|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
910-1126 |
5.16e-15 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 80.33 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 910 RRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEEDRfsRRGADDDRPSW 989
Cdd:PRK12678 79 RAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKA--GEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 990 RNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRG-SWRTADEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRG 1068
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAEAERGERGRREeRGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503509 1069 PRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRgmdDDRGPRRGLDDDRGPWRNADDD 1126
Cdd:PRK12678 237 DARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR---DRRGRRGGDGGNEREPELREDD 291
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
900-1146 |
9.49e-15 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 79.18 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 900 RKGP--EADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEEDRF 977
Cdd:PRK12678 47 RKGEliAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 978 SRRGADDDRPSWRNTDDDRPPRriADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRGGADDER 1057
Cdd:PRK12678 127 ARERRERGEAARRGAARKAGEG--GEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1058 SSWRNADDDRGPRRGLDDDRGPR-RGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGpwRNADDDRIPRRGAEDD 1136
Cdd:PRK12678 205 RRDRREQGDRREERGRRDGGDRRgRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRF--RDRDRRGRRGGDGGNE 282
|
250
....*....|
gi 4503509 1137 RGPWRNMDDD 1146
Cdd:PRK12678 283 REPELREDDV 292
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
916-1163 |
1.52e-13 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 75.33 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 916 KEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRrGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDD 995
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAA-AKAEAAPAARAAAAAAAEAASAPEAAQARERRERG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 996 RPPRRIADEDRGnwrhADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRGpRRGLDD 1075
Cdd:PRK12678 135 EAARRGAARKAG----EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDR-DRRDRR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1076 DRGPRRgmddDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGpwRNADDDRIPRRGAEDDRGPWRNmDDDRLSRRADDD 1155
Cdd:PRK12678 210 EQGDRR----EERGRRDGGDRRGRRRRRDRRDARGDDNREDRG--DRDGDDGEGRGGRRGRRFRDRD-RRGRRGGDGGNE 282
|
....*...
gi 4503509 1156 RFPRRGDD 1163
Cdd:PRK12678 283 REPELRED 290
|
|
| PINT |
smart00088 |
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ... |
426-498 |
3.95e-13 |
|
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.
Pssm-ID: 214509 [Multi-domain] Cd Length: 88 Bit Score: 66.11 E-value: 3.95e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503509 426 QYVPQLQNNTILRLLQQVSQIYQSIEFSRLTSLVPFvDAFQLERAIVDAARHCDLQVRIDHTSRTLSFGSDLN 498
Cdd:smart00088 1 QLVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
968-1168 |
8.51e-12 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 69.93 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 968 PRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMD--DD 1045
Cdd:PRK12678 77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPatEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1046 RGPRRGGADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPWRNADD 1125
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4503509 1126 DRIPRRGAEDDRGPWRNMDDDRLSRRADDDRF-PRRGDDSRPGP 1168
Cdd:PRK12678 237 DARGDDNREDRGDRDGDDGEGRGGRRGRRFRDrDRRGRRGGDGG 280
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
972-1233 |
1.42e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 69.16 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 972 PEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRG 1051
Cdd:PRK12678 68 ATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1052 GADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPWRNADDDRIPRR 1131
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1132 GAEDDRGpwrnmDDDRLSRRADDDRFPRRGDDSRpgpwrplvkpggwrekekareeswgppresrpsEEREWDREKERDR 1211
Cdd:PRK12678 228 GRRRRRD-----RRDARGDDNREDRGDRDGDDGE---------------------------------GRGGRRGRRFRDR 269
|
250 260
....*....|....*....|...
gi 4503509 1212 DNQDREENDKDPERE-RDRERDV 1233
Cdd:PRK12678 270 DRRGRRGGDGGNEREpELREDDV 292
|
|
| PCI |
pfam01399 |
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ... |
405-494 |
3.76e-11 |
|
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15).
Pssm-ID: 460195 Cd Length: 105 Bit Score: 61.08 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 405 ERVTKVLNWVREQPEKEPELQQYVPQLQNNTILRLLQQVSQIYQSIEFSRLTSLVPfVDAFQLERAIVDAARHCDLQVRI 484
Cdd:pfam01399 16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLG-LSVDEVEKILAKLIRDGRIRAKI 94
|
90
....*....|
gi 4503509 485 DHTSRTLSFG 494
Cdd:pfam01399 95 DQVNGIVVFS 104
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
894-1096 |
4.43e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 67.62 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 894 DSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDeeRPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPE 973
Cdd:PRK12678 101 KAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG--AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 974 EDRFSRRGADDDRpswRNTDDDRPPRRIADEDRGNWRHADDDRpPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRGGA 1053
Cdd:PRK12678 179 EDRQAEAERGERG---RREERGRDGDDRDRRDRREQGDRREER-GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDD 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503509 1054 DDERsswrnadDDRGPRRGLDDDRGPRRGMD--DDRGPRRGMDDD 1096
Cdd:PRK12678 255 GEGR-------GGRRGRRFRDRDRRGRRGGDggNEREPELREDDV 292
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
891-1066 |
2.06e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 65.31 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 891 GDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGR----DEDRSHRRDEERPRRLGDDEDREPslRPDDDRVPRRGmddDR 966
Cdd:PRK12678 119 ASAPEAAQARERRERGEAARRGAARKAGEGGEQPateaRADAAERTEEEERDERRRRGDRED--RQAEAERGERG---RR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 967 GPRRGPEEDRFSRRGADDDRpswRNTDDDRPPRriaDEDRGNWRHADDDRPPRRGLDEDRGSWRTADED----RGPRRGM 1042
Cdd:PRK12678 194 EERGRDGDDRDRRDRREQGD---RREERGRRDG---GDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEgrggRRGRRFR 267
|
170 180
....*....|....*....|....
gi 4503509 1043 DDDRGPRRGGADDERSSWRNADDD 1066
Cdd:PRK12678 268 DRDRRGRRGGDGGNEREPELREDD 291
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-784 |
3.14e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKpAHILQEKEEQHQLAVTAYLKNSR-----KEHQRILARRQTIEERKERLEslniQREK 591
Cdd:COG1196 252 EAELEELEAELAELEAELEELR-LELEELELELEEAQAEEYELLAElarleQDIARLEERRRELEERLEELE----EELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimA 671
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-------A 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 672 KQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIpLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMS 751
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELE--ELEEALAEL-EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270
....*....|....*....|....*....|...
gi 4503509 752 RMLEDRDLFVMRlKAARQSVYEEKLKQFEERLA 784
Cdd:COG1196 477 AALAELLEELAE-AAARLLLLLEAEADYEGFLE 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
532-683 |
1.84e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.64 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 532 KALEVIKPAHILQEKEEQHQLavtaylknsRKEHQR-ILARRQTIEERKERLE--SLNIQREKEELEQREAELQKVRKAE 608
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHKL---------RNEFEKeLRERRNELQKLEKRLLqkEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503509 609 EERLRQ-EAKEREKERILQEHeqikkktvRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:PRK12704 120 EQKQQElEKKEEELEELIEEQ--------LQELERI--SGLTAEEAKEILLEKVEeEARHE--AAVLIKEIEEEAKE 184
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
564-858 |
2.87e-08 |
|
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: 58.21 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 564 EHQRILARRQTiEERKERLESLNIQREKEELEQreaELQKVRKAEE-ERLRQEAKER------EKERILQEH----EQIK 632
Cdd:pfam17380 279 QHQKAVSERQQ-QEKFEKMEQERLRQEKEEKAR---EVERRRKLEEaEKARQAEMDRqaaiyaEQERMAMERerelERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 633 KKTVRERLEQIKKTELGAKAFKDIDIEDL--------EELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLqmerqqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 705 EEIPLIksayEEQRIKDMDLWEQQEEERITTMQLEREKALEHKnRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLA 784
Cdd:pfam17380 435 REVRRL----EEERAREMERVRLEEQERQQQVERLRQQEEERK-RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 785 EERHNRLEERKRQRKEERRITYYREKEEEEQRRAEEQMLkereererAERAKREEELREYQERVKKLEEVERKK 858
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEERSRLEAMERER 575
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
517-778 |
2.99e-08 |
|
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: 58.21 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSsvlakaLEVIKPAHILQEKEEQhqlavtaylKNSRKEHQRILARRQTI--EERKERLESLNIQREKEEL 594
Cdd:pfam17380 363 ERIRQEEIAME------ISRMRELERLQMERQQ---------KNERVRQELEAARKVKIleEERQRKIQQQKVEMEQIRA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 595 EQREAELQKVRKAEEERLRQEAKEREKEriLQEHEQIKKKTVRERLEQIKKTELgakafkdidieDLEELDPDFIMAKQV 674
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLEL-----------EKEKRDRKRAEEQRR 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 675 EQLEKEKKELQERLKNQEKKIDYFEraKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML 754
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLE--KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAME 572
|
250 260
....*....|....*....|....
gi 4503509 755 EDRDLFvmrlkaaRQSVYEEKLKQ 778
Cdd:pfam17380 573 REREMM-------RQIVESEKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
575-927 |
1.08e-07 |
|
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: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 575 IEERKERLESLNIQREK--------EELEQREAELQ----KVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQ 642
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 643 ikktelgakAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIplikSAYEEQRIKDM 722
Cdd:COG1196 275 ---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAEL----EEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 723 DLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEER 802
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 803 RityyreKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGDSS 882
Cdd:COG1196 420 E------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 4503509 883 LSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDED 927
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
543-789 |
1.29e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.52 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam02463 215 LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 623 RILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimakQVEQLEKEKKELQERLKNQEKKIDYFERAK 702
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE---------EIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 703 RLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEER 782
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
....*..
gi 4503509 783 LAEERHN 789
Cdd:pfam02463 446 LTEEKEE 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
517-787 |
1.77e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKpahILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERleslnIQREKEELEQ 596
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQA---LLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REAELQKVRKAEEERLRQEAKERE---KERILQEHEQIK--KKTVRERLEQIKKTELG-AKAFKDID--IEDLEELDpdf 668
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIAslERSIAEKERELEDAEERlAKLEAEIDklLAEIEELE--- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 669 imaKQVEQLEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKSAYEEQRIKDMDLWEQQEE--ERITTMQLEREKALEH 746
Cdd:TIGR02169 343 ---REIEEERKRRDKLTEEYAELKE-----ELEDLRAELEEVDKEFAETRDELKDYREKLEKlkREINELKRELDRLQEE 414
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 4503509 747 KNRMSRMLEDrdlfvMRLKAARQsvyEEKLKQFEERLAEER 787
Cdd:TIGR02169 415 LQRLSEELAD-----LNAAIAGI---EAKINELEEEKEDKA 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-934 |
4.08e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 530 LAKALEVIKPAHILQEKEEQHQLAvtAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE 609
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 610 -----ERLRQEAKE-REKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPdfimAKQVEQLEK--EK 681
Cdd:PTZ00121 1488 akkkaEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE----LKKAEELKKaeEK 1563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 682 KELQERLKNQEKKIDYFERA---KRLEE--IPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLED 756
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAeeaKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 757 RDlfVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEERrityyrekeeeeqRRAEEQMLKEREERERAERAK 836
Cdd:PTZ00121 1644 EE--KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-------------KKAAEALKKEAEEAKKAEELK 1708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 837 reeelREYQERVKKLEEVerKKRQRELEIEERERRREEERRLGDSSLSRKDSrwGDRDSEGTWRKGPEADSEWRRgpPEK 916
Cdd:PTZ00121 1709 -----KKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIR--KEK 1777
|
410
....*....|....*...
gi 4503509 917 EWRRGEGRDEDRSHRRDE 934
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRME 1795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-857 |
4.44e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQrilARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAED---AKRVEIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REA--------ELQKVRKAEEERLRQEAKEREKERILQE---HEQIKKKTVRERLEQIKKTELGAKAFKDI----DIEDL 661
Cdd:PTZ00121 1178 AEAarkaeevrKAEELRKAEDARKAEAARKAEEERKAEEarkAEDAKKAEAVKKAEEAKKDAEEAKKAEEErnneEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 662 EELDPDFIMAKQVEQLEKEKKELQERLKNQE-KKIDYFERAKRLEEIPLIKSAYEEQRIKDmDLWEQQEEERITTMQLER 740
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEkKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 741 eKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEERRITYYREKEEEEQRRAEE 820
Cdd:PTZ00121 1337 -KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
330 340 350
....*....|....*....|....*....|....*..
gi 4503509 821 QMLKEREERERAERAKREEELREYQERVKKLEEVERK 857
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
891-1025 |
5.15e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 54.14 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 891 GDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRgpRR 970
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRR--DR 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503509 971 GPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHAD--DDRPPRRGLDED 1025
Cdd:PRK12678 236 RDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDggNEREPELREDDV 292
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
880-1126 |
5.88e-07 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 54.14 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 880 DSSLSRKDSRWGDRDSEGTWRKGPEADSEwrrGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPR 959
Cdd:NF033609 621 DSDSASDSDSASDSDSASDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 960 RGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPR 1039
Cdd:NF033609 698 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1040 RGMDDDRGPRRGGADDERS-SWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRG 1118
Cdd:NF033609 778 SDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSE 857
|
....*...
gi 4503509 1119 PWRNADDD 1126
Cdd:NF033609 858 SDSNSDSE 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-768 |
7.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 545 EKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKE------ELEQREAELQKVRKA----EEERLRQ 614
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineissELPELREELEKLEKEvkelEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 615 EAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDI--DIEDLEELDPDFI----------------------- 669
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKvkELKELKEKAEEYIklsefyeeyldelreiekrlsrl 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 670 ----------------MAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-EEIPLIKSAYEEQRIKDMDLWEQQEEER 732
Cdd:PRK03918 320 eeeingieerikeleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270
....*....|....*....|....*....|....*.
gi 4503509 733 ITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAAR 768
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-785 |
8.24e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 560 NSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRqeAKEREKERILQEHEqikkkTVRER 639
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSL--QSELRRIENRLDELSQELSDASRKIG--EIEKEIEQLEQEEE-----KLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 640 LEQIKktelgakafkdidiEDLEELDPDFIMAKQ-VEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYE--- 715
Cdd:TIGR02169 739 LEELE--------------EDLSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSkle 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 716 -------------EQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKaARQSVYEEKLKQFEER 782
Cdd:TIGR02169 805 eevsriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-EELEELEAALRDLESR 883
|
...
gi 4503509 783 LAE 785
Cdd:TIGR02169 884 LGD 886
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
588-717 |
8.55e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 588 QREKEElEQREAELQKVRKAEEERLRQEAKEREKERilQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPD 667
Cdd:PRK09510 80 QRKKKE-QQQAEELQQKQAAEQERLKQLEKERLAAQ--EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4503509 668 FIMAKQVEQlEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKSAYEEQ 717
Cdd:PRK09510 157 AAAAKKAAA-EAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
552-696 |
2.20e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 552 LAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQI 631
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503509 632 KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKID 696
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
576-787 |
2.40e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 576 EERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEA------KEREKERILQEHEQ---IKKKTVRERLEQIKKT 646
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYyqlkekLELEEEYLLYLDYLklnEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 647 ELGAKAFKDIDIED-LEELDPDFIMAKQVEQLEKEKK---------ELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEE 716
Cdd:pfam02463 252 EIESSKQEIEKEEEkLAQVLKENKEEEKEKKLQEEELkllakeeeeLKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 717 QRIKDMDLWEQQEEE---RITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEER 787
Cdd:pfam02463 332 KEKEEIEELEKELKEleiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-858 |
2.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 516 SEQIRNQLTAMSSVLAKALEVIKPahiLQEKEEQhqlaVTAYLKNSRKEHQRILARRQTIEERKERLESL---------- 585
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINE---ISSELPE----LREELEKLEKEVKELEELKEEIEELEKELESLegskrkleek 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 586 --NIQREKEELEQREAELQKVRKaEEERLRQEAKE-----REKERILQEHEQIKKK--TVRERLEQIKKTelgakafkdi 656
Cdd:PRK03918 261 irELEERIEELKKEIEELEEKVK-ELKELKEKAEEyiklsEFYEEYLDELREIEKRlsRLEEEINGIEER---------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 657 dIEDLEEldpdfiMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-EEIPLIKSAYEEQRIKDMDLWEQQEEERITT 735
Cdd:PRK03918 330 -IKELEE------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 736 MQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQ-------------------------SVYEEKLKQFEERLAEERHNR 790
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 791 LEERKRQRKEERRITYYR---------------EKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVE 855
Cdd:PRK03918 483 RELEKVLKKESELIKLKElaeqlkeleeklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
...
gi 4503509 856 RKK 858
Cdd:PRK03918 563 KKL 565
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
514-758 |
3.70e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 514 MPSEQIRN-QLTAMSSVLA---KALEVIKPAHILQEKEEQHQLavtaylKNSRKEHQRILARRQTIEERKERLESlNIQR 589
Cdd:pfam05483 480 LEKEKLKNiELTAHCDKLLlenKELTQEASDMTLELKKHQEDI------INCKKQEERMLKQIENLEEKEMNLRD-ELES 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 590 EKEELEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQI---KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELD 665
Cdd:pfam05483 553 VREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 666 PDFIMAKQVE-QLEKEKKELQERLKNQEKKIDyferAKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKAL 744
Cdd:pfam05483 633 AYEIKVNKLElELASAKQKFEEIIDNYQKEIE----DKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL 708
|
250
....*....|....*.
gi 4503509 745 --EHKNRMSRMLEDRD 758
Cdd:pfam05483 709 meKHKHQYDKIIEERD 724
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-785 |
3.91e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 562 RKEHQRILARRQT----IEERKERLESLniqreKEELEQREAELQKVRKAEEERLRQEAKEREKE-----RILQEHEQIK 632
Cdd:TIGR02169 722 EKEIEQLEQEEEKlkerLEELEEDLSSL-----EQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 633 KKTVRERLEQIKKTElgaKAFKDIDiEDLEELDPDfimakqVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIPLIKS 712
Cdd:TIGR02169 797 QAELSKLEEEVSRIE---ARLREIE-QKLNRLTLE------KEYLEKEIQELQEQRIDLKEQIK--SIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503509 713 AYEEQrIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKaARQSVYEEKLKQFEERLAE 785
Cdd:TIGR02169 865 ELEEE-LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSE 935
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
572-731 |
4.09e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 572 RQTIEERKERLESLnIQREKEELE--QREAELQKvrKAEEERLRQEAKE--REKERILQEHE---QIKKKTVRERLEQIK 644
Cdd:PRK12704 30 EAKIKEAEEEAKRI-LEEAKKEAEaiKKEALLEA--KEEIHKLRNEFEKelRERRNELQKLEkrlLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 645 KTElgakafkdidiedlEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIplikSAYEEQRIKDMdL 724
Cdd:PRK12704 107 KRE--------------EELE------KKEKELEQKQQELEKKEEELEELIE--EQLQELERI----SGLTAEEAKEI-L 159
|
....*..
gi 4503509 725 WEQQEEE 731
Cdd:PRK12704 160 LEKVEEE 166
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
935-1145 |
4.21e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 935 ERPRRLGDDEDREPSLRPD-DDRVPRRGMDDDRGPRRGPE-----EDRFSRRGADDDRPSWRNTDDDRPPRRiadedrgn 1008
Cdd:PHA03307 198 PPAAASPRPPRRSSPISASaSSPAPAPGRSAADDAGASSSdssssESSGCGWGPENECPLPRPAPITLPTRI-------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1009 WRHADDDRPPRRGLdedRGSWRTADEDRGPRRGMDDDRGPRRGG---ADDERSSWRNADDDRGPRRG-LDDDRGPRRGMD 1084
Cdd:PHA03307 270 WEASGWNGPSSRPG---PASSSSSPRERSPSPSPSSPGSGPAPSsprASSSSSSSRESSSSSTSSSSeSSRGAAVSPGPS 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503509 1085 DDRGPRRGmdDDRGPRRGmddDRGPRRGLDDDRGPWRNADDDRIPRRGAEDDRGPWRNMDD 1145
Cdd:PHA03307 347 PSRSPSPS--RPPPPADP---SSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD 402
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-679 |
4.47e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT--VRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQV 674
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
....*
gi 4503509 675 EQLEK 679
Cdd:COG1196 514 LLLAG 518
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
880-1164 |
4.85e-06 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 51.45 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 880 DSSLSRKDSRWG-DRDSEGTWRKGPEADSEwrrgpPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVP 958
Cdd:NF033609 568 DSGSDSSNSDSGsDSGSDSTSDSGSDSASD-----SDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDS 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 959 RRGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGP 1038
Cdd:NF033609 643 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1039 RRGMDDDrgprrggADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRG 1118
Cdd:NF033609 723 DSDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 4503509 1119 PWRNADDDRIPRRGAEDDRGPWRNMDDDRLSRR-ADDDRFPRRGDDS 1164
Cdd:NF033609 796 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDS 842
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
543-703 |
7.23e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.84 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL-EQREAELQKVRKAEEERLRQE--AKER 619
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAkAKQAAEAKAKAEAEAERKAKEeaAKQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 620 EKERILQEHEQIKKKtvreRLEQIKKTELGAKAFKDIDiedlEELDPDFIMAKQVEQLEKEKKELQERlKNQEKKIDYFE 699
Cdd:TIGR02794 153 EEEAKAKAAAEAKKK----AEEAKKKAEAEAKAKAEAE----AKAKAEEAKAKAEAAKAKAAAEAAAK-AEAEAAAAAAA 223
|
....
gi 4503509 700 RAKR 703
Cdd:TIGR02794 224 EAER 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-790 |
8.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 532 KALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLEslniQREKEELEQREAELQKVRKAEEER 611
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE----ALKKEAEEAKKAEELKKKEAEEKK 1716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 612 LRQEAKEREKERILQEhEQIKKKTVRER--LEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLK 689
Cdd:PTZ00121 1717 KAEELKKAEEENKIKA-EEAKKEAEEDKkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 690 NQEKKIDYFERAKRLEEIPLIKSAYEEQRiKDMDLWEQQEEERITTMQLEREKALE-HK-NRMSRMLEDRDlfvmrlKAA 767
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKEGNLVINDS-KEMEDSAIKEVADSKNMQLEEADAFEkHKfNKNNENGEDGN------KEA 1868
|
250 260
....*....|....*....|...
gi 4503509 768 RQSVYEEKLKQFEERLAEERHNR 790
Cdd:PTZ00121 1869 DFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
530-701 |
1.75e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 530 LAKALEVIKPAHIlQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLN--IQREKEELEQREAELQKVRKA 607
Cdd:COG2433 378 IEEALEELIEKEL-PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeLEEKDERIERLERELSEARSE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 608 EEERLRqeaKEREKERILQEHEQIKKK--TVRERLEQIKKTELGAKAFKDIDIEDleeldpDFIMAKQVEQLEKEK-KEL 684
Cdd:COG2433 457 ERREIR---KDREISRLDREIERLEREleEERERIEELKRKLERLKELWKLEHSG------ELVPVKVVEKFTKEAiRRL 527
|
170
....*....|....*..
gi 4503509 685 QERLKNQEKKIDYFERA 701
Cdd:COG2433 528 EEEYGLKEGDVVYLRDA 544
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
512-757 |
1.90e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 512 QSMPSEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREK 591
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTvrerlEQIKKTELGAKAFKDIDIEDLEELDPdfimA 671
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA-----EALKKEAEEAKKAEELKKKEAEEKKK----A 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 672 KQVEQLEKEKKELQERLKNQEKkidyfERAKRLEEipLIKSAYEEQRIKDMDLWEQQEEERITTMQLER-EKALEHKNRM 750
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAE-----EDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEK 1791
|
....*..
gi 4503509 751 SRMLEDR 757
Cdd:PTZ00121 1792 RRMEVDK 1798
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-786 |
2.05e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REAELQKVRKAEEERLrqEAKEREKERILQEHEQIKK------KTVRERLEQIKKTELgakafkdiDIEDLEEldpdfIM 670
Cdd:PRK12704 34 KEAEEEAKRILEEAKK--EAEAIKKEALLEAKEEIHKlrnefeKELRERRNELQKLEK--------RLLQKEE-----NL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 671 AKQVEQLEKEKKELQERLKNQEKKIDYFEraKRLEEiplIKSAYEEQRikdmdlweqQEEERITTMQLErekalEHKNRM 750
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELE--KKEEE---LEELIEEQL---------QELERISGLTAE-----EAKEIL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 4503509 751 SRMLEDRdlfvMRLKAARQ-SVYEEKLKQFEERLAEE 786
Cdd:PRK12704 160 LEKVEEE----ARHEAAVLiKEIEEEAKEEADKKAKE 192
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-787 |
2.12e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKAL-EVIKPAHILQEKEEQHQLAVTAYLKNSRKEH-QRILARRQTIEERKERLESLNIQREKEEL 594
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEkALAELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 595 EQREAEL-QKVRKAEEERLRQEAK----EREKERILQEHEQIKKK----------------TVRERLEQIKKTelgaKAF 653
Cdd:TIGR02168 760 EAEIEELeERLEEAEEELAEAEAEieelEAQIEQLKEELKALREAldelraeltllneeaaNLRERLESLERR----IAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 654 KDIDIEDLEELDPDfiMAKQVEQLEKEKKELQERLKNQEKKID--YFERAKRLEEIPLIKSAYEEQRiKDMDLWEQQEEE 731
Cdd:TIGR02168 836 TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELESELEalLNERASLEEALALLRSELEELS-EELRELESKRSE 912
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 732 RITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEER 787
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
543-707 |
2.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQlAVTAYLKNSRKEHQRIlarRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQ-------- 614
Cdd:COG4717 83 AEEKEEEYA-ELQEELEELEEELEEL---EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 615 EAKEREKERILQEHEQIKKKTVRERLEqikKTELGAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKK 694
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDL-AEELEELQ------QRLAELEEELEEAQEELEELEEE 228
|
170
....*....|...
gi 4503509 695 IDYFERAKRLEEI 707
Cdd:COG4717 229 LEQLENELEAAAL 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
562-684 |
2.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLE 641
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL-----LEELL 742
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 4503509 642 QIKKTELGAKAFKDIDIEDLEELDpdfimaKQVEQLEKEKKEL 684
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELE------RELERLEREIEAL 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-786 |
2.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 542 ILQEKEEQHQLAVtayLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK-VRKAEEERLRQEAKERE 620
Cdd:COG4913 244 LEDAREQIELLEP---IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 621 KERILQEHEQIKKKTVRERLEQIKktelgakafkdidiedleeldpdfimaKQVEQLEKEKKELQERLKNQEkkidyfER 700
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLE---------------------------REIERLERELEERERRRARLE------AL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 701 AKRLE-EIPLIKSAYEEQR------IKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEdrdlfvmRLKaARQSVYE 773
Cdd:COG4913 368 LAALGlPLPASAEEFAALRaeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-------SLE-RRKSNIP 439
|
250
....*....|...
gi 4503509 774 EKLKQFEERLAEE 786
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
566-685 |
2.94e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.57 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 566 QRILARRQTIEE---RKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEH-EQIKKKTVRERLE 641
Cdd:cd16269 173 QEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHlRQLKEKMEEEREN 252
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 4503509 642 QIKKTELgAKAFKDIDIEDLEELDpdfiMAKQVEQLEKEKKELQ 685
Cdd:cd16269 253 LLKEQER-ALESKLKEQEALLEEG----FKEQAELLQEEIRSLK 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
544-887 |
3.68e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 544 QEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKER 623
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 624 ILQEHEQIKKKTVRERLEQIKKTELG------AKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 698 FERAKRLEE----IPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYE 773
Cdd:pfam02463 814 AELLEEEQLlieqEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 774 EKLKQFEERLAEERHNRLEERKRQRKEERRITYYREKEEEEQRRAEEQmLKEREERERAERAKREEELREYQERVKKLEE 853
Cdd:pfam02463 894 KEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
330 340 350
....*....|....*....|....*....|....
gi 4503509 854 VERKKRQRELEIEERERRREEERRLGDSSLSRKD 887
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-974 |
4.20e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 531 AKALEVIKPAHILQEKEEQHQlavTAYLKNSRKEHQRILARRQTIEERKERLESLN-IQREKEELEQREAELQKVRKAEE 609
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKK---ADAAKKKAEEKKKADEAKKKAEEDKKKADELKkAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 610 ERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKT-ELGAKAFKDIDIEDLEELDPDFIM-AKQVEQLEKEKKELQER 687
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKkADEAKKAAEAKKKADEA 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 688 LKNQEKKidYFERAKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERittmQLEREKALEHKNRMSrmlEDRDLFVMRLKAA 767
Cdd:PTZ00121 1516 KKAEEAK--KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAE---EDKNMALRKAEEA 1586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 768 RQSvyEEKLKQFEERLAEERHNRLEERKRQRKEERRITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQER 847
Cdd:PTZ00121 1587 KKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 848 VKKLEEVERKKRQRELEIEERERRREEERRLGDSSLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDED 927
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 4503509 928 RSH--RRDEERPRRL----GDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEE 974
Cdd:PTZ00121 1745 KAEeaKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
884-1005 |
4.96e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.98 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 884 SRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMD 963
Cdd:PRK12678 173 RRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 4503509 964 DDRGPRRGPEEDRFSRRgaDDDRPSWRNTDDDRPPRRIADED 1005
Cdd:PRK12678 253 DDGEGRGGRRGRRFRDR--DRRGRRGGDGGNEREPELREDDV 292
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
564-707 |
5.26e-05 |
|
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: 46.46 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 564 EHQRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRlkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 642 QIKKtelgAKAFKDIdiedLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEI 707
Cdd:COG1579 84 NVRN----NKEYEAL----QKEIE---SLKRRISDLEDEILELMERIEELEEELA--ELEAELAEL 136
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
575-694 |
7.36e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 575 IEERKErleslNIQREKEELEQ---------REAElQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKK 645
Cdd:PRK00409 504 IEEAKK-----LIGEDKEKLNEliasleeleRELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK-LLEEAEKEAQ 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4503509 646 TELG-AKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK00409 577 QAIKeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-704 |
7.80e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 516 SEQIRNQLTAMSSVLAKALEVIKPAH-ILQEKEEQHQLAVTAYLKNSRKEhQRILARRQTIEERKERLESlNIQREKEEL 594
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQI-ASLNNEIERLEARLERLED-RRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 595 EQREAELQKVRKAE-EERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKafkdidiEDLEELDPDF-IMAK 672
Cdd:TIGR02168 424 EELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLdSLER 496
|
170 180 190
....*....|....*....|....*....|..
gi 4503509 673 QVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-783 |
9.88e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 561 SRKEHQRILARRQTIEErkerleslnIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERL 640
Cdd:TIGR02168 665 SAKTNSSILERRREIEE---------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 641 EQIKKT-ELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDyferaKRLEEIPLIKSAYEEQRI 719
Cdd:TIGR02168 736 ARLEAEvEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDELRA 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 720 KdmdlwEQQEEERITTMQLEREKALEHKNRMSRMLEDRdlfvmrlkaarqsvyEEKLKQFEERL 783
Cdd:TIGR02168 811 E-----LTLLNEEAANLRERLESLERRIAATERRLEDL---------------EEQIEELSEDI 854
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
479-869 |
1.39e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 479 DLQVRIDHTSRTLSFGSDLNYATREDAPIGPHLQSMPSEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQlavTAYL 558
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE---KEEL 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 559 KNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELqKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRE 638
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS-RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 639 RLEQIKKTELGAKAFKDIDIEDLEELDPDfimakQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEipliksayEEQR 718
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEE-----QLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--------ELER 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 719 IKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQR 798
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503509 799 KEERRIT---YYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEV-----ERKKRQRELEIEERE 869
Cdd:pfam02463 939 ELLLEEAdekEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKerleeEKKKLIRAIIEETCQ 1017
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
571-706 |
2.33e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 571 RRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQeaKEREKERiLQEHEQIKKKTVRERLEQIKKTELGA 650
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR--LEEQVER-LEAEVEELEAELEEKDERIERLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 651 KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEE 706
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| COG4253 |
COG4253 |
Uncharacterized conserved protein, DUF2345 family [Function unknown]; |
887-1171 |
2.40e-04 |
|
Uncharacterized conserved protein, DUF2345 family [Function unknown];
Pssm-ID: 443395 [Multi-domain] Cd Length: 900 Bit Score: 45.81 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 887 DSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDrepsLRPDDDRVPRRGMDDDR 966
Cdd:COG4253 232 RRAATAADDAQTTDDARLTADDSAADAGSLSGSGGDGGAAGGSLAEATSSLRVPAASVS----LARYQRARRAAAAAAAA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 967 GPRRGpEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPR---RGLDEDRGSWRTADEDRGPRRGMD 1043
Cdd:COG4253 308 DARAG-GADAAGGVGTGGGRRLAAGLAGAAAEEEEAVGAEARARRRRLLRAARaaiRLLAAAALALLALGRGALAGRSPA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1044 DDRGP-------RRGGADDERSSWRnaDDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDD 1116
Cdd:COG4253 387 AAAGPgivggtdRRARRRATAFVDR--AAGPPPRTQRARRPLLPRPRGAGGPPPRVVSTRAGDTPSADDDDGGRRVVRDD 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 4503509 1117 RGPWRNADDDRIPRRGAEDDRGPWRNMDDDRLSRRADDDRFPRRGDDSRPGPWRP 1171
Cdd:COG4253 465 RRVAWVGGGESWGAGGGAGAGGGVGGGVVPLLGDGDVVIAAEGGGPPAPGGGAPA 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
544-643 |
2.95e-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: 45.50 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 544 QEKEEQHQLAVTAylKNSRKEHQRILARRQT-IEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam17380 499 KELEERKQAMIEE--ERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
90 100
....*....|....*....|.
gi 4503509 623 RILQEHEQIKKKTVRERLEQI 643
Cdd:pfam17380 577 MMRQIVESEKARAEYEATTPI 597
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
562-705 |
3.03e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 562 RKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAE--QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 642 QIKKTELGAKAFKDIDIEDLEEldpdfimAKQvEQLEKEKKELQERLKNQEKKidyfERAKRLE 705
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAE-------AKK-KAEEAKKKAEAEAKAKAEAE----AKAKAEE 193
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
558-785 |
3.07e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR 637
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 638 ERLEQIKKTELGAKAFKDidieDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEE 716
Cdd:pfam05557 94 EKESQLADAREVISCLKN----ELSELRRQIQRAElELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 717 QRIKDMDLWEQQEE-------------ERITTMQLEREKALEHKNRMSRMLEDRDLfvmrLKAARQSvYEEKLKQFEERL 783
Cdd:pfam05557 170 QRIKELEFEIQSQEqdseivknskselARIPELEKELERLREHNKHLNENIENKLL----LKEEVED-LKRKLEREEKYR 244
|
..
gi 4503509 784 AE 785
Cdd:pfam05557 245 EE 246
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
1199-1258 |
3.13e-04 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 44.88 E-value: 3.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1199 EEREWDREKERDRDNQDREENDKDPERERDRERDVDREDRFRRPRDEGGWRRGPAEESSS 1258
Cdd:TIGR01642 3 EEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRS 62
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
532-683 |
3.41e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.34 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 532 KALEVIKPAHILQEKEEQHQL--AVTAYLKNSRKEHQRiLARRqtIEERKERLEslniqREKEELEQREAELQKVRKAEE 609
Cdd:pfam12072 45 KEAETKKKEALLEAKEEIHKLraEAERELKERRNELQR-QERR--LLQKEETLD-----RKDESLEKKEESLEKKEKELE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 610 ERLRQ-EAKEREKERILQEHeqikkktvRERLEQIKKteLGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:pfam12072 117 AQQQQlEEKEEELEELIEEQ--------RQELERISG--LTSEEAKEILLDEVEeELRHE--AAVMIKEIEEEAKE 180
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
517-777 |
3.79e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLEslniqrekEELEQ 596
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ--------EKLEQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQ 676
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEE-LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 677 LEKEKKELQERLKNQEKKIDYFERAKRLEEipliksayEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLED 756
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQL--------VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
250 260
....*....|....*....|.
gi 4503509 757 RDLFVMRLKAARQSVYEEKLK 777
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYK 542
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
543-707 |
4.38e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.79 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQLAVTAYLKNSRKEhqrILARRQTIEERKERLESLNIQ-REK-----EELEQREAELQKV-RKAEEERLRQE 615
Cdd:pfam09728 93 LAKEEEEKRKELSEKFQSTLKD---IQDKMEEKSEKNNKLREENEElREKlksliEQYELRELHFEKLlKTKELEVQLAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 616 AK----EREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFI---------------MAKQVEQ 676
Cdd:pfam09728 170 AKlqqaTEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNksnevfttfkkemekMSKKIKK 249
|
170 180 190
....*....|....*....|....*....|...
gi 4503509 677 LEKEKKELQERLKNQEKKIDYF--ERAKRLEEI 707
Cdd:pfam09728 250 LEKENLTWKRKWEKSNKALLEMaeERQKLKEEL 282
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
915-1036 |
5.24e-04 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 44.50 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 915 EKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREpslRPDDDRVPRRGMDDDRGPRRGPEEDRFSRRgadDDRPSWRNTDD 994
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRF---RDRHRRSRERSYREDSRPRDRRRYDSRSPR---SLRYSSVRRSR 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 4503509 995 DRPPRRIADEDRG-NWRHADDDRPPRRgldedrgSWRTADEDR 1036
Cdd:TIGR01642 76 DRPRRRSRSVRSIeQHRRRLRDRSPSN-------QWRKDDKKR 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
572-686 |
6.02e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 572 RQTIEERKERLESLNIQREKE----ELEQREAELQKVRkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTE 647
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREietaRIAEAEAELAKKK--AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERER 290
|
90 100 110
....*....|....*....|....*....|....*....
gi 4503509 648 LGAKAFKDIDiEDLEELDPDFIMAKQVEQLEKEKKELQE 686
Cdd:COG2268 291 EIELQEKEAE-REEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| FadA |
pfam09403 |
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha ... |
593-704 |
6.03e-04 |
|
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha helices that form an intra-molecular coiled-coil arrangement.
Pssm-ID: 430587 [Multi-domain] Cd Length: 99 Bit Score: 40.34 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 593 ELEQREAELQKVRKAEEERL--RQEAKEREKERiLQEHEQIKKKtVRERLEQIKKTElGAKAFKDidieDLEELdpdfim 670
Cdd:pfam09403 1 RLSALEAELQKLENKEEQRFnkEKAKAEAAAAD-LAKNYELKAE-IEEKLAKLEADS-DVRFYKD----EYKEL------ 67
|
90 100 110
....*....|....*....|....*....|....
gi 4503509 671 akqVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam09403 68 ---LKKYKDLLKELEKEIKEEEKIIDNFEALLSL 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
523-747 |
6.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 523 LTAMSSVLAKALEVIKPAHILQEKEEQHQlAVTAYLKNSRKEHQRILARRQTIEERKERLESLnIQREKEELEQREAELQ 602
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 603 KVRKaEEERLRQEAKEREKE-----RILQEHEQIKKKTVRERLEQIKKTELGAKAFKDI---DIEDLEELDPDFI-MAKQ 673
Cdd:COG4942 87 ELEK-EIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLapaRREQAEELRADLAeLAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 674 VEQLEKEKKELQERLKNQEKKIDYFERAK--RLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHK 747
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
572-681 |
6.63e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 43.18 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 572 RQTIEERKERLESlnIQREKEELEQREAELQKVRKA---EEERLRQEAKEREKERILQEHEQikkKTVRERLEQIKKTEL 648
Cdd:COG4026 134 REELLELKEKIDE--IAKEKEKLTKENEELESELEElreEYKKLREENSILEEEFDNIKSEY---SDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....*....
gi 4503509 649 gakaFKDIDIEDL------EELDPDFIMAKQVEQLEKEK 681
Cdd:COG4026 209 ----LEVFSLEELwkelfpEELPEEDFIYFATENLKPGK 243
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-689 |
6.74e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 566 QRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKktvreRLEQI 643
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALlkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE-AKKEADEIIK-----ELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503509 644 KKTELGAKAFKDIdIEDLEELDPdfiMAKQVEQLEKEKKELQERLK 689
Cdd:PRK00409 597 QKGGYASVKAHEL-IEARKRLNK---ANEKKEKKKKKQKEKQEELK 638
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
563-783 |
8.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 563 KEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE-ERLRQEAKER----EKERILQEHEQIKKKTVR 637
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEaVRTNPEINDRirllEQEVARYKEESGKAQAEV 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 638 ERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKkidyFERAKRLEEIPLIKSAyeeq 717
Cdd:pfam10174 582 ERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQL----LEEARRREDNLADNSQ---- 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503509 718 rikdmdlwEQQEEERITTMQLEREKALEHKNRMS---RMLEDRDLFVMRLKAARQSVYEEKLKQFEERL 783
Cdd:pfam10174 654 --------QLQLEELMGALEKTRQELDATKARLSstqQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
576-721 |
9.01e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 576 EERKERLESLNIQREKEELE-QREAELQKVRKAEEERLRQEAK---EREKERILQEHEQIKKKTVRERLEQIKKTELGAK 651
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEkQRAAEQARQKELEQRAAAEKAAkqaEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 652 AFKDIDIEDLEELDPdfiMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRIKD 721
Cdd:TIGR02794 142 RKAKEEAAKQAEEEA---KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAE 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-790 |
9.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 592 EELEQREAELQKVRKA-EEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDiDIEDLEeldpdfim 670
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEA-ELAELE-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 671 aKQVEQLEKEKKELQERLKNQekkIDYFERAKRLEEIPLIKSA---------------YEEQRIKDMDLWEQQEEErITT 735
Cdd:COG4942 90 -KEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPedfldavrrlqylkyLAPARREQAEELRADLAE-LAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503509 736 MQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVY---EEKLKQFEERLAEERHNR 790
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLarlEKELAELAAELAELQQEA 222
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
927-1066 |
9.87e-04 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 43.34 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 927 DRSHRRDEERPRrlgdDEDREPSLRPDDDRvpRRGMDDDRGPRRGPEEdrfsRRGADDDRPSWRNTDDDRPPRRIADEDR 1006
Cdd:TIGR01642 2 DEEPDREREKSR----GRDRDRSSERPRRR--SRDRSRFRDRHRRSRE----RSYREDSRPRDRRRYDSRSPRSLRYSSV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503509 1007 GNWRHadddRPPRRGLDEDRGSW-RTADEDRGPRRGMDDDRGpRRGGADDERSSWRNADDD 1066
Cdd:TIGR01642 72 RRSRD----RPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDK-KRSLWDIKPPGYELVTAD 127
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
573-784 |
1.15e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.63 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 573 QTIEERKERLESLNIQREKEE-LEQREAELQKVRKAEEERL-----RQEAKEREKERILQEHEqiKKKTVRERLE----- 641
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAaLCKKYAELLEEMKRLQKDLkklkkKQDQLQKEKDQLQSELS--KAILAKSKLEklcre 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 642 ---QIKKTELGAKAFKDIDIEDLEELDPDF------IMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEI--PLI 710
Cdd:pfam09728 79 lqkQNKKLKEESKKLAKEEEEKRKELSEKFqstlkdIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHfeKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 711 KSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEdrdlfvmRLKAARQ--SVYEEKLKQFEERLA 784
Cdd:pfam09728 159 KTKELEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSE-------TEKELREqlNLYVEKFEEFQDTLN 227
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
530-659 |
1.27e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 42.67 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 530 LAKALEVIKpahiLQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKerleslNIQREKEELEQREAEL-QKVRKAE 608
Cdd:pfam07767 201 LQKAVEAEK----KRLKEEEKLERVLEKIAESAATAEAREEKRKTKAQRN------KEKRRKEEEREAKEEKaLKKKLAQ 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 4503509 609 EERLRQEAKE-REKERILQEHEQIKKKTVRERLEQIKKTE---LGAKAFKDIDIE 659
Cdd:pfam07767 271 LERLKEIAKEiAEKEKEREEKAEARKREKRKKKKEEKKLRprkLGKHKVPEPDLE 325
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
572-755 |
1.35e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 572 RQTIEERKERLESlNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRERLEQI-----K 644
Cdd:COG5185 324 EQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIpqnqrG 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 645 KTELGAKAFKD---IDIEDLEELDPDFIMA-KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAyEEQRIK 720
Cdd:COG5185 403 YAQEILATLEDtlkAADRQIEELQRQIEQAtSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKE 481
|
170 180 190
....*....|....*....|....*....|....*
gi 4503509 721 DMDLWEQQEEERITTMQLEREKaleHKNRMSRMLE 755
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEK---LRAKLERQLE 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
558-791 |
1.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 558 LKNSRKEHQRILARRQTIEER-KERLESLNIQREK-EELEQREAELQKvrKAEEERLRQEAKEREKERILQEHEQIKKK- 634
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELiAERRETIEEKRERaEELRERAAELEA--EAEEKREAAAEAEEEAEEAREEVAELNSKl 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 635 -TVRERLEQIKKtelgakafkdidIEDLEELdpdfimakqVEQLEKEKKELQERLKNQEKKIDyfERAKRLeeipliksa 713
Cdd:PRK02224 582 aELKERIESLER------------IRTLLAA---------IADAEDEIERLREKREALAELND--ERRERL--------- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 714 yEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML----EDRDLFVMRLKAARQSVyeEKLKQFEERLA--EER 787
Cdd:PRK02224 630 -AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLdelrEERDDLQAEIGAVENEL--EELEELRERREalENR 706
|
....
gi 4503509 788 HNRL 791
Cdd:PRK02224 707 VEAL 710
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-706 |
1.42e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 558 LKNSRKEHQRILARRQT-IEERKERLESLNIQ-----REKEELEQREAELQK----VRKAEEERLRQEAKEREK-ERILQ 626
Cdd:TIGR02168 328 LESKLDELAEELAELEEkLEELKEELESLEAEleeleAELEELESRLEELEEqletLRSKVAQLELQIASLNNEiERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 627 EHEQIKKKtvRERLEQIKKTELGAKAFKDID--IEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168 408 RLERLEDR--RERLQQEIEELLKKLEEAELKelQAELEELE------EELEELQEELERLEEALEELREELEEAEQALDA 479
|
..
gi 4503509 705 EE 706
Cdd:TIGR02168 480 AE 481
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
543-759 |
1.54e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQ----LAVTAYLKNSRK----EHQRILARrqTIEERKERLESLNiqrEKEELEQREAELQKVRKAEEERLRQ 614
Cdd:cd16269 61 LQELLDLHAacekEALEVFMKRSFKdedqKFQKKLME--QLEEKKEEFCKQN---EEASSKRCQALLQELSAPLEEKISQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 615 E--AKE-------REKERILQEHEQIKKKTVR--ERLE---QIKKTElgAKAfkdidiedleeldpdfIMAKQVEQLEKE 680
Cdd:cd16269 136 GsySVPggyqlylEDREKLVEKYRQVPRKGVKaeEVLQeflQSKEAE--AEA----------------ILQADQALTEKE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 681 KKELQERLKNQEKKidyfERAKRLEEipliKSAYEEQRIKDMdlwEQQEEERIT----TMQLEREKALEHKNRM--SRML 754
Cdd:cd16269 198 KEIEAERAKAEAAE----QERKLLEE----QQRELEQKLEDQ---ERSYEEHLRqlkeKMEEERENLLKEQERAleSKLK 266
|
....*
gi 4503509 755 EDRDL 759
Cdd:cd16269 267 EQEAL 271
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
955-1067 |
1.57e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 42.96 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 955 DRVPRRGMDDDRGPRRGPEEDRFSRRGADDDRpswrntDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADE 1034
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR------FRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSR 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 4503509 1035 DRGPRRGMDDDRGP--RRGGADDERS-SWRNADDDR 1067
Cdd:TIGR01642 76 DRPRRRSRSVRSIEqhRRRLRDRSPSnQWRKDDKKR 111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
544-785 |
1.66e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 544 QEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLeSLNIQREKEELEQREAELQKVRKAEEERLrqeakEREKER 623
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQ-----QEKEEL 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 624 ILQEHEQikKKTVRERLEQIKKtELGAKAFKDIDIED-LEELDPDFIMAK---------QVEQLEKEKKELQERLKNQEK 693
Cdd:TIGR00606 929 ISSKETS--NKKAQDKVNDIKE-KVKNIHGYMKDIENkIQDGKDDYLKQKetelntvnaQLEECEKHQEKINEDMRLMRQ 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 694 KIDYFERAKRLEEIPLIKsayeeqRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMR--LKAARQSV 771
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTL------RKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNhvLALGRQKG 1079
|
250
....*....|....
gi 4503509 772 YEEKLKQFEERLAE 785
Cdd:TIGR00606 1080 YEKEIKHFKKELRE 1093
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
889-1015 |
1.80e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 42.57 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 889 RWGDRDSEgtwrkgpeaDSEWRRGPPEKEWRRGEGRDEDRS---HRRDEERPRRLGD---DEDREPSLRPDDDRVPRRGM 962
Cdd:TIGR01642 3 EEPDRERE---------KSRGRDRDRSSERPRRRSRDRSRFrdrHRRSRERSYREDSrprDRRRYDSRSPRSLRYSSVRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 4503509 963 DDDRGPRRGPEEDRFSR-RGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDD 1015
Cdd:TIGR01642 74 SRDRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYELVTAD 127
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
558-858 |
2.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK---VRKAEEERLRQEAKEREKER---ILQEHEQI 631
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeARKAEDARKAEEARKAEDAKrveIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 632 KKKTVRERLEQIKKTELGAKAfkdIDIEDLEELDPdfimAKQVEQLEKEKKELQERLKNQEKKidyFERAKRLEEIPLIk 711
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKA---EEVRKAEELRK----AEDARKAEAARKAEEERKAEEARK---AEDAKKAEAVKKA- 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 712 sayEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML---EDRDLFVMRlKAARQSVYEEKLKQFEERLAEERH 788
Cdd:PTZ00121 1233 ---EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaeEARKADELK-KAEEKKKADEAKKAEEKKKADEAK 1308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 789 NRLEERKRQRKEERRITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKK 858
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
511-738 |
2.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 511 LQSMPSEQIRNQLTAMSSVLAKaleviKPAHILQEKEEQHQLavtayLKNSRKEHQRILARRQTIEERKERLESLniQRE 590
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGR-----KPELNLKELKELEEE-----LKEAEEKEEEYAELQEELEELEEELEEL--EAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 591 KEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLEQIKKTELGAKAFKDiDIEDLEE------L 664
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL-----EERLEELRELEEELEELEA-ELAELQEeleellE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 665 DPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyferaKRLEEIplIKSAYEEQRIKDMDLWEQQEEERITTMQL 738
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEEL------EEAQEE--LEELEEELEQLENELEAAALEERLKEARL 250
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-743 |
2.17e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 575 IEERKERLESLNiQREKEELEQREAELQKVRKAEEERLRQ-----------------------------EAKEREKERIL 625
Cdd:TIGR04523 347 LKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqindleskiqnqeklnqqkdeqiKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 626 QEHEQIKKKTVRERlEQIKKTElGAKAFKDIDIEDLEELDPDFimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLE 705
Cdd:TIGR04523 426 KEIERLKETIIKNN-SEIKDLT-NQDSVKELIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKELK 499
|
170 180 190
....*....|....*....|....*....|....*...
gi 4503509 706 EIPLIKSAYEEQrIKdmDLWEQQEEERITTMQLEREKA 743
Cdd:TIGR04523 500 KLNEEKKELEEK-VK--DLTKKISSLKEKIEKLESEKK 534
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1049-1272 |
2.40e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1049 RRGGADDERSSWRNADDDRGPRRGlDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPWRNADDDRI 1128
Cdd:PRK12678 58 ARGGGAAAAAATPAAPAAAARRAA-RAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1129 PRRGAEDDRGpwrnMDDDRLSRRADDDRFPRRGDDSRpgpwrplvkpggwreKEKAREESWGPPRESRPSEEREWDREKE 1208
Cdd:PRK12678 137 ARRGAARKAG----EGGEQPATEARADAAERTEEEER---------------DERRRRGDREDRQAEAERGERGRREERG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 1209 RDRDNQDREENDKDpERERDRERDVDREDRFRRPRDEggwRRGPAEESSSWRDSSRRDDRDRDD 1272
Cdd:PRK12678 198 RDGDDRDRRDRREQ-GDRREERGRRDGGDRRGRRRRR---DRRDARGDDNREDRGDRDGDDGEG 257
|
|
| AC_N |
pfam16214 |
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ... |
980-1099 |
2.43e-03 |
|
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.
Pssm-ID: 318454 Cd Length: 415 Bit Score: 41.92 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 980 RGADDDRPSWRNTD-----------DDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSW------RTADEDRGPRRGM 1042
Cdd:pfam16214 18 RGGTEHRSAWGEAEsrangypyapgSARSSTKKQQRLASRWRSEDDDDPPLSGSDPLSGGFgfsfrsKSAWQEHGGESRR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503509 1043 DDDRGPRRGG--ADDERSSWRNADDDRgPRR---GLDDDRGPRRGMDDDRGPrrGMDDDRGP 1099
Cdd:pfam16214 98 QRTRAPPAGGgpGSAAAAASRGGGEVR-PRSvelGLEERRGKGRAAEGGEGS--GDGGSSAP 156
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
517-785 |
2.52e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKpahILQEKEEQHQLAVTAYLKNSRKEHQRILARR----QTIEERKERLESL------- 585
Cdd:pfam06160 89 DEIEELLDDIEEDIKQILEELD---ELLESEEKNREEVEELKDKYRELRKTLLANRfsygPAIDELEKQLAEIeeefsqf 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 586 -----------------NIQREKEELEQR-------EAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRER 639
Cdd:pfam06160 166 eeltesgdylearevleKLEEETDALEELmedipplYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKeiQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 640 LEQ----IKKTELGAKAFKDIDIED-LEELdpdfimakqVEQLEKEKKELQERLKNQEKKIDYFERAKR-----LEEIPL 709
Cdd:pfam06160 246 LEEnlalLENLELDEAEEALEEIEErIDQL---------YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEqnkelKEELER 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503509 710 IKSAYeeqrikdmdlweqqeeeRITTMQLEREKALEhkNRMSRMLEDRDLFVMRLKAARQ--SVYEEKLKQFEERLAE 785
Cdd:pfam06160 317 VQQSY-----------------TLNENELERVRGLE--KQLEELEKRYDEIVERLEEKEVaySELQEELEEILEQLEE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
519-784 |
2.79e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 519 IRNQLTAMSSVLAKALEVIKPAHilQEKEEQ----HQLAVTAYLK---NSRKEHQRILARRQTIEERKERLESLNIqREK 591
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQH--QDRIEQliseHEVEITGLTEkasSARSQANSIQSQLEIIQEQARNQNSMYM-RQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 592 EELE----QREAELQKVRKAEEERLrqeaKEREKERILQEHEQIKKKTVRERLEQikktelgakafkdidiedlEELDPD 667
Cdd:pfam15921 320 SDLEstvsQLRSELREAKRMYEDKI----EELEKQLVLANSELTEARTERDQFSQ-------------------ESGNLD 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 668 FIMAKQVEQLEKEKKELQERlKNQEKKidyferakrleeipliksayeeqrikdmdLWEQQEEERITTMQLEREkalehk 747
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLE-KEQNKR-----------------------------LWDRDTGNSITIDHLRRE------ 420
|
250 260 270
....*....|....*....|....*....|....*..
gi 4503509 748 nrmsrmLEDRDLFVMRLKAARQSVYEEKLKQFEERLA 784
Cdd:pfam15921 421 ------LDDRNMEVQRLEALLKAMKSECQGQMERQMA 451
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
975-1104 |
3.25e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 41.80 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 975 DRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHadddrppRRGLDEDRgswRTADEDRGPRRgmDDDRGPRrggad 1054
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRH-------RRSRERSY---REDSRPRDRRR--YDSRSPR----- 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4503509 1055 DERSSWRNADDDRGPRRGLDDDRGPR-RGMDDDRGPRRGMDDDRGPRRGMD 1104
Cdd:TIGR01642 65 SLRYSSVRRSRDRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWD 115
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
539-635 |
3.31e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 539 PAHI-L-----QEKEEQHQLAvtaylknsRKEHQRILARrQTIEERKERLEslniqREKEELEQREAELQKVRKAEEERL 612
Cdd:PRK05035 422 PSNIpLvqyyrQAKAEIRAIE--------QEKKKAEEAK-ARFEARQARLE-----REKAAREARHKKAAEARAAKDKDA 487
|
90 100
....*....|....*....|...
gi 4503509 613 RQEAKEREKERILQEHEQIKKKT 635
Cdd:PRK05035 488 VAAALARVKAKKAAATQPIVIKA 510
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
890-1255 |
3.40e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 890 WGDRDSEGTWRKGPEADSEWRRGPPEKEWRrgegRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPR 969
Cdd:COG3903 536 LAHGDAELALRLAAALAPFWFLRGLLREGR----RWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 970 RGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPR 1049
Cdd:COG3903 612 AAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1050 RGGADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPW---RNADDD 1126
Cdd:COG3903 692 AALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAAlaaAAAAAA 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1127 RIPRRGAEDDRGPWRNMDDDRLSRRADDDRFPRRGDDSRPGPWRPLVKPGGWREKEKAREESWGPPRESRPSEEREWDRE 1206
Cdd:COG3903 772 LAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAA 851
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 4503509 1207 KERDRDNQDREENDKDPERERDRERDVDREDRFRRPRDEGGWRRGPAEE 1255
Cdd:COG3903 852 AALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAA 900
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
518-785 |
3.67e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 518 QIRNQLTAMSSVLAKALEVIKpahILQEKEEQHQLAVTAYLKNSRKEHQRILARR----QTIEERKERLESLniqreKEE 593
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQ---ELLESEEKNREEVEQLKDLYRELRKSLLANRfsfgPALDELEKQLENL-----EEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 594 LEQREAELQK--VRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAK-------AFKDIDIE----- 659
Cdd:PRK04778 181 FSQFVELTESgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRelveegyHLDHLDIEkeiqd 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 660 ----------DLEELDPDfIMAKQVEQLEKEKKEL-----------QERLKNQEKKIDYFERAKR-----LEEIPLIKSA 713
Cdd:PRK04778 261 lkeqidenlaLLEELDLD-EAEEKNEEIQERIDQLydilerevkarKYVEKNSDTLPDFLEHAKEqnkelKEEIDRVKQS 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503509 714 YEeqrikdmdlweqqeeerITTMQLEREKALEhkNRMSRMLEDRDLFVMRL--KAARQSVYEEKLKQFEERLAE 785
Cdd:PRK04778 340 YT-----------------LNESELESVRQLE--KQLESLEKQYDEITERIaeQEIAYSELQEELEEILKQLEE 394
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
920-1024 |
3.73e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 41.44 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 920 RGEGRDEDRSHRRDEERPRrlgdDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPR 999
Cdd:TIGR01622 5 RERERLRDSSSAGDRDRRR----DKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRRYRPREKRRRRG 80
|
90 100
....*....|....*....|....*
gi 4503509 1000 RIADEDRGNWRHADDDRPPRRGLDE 1024
Cdd:TIGR01622 81 DSYRRRRDDRRSRREKPRARDGTPE 105
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
558-645 |
3.75e-03 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 39.85 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 558 LKNSRKehQRILarrQTIEERKERLESLNiqrekEELEQREAELQKVrKAEEERLRQEA---KEREKERILQeheQIKKK 634
Cdd:CHL00019 52 LLDNRK--QTIL---NTIRNSEERREEAI-----EKLEKARARLRQA-ELEADEIRVNGyseIEREKENLIN---QAKED 117
|
90
....*....|.
gi 4503509 635 TvrERLEQIKK 645
Cdd:CHL00019 118 L--ERLENYKN 126
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
985-1071 |
3.80e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 41.44 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 985 DRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPR----RGGADDERSSW 1060
Cdd:TIGR01622 4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRryrpREKRRRRGDSY 83
|
90
....*....|.
gi 4503509 1061 RNADDDRGPRR 1071
Cdd:TIGR01622 84 RRRRDDRRSRR 94
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
891-1125 |
3.80e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 891 GDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDE----ERPRRLGDDEDREPSLRPDDDRVPRRGM---- 962
Cdd:PHA03307 195 PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDssssESSGCGWGPENECPLPRPAPITLPTRIWeasg 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 963 DDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDR-----PPRRGLDEDRGswrtADEDRG 1037
Cdd:PHA03307 275 WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSStssssESSRGAAVSPG----PSPSRS 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1038 PRRGMDDD----RGPRRGGADDERSSWRNADDDRGPRR---------GLDDDRGPRRGmdddRGPRRGMDDDRGPRRGMD 1104
Cdd:PHA03307 351 PSPSRPPPpadpSSPRKRPRPSRAPSSPAASAGRPTRRraraavagrARRRDATGRFP----AGRPRPSPLDAGAASGAF 426
|
250 260
....*....|....*....|.
gi 4503509 1105 DDRGPRrgLDDDRGPWRNADD 1125
Cdd:PHA03307 427 YARYPL--LTPSGEPWPGSPP 445
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
882-1037 |
3.97e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 882 SLSRKDSRWGDRDSEGTWRKGPEADSEwRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSlRPDDDRVPRRG 961
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRE-RSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSS-ESSRGAAVSPG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 962 MDDDRGPRRGPEEDRF-----SRRGADDDRPSWRNTDDDRPPRRiadedRGNWRHADD----DRPPRRGLDEDRGSWRTA 1032
Cdd:PHA03307 345 PSPSRSPSPSRPPPPAdpsspRKRPRPSRAPSSPAASAGRPTRR-----RARAAVAGRarrrDATGRFPAGRPRPSPLDA 419
|
....*
gi 4503509 1033 DEDRG 1037
Cdd:PHA03307 420 GAASG 424
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
919-1069 |
4.18e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 41.48 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 919 RRGEGRDEDRSHRRDEERPRRLGDDEDREPSLR---PDDDRVPRrgmdDDRGPRRGPEEDRfsrrGADDDRPSWRntddd 995
Cdd:PHA03321 461 RAQRARDAGPEYVDPLGALRRLPAGAAPPPEPAaapSPATYYTR----MGGGPPRLPPRNR----ATETLRPDWG----- 527
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503509 996 rPPRRIADEDRGN-WRHADDDRPPRRgldeDRGSWRTAdedrgprrgmdddRGPRRGGADDERSSWRNADDDRGP 1069
Cdd:PHA03321 528 -PPAAAPPEQMEDpYLEPDDDRFDRR----DGAAAAAT-------------SHPREAPAPDDDPIYEGVSDSEEP 584
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1127-1253 |
4.38e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 1127 RIPRRGAEDDRGPWRNMDDDRLSRRADDDR----------------FPRRGDDSRPGPWRPLVKPGGWREKEKAREESWG 1190
Cdd:PRK14086 100 PHARRTSEPELPRPGRRPYEGYGGPRADDRppglprqdqlptarpaYPAYQQRPEPGAWPRAADDYGWQQQRLGFPPRAP 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 1191 PPRESRPSEEREWDRE---KERDRDNQDREENDKdPERERDRERDVDREDRFRRPRDEGGWRRGPA 1253
Cdd:PRK14086 180 YASPASYAPEQERDREpydAGRPEYDQRRRDYDH-PRPDWDRPRRDRTDRPEPPPGAGHVHRGGPG 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
559-787 |
4.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 559 KNSRKEHQRILARRQTIEERKERLESLNIQREK------------EELEQREAELQKVrKAEEERLRQEAKEREKERILQ 626
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadevlEEHEERREELETL-EAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 627 EHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimakQVEQLEKEKKELQERLKNQ--------------- 691
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA---------RREELEDRDEELRDRLEECrvaaqahneeaeslr 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 692 EKKIDYFERAKRLEE--------IPLIKSAYEEQRIKDMDLWEQQEE--ERITTMQLEREKALEHKnrmSRMLEDRDLFV 761
Cdd:PRK02224 349 EDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFL---EELREERDELR 425
|
250 260
....*....|....*....|....*.
gi 4503509 762 MRLKAARQSvyeekLKQFEERLAEER 787
Cdd:PRK02224 426 EREAELEAT-----LRTARERVEEAE 446
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
543-691 |
4.76e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLniqreKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam09787 77 LQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERL-----QEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503509 623 RilqehEQIKKKT--------VRERLEQIKKTELGAKAFkdidiedLEELDPDF-IMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam09787 152 R-----NQLTSKSqssssqseLENRLHQLTETLIQKQTM-------LEALSTEKnSLVLQLERMEQQIKELQGEGSNG 217
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
910-1019 |
4.99e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 41.06 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 910 RRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRvpRRGMDDDRGPRRGPEEDRFSR----RGADDD 985
Cdd:TIGR01622 1 RYRDRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDR--HRDRDYYRGRERRSRSRRPNRryrpREKRRR 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 4503509 986 RP-SWRNTDDDRPPRR--IADEDRGNWRHADDDRPPR 1019
Cdd:TIGR01622 79 RGdSYRRRRDDRRSRRekPRARDGTPEPLTEDERDRR 115
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
563-701 |
5.05e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 563 KEHQRILARRQTIEERKERLEslniQREKEELEQREAELQKVRKAEEERL-RQEAKEREKERILQEHEqikKKTVRERLE 641
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREE----KHIERALEKQKEELDKLAEELSARLeEVRAADEAQLRLEFERE---REEIRESYE 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 642 QIKKTELGAKA------FKDIDIEDLEELDPDFiMAKQVEQLEKEKKELQERLKNQEKKIDYFERA 701
Cdd:pfam09731 364 EKLRTELERQAeaheehLKDVLVEQEIELQREF-LQDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
571-755 |
5.48e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 571 RRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQE-------AKEREKERILQEHEQIKKKtvRERLE 641
Cdd:TIGR00618 213 MPDTYHERKQVLEKElkHLREALQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELRAQEAVLEETQER--INRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 642 QIKKTELGAKAFKDIDiedleeLDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-----EEIPLIKSAYEE 716
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIE------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtlhsQEIHIRDAHEVA 364
|
170 180 190
....*....|....*....|....*....|....*....
gi 4503509 717 QRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLE 755
Cdd:TIGR00618 365 TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
517-752 |
6.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQ 676
Cdd:COG4372 142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503509 677 LEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSR 752
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
517-701 |
6.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 517 EQIRNQLTAMSSVLAKALEVIKPAHILQE--KEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLN--IQREKE 592
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 593 ELEQREAELQKVRKAEEERLRQEAK-EREKERILQEHEQikkktVRERLEQikktelgakAFKDIDIEDLEELDPDFIMA 671
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRlEKELEQAEEELDE-----LQDRLEA---------AEDLARLELRALLEERFAAA 758
|
170 180 190
....*....|....*....|....*....|
gi 4503509 672 KQVEQLEKEKKELQERLKNQEKKIDYFERA 701
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
570-645 |
6.81e-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: 40.35 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 570 ARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAK------EREKERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam02841 201 AKEKAIEAERAKAEAA--EAEQELLREKQKEEEQMMEAQERSYQEHVKqliekmEAEREQLLAEQERMLEHKLQEQEELL 278
|
..
gi 4503509 644 KK 645
Cdd:pfam02841 279 KE 280
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-798 |
7.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 516 SEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESlniQREKEELE 595
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 596 QREAELQKV-----RKAEEERLRQEAKEREKERILQEHEQIKKKTVRERL----EQIKKTELGAKAFKDIDIEDLEE-LD 665
Cdd:PTZ00121 1322 KKAEEAKKKadaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKkAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 666 PDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEipliKSAYEEQRIKDMdlwEQQEEERITTMQLEREKALE 745
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAE---EAKKAEEAKKKAEEAKKADE 1474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 4503509 746 HKNRMSrmlEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQR 798
Cdd:PTZ00121 1475 AKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
544-690 |
8.74e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 544 QEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL----EQREAELQKVRKAEEERLRQEAKER 619
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqkeEQLDARAEKLDNLENQLEEREKALS 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503509 620 EKERILQEheqiKKKTVRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKELQERLKN 690
Cdd:PRK12705 116 ARELELEE----LEKQLDNELYRV--AGLTPEQARKLLLKLLDaELEEE--KAQRVKKIEEEADLEAERKAQ 179
|
|
| PRK10864 |
PRK10864 |
putative methyltransferase; Provisional |
1064-1139 |
8.98e-03 |
|
putative methyltransferase; Provisional
Pssm-ID: 236779 [Multi-domain] Cd Length: 346 Bit Score: 40.15 E-value: 8.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503509 1064 DDDRGPRRGldddRGPRRGMDDDRGPRRGMDDdrGPRRGMDDDRGPR-RGLDDDRGPWRNadddriPRRGAEDDRGP 1139
Cdd:PRK10864 19 SDDDSDKRT----HNPRTGKGGGRPSGKSRAD--GGRRPARDDRNSQsRDRKWEDSPWRT------VSRAPGDETPE 83
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
1205-1257 |
9.14e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 40.26 E-value: 9.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 4503509 1205 REKERDRDNQDREENDKDPERERDRERDVDReDRFRRPRDEGGWRRGPAEESS 1257
Cdd:TIGR01642 1 RDEEPDREREKSRGRDRDRSSERPRRRSRDR-SRFRDRHRRSRERSYREDSRP 52
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
672-786 |
9.33e-03 |
|
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: 40.32 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 672 KQVEQLEKEKKELQERLKNQEKKIDyFERAKRLEEIPLIKSAYEEQRIKDmdlwEQQEEERITTMQLEREKALEHKNRMS 751
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELE-LEQQRRFEEIRLRKQRLEEERQRQ----EEEERKQRLQLQAAQERARQQQEEFR 429
|
90 100 110
....*....|....*....|....*....|....*
gi 4503509 752 RMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEE 786
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
535-659 |
9.44e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 535 EVIKPAHI---LQEKEEQHQLAvtayLKNSRKEHQRILARRQTieERKERLESLNIQREKEELEQREAELQKVRKAEEER 611
Cdd:COG2268 196 EIIRDARIaeaEAERETEIAIA----QANREAEEAELEQEREI--ETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 4503509 612 LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIE 659
Cdd:COG2268 270 IAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE 317
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
543-652 |
9.68e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503509 543 LQEKEEQHQLavtaylKNSRKEHQRILARrqtiEERKERLEslniQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:PRK09510 92 LQQKQAAEQE------RLKQLEKERLAAQ----EQKKQAEE----AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110
....*....|....*....|....*....|
gi 4503509 623 RILQEHEQIKKKtvRERLEQIKKTELGAKA 652
Cdd:PRK09510 158 AAAKKAAAEAKK--KAEAEAAKKAAAEAKK 185
|
|
| |
