAE--DEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE 312
|
170 180
....*....|....*....|....
gi 1712965699 198 ADIIREQIRlKAAEHRQTVLESIK 221
Cdd:pfam13868 313 ELEEGERLR-EEEAERRERIEEER 335
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
620-762 |
1.42e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.27 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 620 AEVAAPQIQDV-ITQVLEAMPPPSVEAAAPQAQDVATPIAEVTPPPSVEVEPPLVPDVIAPIVEVTPPPSEEAVAAAPLV 698
Cdd:PRK10811 863 EVQVQPVVAEVpVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEV 942
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 699 QDVITPVVEVTPPPSEEAVAAAAAP-LVQDVIAPVVEVTPPPSEEAVAAAAAPLVQDVIAPVVEV 762
Cdd:PRK10811 943 AEHAEPVVEPQDETADIEEAAETAEvVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP 1007
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
340-461 |
1.60e-05 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410932 [Multi-domain] Cd Length: 164 Bit Score: 46.38 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDY-----AIMTGGDVApmgrDGVTAMHKVFDWAnTSRRGLLLFVDEADAFLRKR 414
Cdd:cd19524 34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVA-RELQPSIIFIDEVDSLLSER 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1712965699 415 STEKISEDLRATLNAFLYRTGEQSNKFMLVL---ASNQPEQFDWAINDRI 461
Cdd:cd19524 109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRF 158
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
846-975 |
1.61e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 48.71 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 846 AAPVAEDVIAPVVevTPPLAVEVEAPLAEDVAAPVVEVT-PPPSAEAPLAEDVAAPVVEVTPPPSAEAPL-AEDVAAPVV 923
Cdd:PRK07994 362 AAPLPEPEVPPQS--AAPAASAQATAAPTAAVAPPQAPAvPPPPASAPQQAPAVPLPETTSQLLAARQQLqRAQGATKAK 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 924 EVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEV 975
Cdd:PRK07994 440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKK 491
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
49-214 |
1.99e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQsKIKEYEAAV---EQLKGDQIRIQGEERRKTLNEETKQHQARaQ 125
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREQK-RQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLR-E 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 126 YQDKLARQRYEDQLRQQQILNEENLR------KQEESVQKQEAMRK--------------ATIEHEMELRHKNELLRI-- 183
Cdd:pfam13868 131 EIDEFNEEQAEWKELEKEEEREEDERileylkEKAEREEEREAEREeieeekereiarlrAQQEKAQDEKAERDELRAkl 210
|
170 180 190
....*....|....*....|....*....|....
gi 1712965699 184 ---EAESKARARVERENADIIREQIRLKAAEHRQ 214
Cdd:pfam13868 211 yqeEQERKERQKEREEAEKKARQRQELQQAREEQ 244
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
782-975 |
2.22e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDViAPVVEVT 861
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPA-APAAPAG 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 862 PPLAVEVEAPLAEDVAAPVVE-VTPPPSAEAPLAEDVAAPVVEVTPPPsaEAPLAEDVAAPVVEVTPPPSAEAPLAEDVA 940
Cdd:PRK07764 696 AAPAQPAPAPAATPPAGQADDpAAQPPQAAQGASAPSPAADDPVPLPP--EPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
170 180 190
....*....|....*....|....*....|....*
gi 1712965699 941 APVvevtPPPSAEAPLAEDVAAPVVEVTPPPSAEV 975
Cdd:PRK07764 774 PPP----SPPSEEEEMAEDDAPSMDDEDRRDAEEV 804
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
847-1023 |
2.89e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 847 APVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVvevTPPPSAEAPLAEDVAAPVVEVT 926
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARR---SPAPEALAAARQASARGPGGAP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 927 PPPSAEAPL-AEDVAAPVVEVTPPPSAEA---PLAEDVAAPVVEVTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQ 1002
Cdd:PRK12323 449 APAPAPAAApAAAARPAAAGPRPVAAAAAaapARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPD 528
|
170 180
....*....|....*....|.
gi 1712965699 1003 PAASAETEAKMKKEDKTVSPP 1023
Cdd:PRK12323 529 PATADPDDAFETLAPAPAAAP 549
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
73-211 |
2.94e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 45.69 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 73 RMQEQSTQLEHQSKikEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDKLA---RQRYEdqlRQQQI--LNE 147
Cdd:pfam08614 11 RLLDRTALLEAENA--KLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAelyRSRGE---LAQRLvdLNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 148 ENLRKQEESVQKQEAMRKATIE----------HEMELRHKNEL----------LRIE---AESKARaRVERENADIIREQ 204
Cdd:pfam08614 86 ELQELEKKLREDERRLAALEAEraqleeklkdREEELREKRKLnqdlqdelvaLQLQlnmAEEKLR-KLEKENRELVERW 164
|
....*..
gi 1712965699 205 IRLKAAE 211
Cdd:pfam08614 165 MKRKGQE 171
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
69-193 |
3.47e-05 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 44.61 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 69 LDLARMQEQSTQLEHQSKIKEYEAAVEQLkgDQIRIQGEERRKTLNEETK------QHQARAQYQDKLarqryeDQLRQQ 142
Cdd:TIGR02473 8 LDLREKEEEQAKLELAKAQAEFERLETQL--QQLIKYREEYEQQALEKVGagtsalELSNYQRFIRQL------DQRIQQ 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 143 QILNEENLRKQEEsvQKQEAMRKATIEHEM--ELRHKNELLRIEAESKARARV 193
Cdd:TIGR02473 80 QQQELALLQQEVE--AKRERLLEARRELKAleKLKEKKQKEYRAEEAKREQKE 130
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
852-943 |
5.30e-05 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 45.76 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 852 DVIAPVVEVTP--PLAVEVEAPLAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPP 929
Cdd:PRK11633 54 DMMPAATQALPtqPPEGAAEAVRAGDAAAPSLD--PATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP 131
|
90
....*....|....*
gi 1712965699 930 S-AEAPLAEDVAAPV 943
Cdd:PRK11633 132 KpEPKPVVEEKAAPT 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-214 |
5.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKSRHAKEALDLARMQE-QSTQLEHQSKIKEYEAAVEQLKGDQIRiQGEERRKTlNEETKQHQARA--Q 125
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKA-DEAKKAEEKKKadE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 126 YQDKLARQRYEDQLRQQQilnEENLRKQEESVQK-QEAMRKATIEHEMELRHKNELLRIEAESKArARVERENADIIREQ 204
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKA---EEAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKADA 1382
|
170
....*....|
gi 1712965699 205 IRLKAAEHRQ 214
Cdd:PTZ00121 1383 AKKKAEEKKK 1392
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
853-966 |
5.87e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 47.11 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 853 VIAPVVEVTPPLAVEVEAPlAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSaeaPLAEDVAAPVVEVTPPPSAE 932
Cdd:PRK14950 356 IEALLVPVPAPQPAKPTAA-APSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPP---VPPRPVAPPVPHTPESAPKL 431
|
90 100 110
....*....|....*....|....*....|....
gi 1712965699 933 APLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVE 966
Cdd:PRK14950 432 TRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
622-841 |
5.89e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 47.34 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 622 VAAPQIQDVITQvleamPPPSVEAAAPQAQDVATPiAEVTPPPSVEVEPPLVPDVIAPIVEVTPPPSEEAVAAAPLVQDV 701
Cdd:PRK10811 847 VVRPQDVQVEEQ-----REAEEVQVQPVVAEVPVA-AAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVI 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 702 ITPVVEVTPPpseeavaaaaaplVQDVIAPVVEVTPPPSEEAVAaaaaplVQDVIAPVVEVTPPPSEEAAAAAPLVQDVI 781
Cdd:PRK10811 921 AAPVTEQPQV-------------ITESDVAVAQEVAEHAEPVVE------PQDETADIEEAAETAEVVVAEPEVVAQPAA 981
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDviapvvEVTPPPSEEAVAAAPLVQdviAPVVEVTPPP 841
Cdd:PRK10811 982 PVVAEVAAEVETVTAVEPEVAPA------QVPEATVEHNHATAPMTR---APAPEYVPEA 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-221 |
5.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKE--YEAAVEQLKGDQIRIQGEERRKTlnEETKQHQARAQYQ 127
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKK 1498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 128 DKLARQRYEDQLRQqqilneENLRKQEESvQKQEAMRKATiehemELRHKNELLRIEaeskararvERENADIIREQIRL 207
Cdd:PTZ00121 1499 ADEAKKAAEAKKKA------DEAKKAEEA-KKADEAKKAE-----EAKKADEAKKAE---------EKKKADELKKAEEL 1557
|
170
....*....|....
gi 1712965699 208 KAAEHRQTVLESIK 221
Cdd:PTZ00121 1558 KKAEEKKKAEEAKK 1571
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
782-940 |
6.77e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 46.78 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPP-------PSEEAAAPVAEDVI 854
Cdd:PRK07994 370 VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlqraqgaTKAKKSEPAAASRA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 855 APVVEVTPPLAveveAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAP 934
Cdd:PRK07994 450 RPVNSALERLA----SVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDP 525
|
....*.
gi 1712965699 935 LAEDVA 940
Cdd:PRK07994 526 WAALVS 531
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
53-211 |
7.14e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.61 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 53 AQAAKDLDKSRHAKEAL--DLARMQEQSTQLEHQSKIKE------YEAAVEQLK--GDQIRIQGEE-------------- 108
Cdd:PRK11637 85 SQASRKLRETQNTLNQLnkQIDELNASIAKLEQQQAAQErllaaqLDAAFRQGEhtGLQLILSGEEsqrgerilayfgyl 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 109 ---RRKTLNE--ETKQH--QARAQYQDKLARQR---YEDQLRQQQILNEENLRKQ-----EESVQKQEAMRKATIEHEME 173
Cdd:PRK11637 165 nqaRQETIAElkQTREElaAQKAELEEKQSQQKtllYEQQAQQQKLEQARNERKKtltglESSLQKDQQQLSELRANESR 244
|
170 180 190
....*....|....*....|....*....|....*...
gi 1712965699 174 LRhkNELLRIEAESKARArvEREnadiIREQIRLKAAE 211
Cdd:PRK11637 245 LR--DSIARAEREAKARA--ERE----AREAARVRDKQ 274
|
|
| PTZ00436 |
PTZ00436 |
60S ribosomal protein L19-like protein; Provisional |
782-933 |
7.29e-05 |
|
60S ribosomal protein L19-like protein; Provisional
Pssm-ID: 185616 [Multi-domain] Cd Length: 357 Bit Score: 46.10 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAV---AAAPLVQDVIAPVVEVTPPPseEAAAPVAEDVIAPVV 858
Cdd:PTZ00436 203 AAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAAApakAAAAPAKAAAPPAKAAAPPA--KAAAPPAKAAAPPAK 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 859 EVTPPlaVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEA 933
Cdd:PTZ00436 281 AAAPP--AKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAPVGKKA 353
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
783-914 |
7.36e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.63 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 783 PVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTP 862
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 863 PLAVEVEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEVTPPPSAEAPL 914
Cdd:PRK14951 446 ALAPAPPAQAAPETVAIPVRVAPEPAVASA-APAPAAAPAAARLTPTEEGDV 496
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
826-945 |
7.40e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 46.73 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 826 LVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEvtPPLAVEVEAPLAEDVAAPVvevTPPPSAeaplAEDVAAPVVEVT 905
Cdd:PRK14950 355 VIEALLVPVPAPQPAKPTAAAPSPVRPTPAPSTR--PKAAAAANIPPKEPVRETA---TPPPVP----PRPVAPPVPHTP 425
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1712965699 906 PPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVE 945
Cdd:PRK14950 426 ESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
884-964 |
8.52e-05 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 44.99 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 884 TPPPSA-EAPLAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPS-AEAPLAEDVA 961
Cdd:PRK11633 66 QPPEGAaEAVRAGDAAAPSLD--PATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKpEPKPVVEEKA 143
|
...
gi 1712965699 962 APV 964
Cdd:PRK11633 144 APT 146
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
807-1017 |
8.64e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPP 886
Cdd:PRK07764 583 QVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 887 PSAEAPLAEDVAAPVVEVTPPPSAEAPlaedVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVE 966
Cdd:PRK07764 663 SDGGDGWPAKAGGAAPAAPPPAPAPAA----PAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 967 VTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQPAASAETEAKMKKED 1017
Cdd:PRK07764 739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
340-467 |
8.65e-05 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410925 [Multi-domain] Cd Length: 170 Bit Score: 44.04 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDyaimtGGDVAPMGRDGVTAMHKvfdWANTSRRGL-------------LLFVDE 406
Cdd:cd19517 35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 407 ADAFLRKRST--EKISEDLRATLNAfLYRTGEQSNKFMLVLASNQPEQFDWAIN--DRIDEIVNF 467
Cdd:cd19517 107 IDGLAPVRSSkqEQIHASIVSTLLA-LMDGLDNRGQVVVIGATNRPDALDPALRrpGRFDREFYF 170
|
|
| RecA-like_fidgetin |
cd19523 |
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ... |
340-460 |
1.11e-04 |
|
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410931 [Multi-domain] Cd Length: 163 Bit Score: 43.72 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTG-GDVAPMGRDGVTAMHKVFDWANTsRRGLLLFVDEADAFLRKRSTE- 417
Cdd:cd19523 34 RSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASFLAARC-RQPSVLFISDLDALLSSQDDEa 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1712965699 418 ----KISEDLRATLNAFLyrtGEQSNKFMLVLASNQPEQFDWAINDR 460
Cdd:cd19523 113 spvgRLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
341-411 |
1.20e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 45.82 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 341 NILMYGPPGTGKTLFAKKLAMHSGMDY----AIMtggdvapmgrDGVTAMHKVFDWANTSR---RGLLLFVDE------- 406
Cdd:COG2256 51 SMILWGPPGTGKTTLARLIANATDAEFvalsAVT----------SGVKDIREVIEEARERRaygRRTILFVDEihrfnka 120
|
....*.
gi 1712965699 407 -ADAFL 411
Cdd:COG2256 121 qQDALL 126
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
860-982 |
1.22e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 45.96 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 860 VTPPLAVEVEAPLAEDVAAPV-VEVTPPPSAEAPlaeDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSaeaPLAED 938
Cdd:PRK14950 343 TTSYGQLPLELAVIEALLVPVpAPQPAKPTAAAP---SPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPP---VPPRP 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712965699 939 VAAPVVEVTPPPSAEAPLAEDV-AAPVVEVTPPPSAEVKCTLSDG 982
Cdd:PRK14950 417 VAPPVPHTPESAPKLTRAAIPVdEKPKYTPPAPPKEEEKALIADG 461
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
340-457 |
1.24e-04 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 43.55 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMD-YAIMTGGDVAPMGRDGVTAMHKVFDWAnTSRRGLLLFVDEADAFLRKRST-- 416
Cdd:cd19518 35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKRESaq 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1712965699 417 ----EKISEDLRATLNAFLYRtgEQSNKFMLVL-ASNQPEQFDWAI 457
Cdd:cd19518 114 remeRRIVSQLLTCMDELNNE--KTAGGPVLVIgATNRPDSLDPAL 157
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
619-921 |
1.29e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.23 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 619 SAEVAAPQIQDVITQVLEA-----MPPPSVEAAAPqaqDVATPIAEVTPPPSVEVEPPlvpdVIAPIVEVTPPPSEEAVA 693
Cdd:PRK10263 317 TEPVAVAAAATTATQSWAApvepvTQTPPVASVDV---PPAQPTVAWQPVPGPQTGEP----VIAPAPEGYPQQSQYAQP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 694 AAPLVQDVITPVvevtPPPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEAAAA 773
Cdd:PRK10263 390 AVQYNEPLQQPV----QPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 774 APLVQDVIAPVVEVAPPPSEEAVAAAPVaedviaPVVEVTPPPS------EEAVAAAPLVQDVIAPVVEVTPPPSEEaAA 847
Cdd:PRK10263 466 QTYQQPAAQEPLYQQPQPVEQQPVVEPE------PVVEETKPARpplyyfEEVEEKRAREREQLAAWYQPIPEPVKE-PE 538
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 848 PVAEDVIAPVVEVTPPLAvevEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAP 921
Cdd:PRK10263 539 PIKSSLKAPSVAAVPPVE---AAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRP 609
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
817-944 |
1.32e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 45.73 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 817 SEEAVAA--APLVQDVIAPVVEVTPPPSE-EAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPL 893
Cdd:PRK06995 44 ADSDLAAlaPPAAAAPAAAQPPPAAAPAAvSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERA 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 894 AEDVAAPVVEVTPPPSAEAPLAEDVAApvvevTPPPSAEAPLAEDVAAPVV 944
Cdd:PRK06995 124 AAENAARRLARAAAAAPRPRVPADAAA-----AVADAVKARIERIVNDTVM 169
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
637-973 |
1.65e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.61 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 637 AMPPPSVEAAAPQAQDVATPIAEVTPPPSVEvepplvPDVIAPIVEVTPPPSEEAVAAAPlvqdvITPVVEVTPPPSEEA 716
Cdd:PRK07003 370 GGVPARVAGAVPAPGARAAAAVGASAVPAVT------AVTGAAGAALAPKAAAAAAATRA-----EAPPAAPAPPATADR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 717 VAAaaaPLVQDVIAPVVEVTPPPSEEAVAAAAAplvQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAV 796
Cdd:PRK07003 439 GDD---AADGDAPVPAKANARASADSRCDERDA---QPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 797 AAAPVAEDVIAPVVEVTP--PPSEEAVAAAPLVQDVIAPVVEV---------------TPPPSEEAAAPVAEDVIAPvve 859
Cdd:PRK07003 513 PAAASREDAPAAAAPPAPeaRPPTPAAAAPAARAGGAAAALDVlrnagmrvssdrgarAAAAAKPAAAPAAAPKPAA--- 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 860 vtPPLAVEVEAPLAEDVAApvvEVTPPPSAEAPLAEDVAAPvvevtPPPSAEAPLAEDVAAPVVEVTPPPsaeaplaEDV 939
Cdd:PRK07003 590 --PRVAVQVPTPRARAATG---DAPPNGAARAEQAAESRGA-----PPPWEDIPPDDYVPLSADEGFGGP-------DDG 652
|
330 340 350
....*....|....*....|....*....|....
gi 1712965699 940 AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSA 973
Cdd:PRK07003 653 FVPVFDSGPDDVRVAPKPADAPAPPVDTRPLPPA 686
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
341-452 |
1.68e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 42.66 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 341 NILMYGPPGTGKTLFAKKLA------------MHSGMDYAIMTGG-DVAPMG---RDG--VTAMhkvfdwantsRRGLLL 402
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGaswVDGplVRAA----------REGEIA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 403 FVDEADaflrkrsteKISEDLRATLNAFLY-----------RTGEQSNKFMLVLASNQPEQ 452
Cdd:pfam07728 71 VLDEIN---------RANPDVLNSLLSLLDerrlllpdggeLVKAAPDGFRLIATMNPLDR 122
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
68-214 |
1.69e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 68 ALDLARMQEQSTQLEHQSKIkeyEAAVEQLKGDQIRIQGEERRKTLNEETKQ-HQARAQYQDKLAR--QRYEDQLRQQQI 144
Cdd:pfam07111 480 SLELEQLREERNRLDAELQL---SAHLIQQEVGRAREQGEAERQQLSEVAQQlEQELQRAQESLASvgQQLEVARQGQQE 556
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 145 LNEENLRKQEESVQKQEAMRKATIEH--EMELRHKNELlrieAESKAR---ARVERENADIIREQIRLKAAEHRQ 214
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQALQEKvaEVETRLREQL----SDTKRRlneARREQAKAVVSLRQIQHRATQEKE 627
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
340-482 |
1.83e-04 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 45.67 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---DGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRS- 415
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKREe 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 416 -TEKISEDLRATLNAFLYRTGEQSnKFMLVLASNQPEQFDWAIN--DRIDEIVNFALPGPDERDRLVRLY 482
Cdd:TIGR01243 290 vTGEVEKRVVAQLLTLMDGLKGRG-RVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRARKEILKVH 358
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
783-1028 |
2.10e-04 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 45.30 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 783 PVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTP----PPSEEAVAAAPL-----VQDVIAPVVEVTPPPSEEAAAPVAEDV 853
Cdd:PLN03209 324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPieeePPQPKAVVPRPLspytaYEDLKPPTSPIPTPPSSSPASSKSVDA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 854 IAPVVEVTPPLAVEVEAPLAEDVAAPVVEVT------------------PPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA 915
Cdd:PLN03209 404 VAKPAEPDVVPSPGSASNVPEVEPAQVEAKKtrplspyaryedlkpptsPSPTAPTGVSPSVSSTSSVPAVPDTAPATAA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 916 EDVAApvvevtPPPSAEAPLAedvAAPVVEVTPPPSAEAPlaedvAAPVVEVTPPPSAEVKCTLSDGLDSdntvkaePAS 995
Cdd:PLN03209 484 TDAAA------PPPANMRPLS---PYAVYDDLKPPTSPSP-----AAPVGKVAPSSTNEVVKVGNSAPPT-------ALA 542
|
250 260 270
....*....|....*....|....*....|...
gi 1712965699 996 ETEHLAQPAASAETEAKMKKEDKtvsPPKDGTP 1028
Cdd:PLN03209 543 DEQHHAQPKPRPLSPYTMYEDLK---PPTSPTP 572
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
867-937 |
2.18e-04 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 45.38 E-value: 2.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 867 EVEAPLAEDVAAPVVEVTPPPSAEAplAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAE 937
Cdd:COG5373 32 ELEAELAEAAEAASAPAEPEPEAAA--AATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAA 100
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
50-214 |
2.81e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDlARMQEQSTQLEHQSKIKEY-EAAVEQLKGDQIRIQGEER--RKTLNEETKQHQARAQY 126
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAE-EQLVQANGELEKASREETFaRTALKNARLDLRRLFDEKQseKDKKNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 127 Q-DKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMR-------------KATIEHEmELRHKNELLRIEAESKAR-- 190
Cdd:pfam12128 683 RlNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvvegaldaqlallKAAIAAR-RSGAKAELKALETWYKRDla 761
|
170 180 190
....*....|....*....|....*....|....*
gi 1712965699 191 ---------ARVERENADIIR--EQIRLKAAEHRQ 214
Cdd:pfam12128 762 slgvdpdviAKLKREIRTLERkiERIAVRRQEVLR 796
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
890-958 |
3.31e-04 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 44.61 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712965699 890 EAPLAEDVAAPVVEVTPPPSAEAplAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAE 958
Cdd:COG5373 34 EAELAEAAEAASAPAEPEPEAAA--AATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAA 100
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
782-974 |
3.40e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 782 APVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPlvqdviapvvevtPPPSEEAAAP---VAEDVIAPVV 858
Cdd:PRK07764 583 QVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAA-------------PAPAGAAAAPaeaSAAPAPGVAA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 859 EVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVA--APVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA 936
Cdd:PRK07764 650 PEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAApaAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGAS 729
|
170 180 190
....*....|....*....|....*....|....*...
gi 1712965699 937 EDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:PRK07764 730 APSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPA 767
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
336-411 |
3.43e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 44.31 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 336 NGLYRNILMYGPPGTGKTLFAKKLAMHSGMDY----AIMtggdvapmgrDGVTAMHKVFDWANTSR---RGLLLFVDE-- 406
Cdd:PRK13342 33 AGRLSSMILWGPPGTGKTTLARIIAGATDAPFealsAVT----------SGVKDLREVIEEARQRRsagRRTILFIDEih 102
|
90
....*....|.
gi 1712965699 407 ------ADAFL 411
Cdd:PRK13342 103 rfnkaqQDALL 113
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
780-941 |
3.52e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 44.47 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 780 VIAPVVEVAPPPSEEAVAAAPvaedviAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDvIAPVVE 859
Cdd:PRK07994 374 SAAPAASAQATAAPTAAVAPP------QAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK-SEPAAA 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 860 VTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP--PSAEAPLAEDVAAPvvEVTPPPSAEAPLAE 937
Cdd:PRK07994 447 SRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVatPKALKKALEHEKTP--ELAAKLAAEAIERD 524
|
....
gi 1712965699 938 DVAA 941
Cdd:PRK07994 525 PWAA 528
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
107-214 |
4.49e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.95 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 107 EERRKTLNEETKQHQARAQYQDKLARQRYEDQLRQ---QQILNEENLRKQEESVQKQEAMRKATIE---HEMELRHKNEL 180
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEERLRKEELRRRaeeERARREEEARRLEEERRREEEERQRKAEeeaEEREQREQEEQ 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 1712965699 181 LRIEA---ESKARARVERENADIIREQIRLKAAEHRQ 214
Cdd:pfam05672 97 ERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERL 133
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
69-218 |
4.74e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.39 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 69 LDLARMQ-EQSTQLEHQSKIKEYEAAVEQLkgdqiriqgEERRKTLNEETKQHQArAQYQDKLARQRYEDQLRQQQILne 147
Cdd:pfam12474 1 HQLQKEQqKDRFEQERQQLKKRYEKELEQL---------ERQQKQQIEKLEQRQT-QELRRLPKRIRAEQKKRLKMFR-- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 148 ENLrKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERENADIIREQIRLkAAEHRQTVLE 218
Cdd:pfam12474 69 ESL-KQEKKELKQEVEKLPKFQRKEAKRQRKEELELEQKHEELEFLQAQSEALERELQQL-QNEKRKELAE 137
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-214 |
4.94e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKS-RHAKEALD-----LARMQEQSTQLEHQSKIKEYEAA-----VEQLKG--DQIRIQGEERRKTLNE 115
Cdd:TIGR02168 290 LYALANEISRLEQQkQILRERLAnlerqLEELEAQLEELESKLDELAEELAeleekLEELKEelESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 116 -ETKQHQARAQYQDklARQRYeDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVE 194
Cdd:TIGR02168 370 lESRLEELEEQLET--LRSKV-AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
170 180
....*....|....*....|
gi 1712965699 195 RENADIIREQIRLKAAEHRQ 214
Cdd:TIGR02168 447 EELEELQEELERLEEALEEL 466
|
|
| RecA-like_PEX6_r2 |
cd19527 |
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ... |
342-457 |
5.15e-04 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410935 [Multi-domain] Cd Length: 160 Bit Score: 41.73 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 342 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRDGVTA-MHKVFDWANTSRRGLLLFvDEADAFLRKRST---- 416
Cdd:cd19527 29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEAnVREVFQKARDAKPCVIFF-DELDSLAPSRGNsgds 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712965699 417 ----EKISEDLRATLNAfLYRTGEQsnkFMLVLASNQPEQFDWAI 457
Cdd:cd19527 108 ggvmDRVVSQLLAELDG-MSSSGQD---VFVIGATNRPDLLDPAL 148
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
738-964 |
5.17e-04 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 43.85 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 738 PPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVVEVTPPPS 817
Cdd:COG0515 255 YQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 818 EEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDV 897
Cdd:COG0515 335 ALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712965699 898 AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPV 964
Cdd:COG0515 415 AAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALAL 481
|
|
| RecA-like_NSF-SEC18_r1-like |
cd19504 |
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ... |
340-457 |
5.19e-04 |
|
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410912 [Multi-domain] Cd Length: 177 Bit Score: 42.09 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLA-MHSGMDYAIMTGGDVAP--MGrDGVTAMHKVFDWANTSRRGL-------LLFVDEADA 409
Cdd:cd19504 36 KGILLYGPPGTGKTLMARQIGkMLNAREPKIVNGPEILNkyVG-ESEANIRKLFADAEEEQRRLgansglhIIIFDEIDA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1712965699 410 FLRKRSTEKISEDLRATL-NAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 457
Cdd:cd19504 115 ICKQRGSMAGSTGVHDTVvNQLLSKIDgvEQLNNILVIGMTNRKDLIDEAL 165
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
56-194 |
6.11e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 56 AKDLDKSRhaKEALDLARMQEQSTQLEHQSKIKEYEaaVEQLKGDQIRIQgEERRKTLNEETKQHQaRAQYQDKLARQRY 135
Cdd:pfam17380 445 AREMERVR--LEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAE-EQRRKILEKELEERK-QAMIEEERKRKLL 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 136 EDQL--RQQQILNEENLRKQEESVQK----------QEAMRKATIEHEM--ELRHKNELLRIEAES-KARARVE 194
Cdd:pfam17380 519 EKEMeeRQKAIYEEERRREAEEERRKqqemeerrriQEQMRKATEERSRleAMEREREMMRQIVESeKARAEYE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-200 |
6.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 40 KWSNFDPTGLERAAQAAKDLDKSRHAKEALDLARM--QEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEET 117
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 118 KQHQARAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVEREN 197
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
...
gi 1712965699 198 ADI 200
Cdd:COG1196 774 REI 776
|
|
| PTZ00361 |
PTZ00361 |
26 proteosome regulatory subunit 4-like protein; Provisional |
340-475 |
6.37e-04 |
|
26 proteosome regulatory subunit 4-like protein; Provisional
Pssm-ID: 185575 [Multi-domain] Cd Length: 438 Bit Score: 43.61 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 340 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGD-VAPMGRDG---VTAMHKVFDWANTSrrglLLFVDEADAFLRKR- 414
Cdd:PTZ00361 218 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSElIQKYLGDGpklVRELFRVAEENAPS----IVFIDEIDAIGTKRy 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 415 -STEKISEDLRATLNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEIVNFalPGPDER 475
Cdd:PTZ00361 294 dATSGGEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEF--PNPDEK 357
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
898-1017 |
6.72e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.70 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 898 AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEdvAAPVVEVTPPPSAEVKc 977
Cdd:PRK07994 364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLA--ARQQLQRAQGATKAKK- 440
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1712965699 978 tlSDGLDSDNTVKAEPASETEHLAQPAASAETEAKMKKED 1017
Cdd:PRK07994 441 --SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEA 478
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
808-958 |
6.79e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 43.44 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 808 PVVEVTPPPSEEAVAAAPL---VQDVIAPVVEVTPPPSEEAAAP-VAEDVIAPVVeVTPPLAVEVEAPLAEDVAAPVVEV 883
Cdd:PRK12727 117 PVSVPRQAPAAAPVRAASIpspAAQALAHAAAVRTAPRQEHALSaVPEQLFADFL-TTAPVPRAPVQAPVVAAPAPVPAI 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 884 TPPPSAEAPLAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVevtpPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAE 958
Cdd:PRK12727 196 AAALAAHAAYAQDDDEQLDD--DGFDLDDALPQILPPAAL----PPIVVAPAAPAALAAVAAAAPAPQNDEELKQ 264
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
887-973 |
7.03e-04 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 40.45 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 887 PSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPvvevtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlaedvAAPVVE 966
Cdd:pfam12526 29 FSPPESAHPDPPPPVGDPRPPVVDTPPPVSAVWVL-----PPPSEPAAPEPDLVPPVTGPAGPPSPLAP-----PAPAQK 98
|
....*..
gi 1712965699 967 VTPPPSA 973
Cdd:pfam12526 99 PPLPPPR 105
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
707-936 |
7.13e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 707 EVTPPPSEEAVAAAAAPlvqdVIAPVVEVTPPPSEEAVAAAAAPLVQDVIAPVVEVTPPPSEEAAAAAPLVQ-DVIAPVV 785
Cdd:PRK12323 371 GAGPATAAAAPVAQPAP----AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQaSARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 786 EVAPPPSEEavaAapvaedviAPVVEVTPPPSEEAVAAAPLVQdviapvvevTPPPSEEAAAPVAEDVIAPVVEVTPP-L 864
Cdd:PRK12323 447 APAPAPAPA---A--------APAAAARPAAAGPRPVAAAAAA---------APARAAPAAAPAPADDDPPPWEELPPeF 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 865 AVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVvevtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA 936
Cdd:PRK12323 507 ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAP----APAAAPAPRAAAATEPVVAPRPPRASASGLP 574
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
633-1028 |
7.35e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 43.60 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 633 QVLEAMPPP--SVEAAAPQAQDVATPIAEVTPPPSVEVEPPLVPDVIAPiveVTPPPSEEAVAAAP--LVQDVITPVVEV 708
Cdd:pfam03154 165 QILQTQPPVlqAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA---TSQPPNQTQSTAAPhtLIQQTPTLHPQR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 709 TPPPSeeavaaaaaPLVQDVIAPvvevtPPPSEEAVAAAAAPLVQDVIAPV---VEVTPPPSEEAAAAAPLVQDVIAPVV 785
Cdd:pfam03154 242 LPSPH---------PPLQPMTQP-----PPPSQVSPQPLPQPSLHGQMPPMphsLQTGPSHMQHPVPPQPFPLTPQSSQS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 786 EVAPPPSEEAVAAAPVAEDVIAPVVEVTP--PPSEEAVAAAPLvqdviaPVVEVTPPPSeeaaapvaedviAPVVEVTPP 863
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSqqPPREQPLPPAPL------SMPHIKPPPT------------TPIPQLPNP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 864 LAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVE--------VTPPPSAEAPl 935
Cdd:pfam03154 370 QSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQppvltqsqSLPPPAASHP- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 936 aeDVAAPVVEVTPPPSAEAPLAEDVAAPVVE-VTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQPAASAETEAKMK 1014
Cdd:pfam03154 449 --PTSGLHQVPSQSPFPQHPFVPGGPPPITPpSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDE 526
|
410
....*....|....
gi 1712965699 1015 KEDKTVSPPKDGTP 1028
Cdd:pfam03154 527 AEEPESPPPPPRSP 540
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
877-1024 |
8.04e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.32 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 877 AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlAEDVAAPVVEvtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPL 956
Cdd:PRK07994 364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVP-PPPASAPQQA--PAVPLPETTSQLLAARQQLQRAQGATKAKK 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 957 AEDVAAPVVEVTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQPAASAETEAKMKKEDKTVSPPK 1024
Cdd:PRK07994 441 SEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEK 508
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
750-895 |
9.96e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.93 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 750 PLVQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAPPPSEEAVAAAPVAEDVIAPVV-----EVTPPPSEEAVAA- 823
Cdd:PRK07994 368 PEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQlqraqGATKAKKSEPAAAs 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712965699 824 -APLVQDVIAPVVEVTPPPSEEAAAPVAEDviAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAE 895
Cdd:PRK07994 448 rARPVNSALERLASVRPAPSALEKAPAKKE--AYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-214 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 71 LARMQEQSTQ----LEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDKLARQRyeDQLRQQQiln 146
Cdd:COG1196 202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLEL--- 276
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 147 eENLRKQEESVQKQEAMRKATIEhEMELRHKNELLRIEAESKARARVERENADIIREQIRLKAAEHRQ 214
Cdd:COG1196 277 -EELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
839-998 |
1.09e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.66 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 839 PPPSEEAAAPVAED--VIAPVVEVTPPLAVEVeaplAEDVAAPVVEVTPPPSAEAPLAEDV----AAPVVEVTPPPSAEA 912
Cdd:PRK13108 298 REPAELAAAAVASAasAVGPVGPGEPNQPDDV----AEAVKAEVAEVTDEVAAESVVQVADrdgeSTPAVEETSEADIER 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 913 PLAEDVAAPVVEVtpPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEVKCTLSDGLDSDNTVKAE 992
Cdd:PRK13108 374 EQPGDLAGQAPAA--HQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQD 451
|
....*.
gi 1712965699 993 PASETE 998
Cdd:PRK13108 452 DFSSRR 457
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
56-194 |
1.13e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 56 AKDLDKSRHAKEALDLARMQEQstQLEHQSKIKEYEAavEQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDKLARQRY 135
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQK--QAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712965699 136 EDQLRQ-----QQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNEL-LRIEAESKARARVE 194
Cdd:PRK09510 150 EAEAKRaaaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAkKKAEAEAKKKAAAE 214
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
855-971 |
1.21e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 42.45 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 855 APVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTP-PPSAEA 933
Cdd:NF040712 200 ATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEaTRDAGE 279
|
90 100 110
....*....|....*....|....*....|....*...
gi 1712965699 934 PLAEDVAAPVVEVTPPPSAEAPLAEDvAAPVVEVTPPP 971
Cdd:NF040712 280 PPAPGAAETPEAAEPPAPAPAAPAAP-AAPEAEEPARP 316
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
44-210 |
1.25e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 44 FDPTGLERAAQAAKDLDKSRHAKEALdlarMQEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQAR 123
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERE----TEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 124 AQyQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRK-ATIEHEMELRHKNELLRIEAESKARARVERENADIIR 202
Cdd:COG2268 262 AE-AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREeAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEA 340
|
....*...
gi 1712965699 203 EQIRLKAA 210
Cdd:COG2268 341 EGKRALAE 348
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
68-213 |
1.27e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.33 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 68 ALDLARMQEQSTQLEHQskikeYEAAV---EQLKGDQIRIQGEERRKTLNEETKQHQARAQYQDKLARQRYE-----DQL 139
Cdd:pfam15558 11 ALMLARHKEEQRMRELQ-----QQAALaweELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREerrraDRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 140 RQQQILNE----------ENLRK----------------QEESVQKQEAMRKATIEHEMELRHKNELL----RIEAESKA 189
Cdd:pfam15558 86 EKQVIEKEsrwreqaedqENQRQeklerarqeaeqrkqcQEQRLKEKEEELQALREQNSLQLQERLEEachkRQLKEREE 165
|
170 180
....*....|....*....|....*
gi 1712965699 190 RARVEREN-ADIIREQIRLKAAEHR 213
Cdd:pfam15558 166 QKKVQENNlSELLNHQARKVLVDCQ 190
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
566-714 |
1.33e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 42.72 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 566 LHAEEEAQAKTLTPPKPEGTSGGKMGFVLPLSEAPQAKDVVAPVVEVTPPPPPSAEVAAPQIQDVITQVLEAMPPPSVEA 645
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITES 934
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 646 AAPQAQDVA---TPIAEVTPPPSVEVEPPLVPDVIA--PIVEVTPPPSEEAVAAAPLVQDVITPVVEVTPPPSE 714
Cdd:PRK10811 935 DVAVAQEVAehaEPVVEPQDETADIEEAAETAEVVVaePEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPE 1008
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
597-974 |
1.37e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 597 SEAPQAKDVVAPVVEVTPPPPPSAEVAAPQIQDVITQVLEAMPPPSVEAAAPQAQDVATPIAEVTPPPSVEVEPPL---- 672
Cdd:PHA03247 2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrpr 2684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 673 ---VPDVIAPIVEVT-PPPSEEAVAAAPlvqdviTPVVEVTPPPSEEAVAAAAAPlvqdvIAPVVEVTPPPSEeavaaaa 748
Cdd:PHA03247 2685 rraARPTVGSLTSLAdPPPPPPTPEPAP------HALVSATPLPPGPAAARQASP-----ALPAAPAPPAVPA------- 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 749 aplvqdviAPVVEVTPPPSEEAAAAAPLVQDViAPVVEVAPPP--SEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPL 826
Cdd:PHA03247 2747 --------GPATPGGPARPARPPTTAGPPAPA-PPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 827 VQDVIAPVVEVTPPPSEEAAAPvaedviapvveVTPPLAVEVEAPLAEDVA--APVVEVTPPPSAEAPLAEDVAAPVVEV 904
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAP-----------PPPPGPPPPSLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRL 2886
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 905 TPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-215 |
1.40e-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: 42.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 75 QEQSTQLEHQSKIKEYEAAVEQLKGD--QIRIQGEERRKTLNE-ETKQHQARAQYQDKLARQRYEDQLRQQQILNEENLR 151
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKiaELEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712965699 152 KQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESK-----ARARVERENADIIREQIRLKAAEHRQT 215
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeleAQIEQLKEELKALREALDELRAELTLL 815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
50-210 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKGDQI-RIQGEERRKTLNEETKQhQARAQYQD 128
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEERE-RRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 129 KLA---------RQRYEDQLRQ-QQILneENLRKQEESVQKQEAMRKATIEhemelRHKNELLRIEAEskaRARVERENA 198
Cdd:COG4913 367 LLAalglplpasAEEFAALRAEaAALL--EALEEELEALEEALAEAEAALR-----DLRRELRELEAE---IASLERRKS 436
|
170
....*....|..
gi 1712965699 199 DIIREQIRLKAA 210
Cdd:COG4913 437 NIPARLLALRDA 448
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
107-313 |
1.76e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 42.42 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 107 EERRKTLNEETKQHQARAQY-----QDKLARQRYEDQLRQQQILNEENLRKQEesVQKQEAMRKATIEHEMELRHKNELL 181
Cdd:PTZ00266 407 DDRKYPQDGATHCHAVNGHYggrvdKDHAERARIEKENAHRKALEMKILEKKR--IERLEREERERLERERMERIERERL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 182 ---RIEAESKARARVERENADIIR-------EQIRLKAAEHRQTVLESIK---TAGAVFGEGfrafvsdwdkvtATVAGL 248
Cdd:PTZ00266 485 ereRLERERLERDRLERDRLDRLErervdrlERDRLEKARRNSYFLKGMEnglSAGGGPGDG------------PGVGAG 552
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 249 TLLAVGVYSARNATGV-AGRYIEARLGKPSLVRETSRFTVGEAIKHPVKtvKRLKSKPQDALEGVV 313
Cdd:PTZ00266 553 VGAGVGTSDGRNHSGVrSGIHCSIQSSARGGVHDSVRSGVHDSVRGGVH--DSMRSGVHDSLRGGV 616
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
816-962 |
2.09e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 816 PSEEAVAAApLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAE 895
Cdd:PRK07764 365 PSASDDERG-LLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712965699 896 DVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAA 962
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
79-177 |
2.14e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.50 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 79 TQLEHQSKIKEYEAAVEQLKGDQIRIQgeerRKTLNEETKQHQARAQYQDKlarqRYEDQLRQ--------QQILNEENL 150
Cdd:pfam02841 193 LQTDQALTAKEKAIEAERAKAEAAEAE----QELLREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQE 264
|
90 100
....*....|....*....|....*..
gi 1712965699 151 RKQEESVQKQEAMRKATIEHEMELRHK 177
Cdd:pfam02841 265 RMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| HflB |
COG0465 |
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones]; |
342-360 |
2.24e-03 |
|
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440233 [Multi-domain] Cd Length: 583 Bit Score: 41.95 E-value: 2.24e-03
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
620-1029 |
2.29e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 42.02 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 620 AEVAAPQIQDVITQVLEAMPPPSVEAAAPQAQ---------DVATPIAEVTPPPSVEVEPPLVPDVIAPIVEVTPPPSEE 690
Cdd:PRK14949 372 AEISLPEGQTPSALAAAVQAPHANEPQFVNAApaekktaltEQTTAQQQVQAANAEAVAEADASAEPADTVEQALDDESE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 691 AVAAAPLVQDVI-------------------TPVVEVTPPPSEEavaAAAAPLVQDVIAPVVEVTPppseeavaaaaaPL 751
Cdd:PRK14949 452 LLAALNAEQAVIlsqaqsqgfeasssldadnSAVPEQIDSTAEQ---SVVNPSVTDTQVDDTSASN------------NS 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 752 VQDVIAPVVEVTPPPSEEAAAAAPLVQDVIAPVVEVAppPSEEAVAAAPVAEDVIAPVVEVTPPPseeavAAAPLVQDVI 831
Cdd:PRK14949 517 AADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAYQ--DDYVAFSSESYNALSDDEQHSANVQS-----AQSAAEAQPS 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 832 APVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEA--PLAEDVAAPVVEVTP--PPSAEAPlaedVAAPVVEVTPP 907
Cdd:PRK14949 590 SQSLSPISAVTTAAASLADDDILDAVLAARDSLLSDLDAlsPKEGDGKKSSADRKPktPPSRAPP----ASLSKPASSPD 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 908 PSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTP---PPSAEAPlaEDVAAPVVEVTPPPSAEVKCTLSDGLD 984
Cdd:PRK14949 666 ASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPydrPPWEEAP--EVASANDGPNNAAEGNLSESVEDASNS 743
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1712965699 985 SDNTVkaEPASETEHLAQPAASAET-EAKMKKEDKTVSPPKDGTPV 1029
Cdd:PRK14949 744 ELQAV--EQQATHQPQVQAEAQSPAsTTALTQTSSEVQDTELNLVL 787
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
808-968 |
2.31e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 41.90 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 808 PVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIApVVEVTPPLAVEVEAPLAEDV----------- 876
Cdd:PRK12727 63 PATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIA-AMALRQPVSVPRQAPAAAPVraasipspaaq 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 877 -AAPVVEVTPPPSAEAPLA---EDV-AAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVV------- 944
Cdd:PRK12727 142 aLAHAAAVRTAPRQEHALSavpEQLfADFLTTAPVPRAPVQAPVVAAPAPVPAIAAALAAHAAYAQDDDEQLDddgfdld 221
|
170 180
....*....|....*....|....
gi 1712965699 945 EVTPPPSAEAPLAEDVAAPVVEVT 968
Cdd:PRK12727 222 DALPQILPPAALPPIVVAPAAPAA 245
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
69-185 |
2.51e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 69 LDLARMQEQSTQLEHQSKIKEYEAAVEQLkgDQIRIQGEERRKTLNEETKQHQARAQYQDklaRQRYEDQLRQ---QQIL 145
Cdd:COG2882 11 LDLAEKEEDEAARELGQAQQALEQAEEQL--EQLEQYREEYEQRLQQKLQQGLSAAQLRN---YQQFIARLDEaieQQQQ 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712965699 146 NEENLRKQEESVQK--QEAMRK-ATIEHEMElRHKNELLRIEA 185
Cdd:COG2882 86 QVAQAEQQVEQARQawLEARQErKALEKLKE-RRREEERQEEN 127
|
|
| SPS1 |
COG0515 |
Serine/threonine protein kinase [Signal transduction mechanisms]; |
790-1011 |
2.78e-03 |
|
Serine/threonine protein kinase [Signal transduction mechanisms];
Pssm-ID: 440281 [Multi-domain] Cd Length: 482 Bit Score: 41.54 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 790 PPSEEAVAAAPVAEDVIAPVVEVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVE 869
Cdd:COG0515 255 YQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 870 APLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP 949
Cdd:COG0515 335 ALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1712965699 950 PSAEAPLAEDVAAPVVEVTPPPSAEVKCTLSDGLDSDNTVKAEPASETEHLAQPAASAETEA 1011
Cdd:COG0515 415 AAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAA 476
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
814-955 |
2.91e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 814 PPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEdvAAPVVEVTPPPSAEAPL 893
Cdd:PRK13108 298 REPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGE--STPAVEETSEADIEREQ 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 894 AEDVAAPVVEVtpPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPP--PSAEAP 955
Cdd:PRK13108 376 PGDLAGQAPAA--HQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPdeLAVAGP 437
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
73-188 |
2.91e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 39.39 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 73 RMQEQSTQLEHQSKIKEyeaaveqlkgdqiriQGEERRKTLNEETKQHQARAQYQD-KLARQ------RYEDQLRQQQIL 145
Cdd:pfam15236 47 RERKRQKALEHQNAIKK---------------QLEEKERQKKLEEERRRQEEQEEEeRLRREreeeqkQFEEERRKQKEK 111
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712965699 146 NEENLRKQEESVQkqeAMRKAtieHEMELRHKNELLRIEAESK 188
Cdd:pfam15236 112 EEAMTRKTQALLQ---AMQKA---QELAQRLKQEQRIRELAEK 148
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
75-221 |
2.95e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 75 QEQSTQLEHQSKIKEYEAAVEQLKGDQIRIQGEERRKTLNEETKQHQARAQyqdklARQRYEDQLRQQQI---------- 144
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE-----ERKRELERIRQEEIameisrmrel 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 145 --LNEENLRKQEESVQKQEAMRKATIEHE------MELRHKNELLRIEAESKARARVERENADIIREQIRLKAAE-HRQT 215
Cdd:pfam17380 381 erLQMERQQKNERVRQELEAARKVKILEEerqrkiQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEqERQQ 460
|
....*.
gi 1712965699 216 VLESIK 221
Cdd:pfam17380 461 QVERLR 466
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
859-976 |
3.55e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 40.94 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 859 EVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVvevtpPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAED 938
Cdd:PRK12373 199 EEAGKARYNASKALAEDIGDTVKRIDGTEVPLLAPWQGDAAPV-----PPSEAARPKSADAETNAALKTPATAPKAAAKN 273
|
90 100 110
....*....|....*....|....*....|....*...
gi 1712965699 939 VAAPVVEVTPPPSAEAPLAEDVAAPVVEVTpPPSAEVK 976
Cdd:PRK12373 274 AKAPEAQPVSGTAAAEPAPKEAAKAAAAAA-KPALEDK 310
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-222 |
3.61e-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: 40.90 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 50 ERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSKIKEYEAAVEQLKG------DQIRIQGEERRKTLNEETKQHQAR 123
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriraleQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 124 AQYQDKLARQRYEDQLRQQQ-----ILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLR--IEAESKARARVERE 196
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalRAELEAERAELEAL 179
|
170 180
....*....|....*....|....*..
gi 1712965699 197 NADIIREQIRLKAAEH-RQTVLESIKT 222
Cdd:COG4942 180 LAELEEERAALEALKAeRQKLLARLEK 206
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
814-1025 |
3.61e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 814 PPPSEEAVAAAPLVQDVIAPVVEV-TPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAP 892
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACDRFEPpTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 893 LAedvaapvvevtPPPSAEAPLAEDvAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLA---EDVAAPVveVTP 969
Cdd:PHA03307 124 AS-----------PPPSPAPDLSEM-LRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLsspEETARAP--SSP 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712965699 970 PPSAEVKCTLSDGLDSDNTVKAEPASETEHLA-QPAASAETEAKMKKEDKTVSPPKD 1025
Cdd:PHA03307 190 PAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGASSSDSSSSESSG 246
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
833-955 |
3.62e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.91 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 833 PVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPL-AVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTP-PPSA 910
Cdd:NF040712 198 PLATVPRLAREPADARPEEVEPAPAAEGAPATdSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEaTRDA 277
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1712965699 911 EAPLAEDVAAPVVEVTPPPSAEAPLAEDvAAPVVEVTPPPSAEAP 955
Cdd:NF040712 278 GEPPAPGAAETPEAAEPPAPAPAAPAAP-AAPEAEEPARPEPPPA 321
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
871-952 |
3.64e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 38.13 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 871 PLAEDVAAPVVEVTPPPSAEAPLAEDVAAPvvevtPPPSAEAPLAEDVAAPVVEVTPPPSAEAPlaedvAAPVVEVTPPP 950
Cdd:pfam12526 34 SAHPDPPPPVGDPRPPVVDTPPPVSAVWVL-----PPPSEPAAPEPDLVPPVTGPAGPPSPLAP-----PAPAQKPPLPP 103
|
..
gi 1712965699 951 SA 952
Cdd:pfam12526 104 PR 105
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
341-359 |
3.85e-03 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 39.83 E-value: 3.85e-03
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
121-360 |
3.92e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 40.91 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 121 QARAQYQDKLARQRYEDQLRQQQILNEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAESKARARVERE---- 196
Cdd:COG1401 2 LRPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVvlll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 197 -----NADIIREQIRLKAAEHRQTVLESIKTAGAVFGEGFRAFVSDWDKVTATVAGLTLLAVGVYSARNATGVAGRYIEA 271
Cdd:COG1401 82 dlekvELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 272 RLG----KPSLVRETSRFTVGEAIKHPVKTVKRLKSKPQDALEGVVlsptlEERVRDVAIATRNTRqnnglyrNILMYGP 347
Cdd:COG1401 162 LEEllaaPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKF-----EETLEAFLAALKTKK-------NVILAGP 229
|
250
....*....|...
gi 1712965699 348 PGTGKTLFAKKLA 360
Cdd:COG1401 230 PGTGKTYLARRLA 242
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
846-975 |
4.06e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 846 AAPVAEDVIAPVVE-----VTPPLAVEVEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEvtpPPSAEAPLAEdvAA 920
Cdd:PRK07764 366 SASDDERGLLARLErlerrLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAA---PQPAPAPAPA--PA 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 921 PVVEVTPPPSAEAPLAEDVAAPVVEVTPPP-SAEAPLAEDVAAPVVEVTPPPSAEV 975
Cdd:PRK07764 441 PPSPAGNAPAGGAPSPPPAAAPSAQPAPAPaAAPEPTAAPAPAPPAAPAPAAAPAA 496
|
|
| RecA-like_PEX1_r2 |
cd19526 |
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ... |
338-414 |
4.27e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410934 [Multi-domain] Cd Length: 158 Bit Score: 38.95 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712965699 338 LYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP--MGRDGvTAMHKVFDWANtSRRGLLLFVDEADAFLRKR 414
Cdd:cd19526 26 LRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyIGASE-QNVRDLFSRAQ-SAKPCILFFDEFDSIAPKR 102
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
809-963 |
4.73e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 40.56 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 809 VVEVTPPPSEEAVAAAPLVQdvIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTpplAVEVE-APLAEDVAAPVvevtpPP 887
Cdd:PRK12373 174 GPVVKPGPQIGRYASEPAGG--LTSLTEEAGKARYNASKALAEDIGDTVKRID---GTEVPlLAPWQGDAAPV-----PP 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712965699 888 SAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAP 963
Cdd:PRK12373 244 SEAARPKSADAETNAALKTPATAPKAAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAAAAAKPALEDKPRPLGIARP 319
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
866-976 |
4.83e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 40.72 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 866 VEVEAPLAEDVAA-------PVVEVTPPPSAEAPLAEDVAAPVVEVTPPPS---------AEAPLAEDVAAPVVEVTPPP 929
Cdd:PRK06995 38 VEIVALADSDLAAlappaaaAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVehakrltaqREQLVARAAAPAAPEAQAPA 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1712965699 930 SAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEVK 976
Cdd:PRK06995 118 APAERAAAENAARRLARAAAAAPRPRVPADAAAAVADAVKARIERIV 164
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
911-974 |
5.06e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 40.75 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712965699 911 EAPLAEDVAAPVVEVTPPPSAEAplAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAE 974
Cdd:COG5373 34 EAELAEAAEAASAPAEPEPEAAA--AATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEA 95
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
84-221 |
5.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 84 QSKIKEYEAAVEQLKgDQIRIQGEERRKTLNEETKQ--HQARAQYQDKLARQRYEDQLRQQQILN-EENLRKQEESVQKQ 160
Cdd:PRK12704 30 EAKIKEAEEEAKRIL-EEAKKEAEAIKKEALLEAKEeiHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712965699 161 eamrkatiEHEMELRHKNELLRIEAESKARARVERenadIIREQIR-------LKAAEHRQTVLESIK 221
Cdd:PRK12704 109 --------EEELEKKEKELEQKQQELEKKEEELEE----LIEEQLQelerisgLTAEEAKEILLEKVE 164
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
907-1028 |
5.27e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.85 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 907 PPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAeaplaedvAAPVVEVTPPPSAEVKCTLSDGLDSd 986
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAA--------SAPAAPPAAAPPAPVAAPAAAAPAA- 436
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1712965699 987 ntvkAEPASETEHLAQPAASAETEAKMKKEDKTVSPPKDGTP 1028
Cdd:PRK14951 437 ----APAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVAS 474
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
342-362 |
5.42e-03 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 37.58 E-value: 5.42e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
69-220 |
5.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 69 LDLARMQEQSTQLEHQ-----SKIKEYEAAVEQLKGDQIRIQGE-----ERRKTLNEETKQHQAR-AQYQDKLARQRYED 137
Cdd:COG1579 10 LDLQELDSELDRLEHRlkelpAELAELEDELAALEARLEAAKTEledleKEIKRLELEIEEVEARiKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 138 QL-----------RQQQILNEENLRKQEESVQKQEAMRKAtiehemelrhKNELLRIEAESKA-RARVERENADIIREQI 205
Cdd:COG1579 90 EYealqkeieslkRRISDLEDEILELMERIEELEEELAEL----------EAELAELEAELEEkKAELDEELAELEAELE 159
|
170
....*....|....*
gi 1712965699 206 RLKAAehRQTVLESI 220
Cdd:COG1579 160 ELEAE--REELAAKI 172
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
807-924 |
7.81e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.18 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPP-PSEEAVAAAPLVQDVIAPVvevTPPPSEEAA-APVAEdviaPVVEVTPPlavevEAPLAEDVAAPVVEVT 884
Cdd:PRK14950 358 ALLVPVPAPqPAKPTAAAPSPVRPTPAPS---TRPKAAAAAnIPPKE----PVRETATP-----PPVPPRPVAPPVPHTP 425
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1712965699 885 PPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVE 924
Cdd:PRK14950 426 ESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
341-360 |
7.98e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 40.03 E-value: 7.98e-03
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
811-963 |
8.11e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 40.19 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 811 EVTPPPSEEAVAAAPLVQDVIAPVVEVTPPPSEEAAAPVAEDVIAP---------VVE--VTPPLAVEVEAPLAE----- 874
Cdd:PRK11855 80 AAAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPdigeiteveVIEwlVKVGDTVEEDQSLITvetdk 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 875 ---DVAAP----VVEVTPPPSAEAPlaedVAAPVVEVTpppsAEAPLAEDVAAPVVEVTPPPSAEAPlaedVAAPVVEVT 947
Cdd:PRK11855 160 atmEIPSPvagvVKEIKVKVGDKVS----VGSLLVVIE----VAAAAPAAAAAPAAAAPAAAAAAAP----APAPAAAAA 227
|
170
....*....|....*.
gi 1712965699 948 PPPSAEAPLAEDVAAP 963
Cdd:PRK11855 228 PAAAAPAAAAAPGKAP 243
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
883-966 |
8.66e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.26 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 883 VTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDV-- 960
Cdd:PRK12270 42 AAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPlr 121
|
....*...
gi 1712965699 961 --AAPVVE 966
Cdd:PRK12270 122 gaAAAVAK 129
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
826-892 |
8.78e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 39.98 E-value: 8.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712965699 826 LVQDVIAPVVEVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAP--VVEVTPPPSAEAP 892
Cdd:COG5373 33 LEAELAEAAEAASAPAEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPaaAAPPAEAEPAAAP 101
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
341-360 |
8.97e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 39.76 E-value: 8.97e-03
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-213 |
9.17e-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: 40.04 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 49 LERAAQAAKDLDKSRHAKEALDLARMQEQSTQLEHQSK-IKEYEAAVEQLKgDQIRIQGEERRKTLNEETKQHQARAQYQ 127
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLE-ERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 128 DKLARQryedqlrqqqilnEENLRKQEESVQKQEAMRKATIEHEMELRHKNELLRIEAeSKARARVERENADIIREQIRL 207
Cdd:TIGR02168 775 EELAEA-------------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAATERRL 840
|
....*.
gi 1712965699 208 KAAEHR 213
Cdd:TIGR02168 841 EDLEEQ 846
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
341-359 |
9.18e-03 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 39.64 E-value: 9.18e-03
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
807-920 |
9.42e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.97 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712965699 807 APVVEVTPPPSEEAVAAAPLVQDVIAPVV---EVTPPPSEEAAAPVAEDVIAPVVEVTPPLAVEVEAPLAEDVAAPvvev 883
Cdd:PRK07764 399 PSAAAAAPAAAPAPAAAAPAAAAAPAPAAapqPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP---- 474
|
90 100 110
....*....|....*....|....*....|....*..
gi 1712965699 884 tPPPSAEAPLAEDVAAPVVEVTPPPSAEAPLAEDVAA 920
Cdd:PRK07764 475 -EPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| PspF |
COG1221 |
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ... |
335-369 |
9.62e-03 |
|
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];
Pssm-ID: 440834 [Multi-domain] Cd Length: 835 Bit Score: 40.09 E-value: 9.62e-03
10 20 30
....*....|....*....|....*....|....*
gi 1712965699 335 NNGLyrNILMYGPPGTGKTLFAKklAMHSgmdYAI 369
Cdd:COG1221 128 PKGL--HTLILGPTGVGKSFFAE--LMYE---YAI 155
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
335-359 |
9.88e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 39.45 E-value: 9.88e-03
10 20
....*....|....*....|....*
gi 1712965699 335 NNGLYRNILMYGPPGTGKTLFAKKL 359
Cdd:COG1474 47 RGERPSNVLIYGPTGTGKTAVAKYV 71
|
|
| |
