|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
891-1104 |
7.77e-15 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 79.56 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 891 GEREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDAslRKDEEQVSRPDGEEEKGGSWRGTDDRGPKRG 970
Cdd:PRK12678 85 AAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR--ERGEAARRGAARKAGEGGEQPATEARADAAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 971 LEEDRGPRRGFEDDRGPRRGlDDDRGPRRGLDDDRvpRRGLDDDRGPRRGIDDDRAPRRGfDEDRGPRRGiDDDSGPRRG 1050
Cdd:PRK12678 163 RTEEEERDERRRRGDREDRQ-AEAERGERGRREER--GRDGDDRDRRDRREQGDRREERG-RRDGGDRRG-RRRRRDRRD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1726249934 1051 FDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFEDD 1104
Cdd:PRK12678 238 ARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELREDD 291
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
894-1114 |
2.05e-14 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 78.41 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 894 EESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEEEKGgswRGTDDRGPKRGLEE 973
Cdd:PRK12678 82 RAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK---AGEGGEQPATEARA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 974 DRGPRRgfEDDRGPRRGLDDDRGPRRGLDDDRVPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGpRRGIDDDSGPRRGFDD 1053
Cdd:PRK12678 159 DAAERT--EEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERG-RRDGGDRRGRRRRRDR 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726249934 1054 DRGPRRGFDDDRGPRRGfdDDRGPRRGfddDRGPRRGFDDDRGPRRGFEDDRVPRRGFEDD 1114
Cdd:PRK12678 236 RDARGDDNREDRGDRDG--DDGEGRGG---RRGRRFRDRDRRGRRGGDGGNEREPELREDD 291
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
901-1144 |
2.62e-14 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 78.02 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 901 GEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEEEKGGSwRGTDDRGPKRGLEEDRGPRRG 980
Cdd:PRK12678 62 GAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAA-SAPEAAQARERRERGEAARRG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 981 FEDDRGprrglDDDRGPRRGLDDDRVPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGPRRgiDDDSGPRRGFDDDRGPRRG 1060
Cdd:PRK12678 141 AARKAG-----EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE--ERGRDGDDRDRRDRREQGD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1061 FDDDRGpRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGfeDDRVPRRGfedDRGPRRGFEEDRGPRRGFDEDRGPRRG 1140
Cdd:PRK12678 214 RREERG-RRDGGDRRGRRRRRDRRDARGDDNREDRGDRDG--DDGEGRGG---RRGRRFRDRDRRGRRGGDGGNEREPEL 287
|
....
gi 1726249934 1141 FEDD 1144
Cdd:PRK12678 288 REDD 291
|
|
| PINT |
smart00088 |
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ... |
426-498 |
5.20e-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: 65.73 E-value: 5.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726249934 426 QYVPQLQSNTVLRLLQQVAQIYQTIEFSRLASLLPFvDAFLLERAIVDAARHCNLQVRIDHTSRTLSFGSDLN 498
Cdd:smart00088 1 QLVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
982-1211 |
5.08e-12 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 70.32 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 982 EDDRGPRRGLDDDRGPRRGLDDDRVPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGPRRGIDDDSGPRRGFDDDRGPRRgf 1061
Cdd:PRK12678 72 APAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGG-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1062 DDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFEDDRVPRRGFEDDRGPRRGFEEDRGPRRGFDEDRGPRRGF 1141
Cdd:PRK12678 150 EQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGR 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1142 EDDRAPRRGFDEDRtpsrgfDDDRGSWRGAADEDRGPRRGaadedrgpRRGADEDRGPRRGADEDRGQTP 1211
Cdd:PRK12678 230 RRRRDRRDARGDDN------REDRGDRDGDDGEGRGGRRG--------RRFRDRDRRGRRGGDGGNEREP 285
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
892-1084 |
1.09e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 69.55 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 892 EREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDASLRKDEEQVSR-PDGEEEKGGSWRGTDDRGPKRG 970
Cdd:PRK12678 104 AAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAaERTEEEERDERRRRGDREDRQA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 971 LEEDRGPRRGFEDDRGPRRGLDDDRGPRRGLDDDRvPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGPRRGIDDDsgprrg 1050
Cdd:PRK12678 184 EAERGERGRREERGRDGDDRDRRDRREQGDRREER-GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE------ 256
|
170 180 190
....*....|....*....|....*....|....*.
gi 1726249934 1051 FDDDRGPRRGFDDDRGPRRGFD--DDRGPRRGFDDD 1084
Cdd:PRK12678 257 GRGGRRGRRFRDRDRRGRRGGDggNEREPELREDDV 292
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-945 |
2.12e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 517 EHIRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQrilARRQTIEERKERLENLNIQREKEEHEQ 596
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAED---AKRVEIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 597 REA--------ELQKVRKAEEERLRQEAKEREKERILQE---HEQIKKKTVRERLEQIKKTEFGAKAFKDI----DIENL 661
Cdd:PTZ00121 1178 AEAarkaeevrKAEELRKAEDARKAEAARKAEEERKAEEarkAEDAKKAEAVKKAEEAKKDAEEAKKAEEErnneEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 662 EELDPDFIMAKQVEQLEKEKRELQDRLKNQE-KKIDYFERAKRLEEIPPLKKAYDEQRISDmELWEQQEEERISTLLLER 740
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEkKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 741 eKAVEHKNRMSRMLEDKESFVSELKASRQSVFEAKLKQFQERLAEEKHARLEERKRQRKEERRIAyyrdkeeEEQRLKEE 820
Cdd:PTZ00121 1337 -KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-------EEDKKKAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 821 QLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKKRQRELEIEERERKREEERrggddtlRKDTSRWGEREESGWRR 900
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK-------KAEEAKKADEAKKKAEE 1481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1726249934 901 GEEPDERKQAPPESiwRRAGQDSKPVRDEDHEADEdasLRKDEEQ 945
Cdd:PTZ00121 1482 AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADE---AKKAEEA 1521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-975 |
2.35e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 530 LSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQtieERKERLENLniqrEKEEHEQREAELQKvRKAEE 609
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA---EEAKKAEEA----KKKAEEAKKADEAK-KKAEE 1481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 610 ERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEFGAKAfkdidienlEEldpdfimAKQVEqlekEKRELQDRLK 689
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA---------DE-------AKKAE----EAKKADEAKK 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 690 NQEKKidyfeRAKRLEEIPPLKKAYDEQRISDmelwEQQEEERISTLLLERE--KAVEHKNRMSRMLEDKESFVSELKAS 767
Cdd:PTZ00121 1542 AEEKK-----KADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 768 RQSVfEAKLKQFQERLAEEKHARLEERKRQRKEERRIAYYRDKEEEEQrlkeeqLKQEQEEREKIENEKREAEQ-REYQE 846
Cdd:PTZ00121 1613 KKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN------KIKAAEEAKKAEEDKKKAEEaKKAEE 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 847 RIKKLEEQERKKRQRELEIEERERKREEERRGGDDTLRKDTSRWGEREESgwRRGEEPDERKqappesiwrragqdSKPV 926
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--KKEAEEDKKK--------------AEEA 1749
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1726249934 927 RDEDHEADEDASLRKDEEQVSRPDGEEEKGGSWRGTDDRGPKRGLEEDR 975
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PCI |
pfam01399 |
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ... |
405-494 |
1.17e-10 |
|
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: 59.92 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 405 DRVTKVLDWIKEQAEKEPELQQYVPQLQSNTVLRLLQQVAQIYQTIEFSRLASLLPFVDAFlLERAIVDAARHCNLQVRI 484
Cdd:pfam01399 16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLGLSVDE-VEKILAKLIRDGRIRAKI 94
|
90
....*....|
gi 1726249934 485 DHTSRTLSFG 494
Cdd:pfam01399 95 DQVNGIVVFS 104
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
943-1196 |
3.52e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 64.54 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 943 EEQVSRPDGEEEKGGSWRGTDDRGPKRGLEEDRGPRRGFEDDRGPRRGLDDDRGPRRGLDDDRVPRRGLDDDRGPRRGID 1022
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1023 DDRAPRRGFDEDRGPRRGIDDDSGPRRGfDDDRGPRRgfDDDRGPRRGFDDDRGPRRgfDDDRGPRRGFDDDRGPRRGFE 1102
Cdd:PRK12678 147 EGGEQPATEARADAAERTEEEERDERRR-RGDREDRQ--AEAERGERGRREERGRDG--DDRDRRDRREQGDRREERGRR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1103 DDrvprrgfEDDRGPRRGFEEDRGPRRGFDEDRGPRRGfeDDRAPRRGFDEDRtpsrgfDDDRgswrgaadEDRGPRRGA 1182
Cdd:PRK12678 222 DG-------GDRRGRRRRRDRRDARGDDNREDRGDRDG--DDGEGRGGRRGRR------FRDR--------DRRGRRGGD 278
|
250
....*....|....
gi 1726249934 1183 ADEDRGPRRGADED 1196
Cdd:PRK12678 279 GGNEREPELREDDV 292
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
835-1064 |
3.71e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 64.54 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 835 EKREAEQREYQERIKKLEEQERKKRQRELEIEERERKREEERRGGDDTLRKDTSRWGEREESGWRRGEEPDERKQAPPES 914
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 915 iwRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEEEKGGSWRGTDDRGPKRGLEEDRGPRRGFEDDRGPRRGLDDD 994
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 995 RGPRRGLDDDRVPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGPRRgiDDDSGPRRGFDDDRGPRRGFDDD 1064
Cdd:PRK12678 225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNEREPELREDDV 292
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-928 |
1.36e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 530 LSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKvRKAEE 609
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK-KKADE 1501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 610 ERLRQEAKEREKEriLQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELDpDFIMAKQVEQLEKEKRELQDRLK 689
Cdd:PTZ00121 1502 AKKAAEAKKKADE--AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 690 NQEKKidyfERAKRLEE--IPPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKEsfVSELKAS 767
Cdd:PTZ00121 1579 ALRKA----EEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE--KKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 768 RQSVFEAKLKQFQERLAEEKHARLEERKRQRKEERRIAyyrdkeEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQER 847
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 848 IKKLEEQERKKRQRELEIEererkREEERRGGDDTLRKDTSRWGEREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVR 927
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKK-----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
.
gi 1726249934 928 D 928
Cdd:PTZ00121 1802 D 1802
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
829-1054 |
5.10e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 60.69 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 829 REKIENEKREAEQREYQERIKKLEEQERKKRQRELEIEERERKREEERRGGDDTLRKDTSRWGEREESGWRRGEEPDERK 908
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 909 QAPPESiwRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEE--EKGGSWRGTDDRGPKRGLEEDRGPRRGFEDDRG 986
Cdd:PRK12678 147 EGGEQP--ATEARADAAERTEEEERDERRRRGDREDRQAEAERGErgRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726249934 987 PRRG--LDDDRGPRRGLDDDRVPRRGLDDDRGPRRGidddRAPRRGFDEDRGPRRGIDDDSG--PRRGFDDD 1054
Cdd:PRK12678 225 DRRGrrRRRDRRDARGDDNREDRGDRDGDDGEGRGG----RRGRRFRDRDRRGRRGGDGGNErePELREDDV 292
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-853 |
6.84e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 564 EHQRILARR-QTIEERKERLENL-------NIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT 635
Cdd:COG1196 206 ERQAEKAERyRELKEELKELEAEllllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 636 VRERLEQIKKTEfgAKAFKDIDIENLEELDpdfiMAKQVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEIPPLKKAYD 715
Cdd:COG1196 286 AQAEEYELLAEL--ARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 716 EQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESfVSELKASRQSVFEAKLKQFQERLAEEKHARLEERK 795
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726249934 796 RQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEE 853
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-791 |
7.44e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 540 AHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENL-----NIQREKEEHEQREAELQKVRKAEEERLRQ 614
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELeeeleELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 615 EAKEREKERILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELdpdfimAKQVEQLEKEKRELQDRLKNQEKK 694
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------LERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 695 IDYFERAKRLEEippLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEA 774
Cdd:COG1196 437 EEEEEEALEEAA---EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
250
....*....|....*..
gi 1726249934 775 KLKQFQERLAEEKHARL 791
Cdd:COG1196 514 LLLAGLRGLAGAVAVLI 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-791 |
1.11e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 540 AHVLQEKEEQHQIAIVSYQKNSRKEHQRILarRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKER 619
Cdd:COG1196 215 YRELKEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 620 EKERILQ-----EHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELdpdfimAKQVEQLEKEKRELQDRLKNQEKk 694
Cdd:COG1196 293 LLAELARleqdiARLEERRRELEERLEELEEELAELEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEE- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 695 idyfERAKRLEEIPPLKKAYDEQRISDMELwEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEA 774
Cdd:COG1196 366 ----ALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250
....*....|....*..
gi 1726249934 775 KLKQFQERLAEEKHARL 791
Cdd:COG1196 441 EEALEEAAEEEAELEEE 457
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
549-860 |
1.44e-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: 59.37 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 549 QHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEaKEREKERILQEH 628
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 629 EqikkktvRERLEQIKKTEFGakafkdIDIENLEELDpdfimAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRL-EEI 707
Cdd:pfam17380 358 R-------KRELERIRQEEIA------MEISRMRELE-----RLQMERQQKNERVRQELEAARKVKILEEERQRKIqQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 708 PPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESfvselkaSRQSVFEAKLKQFQERLAEEK 787
Cdd:pfam17380 420 VEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE-------RKRKKLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726249934 788 HARLEERKRQRKEERRIAYYRdkeeeeqrlkeeqlkqeqeEREKIENEKREAEQREYQERIKKLEEQERKKRQ 860
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEER-------------------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQ 546
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
558-769 |
2.41e-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: 58.60 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 558 QKNSRKEHQRILARRQTI--EERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT 635
Cdd:pfam17380 389 QKNERVRQELEAARKVKIleEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 636 VRERLEQIKKTEFGAKAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEipplkkayd 715
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE--------- 539
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1726249934 716 EQRISDMELWEQ---QEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQ 769
Cdd:pfam17380 540 EERRKQQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
558-975 |
3.98e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 558 QKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQK---VRKAEEERLRQEAKEREKER---ILQEHEQI 631
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeARKAEDARKAEEARKAEDAKrveIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 632 KKKTVRERLEQIKKTEFGAKAfkdIDIENLEELDP--DFIMAKQVEQLEKEKRELQDRLKNQEKKIdyfERAKRLEEI-P 708
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKA---EEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAkK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 709 PLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESF--VSELKAS--RQSVFEAKLKQFQERLA 784
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkADEAKKAeeKKKADEAKKKAEEAKKA 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 785 EE---KHARLEERKRQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEE----QERK 857
Cdd:PTZ00121 1318 DEakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkaDEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 858 KRQRELEIEERERKREEERRGGDDTLRKDTSRWGEREESGwRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEda 937
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE-- 1474
|
410 420 430
....*....|....*....|....*....|....*...
gi 1726249934 938 sLRKDEEQVSRPDGEEEKGGSWRGTDDRGPKRGLEEDR 975
Cdd:PTZ00121 1475 -AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
541-858 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 541 HVLQEKEEQHQIAIvsyQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKERE 620
Cdd:pfam02463 202 LKEQAKKALEYYQL---KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 621 KERILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDidienleeldpdfimaKQVEQLEKEKRELQDRLKNQEKKIDYFER 700
Cdd:pfam02463 279 KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE----------------EKLKESEKEKKKAEKELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 701 AKRLEEIpplKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSvfEAKLKQFQ 780
Cdd:pfam02463 343 ELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL--LLELARQL 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726249934 781 ERLAEEKHARLEERKRQRKEERRIAyYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIELK-QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
519-768 |
2.79e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 519 IRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLniqrekeehEQRE 598
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---------EEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 599 AELQKVRKAEEERLRQeakEREKERILQEHEQIKKK--TVRERLEQIKKtefgakafkdiDIENLEEldpdfiMAKQVEQ 676
Cdd:PRK03918 283 KELKELKEKAEEYIKL---SEFYEEYLDELREIEKRlsRLEEEINGIEE-----------RIKELEE------KEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 677 LEKEKRELQDRLKNQEKKIDYFERAKRL-EEIPPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLE 755
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
250
....*....|...
gi 1726249934 756 DKESFVSELKASR 768
Cdd:PRK03918 423 ELKKAIEELKKAK 435
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
576-858 |
4.05e-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: 54.98 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 576 EERKERLENLNIQREKEEHEQREAELQKVRKAEEERL-------RQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEF 648
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 649 GAKAFKDIDIENLEELDPDFIMAKQVEQlEKEKRELQDRLKNQEKKidyferakrlEEIPPLKKAYDEQRISDMELWEQQ 728
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEI-EKEEEKLAQVLKENKEE----------EKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 729 EEERISTLLLEREKAVEHKNRMSRmLEDKESFVSELKASRQSVFEAKLKQFQERLAEEKHARLEERKRQRKEERRIAYYR 808
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKK-AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1726249934 809 DKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE 430
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
879-1043 |
4.16e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 54.52 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 879 GDDTLRKDTSRWGEREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEEEKGGS 958
Cdd:PRK12678 137 ARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 959 WRGTDDRGPKRGlEEDRGPRRGFEDDRGPRRGLDDDRGPRRGLDDDRvPRRGLDDDRGPRRGID--DDRAPRRGFDEDRG 1036
Cdd:PRK12678 217 ERGRRDGGDRRG-RRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRR-GRRFRDRDRRGRRGGDggNEREPELREDDVLV 294
|
....*..
gi 1726249934 1037 PRRGIDD 1043
Cdd:PRK12678 295 PVAGILD 301
|
|
| COG4253 |
COG4253 |
Uncharacterized conserved protein, DUF2345 family [Function unknown]; |
880-1147 |
5.58e-07 |
|
Uncharacterized conserved protein, DUF2345 family [Function unknown];
Pssm-ID: 443395 [Multi-domain] Cd Length: 900 Bit Score: 54.28 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 880 DDTLRKDTSRWGEREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDASLRKDEEQVSRPDGEEEKGGSW 959
Cdd:COG4253 254 SAADAGSLSGSGGDGGAAGGSLAEATSSLRVPAASVSLARYQRARRAAAAAAAADARAGGADAAGGVGTGGGRRLAAGLA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 960 RGTDDRGPKRGLEEDRGPRRGFEDDRGPRRGLDDDRGPRRGLDDDRVPRRGLDDDRGP------RRGIDDDRAPRRGFDE 1033
Cdd:COG4253 334 GAAAEEEEAVGAEARARRRRLLRAARAAIRLLAAAALALLALGRGALAGRSPAAAAGPgivggtDRRARRRATAFVDRAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1034 DRGPRRGIDDDSGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFEDDRVPRRGFED 1113
Cdd:COG4253 414 GPPPRTQRARRPLLPRPRGAGGPPPRVVSTRAGDTPSADDDDGGRRVVRDDRRVAWVGGGESWGAGGGAGAGGGVGGGVV 493
|
250 260 270
....*....|....*....|....*....|....
gi 1726249934 1114 DRGprRGFEEDRGPRRGFDEDRGPRRGFEDDRAP 1147
Cdd:COG4253 494 PLL--GDGDVVIAAEGGGPPAPGGGAPAAHSAAH 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-790 |
5.98e-07 |
|
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: 54.29 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 516 SEHIRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIV--SYQKNSRKEHQrilarrqtIEERKERLENLNIQREKEE 593
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQ--------KQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 594 HEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT----VRERLEQIKKTEFGAKAFKDIDIENLEELdpdfi 669
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaeleELESRLEELEEQLETLRSKVAQLELQIAS----- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 670 MAKQVEQLEKEKRELQDRLKNQEKkidyfERAKRLEEIPPLKKAYDEQRIS--DMELWEQQEE-ERISTLLLEREKAVEH 746
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQ-----EIEELLKKLEEAELKELQAELEelEEELEELQEElERLEEALEELREELEE 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1726249934 747 KNRMSRMLEDKESFVSELKASRQSVFEaKLKQFQERLAEEKHAR 790
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQE-NLEGFSEGVKALLKNQ 515
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
543-854 |
6.17e-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: 54.30 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERlenlnIQREKEEHEQREAELQKVRKAEEERLRQEAKERE-- 620
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlr 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 621 -KERILQEHEQIKK--KTVRERLEQIKKTEFG-AKAFKDID--IENLEELDpdfimaKQVEQLEKEKRELQDRLKNQEKk 694
Cdd:TIGR02169 292 vKEKIGELEAEIASleRSIAEKERELEDAEERlAKLEAEIDklLAEIEELE------REIEEERKRRDKLTEEYAELKE- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 695 idyfERAKRLEEIPPLKKAYDEQRISDMelweqQEEERISTLLLEREkavEHKNRMSRMLEDKESFVSELKASRQ--SVF 772
Cdd:TIGR02169 365 ----ELEDLRAELEEVDKEFAETRDELK-----DYREKLEKLKREIN---ELKRELDRLQEELQRLSEELADLNAaiAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 773 EAKLKQFQERLaEEKHARLEERKRQRKEERRIayyrdkeeeeqrlkeeqlkqeqeeREKIENEKR--EAEQREYQERIKK 850
Cdd:TIGR02169 433 EAKINELEEEK-EDKALEIKKQEWKLEQLAAD------------------------LSKYEQELYdlKEEYDRVEKELSK 487
|
....
gi 1726249934 851 LEEQ 854
Cdd:TIGR02169 488 LQRE 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
562-858 |
9.52e-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: 53.82 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 562 RKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQK-VRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERL 640
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 641 EQIKKTEFGAKAFKDIDIENLEELDpdfiMAKQVEQLEKEKRELQDRLKNQEKKIdyFERAKRLEEIPPLKKAYDEQRIS 720
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENK----EEEKEKKLQEEELKLLAKEEEELKSE--LLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 721 DMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEAKLKQFQERLAEEKhaRLEERKRQRKE 800
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK--LKEEELELKSE 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726249934 801 ERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
480-858 |
1.19e-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: 53.44 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 480 LQVRIDHTSRTLSFGSDLNYSTREDAPVGPFLQNMPSEHIRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIVsyQK 559
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL--KK 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 560 NSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLrqEAKEREKERILQEHEQIKKKTVRER 639
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEK 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 640 LEQIKKTEFGAKAFKDIDIENLEELDPDfimakQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIPPLKKAYDEQRI 719
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEE-----QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 720 SDMELWEQQEEERISTLLLEREKAVEHKNrmsrmlEDKESFVSELKASRQSVFEAKLKQFQERLAEEKHARLEERKRQRK 799
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL 941
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726249934 800 EERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
562-975 |
1.97e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 562 RKEHQRILARRQTIEERKERLENLNIQREKEEhEQREAElqKVRKAEEERLRQEAKEREKERILQEHEQiKKKTVRERLE 641
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKAD--ELKKAEEKKKADEAKKAEEKKKADEAKK-KAEEAKKADE 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 642 QIKKTEFGAKAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEippLKKAYDEQRISD 721
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADA---AKKKAEEKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 722 mELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKA---SRQSVFEAKLKQFQERLAEEKHARLEERKRQR 798
Cdd:PTZ00121 1395 -EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 799 KEERRIAYYRDKEEEEQRLKEEQLKQEQEerEKIENEKREAEQREYQERIKKLEE----QERKKRQRELEIEERERKREE 874
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKADEakkaEEAKKADEAKKAEEKKKADEL 1551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 875 ERRggdDTLRK--------DTSRWGEREESGWRRGEEPDERKQAPPESIWRRAGQDSKPVRDEDHEADEDaslRKDEEQV 946
Cdd:PTZ00121 1552 KKA---EELKKaeekkkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEEL 1625
|
410 420
....*....|....*....|....*....
gi 1726249934 947 SRPDgEEEKGGSWRGTDDRGPKRGLEEDR 975
Cdd:PTZ00121 1626 KKAE-EEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-785 |
2.35e-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: 52.38 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 562 RKEHQRILARRQT----IEERKERLENLniQREKEEHEQREAELQKVRKAEEERLRQEAKERE--KERILQEHEQIKKKT 635
Cdd:TIGR02169 722 EKEIEQLEQEEEKlkerLEELEEDLSSL--EQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQAE 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 636 VRERLEQIKKTEfgaKAFKDIDIEnLEELDPDfimakqVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEIpPLKKAYD 715
Cdd:TIGR02169 800 LSKLEEEVSRIE---ARLREIEQK-LNRLTLE------KEYLEKEIQELQEQRIDLKEQIK--SIEKEIENL-NGKKEEL 866
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 716 EQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVsELKASRQSVFEAKLKQFQERLAE 785
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSE 935
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
514-775 |
3.69e-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: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 514 MPSEHIRN-QLTAMSSVLS---KAVATIKPAHVLQEKEEQHQIaivsyqKNSRKEHQRILARRQTIEERKERLENlNIQR 589
Cdd:pfam05483 480 LEKEKLKNiELTAHCDKLLlenKELTQEASDMTLELKKHQEDI------INCKKQEERMLKQIENLEEKEMNLRD-ELES 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 590 EKEEHEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQI---KKKTVRERLEQIKKTEFGAKAFKDIDIENLEELD 665
Cdd:pfam05483 553 VREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 666 PDFIMAKQVE-QLEKEKRELQDRLKNQEKKID--YFERAKRLEEIPPLKKAYDEQRISDMELwEQQEEERISTLLLEREK 742
Cdd:pfam05483 633 AYEIKVNKLElELASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEAVKLQKEI-DKRCQHKIAEMVALMEK 711
|
250 260 270
....*....|....*....|....*....|...
gi 1726249934 743 aveHKNRMSRMLEDKESFVSELKASRQSVFEAK 775
Cdd:pfam05483 712 ---HKHQYDKIIEERDSELGLYKNKEQEQSSAK 741
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
532-687 |
4.38e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 532 KAVATIKPAHVLQEKEEQHQIaivsyqknsRKEHQR-ILARRQTIEERKERL----ENLNiqREKEEHEQREAELQKVRK 606
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHKL---------RNEFEKeLRERRNELQKLEKRLlqkeENLD--RKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 607 AEEERLRQ-EAKEREKERILQEHeqikkktvRERLEQIKK-TEFGAKAfkdIDIENLE-ELDPDfiMAKQVEQLEKEKRE 683
Cdd:PRK12704 118 ELEQKQQElEKKEEELEELIEEQ--------LQELERISGlTAEEAKE---ILLEKVEeEARHE--AAVLIKEIEEEAKE 184
|
....
gi 1726249934 684 LQDR 687
Cdd:PRK12704 185 EADK 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-858 |
7.55e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 555 VSYQKNSRKEHQRILARRQT--------IEERKERLENLNIQREK------------------------EEHEQREAELQ 602
Cdd:TIGR02168 167 ISKYKERRKETERKLERTREnldrlediLNELERQLKSLERQAEKaerykelkaelrelelallvlrleELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 603 KVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKKTEFGAKAFKDIDIENLEELDpdfimaKQVEQLEKEKR 682
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILR------ERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 683 ELQDRL-KNQEKKIDYFERAKRLE-EIPPLKKAYDEQRISDMELWEQQEEerISTLLLEREKAVEHKNRMSRMLEDKEsf 760
Cdd:TIGR02168 320 ELEAQLeELESKLDELAEELAELEeKLEELKEELESLEAELEELEAELEE--LESRLEELEEQLETLRSKVAQLELQI-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 761 vsELKASRQSVFEAKLKQFQERLaeekhARLEERKRQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAE 840
Cdd:TIGR02168 396 --ASLNNEIERLEARLERLEDRR-----ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
330
....*....|....*....
gi 1726249934 841 Q-REYQERIKKLEEQERKK 858
Cdd:TIGR02168 469 ElEEAEQALDAAERELAQL 487
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1026-1232 |
1.05e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.90 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1026 APRRGFDEDRGPRRGIDDDSGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFDDDRGPRRGFEDDR 1105
Cdd:PRK12678 64 AAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAAR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1106 VPRRGFEDDRGPRRGFEEDRGPRRGFDEDRGPRRGFEDDRAPRRGFDEDRTPSRGFDDDRGSWRGAADEDRGPRRGaaDE 1185
Cdd:PRK12678 144 KAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERG--RR 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1726249934 1186 DRGPRRGaDEDRGPRRGADEDRGQTPWKPIVASRPGGWREREKARED 1232
Cdd:PRK12678 222 DGGDRRG-RRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFR 267
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
544-858 |
1.08e-05 |
|
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: 50.07 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 544 QEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEER----KERLENL--NIQREKEEHEQREAELQKVRKAEEERLRQEAK 617
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeeklKERLEELeeDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 618 EREKE-----RILQEHEQIKKKTVRERLEQIKKTEfgaKAFKDIDIEnLEELDPDfimakqVEQLEKEKRELQDRLKNQE 692
Cdd:TIGR02169 777 LEEALndleaRLSHSRIPEIQAELSKLEEEVSRIE---ARLREIEQK-LNRLTLE------KEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 693 KKIDyfERAKRLEEIPpLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVsELKASRQSVF 772
Cdd:TIGR02169 847 EQIK--SIEKEIENLN-GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI-EKKRKRLSEL 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 773 EAKLKQFQERLA--EEKHARLEERKRQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIE------NEKREAEQREY 844
Cdd:TIGR02169 923 KAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLkrldelKEKRAKLEEER 1002
|
330
....*....|....
gi 1726249934 845 QERIKKLEEQERKK 858
Cdd:TIGR02169 1003 KAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
572-857 |
1.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 572 RQTIEERKERLENL-----NIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKerilqeheqikkktVRERLEQIKKT 646
Cdd:PRK03918 171 IKEIKRRIERLEKFikrteNIEELIKEKEKELEEVLREINEISSELPELREELEK--------------LEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 647 EfgakafkdidiENLEELDpdfimaKQVEQLEKEKRELQDRLKNQEKKI--------DYFERAKRLEEIPPLKKAYDEQR 718
Cdd:PRK03918 237 K-----------EEIEELE------KELESLEGSKRKLEEKIRELEERIeelkkeieELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 719 isdmELWEQQEEErISTLLLEREKAVEHKNRMSRMLEDKESFVSELKAsrqsvFEAKLKQFQERLAE-EKHARLeerkrq 797
Cdd:PRK03918 300 ----EFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEKEERLEE-----LKKKLKELEKRLEElEERHEL------ 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 798 rkeerriayYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREyqeriKKLEEQERK 857
Cdd:PRK03918 364 ---------YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK-----EEIEEEISK 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
575-858 |
1.76e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 575 IEERKERLENLNIQREK--------EEHEQREAELQ----KVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQ 642
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 643 ikktefgakAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEIpplkkaydEQRIsdm 722
Cdd:COG1196 275 ---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAEL--------EEEL--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 723 elweQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEAKLKQFQERLAEEkharleerkrqrkeer 802
Cdd:COG1196 333 ----EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL---------------- 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1726249934 803 riayyRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:COG1196 393 -----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
556-791 |
2.03e-05 |
|
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: 49.30 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 556 SYQKNSRKEHQRILARRQTIEERKERLENLniQREKEEHEQREAELQKVRKAEEERLRqeAKEREKERILQEHEqikkkT 635
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSL--QSELRRIENRLDELSQELSDASRKIG--EIEKEIEQLEQEEE-----K 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 636 VRERLEQ----IKKTEFGAKAFKDIDIENLEELDPdfiMAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIPPLK 711
Cdd:TIGR02169 735 LKERLEEleedLSSLEQEIENVKSELKELEARIEE---LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 712 KAYD--EQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKAsrqsvfEAKLKQFQERLAEEKHA 789
Cdd:TIGR02169 812 ARLReiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE------ELEELEAALRDLESRLG 885
|
..
gi 1726249934 790 RL 791
Cdd:TIGR02169 886 DL 887
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
588-731 |
2.95e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 588 QREKEEhEQREAELQKVRKAEEERLRQEAKEREKERilQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELDPD 667
Cdd:PRK09510 80 QRKKKE-QQQAEELQQKQAAEQERLKQLEKERLAAQ--EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726249934 668 FIMAKQVEQlEKEKRELQDRLKNQEKkidyfERAKRLEEIPPLKKAYDEQRISDMELWEQQEEE 731
Cdd:PRK09510 157 AAAAKKAAA-EAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
537-787 |
3.00e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 537 IKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLEnlniQREKEEHEQREAELQKVRKAEEERLRQEA 616
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE----ALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 617 KEREKERILQEhEQIKKKTVRER--LEQIKKTEFGAKAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKK 694
Cdd:PTZ00121 1722 KKAEEENKIKA-EEAKKEAEEDKkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 695 IDYFERAKRLEEIPPLKKAYDEQRiSDMELWEQQEEERISTLLLEREKAVEhKNRMSRMLEDKESFVSELKASRQSVFea 774
Cdd:PTZ00121 1801 KDIFDNFANIIEGGKEGNLVINDS-KEMEDSAIKEVADSKNMQLEEADAFE-KHKFNKNNENGEDGNKEADFNKEKDL-- 1876
|
250
....*....|...
gi 1726249934 775 kLKQFQERLAEEK 787
Cdd:PTZ00121 1877 -KEDDEEEIEEAD 1888
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
566-685 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 566 QRILARRQTIEE---RKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEH-EQIKKKTVRERLE 641
Cdd:cd16269 173 QEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHlRQLKEKMEEEREN 252
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1726249934 642 QIKKTEfGAKAFKDIDIENLEELDpdfiMAKQVEQLEKEKRELQ 685
Cdd:cd16269 253 LLKEQE-RALESKLKEQEALLEEG----FKEQAELLQEEIRSLK 291
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
558-785 |
3.84e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 558 QKNSRKEHQRILARRQTIEERKERLENLNIQREK------------EEHEQREAELQKVrKAEEERLRQEAKEREKERIL 625
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadevlEEHEERREELETL-EAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 626 QEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEEldpdfimakQVEQLEKEKRELQDRLKNQEKKIDYF------- 698
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA---------RREELEDRDEELRDRLEECRVAAQAHneeaesl 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 699 -ERAKRLEEipPLKKAYDEQRISDMELWEQQE-----EERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSV- 771
Cdd:PRK02224 348 rEDADDLEE--RAEELREEAAELESELEEAREavedrREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELr 425
|
250
....*....|....*....
gi 1726249934 772 -----FEAKLKQFQERLAE 785
Cdd:PRK02224 426 ereaeLEATLRTARERVEE 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-696 |
4.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 569 LARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIkktef 648
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE----- 736
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1726249934 649 gakafkdIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKID 696
Cdd:COG1196 737 -------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
543-858 |
4.81e-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: 48.13 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEHQRilARRQTIEERKERLENL--NIQREKEEHEQREAELQKVRKAEEE--------RL 612
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELE--ELQEELKEAEEELEELtaELQELEEKLEELRLEVSELEEEIEElqkelyalAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 613 RQEAKEREKERILQEHEQIKKKTVR--ERLEQIKKTefgakafKDIDIENLEELdpdfimAKQVEQLEKEKRELQDRLKN 690
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEEleAQLEELESK-------LDELAEELAEL------EEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 691 QEKKidYFERAKRLEEippLKKAYDEQR--ISDMELWEQQEEERISTLllerekavehKNRMSRMLEDKESFVSELKASR 768
Cdd:TIGR02168 363 LEAE--LEELESRLEE---LEEQLETLRskVAQLELQIASLNNEIERL----------EARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 769 QSVFEAKLKQFQERLAEEKHARLEERKRQRKEERRIAYYRDKEEEeqrlkeeqlkqeqeEREKIENEKREAEQreYQERI 848
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE--------------AEQALDAAERELAQ--LQARL 491
|
330
....*....|
gi 1726249934 849 KKLEEQERKK 858
Cdd:TIGR02168 492 DSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
562-781 |
4.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 562 RKEHQRILARRQT---IEERKERLENLNIQ---REKEEHEQREAELQKVrKAEEERLRQEAK---EREKERILQEHeqiK 632
Cdd:PRK03918 489 LKKESELIKLKELaeqLKELEEKLKKYNLEeleKKAEEYEKLKEKLIKL-KGEIKSLKKELEkleELKKKLAELEK---K 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 633 KKTVRERLEQIKK--TEFGAKAFKDID--IENLEELDPDFIMAKQVEQ--------LEKEKRELQDRLKNQEKKIDYFER 700
Cdd:PRK03918 565 LDELEEELAELLKelEELGFESVEELEerLKELEPFYNEYLELKDAEKelereekeLKKLEEELDKAFEELAETEKRLEE 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 701 A-KRLEEippLKKAYDEQRI------------------SDMELWEQQEEERISTL------LLEREKAVEHKNRMSRMLE 755
Cdd:PRK03918 645 LrKELEE---LEKKYSEEEYeelreeylelsrelaglrAELEELEKRREEIKKTLeklkeeLEEREKAKKELEKLEKALE 721
|
250 260
....*....|....*....|....*.
gi 1726249934 756 DKESFVSELKASRQSVFEAKLKQFQE 781
Cdd:PRK03918 722 RVEELREKVKKYKALLKERALSKVGE 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-786 |
5.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 563 KEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQK-VRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDALREELDELEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 642 QIKktefgakafkdidienleeldpdfimaKQVEQLEKEKRELQDRLKNQEkkidyfERAKRLE-EIPPLKKAYDEQRIS 720
Cdd:COG4913 342 QLE---------------------------REIERLERELEERERRRARLE------ALLAALGlPLPASAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1726249934 721 DMELWEQQEEERISTllleREKAVEHKNRMSRMLEDKESFVSELKA--SRQSVFEAKLKQFQERLAEE 786
Cdd:COG4913 389 AAALLEALEEELEAL----EEALAEAEAALRDLRRELRELEAEIASleRRKSNIPARLLALRDALAEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-942 |
5.81e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 517 EHIRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQ 596
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR-ERLEQIKKTEFGAKAFKDIDIENLEELDPDFIMAKQVE 675
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 676 QLEKEKRELQDRLKNQ---EKKIDYFERAKRLEEIPPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSR 752
Cdd:COG1196 514 LLLAGLRGLAGAVAVLigvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 753 MLEdkESFVSELKASRQSVFEAKLKQFQERLAEEKHARLEERKRQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKI 832
Cdd:COG1196 594 RGA--IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 833 ENEKREAEQREYQERIKKLEEQERKKRQRELEIeererkREEERRGGDDTLRKDTSRWGEREESGWRRGEEPDERKQAPP 912
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEE------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
410 420 430
....*....|....*....|....*....|
gi 1726249934 913 ESIWRRAGQDSKPVRDEDHEADEDASLRKD 942
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
587-757 |
6.14e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 587 IQREKEEHEQREAELQKVRKAEEERLrqEAKEREKERILQEHEQIKK------KTVRERLEQIKKTEfgaKAFKDiDIEN 660
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKK--EAEAIKKEALLEAKEEIHKlrnefeKELRERRNELQKLE---KRLLQ-KEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 661 LEeldpdfimaKQVEQLEKEKRELQDRLKNQEKKIDYFE-RAKRLEEIppLKKAYDE-QRISDMelweQQEEERisTLLL 738
Cdd:PRK12704 98 LD---------RKLELLEKREEELEKKEKELEQKQQELEkKEEELEEL--IEEQLQElERISGL----TAEEAK--EILL 160
|
170 180
....*....|....*....|.
gi 1726249934 739 E--REKAVEHKNRMSRMLEDK 757
Cdd:PRK12704 161 EkvEEEARHEAAVLIKEIEEE 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-853 |
6.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 545 EKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKerlenlniqreKEEHEQREAELQKVRKAEEERLRQEAKEREKERI 624
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELI-----------KEKEKELEEVLREINEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 625 LQEHEQIKkktvrERLEQIKKtefgakafkdiDIENLEeldpdfimaKQVEQLEKEKRELQDRLKNQEKKIDYFE-RAKR 703
Cdd:PRK03918 230 VKELEELK-----EEIEELEK-----------ELESLE---------GSKRKLEEKIRELEERIEELKKEIEELEeKVKE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 704 LEEIPPLKKAYDEQRisdmELWEQQEEErISTLLLEREKAVEHKNRMSRMLEDKESFVSELKAsrqsvFEAKLKQFQERL 783
Cdd:PRK03918 285 LKELKEKAEEYIKLS----EFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEKEERLEE-----LKKKLKELEKRL 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726249934 784 AE-EKHARLeerkrqrkeerriayYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQR--EYQERIKKLEE 853
Cdd:PRK03918 355 EElEERHEL---------------YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkeEIEEEISKITA 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-698 |
8.69e-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: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 521 NQLTAMSSVLSKAVATIK-PAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREkEEHEQREA 599
Cdd:TIGR02168 799 KALREALDELRAELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEA 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 600 ELQKVRKAEEERLRQEAKEREKERILQEHEQIKKK------TVRERLEQIKKTEFGAKAFKDIDIENLEE---LDPDFIM 670
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSElrreleELREKLAQLELRLEGLEVRIDNLQERLSEeysLTLEEAE 957
|
170 180
....*....|....*....|....*...
gi 1726249934 671 AKQVEqLEKEKRELQDRLKNQEKKIDYF 698
Cdd:TIGR02168 958 ALENK-IEDDEEEARRRLKRLENKIKEL 984
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
543-657 |
8.84e-05 |
|
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: 46.38 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEE-HEQREAELQKVRKAEEERLRQE--AKER 619
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEaKAKQAAEAKAKAEAEAERKAKEeaAKQA 152
|
90 100 110
....*....|....*....|....*....|....*...
gi 1726249934 620 EKERILQEHEQIKKKtvreRLEQIKKTEFGAKAFKDID 657
Cdd:TIGR02794 153 EEEAKAKAAAEAKKK----AEEAKKKAEAEAKAKAEAE 186
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1133-1336 |
8.87e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1133 EDRGPRRGfEDDRAPRRGFDEDRTPSRGFDDDRGSWRGAADEDRGPRRGAADEDRGPRRGADEDRGPRRGADEDRGQTPW 1212
Cdd:PHA03307 203 SPRPPRRS-SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1213 KPIVASRPG-GWREREKAREDSWGPPHESKPAEERSWAkRGEESEKDSERDKHPVREESVWRRGGDDNVTPRKVSPGDKS 1291
Cdd:PHA03307 282 PGPASSSSSpRERSPSPSPSSPGSGPAPSSPRASSSSS-SSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1726249934 1292 TDDKTEPRDRRRVPPKTDEASPWRRDEEKESRQE-ERGTPRGAPAV 1336
Cdd:PHA03307 361 DPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVaGRARRRDATGR 406
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
576-854 |
1.02e-04 |
|
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: 46.94 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 576 EERKERLENLNIQreKEEHEQREAELQKVRKAEEERLRQeaKEREKERILQEHEQIKKKTVRERlEQIKKTEfGAKAFKD 655
Cdd:TIGR04523 380 QSYKQEIKNLESQ--INDLESKIQNQEKLNQQKDEQIKK--LQQEKELLEKEIERLKETIIKNN-SEIKDLT-NQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 656 IDIENLEELDPDFimAKQVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEIPPLKKAYdEQRISDMElweqqeeERIST 735
Cdd:TIGR04523 454 LIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKELKKLNEEKKEL-EEKVKDLT-------KKISS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 736 LLLEREKAVEHKNRMSRMLEDKESFVSELKAS-RQSVFEAKLKQFQERLAEEKHarleerkrqrkeerriayyrdkeeee 814
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQ-------------------------- 575
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1726249934 815 qrlkeeqlkqeqeerekiENEKREAEQREYQERIKKLEEQ 854
Cdd:TIGR04523 576 ------------------TQKSLKKKQEEKQELIDQKEKE 597
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1122-1351 |
1.53e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.05 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1122 EEDRGPRRGFDEDRGPRRGFEDDRAPRRGFDEDRTPSRGFDDDRGSWRGAADEDRGPRRGAADEDRGpRRGADEDRGPRR 1201
Cdd:PRK12678 71 AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAA-RRGAARKAGEGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1202 GAD--EDRGQTPWKPIVASRPGGWREREKAREDSWGPPHESKPAEERswAKRGEESEKDSERDKHPVREESVWRRGGDDN 1279
Cdd:PRK12678 150 EQPatEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREER--GRDGDDRDRRDRREQGDRREERGRRDGGDRR 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1726249934 1280 VTPRKVSPGDKSTDDKTEPRDRRRvppkTDEASPWRRDEEKESRQEERGTPRGapavDREKPSWNTEKEEKD 1351
Cdd:PRK12678 228 GRRRRRDRRDARGDDNREDRGDRD----GDDGEGRGGRRGRRFRDRDRRGRRG----GDGGNEREPELREDD 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
562-852 |
1.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 562 RKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKktVRERLE 641
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK--LKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 642 QIKKTEFGAKAfkdiDIENLEELDpdfimaKQVEQLEKEKRELQDRLKNQEKKI------DYFERAKRLEEIPPLKKAYD 715
Cdd:PRK03918 536 KLKGEIKSLKK----ELEKLEELK------KKLAELEKKLDELEEELAELLKELeelgfeSVEELEERLKELEPFYNEYL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 716 EQRISDMELweQQEEERISTLLLEREKAVEhknrmsrMLEDKESFVSELKAsrqsvfeaKLKQFQERLAEEKHARLEERk 795
Cdd:PRK03918 606 ELKDAEKEL--EREEKELKKLEEELDKAFE-------ELAETEKRLEELRK--------ELEELEKKYSEEEYEELREE- 667
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726249934 796 rqrkeerriayYRDKEEEEQRLKEEQLKQEQEERE---KIENEKREAEQR-EYQERIKKLE 852
Cdd:PRK03918 668 -----------YLELSRELAGLRAELEELEKRREEikkTLEKLKEELEEReKAKKELEKLE 717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
543-707 |
1.94e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQiAIVSYQKNSRKEHQRIlarRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQ-------- 614
Cdd:COG4717 83 AEEKEEEYA-ELQEELEELEEELEEL---EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 615 EAKEREKERILQEHEQIKKKTVRERLEQIKKTEfgaKAFKDIdIENLEELDpdfimaKQVEQLEKEKRELQDRLKNQEKK 694
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATE---EELQDL-AEELEELQ------QRLAELEEELEEAQEELEELEEE 228
|
170
....*....|...
gi 1726249934 695 IDYFERAKRLEEI 707
Cdd:COG4717 229 LEQLENELEAAAL 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-854 |
2.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 561 SRKEHQRILARRQTIEERKERLENL---------NIQREKEEHEQREAELQKVRKAEEERLRQEAKEREK-ERILQEHEQ 630
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELeekiaelekALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 631 ikkktVRERLEQIKKTEFGAKAFKDIDIENLEELDPDFIMAKQV-EQLEKEKRELQDRLKNQEKKIDYFERAKRLEEI-- 707
Cdd:TIGR02168 745 -----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEea 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 708 --PPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEA------KLKQF 779
Cdd:TIGR02168 820 anLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAlallrsELEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 780 QERLAEEKHARLEERKRQRKEERRIAYYRdkeeeeqrLKEEQ-LKQEQEEREKIENE-------------KREAEQREYQ 845
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLE--------LRLEGlEVRIDNLQERLSEEysltleeaealenKIEDDEEEAR 971
|
....*....
gi 1726249934 846 ERIKKLEEQ 854
Cdd:TIGR02168 972 RRLKRLENK 980
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
564-745 |
2.88e-04 |
|
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: 44.15 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 564 EHQRILARRQTIEERKERLEnlniqREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQI 643
Cdd:COG1579 4 EDLRALLDLQELDSELDRLE-----HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 644 KKTEFGAKAFKdiDIENLE-ELDpdfIMAKQVEQLEKEKRELQDRLKNQEKKIDYFE--RAKRLEEIPPLKKAYDEQris 720
Cdd:COG1579 79 EEQLGNVRNNK--EYEALQkEIE---SLKRRISDLEDEILELMERIEELEEELAELEaeLAELEAELEEKKAELDEE--- 150
|
170 180
....*....|....*....|....*
gi 1726249934 721 dmelwEQQEEERISTLLLEREKAVE 745
Cdd:COG1579 151 -----LAELEAELEELEAEREELAA 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
572-707 |
3.29e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 572 RQTIEERKERLENLNIQREKE-EHEQREAELQKvrKAEEERLRQEA----KEREKE------RILQEHEQIKKKtvrerL 640
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEaEAIKKEALLEA--KEEIHKLRNEFekelRERRNElqklekRLLQKEENLDRK-----L 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1726249934 641 EQIKKTEfgakafkdidienlEELDpdfimaKQVEQLEKEKRELQDRLKNQEKKIDyfERAKRLEEI 707
Cdd:PRK12704 103 ELLEKRE--------------EELE------KKEKELEQKQQELEKKEEELEELIE--EQLQELERI 147
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
543-645 |
3.83e-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: 45.11 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRK-------------AEE 609
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKllekemeerqkaiYEE 532
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1726249934 610 ERLRQEAKEREKERILQEHEQIKKKTV-----RERLEQIKK 645
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRkateeRSRLEAMER 573
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
996-1220 |
4.23e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 996 GPRRGLDDDRVPRRGLDDDRGPRRGIDDDRAPRRGFDEDRGPRRGIDDDSGPRRGFDDDRGPR--------RGFDDDRGP 1067
Cdd:PHA03307 190 PAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPEnecplprpAPITLPTRI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1068 RRGF-DDDRGPRRGFDDDRGPRRGFDDDRGPRRGFEDDRVPRRGFEDDRGPRRGFEEDRGPRRGF-DEDRGPRRGFEDDR 1145
Cdd:PHA03307 270 WEASgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSEsSRGAAVSPGPSPSR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1146 APRRG-----FDEDRTPSRGFDDDRGSWRGAADEDRGPRRGAADEDRGPRRgadEDRGPRRGADEDRGQTPWKPIVASRP 1220
Cdd:PHA03307 350 SPSPSrppppADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARR---RDATGRFPAGRPRPSPLDAGAASGAF 426
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
542-643 |
4.54e-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: 44.73 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 542 VLQEKEEQHQIAIVSyQKNSRKEHQRILARRQT-IEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKERE 620
Cdd:pfam17380 496 ILEKELEERKQAMIE-EERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
90 100
....*....|....*....|...
gi 1726249934 621 KERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam17380 575 REMMRQIVESEKARAEYEATTPI 597
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-713 |
4.64e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 566 QRILAR-RQTIEERKERLENLnIqrEKEEHEQREAElQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQik 644
Cdd:PRK00409 501 ENIIEEaKKLIGEDKEKLNEL-I--ASLEELERELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK-LLEEAEK-- 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 645 ktefgaKAFKDIDienleeldpdfiMAKQ-VEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIPPLKKA 713
Cdd:PRK00409 574 ------EAQQAIK------------EAKKeADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
559-858 |
4.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 559 KNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEE------RLRQEAKEREKERILQEHEQIK 632
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKitarigELKKEIKELKKAIEELKKAKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 633 KKTVRERLEQIKKTEFGAKAFKDI-DIEN-LEELDpdfimaKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIPPL 710
Cdd:PRK03918 438 CPVCGRELTEEHRKELLEEYTAELkRIEKeLKEIE------EKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 711 KKAYDEQRIS-DMELWEQQEEE------RISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQSVFEAKLKQFQE-- 781
Cdd:PRK03918 512 LKKYNLEELEkKAEEYEKLKEKliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEle 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 782 ---RLAEEKHARLEERKRQRKEERRIAYYRDKEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:PRK03918 592 erlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
542-701 |
5.23e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 542 VLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLN--IQREKEEHEQREAELQKVRKAEEERLRqeaKER 619
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeLEEKDERIERLERELSEARSEERREIR---KDR 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 620 EKERILQEHEQIKKK--TVRERLEQIKKTEFGAKAFKDIDIENleeldpDFIMAKQVEQLEKEK-RELQDRLKNQEKKID 696
Cdd:COG2433 466 EISRLDREIERLEREleEERERIEELKRKLERLKELWKLEHSG------ELVPVKVVEKFTKEAiRRLEEEYGLKEGDVV 539
|
....*
gi 1726249934 697 YFERA 701
Cdd:COG2433 540 YLRDA 544
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
833-1027 |
5.79e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 833 ENEKREAEQREYQERIKKLEEQERKkRQRELEIEERERKREEERRGGDDTLRKdtsrwGEREESGWRRGEEPDERKQApp 912
Cdd:PRK12678 127 ARERRERGEAARRGAARKAGEGGEQ-PATEARADAAERTEEEERDERRRRGDR-----EDRQAEAERGERGRREERGR-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 913 esiwrragqdskpvRDEDHEADEDASLRKDEEQVSRPDGEEEKGGSWRGTDDRGPKRGLEEDRGPRRGfeDDRGPRRGLD 992
Cdd:PRK12678 199 --------------DGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDG--DDGEGRGGRR 262
|
170 180 190
....*....|....*....|....*....|....*
gi 1726249934 993 DDRGPRRglDDDRVPRRGLDDDRGPRRGIDDDRAP 1027
Cdd:PRK12678 263 GRRFRDR--DRRGRRGGDGGNEREPELREDDVLVP 295
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
563-783 |
6.69e-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: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 563 KEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEE-ERLRQEAKER----EKERILQEHEQIKKKTVR 637
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEaVRTNPEINDRirllEQEVARYKEESGKAQAEV 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 638 ERLEQIKKTEFGAKAFKDIDIENLEELDPdfimaKQVEQLEKEKRELQDrLKNQEKKidyfERAKRLEEipPLKKAYDEQ 717
Cdd:pfam10174 582 ERLLGILREVENEKNDKDKKIAELESLTL-----RQMKEQNKKVANIKH-GQQEMKK----KGAQLLEE--ARRREDNLA 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1726249934 718 RISDmelwEQQEEERISTLLLEREKAVEHKNRMS---RMLEDKESFVSELKASRQSVFEAKLKQFQERL 783
Cdd:pfam10174 650 DNSQ----QLQLEELMGALEKTRQELDATKARLSstqQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
543-712 |
7.10e-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: 43.40 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEhqrILARRQTIEERKERLENLNIQ-REK-----EEHEQREAELQKV-RKAEEERLRQE 615
Cdd:pfam09728 93 LAKEEEEKRKELSEKFQSTLKD---IQDKMEEKSEKNNKLREENEElREKlksliEQYELRELHFEKLlKTKELEVQLAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 616 AK----EREKERILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELDpDFI----------------MAKQVE 675
Cdd:pfam09728 170 AKlqqaTEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQ-DTLnksnevfttfkkemekMSKKIK 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 1726249934 676 QLEKEKRELQDRLKNQEKKIDYF--ERAKRLEEIPPLKK 712
Cdd:pfam09728 249 KLEKENLTWKRKWEKSNKALLEMaeERQKLKEELEKLQK 287
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
572-683 |
9.73e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 572 RQTIEERKERLENLNIQREKE----EHEQREAELQKVRkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTe 647
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREietaRIAEAEAELAKKK--AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE- 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 1726249934 648 fgakafKDIDIENLEEldpdfimAKQVEQLEKEKRE 683
Cdd:COG2268 290 ------REIELQEKEA-------EREEAELEADVRK 312
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
571-706 |
1.31e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 571 RRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQeaKEREKERiLQEHEQIKKKTVRERLEQIK------ 644
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR--LEEQVER-LEAEVEELEAELEEKDERIErlerel 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1726249934 645 ---KTEFGAKAFKDIDIENLEEldpdfimakQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEE 706
Cdd:COG2433 451 seaRSEERREIRKDREISRLDR---------EIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
974-1092 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 974 DRGPRRGFEDDRGPRRGLDDDRGPRRGLDDDRVPRRgldDDRGPRRGIDDDRAPRRGFDEDRGPRRGIDDDSgprRGFDD 1053
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDR---HRRSRERSYREDSRPRDRRRYDSRSPRSLRYSS---VRRSR 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1726249934 1054 DRGPRRGFDDDRGPR-RGFDDDRGPRRGFDDDRGPRRGFD 1092
Cdd:TIGR01642 76 DRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWD 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
511-756 |
1.50e-03 |
|
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: 43.13 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 511 LQNMPSEHIRNQLTAMSSVLSKAVATIKPA--HVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQtIEERKERLENLNIQ 588
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-IKSIEKEIENLNGK 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 589 reKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELDPDF 668
Cdd:TIGR02169 863 --KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 669 IMAKQV-------EQLEKEKRELQDRLKNQE----KKIDYFER-AKRLEEIPPLKKAYDEQRISDMELWEQQEEERISTL 736
Cdd:TIGR02169 941 GEDEEIpeeelslEDVQAELQRVEEEIRALEpvnmLAIQEYEEvLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVF 1020
|
250 260
....*....|....*....|
gi 1726249934 737 LLEREKAVEHKNRMSRMLED 756
Cdd:TIGR02169 1021 MEAFEAINENFNEIFAELSG 1040
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
544-635 |
1.69e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 544 QEKEEQHQIAivsyqknsRKEHQRILARrQTIEERKERLEnlniqREKEEHEQREAELQKVRKAEEERLRQEAKEREKER 623
Cdd:PRK05035 433 QAKAEIRAIE--------QEKKKAEEAK-ARFEARQARLE-----REKAAREARHKKAAEARAAKDKDAVAAALARVKAK 498
|
90
....*....|..
gi 1726249934 624 ILQEHEQIKKKT 635
Cdd:PRK05035 499 KAAATQPIVIKA 510
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
985-1230 |
1.74e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 42.64 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 985 RGPRRGLDDDRGPRRGLDDDRVPRRGLDDDRGPrrgidDDRAPRRGFDEdrgprRGIDDDSGPRRGFDDDRGP-RRGfdd 1063
Cdd:PHA03321 458 RRARAQRARDAGPEYVDPLGALRRLPAGAAPPP-----EPAAAPSPATY-----YTRMGGGPPRLPPRNRATEtLRP--- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1064 DRGPRRGF--DDDRGPRRGFDDDRGPRR----GFDDDRGPRRGFEDDRVPRRGFEDDRGPRrgFEEDRGPRRGFDEDRGP 1137
Cdd:PHA03321 525 DWGPPAAAppEQMEDPYLEPDDDRFDRRdgaaAAATSHPREAPAPDDDPIYEGVSDSEEPV--YEEIPTPRVYQNPLPRP 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1138 RRGFE---DDRAPRRGFDEDRTPSRGFDDD-RGSWRGAAdedrgpRRGAADEDRGPRRGADEDRGPRRGADEDRGQTPWK 1213
Cdd:PHA03321 603 MEGAGeppDLDAPTSPWVEEENPIYGWGDSpLFSPPPAA------RFPPPDPALSPEPPALPAHRPRPGALAPDGPANLA 676
|
250
....*....|....*..
gi 1726249934 1214 PIVASRPGGWREREKAR 1230
Cdd:PHA03321 677 ALSAMLTKLRHDRRHSW 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
571-858 |
1.98e-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: 42.65 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 571 RRQTIEERKERLENL--NIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKK--TVRERLEQIKKT 646
Cdd:TIGR00618 213 MPDTYHERKQVLEKElkHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVleETQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 647 EfgakafkdidienleeldPDFIMAKQVEQLEKEKRELQDRLKNQEKkidyfERAKRLEEIPPLKK---AYDEQRISDME 723
Cdd:TIGR00618 293 A------------------PLAAHIKAVTQIEQQAQRIHTELQSKMR-----SRAKLLMKRAAHVKqqsSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 724 LWEQQEEERIST-----LLLEREKAVEHKNRMSRMLEDKESFVSELKAsrqsvfeakLKQFQERLAEEKHARLEERKRQR 798
Cdd:TIGR00618 350 LHSQEIHIRDAHevatsIREISCQQHTLTQHIHTLQQQKTTLTQKLQS---------LCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 799 KEERRIAYYRdkEEEEQRLKEEQLKQEQEEREKIENEKREAEQREYQERIKKLEEQERKK 858
Cdd:TIGR00618 421 DLQGQLAHAK--KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
416-789 |
2.78e-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: 42.26 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 416 EQAEKEPELQQYVPQLQsnTVLRLLQQVAQIYQTIEFSRLASLLPFVDAFLLERAIVDAARHCNLQVRIDHTSRTLSFGS 495
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIE--ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 496 DLNYSTREDAPVGPFLQNMPSEHIR-----NQLTAMSSVLSKAVATIKPAHVLQE-------------------KEEQHQ 551
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHirdahEVATSIREISCQQHTLTQHIHTLQQqkttltqklqslckeldilQREQAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 552 IAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAkerEKERILQEHEQi 631
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---TKEQIHLQETR- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 632 KKKTVRERLEQIKKTEFGAK------AFKDIDIENLEELDPdfimakQVEQLEKEKRELQDRLKNQEKKIDYF-ERAKRL 704
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCgscihpNPARQDIDNPGPLTR------RMQRGEQTYAQLETSEEDVYHQLTSErKQRASL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 705 -EEIPPLKKAYDEQRISDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVS-ELKASRQSVfEAKLKQFQER 782
Cdd:TIGR00618 562 kEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKlQPEQDLQDV-RLHLQQCSQE 640
|
....*..
gi 1726249934 783 LAEEKHA 789
Cdd:TIGR00618 641 LALKLTA 647
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
543-791 |
3.08e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 543 LQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 623 RILQEHEQIKKKtVRERLEQIKKTEfgakafkdidiENLEELDPDFIMAKQVEQL-EKEKRELQDRLKNQEKKIDYFERA 701
Cdd:pfam13868 177 EIEEEKEREIAR-LRAQQEKAQDEK-----------AERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 702 KRLEEIPPLKKAYDEQRISDMELWEQQEEERISTLLLE--REKAVEHKNRMSRMLEDKESFVSELKASRQSVFEAKLKQF 779
Cdd:pfam13868 245 IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEkrRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
250
....*....|..
gi 1726249934 780 QERLAEEKHARL 791
Cdd:pfam13868 325 AERRERIEEERQ 336
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
573-790 |
3.18e-03 |
|
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: 42.02 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 573 QTIEERKERLENLNiqREKEEHEQREAELQKVRKAEEERLRQEAKEREKE----RILQEHEQIKKKTVRERLEQIKKTEF 648
Cdd:pfam05483 328 QLTEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 649 GAKAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKIDYFE---------RAKRLEEIPPLKKAYDEQRI 719
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltaiktsEEHYLKEVEDLKTELEKEKL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1726249934 720 SDMELWEQQEEeristLLLEREKAVEHKNRMSRMLEDKESFVSELKASRqsvfEAKLKQFQERLAEEKHAR 790
Cdd:pfam05483 486 KNIELTAHCDK-----LLLENKELTQEASDMTLELKKHQEDIINCKKQE----ERMLKQIENLEEKEMNLR 547
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
566-759 |
3.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 566 QRILARRQTIEERKERLENLNIQREKEEHEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtvRERLEQIKK 645
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 646 TEFGAKAFKDIDIEnLEELDP--DFIMAK--QVEQLEKEKRELQDRLKNQEKKIDyferaKRLEEIPPLKKAYDEQRISD 721
Cdd:COG4717 127 LLPLYQELEALEAE-LAELPErlEELEERleELRELEEELEELEAELAELQEELE-----ELLEQLSLATEEELQDLAEE 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 1726249934 722 MELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKES 759
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
575-694 |
4.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 575 IEERKERLENLNIqrekeEHEQREAELQKVRKaEEERLRQEAKEREKEriLQEHEQIKKKTVRERLEQIKKTefgAKAFK 654
Cdd:PRK00409 518 LNELIASLEELER-----ELEQKAEEAEALLK-EAEKLKEELEEKKEK--LQEEEDKLLEEAEKEAQQAIKE---AKKEA 586
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1726249934 655 DIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKK 694
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
576-758 |
4.15e-03 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 576 EERKERLENLNIQREKEEHEQREAELQKVR--KAEEERLRQEAKEREK---ERILQEHEQIKKKTVRERLeQIKKTEFGA 650
Cdd:pfam12297 213 EEYERKMAALAAECNLETREKMEAQHQREMaeKEEAEELLKHADEQEAlecSSLLDKLHKLEQEHLQRSL-LLRQEEDFA 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 651 KAFKDIDIENLEELDPDF----IMAKQVEQLEKE--KRELQDRLKNQ---EKKIDYFERAKR--LEEipplKKAYDEQRI 719
Cdd:pfam12297 292 KAQRQLAVFQRVELHKIFftqlKEATRKGELKPEaaKRLLQDYSKIQeqiEELMDFFQANQRyhLSE----RFAQREYLV 367
|
170 180 190
....*....|....*....|....*....|....*....
gi 1726249934 720 SDMELWEQQEEERISTLLLEREKAVEHKNRMSRMLEDKE 758
Cdd:pfam12297 368 QSLQSLETRVSGLLNTAATQLTSLIQKMERAGYLDEEQM 406
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
539-749 |
4.74e-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: 41.09 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 539 PAHVLQEKEEQHQIAivsyqkNSRKEHQRILARRQTIE-ERKERLENLNIQREKEEHEQR---EAELQKVRKAEEERLRQ 614
Cdd:pfam15709 320 PSKALLEKREQEKAS------RDRLRAERAEMRRLEVErKRREQEEQRRLQQEQLERAEKmreELELEQQRRFEEIRLRK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 615 EAKEREKERilQEHEQIKK----KTVRERLEQiKKTEFGAKAFKDIDIENLEEldpdfimAKQVEQLEKEKRELQDRLKN 690
Cdd:pfam15709 394 QRLEEERQR--QEEEERKQrlqlQAAQERARQ-QQEEFRRKLQELQRKKQQEE-------AERAEAEKQRQKELEMQLAE 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1726249934 691 QEKKIDYFERAKRLEEIPPLKKAyDEQRISDMELWEQQEEERISTLLLEREKAVEHKNR 749
Cdd:pfam15709 464 EQKRLMEMAEEERLEYQRQKQEA-EEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
575-717 |
4.99e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 575 IEERKErlenlNIQREKEEHEqreaelQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKKTEfgakafk 654
Cdd:PRK00409 504 IEEAKK-----LIGEDKEKLN------ELIASLEELERELEQKAEEAEALLKEAEKLKEE-LEEKKEKLQEEE------- 564
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726249934 655 DIDIENLEEldpdfIMAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIpplKKAYDEQ 717
Cdd:PRK00409 565 DKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEA---RKRLNKA 619
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
544-838 |
5.07e-03 |
|
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: 41.50 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 544 QEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLNIQREKEEHEQREAELQKvrkaEEERLRQEAKEREKER 623
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE----EEQLLIEQEEKIKEEE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 624 ILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKidyfERAKR 703
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEE----SQKLN 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 704 LEEIPPLKKAYDEQRISDMELwEQQEEERISTLLLEREKAVEHKNRMSRMLEDKESFVSELKASRQ---SVFEAKLKQFQ 780
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILL-KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlmAIEEFEEKEER 989
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1726249934 781 ERLAEEKHARLEERKRQRKeerriayYRDKEEEEQRLKEEQLKQEQEEREKIENEKRE 838
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLI-------RAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
552-784 |
5.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 552 IAIVSYQKNSRKEHQRILARRQTIEERkERLENLNIQREKEEHEqREAELQKVRKAEEERLRQEAKEREKErILQEHEQI 631
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPAL-EELEEEELEELLAALG-LPPDLSPEELLELLDRIEELQELLRE-AEELEEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 632 KKKTVRERLEQIkktefgakaFKDIDIENLEELDPDFIMAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIpplk 711
Cdd:COG4717 364 QLEELEQEIAAL---------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---- 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1726249934 712 kaydEQRISDMELWEQQEEERISTLlleREKAVEHKNRMSRMLEDKEsfVSELKASRQSVfEAKLKQFQERLA 784
Cdd:COG4717 431 ----EEELEELEEELEELEEELEEL---REELAELEAELEQLEEDGE--LAELLQELEEL-KAELRELAEEWA 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
544-652 |
5.47e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 544 QEKEEQHQIAIVSYQKNSRKEHQRILA---RRQTIEERKERLENlniQREKEEHEQREAELQKVR-KAEEERLRQEAKER 619
Cdd:PRK09510 87 QQAEELQQKQAAEQERLKQLEKERLAAqeqKKQAEEAAKQAALK---QKQAEEAAAKAAAAAKAKaEAEAKRAAAAAKKA 163
|
90 100 110
....*....|....*....|....*....|...
gi 1726249934 620 EKERILQEHEQIKKKTVRerlEQIKKTEFGAKA 652
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAA---EAKKKAEAEAAA 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-745 |
5.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 519 IRNQLTAMSSVLSKAVATIKPAHVLQEKEEQHQIAIVSYQK---NSRKEHQRILARRQTIEERKERLENLnIQREKEEHE 595
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKelaALKKEEKALLKQLAALERRIAALARR-IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 596 QREAELQKVRKaEEERLRQEAKEREKE-----RILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDI---DIENLEELDPD 667
Cdd:COG4942 80 ALEAELAELEK-EIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLapaRREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 668 FI-MAKQVEQLEKEKRELQDRLKNQEKKIDYFERAK----RLEEIPPLKKAYDEQRISDMELWEQQEEERISTLLLEREK 742
Cdd:COG4942 159 LAeLAALRAELEAERAELEALLAELEEERAALEALKaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
...
gi 1726249934 743 AVE 745
Cdd:COG4942 239 AAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-702 |
5.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 530 LSKAVATIKPAHVLQEKEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLniqREKEEHEQREAELQKVRKAEE 609
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEEDKKKAEEAKKDEEEK 1756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 610 ERLRQEAKEREK--ERILQEH-----EQIKKKTVRERLEQIKKTEFGAKAFKDIdIENLEELDPDFIMAKQVEqlEKEKR 682
Cdd:PTZ00121 1757 KKIAHLKKEEEKkaEEIRKEKeavieEELDEEDEKRRMEVDKKIKDIFDNFANI-IEGGKEGNLVINDSKEME--DSAIK 1833
|
170 180
....*....|....*....|
gi 1726249934 683 ELQDRLKNQEKKIDYFERAK 702
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHK 1853
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
1104-1201 |
7.50e-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: 40.65 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 1104 DRVPRRGFEDDRGPRRGFEEDRGPRRGFDEDR--------GPRRGFEDDRAPRRGFDEDRTPSRGFDDDRGSWRGAADED 1175
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRfrdrhrrsRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPRRR 81
|
90 100
....*....|....*....|....*.
gi 1726249934 1176 RGPRRGAADEDRGPRrgadeDRGPRR 1201
Cdd:TIGR01642 82 SRSVRSIEQHRRRLR-----DRSPSN 102
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
559-622 |
7.71e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 40.24 E-value: 7.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1726249934 559 KNSRKEHQRILARrqtiEERKERLENLNIQREKEEHEQREAELQKVrkAEEERLRQEAKEREKE 622
Cdd:pfam07946 263 KKTREEEIEKIKK----AAEEERAEEAQEKKEEAKKKEREEKLAKL--SPEEQRKYEEKERKKE 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
517-695 |
9.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 517 EHIRNQLTAMSSVLSKAVATIKPAHVLQE--KEEQHQIAIVSYQKNSRKEHQRILARRQTIEERKERLENLN--IQREKE 592
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726249934 593 EHEQREAELQKVRKAEEERLRQEAK-EREKERILQEHEQikkktVRERLEQIKKTEFGAKAFkDIDiENLEELDPDFIMA 671
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRlEKELEQAEEELDE-----LQDRLEAAEDLARLELRA-LLE-ERFAAALGDAVER 765
|
170 180
....*....|....*....|....
gi 1726249934 672 KQVEQLEKEKRELQDRLKNQEKKI 695
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEEL 789
|
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| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
588-740 |
9.59e-03 |
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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: 39.83 E-value: 9.59e-03
10 20 30 40 50 60 70 80
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gi 1726249934 588 QREKEEHEQREAELQKVRKAEEERLRQ---------EAKEREKER--ILQEHEQIKKKTVRERLEQIKKTEFGAKAFKDI 656
Cdd:TIGR02794 67 QERQKKLEQQAEEAEKQRAAEQARQKEleqraaaekAAKQAEQAAkqAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE 146
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90 100 110 120 130 140 150 160
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gi 1726249934 657 DIENLEELDPdfiMAKQVEQLEKEKRELQDRLKNQEKKIDYFERAKRLEEIPPLKKAYDEQRISDMELWEQQEEERISTL 736
Cdd:TIGR02794 147 EAAKQAEEEA---KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
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gi 1726249934 737 LLER 740
Cdd:TIGR02794 224 EAER 227
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