|
Name |
Accession |
Description |
Interval |
E-value |
| PINT |
smart00088 |
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ... |
426-498 |
6.19e-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: 6.19e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146219837 426 QYVPQLQNNTILRLLQQVAQIYQSIEFSRLTSLVPFvDAFQLERAIVDAARHCDLQVRIDHTSRTLSFGSDLN 498
Cdd:smart00088 1 QLVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
900-1127 |
1.24e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 69.16 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 900 RKGPEADSEWRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRFSR 979
Cdd:PRK12678 59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 980 RGTDDDRPswRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGLDDERGSWRTADEDRGPR-RGMDDDRGPRRGGADDERS 1058
Cdd:PRK12678 139 RGAARKAG--EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERgRDGDDRDRRDRREQGDRRE 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146219837 1059 SWRNADDDRGPRRGMDDDRGPRRGLDDDRGPWRNAAEDRISRRGADDDRGPWRNmDDDRVPRRGDDARP 1127
Cdd:PRK12678 217 ERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD-RRGRRGGDGGNERE 284
|
|
| PCI |
pfam01399 |
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ... |
405-494 |
5.28e-11 |
|
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15).
Pssm-ID: 460195 Cd Length: 105 Bit Score: 60.69 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 405 ERVTKVLNWVREQPEKEPELQQYVPQLQNNTILRLLQQVAQIYQSIEFSRLTSLVPfVDAFQLERAIVDAARHCDLQVRI 484
Cdd:pfam01399 16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLG-LSVDEVEKILAKLIRDGRIRAKI 94
|
90
....*....|
gi 146219837 485 DHTSRTLSFG 494
Cdd:pfam01399 95 DQVNGIVVFS 104
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
549-804 |
1.29e-10 |
|
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: 65.92 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 549 QHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEaKEREKERILQEH 628
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 629 EqikkktvRERLEQIKKTELGAKAFKdidIEDLEELdpdfimakQVEQLEKEKKELQERLKNQEKKIDYFERAKRLE--- 705
Cdd:pfam17380 358 R-------KRELERIRQEEIAMEISR---MRELERL--------QMERQQKNERVRQELEAARKVKILEEERQRKIQqqk 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 706 -EIPLIKSAYEEQRVKDMDLWEQQ---EEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEE 781
Cdd:pfam17380 420 vEMEQIRAEQEEARQREVRRLEEErarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260
....*....|....*....|...
gi 146219837 782 RLAEERHSRLEDRKRQRKEERKI 804
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEM 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
564-804 |
3.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 564 EHQRILARR-QTIEERKERLESL-------NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT 635
Cdd:COG1196 206 ERQAEKAERyRELKEELKELEAEllllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 636 VRERLEQIKKTELGAKAFKDIDIEDLEELDPDFI-MAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSA- 713
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEe 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 714 ----YEEQRVKDMDLWEQQEEERITTMQ--LEREKALEHKNRMSRMLEDRDLfvmRLKAARQSVyEEKLKQFEERLAEER 787
Cdd:COG1196 366 alleAEAELAEAEEELEELAEELLEALRaaAELAAQLEELEEAEEALLERLE---RLEEELEEL-EEALAELEEEEEEEE 441
|
250
....*....|....*..
gi 146219837 788 HSRLEDRKRQRKEERKI 804
Cdd:COG1196 442 EALEEAAEEEAELEEEE 458
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
880-1086 |
4.68e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 64.15 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 880 DDPLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEkewRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPR 959
Cdd:PRK12678 91 EQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQ---ARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 960 RGLDDDRGPRRGPDEDRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHTDDDrpprrglDDERGSWRTADEDRGPR 1039
Cdd:PRK12678 168 ERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDG-------GDRRGRRRRRDRRDARG 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 146219837 1040 RGMDDDRGPRRGGADDERsswrnadDDRGPRRGMDDDRGPRRGLDDD 1086
Cdd:PRK12678 241 DDNREDRGDRDGDDGEGR-------GGRRGRRFRDRDRRGRRGGDGG 280
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
903-1066 |
6.31e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 63.77 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 903 PEADSEWRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRfSRRGT 982
Cdd:PRK12678 123 EAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREER-GRDGD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 983 DDDRPSWRNADDDRP--PRRIGDDDRGSWRHTDDDRPPRRGLDDERGSWRTAD-EDRG---PRRGMDDDRGPRRGGADDE 1056
Cdd:PRK12678 202 DRDRRDRREQGDRREerGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDgEGRGgrrGRRFRDRDRRGRRGGDGGN 281
|
170
....*....|
gi 146219837 1057 RSSWRNADDD 1066
Cdd:PRK12678 282 EREPELREDD 291
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-858 |
1.61e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 530 LAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKvRKAEE 609
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK-KKADE 1501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 610 ERLRQEAKEREKEriLQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLeeldpdfimaKQVEQLEK--EKKELQER 687
Cdd:PTZ00121 1502 AKKAAEAKKKADE--AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL----------KKAEELKKaeEKKKAEEA 1569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 688 LKNQEKKIDYFERA---KRLEE--IPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDrdlfvm 762
Cdd:PTZ00121 1570 KKAEEDKNMALRKAeeaKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA------ 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 763 rlkaarqsvyEEKLKQFEERLAEERHS-RLEDRKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAER-AKREEE 840
Cdd:PTZ00121 1644 ----------EEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAE 1713
|
330
....*....|....*...
gi 146219837 841 LREYQERVKKLEEVERKK 858
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-822 |
2.93e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 530 LAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRK----EHQRILARRQTIEERKERLESLniQREKEELEQREAELQK-- 603
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadEAKKKAEEAKKADEAKKKAEEA--KKKADEAKKAAEAKKKad 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 604 -VRKAEEERLRQEAKEREKERilqEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIM----AKQVEQLE 678
Cdd:PTZ00121 1514 eAKKAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMalrkAEEAKKAE 1590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 679 KEKKELQERLKNQEKKIDYfERAKRLEEIPL----IKSAyEEQRVKDMDLWEQQEEERITTMQLEREkalEHKNRMSRML 754
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKA-EEAKKAEEAKIkaeeLKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA---EEENKIKAAE 1665
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 755 EDRDLFVMRLKAARQSVYEEKLKQFEERLA--EERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQM 822
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-857 |
3.13e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 531 AKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQrilARRqtIEERKERLESLNIQREKEELEQREAElqKVRKAEEE 610
Cdd:PTZ00121 1127 ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED---ARK--AEEARKAEDAKKAEAARKAEEVRKAE--ELRKAEDA 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 611 RLRQEAKEREKERILQE---HEQIKKKTVRERLEQIKKTELGAKAFKDI----DIEDLEELDPDFIMAKQVEQLEKEKKE 683
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEarkAEDAKKAEAVKKAEEAKKDAEEAKKAEEErnneEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 684 LQERLKNQE-KKIDYFERAKRLEEIPLIKSAYEEQRVKDmDLWEQQEEERITTMQLEReKALEHKNRMSRMLEDRDLFVM 762
Cdd:PTZ00121 1280 ADELKKAEEkKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 763 RLKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELR 842
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
330
....*....|....*
gi 146219837 843 EYQERVKKLEEVERK 857
Cdd:PTZ00121 1438 KKAEEAKKADEAKKK 1452
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
900-1124 |
3.17e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 61.46 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 900 RKGP--EADSEWRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRF 977
Cdd:PRK12678 47 RKGEliAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 978 SRRGTDDDRPSWRNADDDRpprrigdddrgswrHTDDDRPPRRGLDDERGSWRTADEDRGPRRGMDDDRGPRRGGADDER 1057
Cdd:PRK12678 127 ARERRERGEAARRGAARKA--------------GEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGR 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 1058 SSWRNADDDRG--PRRGMDDDRGPRRG---LDDDRGPWRNAAEDRISRRGADDDRGPWRNMDDD----RVPRRGDD 1124
Cdd:PRK12678 193 REERGRDGDDRdrRDRREQGDRREERGrrdGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEgrggRRGRRFRD 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-806 |
3.27e-09 |
|
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: 61.61 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 561 SRKEHQRILARRQTIEErkerleslnIQREKEELEQREAELQKVRKAEEERLRQ-----EAKEREKERILQEHEQIKKK- 634
Cdd:TIGR02168 665 SAKTNSSILERRREIEE---------LEEKIEELEEKIAELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDl 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 635 --------TVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQV-EQLEKEKKELQERLKNQEKKIDYFERAKRLE 705
Cdd:TIGR02168 736 arleaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 706 EiplIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKlKQFEERLAE 785
Cdd:TIGR02168 816 N---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-ASLEEALAL 891
|
250 260
....*....|....*....|.
gi 146219837 786 ERHSRLEDRKRQRKEERKITY 806
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSE 912
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
517-778 |
1.23e-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: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSsvlakaLEVIRPAHILQEKEEQhqlavnaylKNSRKEHQRILARRQTI--EERKERLESLNIQREKEEL 594
Cdd:pfam17380 363 ERIRQEEIAME------ISRMRELERLQMERQQ---------KNERVRQELEAARKVKIleEERQRKIQQQKVEMEQIRA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 595 EQREAELQKVRKAEEERLRQEAKEREKEriLQEHEQIKKKTVRERLEQIKKTELgakafkdidieDLEELDPDFIMAKQV 674
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLEL-----------EKEKRDRKRAEEQRR 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 675 EQLEKEKKELQERLKNQEKKIDYFEraKRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML 754
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLE--KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAME 572
|
250 260
....*....|....*....|....
gi 146219837 755 EDRDLFvmrlkaaRQSVYEEKLKQ 778
Cdd:pfam17380 573 REREMM-------RQIVESEKARA 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-804 |
1.43e-08 |
|
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: 59.70 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 560 NSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRqeAKEREKERILQEHEqikkkTVRER 639
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSL--QSELRRIENRLDELSQELSDASRKIG--EIEKEIEQLEQEEE-----KLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 640 LEQIKktelgakafkdidiEDLEELDPDFIMAKQ-VEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYE--- 715
Cdd:TIGR02169 739 LEELE--------------EDLSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSkle 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 716 -------------EQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKaARQSVYEEKLKQFEER 782
Cdd:TIGR02169 805 eevsriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-EELEELEAALRDLESR 883
|
250 260
....*....|....*....|..
gi 146219837 783 LAEERHSRLEDRKRQRKEERKI 804
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKI 905
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
516-858 |
3.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 516 SEQIRNQLTAMSSVLAKALEVIRPahiLQEKEEQhqlaVNAYLKNSRKEHQRILARRQTIEERKERLESL---------- 585
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINE---ISSELPE----LREELEKLEKEVKELEELKEEIEELEKELESLegskrkleek 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 586 --NIQREKEELEQREAELQKVRKaEEERLRQEAKE-----REKERILQEHEQIKKK--TVRERLEQIKKTelgakafkdi 656
Cdd:PRK03918 261 irELEERIEELKKEIEELEEKVK-ELKELKEKAEEyiklsEFYEEYLDELREIEKRlsRLEEEINGIEER---------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 657 dIEDLEEldpdfiMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-EEIPLIKSAYEEQRVKDMDLWEQQEEERITT 735
Cdd:PRK03918 330 -IKELEE------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 736 MQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQ------------------SVYEEKLKQFEERLAE--ERHSRLEDRK 795
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkellEEYTAELKRIEKELKEieEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 796 RQ----RKEERKITYYRE----------------KEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVE 855
Cdd:PRK03918 483 RElekvLKKESELIKLKElaeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
...
gi 146219837 856 RKK 858
Cdd:PRK03918 563 KKL 565
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-889 |
3.46e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLAVNAylknSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAElqKVRKAEEER 611
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEA----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKKAEEKK 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 612 LRQEAKEREKERILQEHE-QIKKKTVRERLEQIKKTELGAKAFKdidIEDLEELDPDFIMAKQVEQLEKEKKELQERLKN 690
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMK---AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 691 QEKKIDYFERAKRLEEIPLIKSAY-----EEQRVKDMDLWEQQEEERITTMQLEREKAlehknrmsrmlEDRDLFVMRLK 765
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEeakkaEEDKKKAEEAKKAEEDEKKAAEALKKEAE-----------EAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 766 AARQSVYEEKLKQFEErlaeERHSRLEDRKRQRKEERKityyrekeeeeqrraeeqmlkeREERERAERAKREEELREYQ 845
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEE----ENKIKAEEAKKEAEEDKK----------------------KAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 146219837 846 ERVKKLEEVERKKRQRELEIEERerrrEEERRLGDDPLSRKDSR 889
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDE----EDEKRRMEVDKKIKDIF 1804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
517-805 |
4.57e-08 |
|
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: 57.77 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALeviRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERleslnIQREKEELEQ 596
Cdd:TIGR02169 194 DEKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 597 REAELQKVRKAEEERLRQEAKERE---KERILQEHEQIK--KKTVRERLEQIKKTELG-AKAFKDID--IEDLEELDpdf 668
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIAslERSIAEKERELEDAEERlAKLEAEIDklLAEIEELE--- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 669 imaKQVEQLEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKSAYEEQRVKDMDLWEQQEE--ERITTMQLEREKALEH 746
Cdd:TIGR02169 343 ---REIEEERKRRDKLTEEYAELKE-----ELEDLRAELEEVDKEFAETRDELKDYREKLEKlkREINELKRELDRLQEE 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 146219837 747 KNRMSRMLEDRDLFVMRLKAARQSVYEEKL-KQFEERLAEERHSRL-EDRKRQRKEERKIT 805
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLaADLSKYEQELYDLK 475
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
576-803 |
5.33e-08 |
|
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: 57.67 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 576 EERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEA------KEREKERILQEHEQ---IKKKTVRERLEQIKKT 646
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYyqlkekLELEEEYLLYLDYLklnEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 647 ELGAKAFKDIDIED-LEELDPDFIMAKQVEQLEKEKK---------ELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEE 716
Cdd:pfam02463 252 EIESSKQEIEKEEEkLAQVLKENKEEEKEKKLQEEELkllakeeeeLKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 717 QRVKDMDLWEQQEEE---RITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHSRLED 793
Cdd:pfam02463 332 KEKEEIEELEKELKEleiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250
....*....|
gi 146219837 794 RKRQRKEERK 803
Cdd:pfam02463 412 ELARQLEDLL 421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-800 |
5.86e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 545 EKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKE------ELEQREAELQKVRKA----EEERLRQ 614
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineissELPELREELEKLEKEvkelEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 615 EAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDIdIEDLEELDPDfimAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEK-VKELKELKEK---AEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 695 IDYFER-----AKRLEEIPLIKSAYEEQRVKDMDLweQQEEERITTMQLEREKALEHKNRMSRMLEDR-DLFVMRLKAAR 768
Cdd:PRK03918 316 LSRLEEeingiEERIKELEEKEERLEELKKKLKEL--EKRLEELEERHELYEEAKAKKEELERLKKRLtGLTPEKLEKEL 393
|
250 260 270
....*....|....*....|....*....|...
gi 146219837 769 QSVYEEKLKQFEERLA-EERHSRLEDRKRQRKE 800
Cdd:PRK03918 394 EELEKAKEEIEEEISKiTARIGELKKEIKELKK 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
543-802 |
6.16e-08 |
|
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: 57.67 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEHQRILARRQtiEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQ--ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 623 RILQEHEQIKKKTVRERLEQIKKTElgakafKDIDIEDLEELDPDFIMAKQV-EQLEKEKKELQERLKNQEKKIDYFERA 701
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEK------LKESEKEKKKAEKELKKEKEEiEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 702 KRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEE 781
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
250 260
....*....|....*....|.
gi 146219837 782 RLAEERHSRLEDRKRQRKEER 802
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDEL 465
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
532-683 |
7.89e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLavnaylknsRKEHQR-ILARRQTIEERKERLE--SLNIQREKEELEQREAELQKVRKAE 608
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHKL---------RNEFEKeLRERRNELQKLEKRLLqkEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146219837 609 EERLRQ-EAKEREKERILQEHeqikkktvRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:PRK12704 120 EQKQQElEKKEEELEELIEEQ--------LQELERI--SGLTAEEAKEILLEKVEeEARHE--AAVLIKEIEEEAKE 184
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
414-869 |
3.32e-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: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 414 VREQPEKEPELQQYVPQLQNNTILRLLQQVAQIYQSIEFSRLTSLVPFVDAFQLERA-IVDAARHCDLQVRIDHTSRTLS 492
Cdd:pfam02463 570 LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEgILKDTELTKLKESAKAKESGLR 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 493 FGSDLNYATREDAPVGPHLQSMPSEQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVnayLKNSRKEHQRILARR 572
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE---LKKLKLEAEELLADR 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 573 QTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRER-LEQIKKTELGAK 651
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeKLKAQEEELRAL 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 652 AFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSayEEQRVKDMDLWEQQEEE 731
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE--LLQELLLKEEELEEQKL 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 732 RITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQsvYEEKLKQFEERLAEERHSRLEDRKRQRKEERKItyyREKE 811
Cdd:pfam02463 885 KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER--IKEEAEILLKYEEEPEELLLEEADEKEKEENNK---EEEE 959
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 146219837 812 EEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERE 869
Cdd:pfam02463 960 ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
575-858 |
9.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 575 IEERKERLESLNIQREK--------EELEQREAELQ----KVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQ 642
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 643 ikktelgakAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEkkidyfERAKRLEEipliksayEEQRVKDM 722
Cdd:COG1196 275 ---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE------ERLEELEE--------ELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 723 DLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLfvmRLKAARQSVyEEKLKQFEERLAEERHSRLEDRKRQRKEER 802
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALL---EAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 803 KITyyrekeeeeqrraeeqmlkeREERERAERAKREEELREYQERVKKLEEVERKK 858
Cdd:COG1196 408 AEE--------------------ALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
552-696 |
1.33e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 552 LAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQI 631
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146219837 632 KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKID 696
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
588-717 |
1.46e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 588 QREKEElEQREAELQKVRKAEEERLRQEAKEREKERilQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPD 667
Cdd:PRK09510 80 QRKKKE-QQQAEELQQKQAAEQERLKQLEKERLAAQ--EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 146219837 668 FIMAKQVEQlEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKSAYEEQ 717
Cdd:PRK09510 157 AAAAKKAAA-EAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
514-804 |
1.56e-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: 52.80 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 514 MPSEQIRN-QLTAMSSVLA-KALEVIRPAHILQEKEEQHQLAVNaylkNSRKEHQRILARRQTIEERKERLESlNIQREK 591
Cdd:pfam05483 480 LEKEKLKNiELTAHCDKLLlENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEEKEMNLRD-ELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 592 EELEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQI---KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPD 667
Cdd:pfam05483 555 EEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 668 FIMAKQVE-QLEKEKKELQERLKNQEKKID--YFERAKRLEEIPLIKSAYEEQrVKDMDLWEQQEEERITTMQLEREKal 744
Cdd:pfam05483 635 EIKVNKLElELASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEA-VKLQKEIDKRCQHKIAEMVALMEK-- 711
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146219837 745 eHKNRMSRMLEDRD--LFVMRLKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEERKI 804
Cdd:pfam05483 712 -HKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
544-974 |
1.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 544 QEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKER 623
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 624 ILQEHEQIKKKTVRERLEQIKKT-ELGAKAFKDIDIEDLEE-LDPDFIMAKQVEQLEKEKKELQERLKNQEKKidYFERA 701
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKkAEEAKKKADEAKKAAEAKKKADEAKKAEEAK--KADEA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 702 KRLEEIPLIKSAYEEQRVKDMDLWEQQEEERittmQLEREKALEHKNRMSrmlEDRDLFVMRLKAARQSvyEEKLKQFEE 781
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAE---EDKNMALRKAEEAKKA--EEARIEEVM 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 782 RLAEERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQR 861
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 862 ELEIEERERRREEERRLGDDPLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRETRDDERPHRRDEDRL----- 936
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkk 1758
|
410 420 430
....*....|....*....|....*....|....*....
gi 146219837 937 -RRLGGDDEERESSLRPDDDRIPRRGLDDDRGPRRGPDE 974
Cdd:PTZ00121 1759 iAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-801 |
2.54e-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: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 562 RKEHQRILARRQT----IEERKERLESLniqreKEELEQREAELQKVRKAEEERLRQEAKEREKE-----RILQEHEQIK 632
Cdd:TIGR02169 722 EKEIEQLEQEEEKlkerLEELEEDLSSL-----EQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 633 KKTVRERLEQIKKTElgaKAFKDIDiEDLEELDPDfimakqVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIPLIKS 712
Cdd:TIGR02169 797 QAELSKLEEEVSRIE---ARLREIE-QKLNRLTLE------KEYLEKEIQELQEQRIDLKEQIK--SIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 713 AYEEQrVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKaARQSVYEEKLKQFEERLAEerhsrLE 792
Cdd:TIGR02169 865 ELEEE-LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-KRLSELKAKLEALEEELSE-----IE 937
|
....*....
gi 146219837 793 DRKRQRKEE 801
Cdd:TIGR02169 938 DPKGEDEEI 946
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
538-858 |
2.68e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 538 RPAHILQEKEEQHQLAVNAY--LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK---VRKAEEERL 612
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDFDFdaKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeARKAEDARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 613 RQEAKEREKER---ILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpDFIMAKQVEQLEKEKKELQERLK 689
Cdd:PTZ00121 1142 AEEARKAEDAKrveIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 690 NQEKKIdyfERAKRLEEIPliKSAYEEQRVKdmdlwEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRlKAARQ 769
Cdd:PTZ00121 1221 EDAKKA---EAVKKAEEAK--KDAEEAKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 770 SVYEEKLKQFEERLAEERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVK 849
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
....*....
gi 146219837 850 KLEEVERKK 858
Cdd:PTZ00121 1370 EKKKEEAKK 1378
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-803 |
2.89e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 516 SEQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESlniQREKEELE 595
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 596 QREAELQKV-----RKAEEERLRQEAKEREKERILQEHEQIKKKTVRERL----EQIKKTELGAKAFKDIDIEDLEE-LD 665
Cdd:PTZ00121 1322 KKAEEAKKKadaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKkAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 666 PDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEipliKSAYEEQRVKDMdlwEQQEEERITTMQLEREKALE 745
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAE---EAKKAEEAKKKAEEAKKADE 1474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 146219837 746 HKNRMSrmlEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEERK 803
Cdd:PTZ00121 1475 AKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-894 |
3.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT--VRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQV 674
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 675 EQLEKEKKELQ-----------------------------ERLKNQEKKIDYFERAK--RLEEIPLIKSAYEEQRVKDmD 723
Cdd:COG1196 514 LLLAGLRGLAGavavligveaayeaaleaalaaalqnivvEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAA-L 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 724 LWEQQEEERITTMQLEREKALEHKNRMSRMLE---DRDLFVMRLKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKE 800
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 801 ERKItyyREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGD 880
Cdd:COG1196 673 ALLE---AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
410
....*....|....
gi 146219837 881 DPLSRKDSRWGDRD 894
Cdd:COG1196 750 EEALEELPEPPDLE 763
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-746 |
5.87e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKK------TVRERLEQIKKTELGAKAFKDIDIEDLEELDP--DF 668
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeleeAEEALLERLERLEEELEELEEALAELEEEEEEeeEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 669 IMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEI--PLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEH 746
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELleELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-795 |
6.48e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAyLKNSRKEHQRILARRQTIEERK--ERLESLNIQREKEEL 594
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKKAEEEKKkvEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 595 EQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTvrerlEQIKKTElgakafkdidiedlEEldpdfimAKQV 674
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA-----EALKKEA--------------EE-------AKKA 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 675 EQLekEKKELQERLKNQEkkidyferakrleeiplIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKalEHKNRMSRML 754
Cdd:PTZ00121 1705 EEL--KKKEAEEKKKAEE-----------------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLK 1763
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 146219837 755 EDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHSRLEDRK 795
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
543-703 |
7.01e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.84 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL-EQREAELQKVRKAEEERLRQE--AKER 619
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAkAKQAAEAKAKAEAEAERKAKEeaAKQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 620 EKERILQEHEQIKKKtvreRLEQIKKTELGAKAFKDIDiedlEELDPDFIMAKQVEQLEKEKKELQERlKNQEKKIDYFE 699
Cdd:TIGR02794 153 EEEAKAKAAAEAKKK----AEEAKKKAEAEAKAKAEAE----AKAKAEEAKAKAEAAKAKAAAEAAAK-AEAEAAAAAAA 223
|
....
gi 146219837 700 RAKR 703
Cdd:TIGR02794 224 EAER 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-745 |
7.93e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLEslniQREKEELEQREAELQKVRKAEEER 611
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE----ALKKEAEEAKKAEELKKKEAEEKK 1716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 612 LRQEAKEREKERILQEhEQIKKKTVRER--LEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLK 689
Cdd:PTZ00121 1717 KAEELKKAEEENKIKA-EEAKKEAEEDKkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 690 NQEKKIDYFERAKRLEEIPLIKSAYEEQRvKDMDLWEQQEEERITTMQLEREKALE 745
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKEGNLVINDS-KEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-786 |
8.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 542 ILQEKEEQHQLAVnayLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK-VRKAEEERLRQEAKERE 620
Cdd:COG4913 244 LEDAREQIELLEP---IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 621 KERILQEHEQIKKKTVRERLEQIKktelgakafkdidiedleeldpdfimaKQVEQLEKEKKELQERLKNQEkkidyfER 700
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLE---------------------------REIERLERELEERERRRARLE------AL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 701 AKRLE-EIPLIKSAYEEQR------VKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEdrdlfvmRLKaARQSVYE 773
Cdd:COG4913 368 LAALGlPLPASAEEFAALRaeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-------SLE-RRKSNIP 439
|
250
....*....|...
gi 146219837 774 EKLKQFEERLAEE 786
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
881-1125 |
1.29e-05 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 49.91 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 881 DPLSRKDSrwgDRDSEGTWRKGPEADSEwRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPRR 960
Cdd:NF033609 653 DSDSDSDS---DSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 961 GLDDDRGPRRGPDEDRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHTDDDRpprrglDDERGSWRTADEDRGPRR 1040
Cdd:NF033609 729 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------DSDSDSDSDSDSDSDSDS 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1041 GMDDDrgprrGGADDERSSWRNADDDRGPRRGMDDDRGPRRGLDDDRGPWRNAAEDRISRR--GADDDRGPWRNMDDDRV 1118
Cdd:NF033609 803 DSDSD-----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESdsNSDSESGSNNNVVPPNS 877
|
....*..
gi 146219837 1119 PRRGDDA 1125
Cdd:NF033609 878 PKNGTNA 884
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-786 |
2.20e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 597 REAELQKVRKAEEERLrqEAKEREKERILQEHEQIKK------KTVRERLEQIKKTELgakafkdiDIEDLEEldpdfIM 670
Cdd:PRK12704 34 KEAEEEAKRILEEAKK--EAEAIKKEALLEAKEEIHKlrnefeKELRERRNELQKLEK--------RLLQKEE-----NL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 671 AKQVEQLEKEKKELQERLKNQEKKIDYFEraKRLEEiplIKSAYEEQRvkdmdlweqQEEERITTMQLErekalEHKNRM 750
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELE--KKEEE---LEELIEEQL---------QELERISGLTAE-----EAKEIL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 146219837 751 SRMLEDRdlfvMRLKAARQ-SVYEEKLKQFEERLAEE 786
Cdd:PRK12704 160 LEKVEEE----ARHEAAVLiKEIEEEAKEEADKKAKE 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
511-742 |
2.33e-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: 48.91 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 511 LQSMPSEQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQT-IEERKERLESLNIQr 589
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGK- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 590 eKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFI 669
Cdd:TIGR02169 863 -KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 670 MAKQV-------EQLEKEKKELQERLKNQE----KKIDYFER-AKRLEEipliksaYEEQRVKdmdLWEQQEEERITTMQ 737
Cdd:TIGR02169 942 EDEEIpeeelslEDVQAELQRVEEEIRALEpvnmLAIQEYEEvLKRLDE-------LKEKRAK---LEEERKAILERIEE 1011
|
....*
gi 146219837 738 LEREK 742
Cdd:TIGR02169 1012 YEKKK 1016
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
543-707 |
2.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQlAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQ-------- 614
Cdd:COG4717 80 LKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 615 EAKEREKERILQEHEQIKKKTVRERLEqikKTELGAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKK 694
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDL-AEELEELQ------QRLAELEEELEEAQEELEELEEE 228
|
170
....*....|...
gi 146219837 695 IDYFERAKRLEEI 707
Cdd:COG4717 229 LEQLENELEAAAL 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-756 |
2.91e-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: 48.90 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 516 SEQIRNQLTAMSSVLAKALEVIRPAHilQEKEEQHQLAVNAYLkNSRKEHQRILARRQTIEERKERL----ESLNIQRE- 590
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEV--SELEEEIEELQKELY-ALANEISRLEQQKQILRERLANLerqlEELEAQLEe 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 591 ----KEELEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQiKKKTVRERLEQIKKTELGAKafkdidiEDLEELD 665
Cdd:TIGR02168 328 leskLDELAEELAELEeKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVAQLE-------LQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 666 PDFI-MAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRVKDMDLWEQ-----QEEERITTMQLE 739
Cdd:TIGR02168 400 NEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAleelrEELEEAEQALDA 479
|
250
....*....|....*..
gi 146219837 740 REKALEHKNRMSRMLED 756
Cdd:TIGR02168 480 AERELAQLQARLDSLER 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
530-701 |
3.13e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 530 LAKALEVIRPAHIlQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLN--IQREKEELEQREAELQKVRKA 607
Cdd:COG2433 378 IEEALEELIEKEL-PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeLEEKDERIERLERELSEARSE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 608 EEERLRqeaKEREKERILQEHEQIKKK--TVRERLEQIKKTELGAKAFKDIDIEDleeldpDFIMAKQVEQLEKEK-KEL 684
Cdd:COG2433 457 ERREIR---KDREISRLDREIERLEREleEERERIEELKRKLERLKELWKLEHSG------ELVPVKVVEKFTKEAiRRL 527
|
170
....*....|....*..
gi 146219837 685 QERLKNQEKKIDYFERA 701
Cdd:COG2433 528 EEEYGLKEGDVVYLRDA 544
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
566-685 |
4.45e-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: 46.80 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 566 QRILARRQTIEE---RKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEH-EQIKKKTVRERLE 641
Cdd:cd16269 173 QEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHlRQLKEKMEEEREN 252
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 146219837 642 QIKKTELgAKAFKDIDIEDLEELDpdfiMAKQVEQLEKEKKELQ 685
Cdd:cd16269 253 LLKEQER-ALESKLKEQEALLEEG----FKEQAELLQEEIRSLK 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
564-707 |
5.43e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 564 EHQRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRlkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 642 QIKKtelgAKAFKDIdiedLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEI 707
Cdd:COG1579 84 NVRN----NKEYEAL----QKEIE---SLKRRISDLEDEILELMERIEELEEELA--ELEAELAEL 136
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
479-806 |
5.44e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 479 DLQVRIDHTSRTLSFGSDLNYATREDAPVGPHLQSMPSEQIRNQLTAM-SSVLAKALEVIRPAHILQEKEEQhqlAVNAY 557
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVlKEAISKAESATAVAKEAKDDAIQ---AVKAH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKN-----SRKEHQRILAR---RQTIEERKERLESLNI---QREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQ 626
Cdd:pfam09731 163 TDSlkeasDTAEISREKATdsaLQKAEALAEKLKEVINlakQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 627 EH-EQIKKKTVRERleQIKKTELgAKAFKDIDI-----EDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyfER 700
Cdd:pfam09731 243 KLvDQYKELVASER--IVFQQEL-VSIFPDIIPvlkedNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHI---ER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 701 AkrleeiplIKSAYEEQRVKDMDLWEQQEEERITT---MQLEREKALEHKnrmsrmledrdlfvmrlkaarQSVYEEKLK 777
Cdd:pfam09731 317 A--------LEKQKEELDKLAEELSARLEEVRAADeaqLRLEFEREREEI---------------------RESYEEKLR 367
|
330 340
....*....|....*....|....*....
gi 146219837 778 QFEERLAEERHSRLEDRKRQRKEERKITY 806
Cdd:pfam09731 368 TELERQAEAHEEHLKDVLVEQEIELQREF 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-704 |
5.48e-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: 47.74 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 516 SEQIRNQLTAMSSVLAKALEVIRPAH-ILQEKEEQHQLAVNAYLKNSRKEhQRILARRQTIEERKERLESlNIQREKEEL 594
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQI-ASLNNEIERLEARLERLED-RRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 595 EQREAELQKVRKAE-EERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKafkdidiEDLEELDPDF-IMAK 672
Cdd:TIGR02168 424 EELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLdSLER 496
|
170 180 190
....*....|....*....|....*....|..
gi 146219837 673 QVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
558-793 |
7.60e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKEHQRILARRQTIEER-KERLESLNIQREK-EELEQREAELQKvrKAEEERLRQEAKEREKERILQEHEQIKKK- 634
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELiAERRETIEEKRERaEELRERAAELEA--EAEEKREAAAEAEEEAEEAREEVAELNSKl 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 635 -TVRERLEQikktelgakafkdidIEDLEELDPDfimakqVEQLEKEKKELQERLKNQEKKIDyfERAKRLeeipliksa 713
Cdd:PRK02224 582 aELKERIES---------------LERIRTLLAA------IADAEDEIERLREKREALAELND--ERRERL--------- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 714 yEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML----EDRDLFVMRLKAARQSVyeEKLKQFEERLA--EER 787
Cdd:PRK02224 630 -AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLdelrEERDDLQAEIGAVENEL--EELEELRERREalENR 706
|
....*.
gi 146219837 788 HSRLED 793
Cdd:PRK02224 707 VEALEA 712
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
575-694 |
8.51e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 575 IEERKErleslNIQREKEELEQ---------REAElQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKK 645
Cdd:PRK00409 504 IEEAKK-----LIGEDKEKLNEliasleeleRELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK-LLEEAEKEAQ 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 146219837 646 TELG-AKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK00409 577 QAIKeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
542-858 |
9.55e-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: 46.98 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 542 ILQEKEEQHQLAVNAY--LKNSRKEHQRILARRQTIEER----KERLESL--NIQREKEELEQREAELQKVRKAEEERLR 613
Cdd:TIGR02169 693 LQSELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEeeklKERLEELeeDLSSLEQEIENVKSELKELEARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 614 QEAKEREKE-----RILQEHEQIKKKTVRERLEQIKKTElgaKAFKDIDiEDLEELDPDfimakqVEQLEKEKKELQERL 688
Cdd:TIGR02169 773 DLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIE---ARLREIE-QKLNRLTLE------KEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 689 KNQEKKIDyfERAKRLEEIPLIKSAYEEQrVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAaR 768
Cdd:TIGR02169 843 IDLKEQIK--SIEKEIENLNGKKEELEEE-LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK-R 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 769 QSVYEEKLKQFEERLAEerhsrLEDRKRQRKEERKITYYREKEEEEQRRAEEQM--LKEREERERAERAKREEELREYQE 846
Cdd:TIGR02169 919 LSELKAKLEALEEELSE-----IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIraLEPVNMLAIQEYEEVLKRLDELKE 993
|
330
....*....|..
gi 146219837 847 rvkKLEEVERKK 858
Cdd:TIGR02169 994 ---KRAKLEEER 1002
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
562-803 |
9.57e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKErilqEHEQIKKKTVRERLE 641
Cdd:pfam02029 70 KREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE----EETEIREKEYQENKW 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 642 QIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKN----QEKKIDYFERAKRLEEIPLIKSAYEEQ 717
Cdd:pfam02029 146 STEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvflDQKRGHPEVKSQNGEEEVTKLKVTTKR 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 718 RVKDMDLWEQQEEEriTTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKqfeeRLAEERHSRLEDRKRQ 797
Cdd:pfam02029 226 RQGGLSQSQEREEE--AEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELK----KKREERRKLLEEEEQR 299
|
....*.
gi 146219837 798 RKEERK 803
Cdd:pfam02029 300 RKQEEA 305
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
571-706 |
1.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 571 RRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQeaKEREKERiLQEHEQIKKKTVRERLEQIKKTELGA 650
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR--LEEQVER-LEAEVEELEAELEEKDERIERLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 651 KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEE 706
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
532-643 |
1.79e-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: 45.88 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLAVNAylKNSRKEHQRILARRQT-IEERKERLESLNIQREKEELEQREAELQKVRKAEEE 610
Cdd:pfam17380 487 KRAEEQRRKILEKELEERKQAMIEE--ERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
90 100 110
....*....|....*....|....*....|...
gi 146219837 611 RLRQEAKEREKERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
542-731 |
2.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 542 ILQEKEEQHQLAVNAYLKNSRKE-----HQRILARRQTIEERKERLEslniqrekEELEQREAELQKVrkaeEERLRQea 616
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEaeaikKEALLEAKEEIHKLRNEFE--------KELRERRNELQKL----EKRLLQ-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 617 kerekerilqeheqiKKKTVRERLEQIKKTElgakafkdidiedlEELDpdfimaKQVEQLEKEKKELQERLKNQEKKID 696
Cdd:PRK12704 94 ---------------KEENLDRKLELLEKRE--------------EELE------KKEKELEQKQQELEKKEEELEELIE 138
|
170 180 190
....*....|....*....|....*....|....*
gi 146219837 697 yfERAKRLEEIplikSAYEEQRVKDMdLWEQQEEE 731
Cdd:PRK12704 139 --EQLQELERI----SGLTAEEAKEI-LLEKVEEE 166
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
542-769 |
3.46e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 542 ILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREK 621
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 622 ----ERILQEHEQIKKKTVRERLEQIKKTELGAKAfkdIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:pfam02463 873 llkeEELEEQKLKDELESKEEKEKEEKKELEEESQ---KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146219837 698 FERAKRLEEIPLIK---SAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQ 769
Cdd:pfam02463 950 KEENNKEEEEERNKrllLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
558-799 |
3.97e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR 637
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 638 ERLEQIKKTELGAKAFKDidieDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEE 716
Cdd:pfam05557 94 EKESQLADAREVISCLKN----ELSELRRQIQRAElELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 717 QRVKDMDLWEQQEE-------------ERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAarqsvYEEKLKQFEERL 783
Cdd:pfam05557 170 QRIKELEFEIQSQEqdseivknskselARIPELEKELERLREHNKHLNENIENKLLLKEEVED-----LKRKLEREEKYR 244
|
250
....*....|....*.
gi 146219837 784 AEERHSRLEDRKRQRK 799
Cdd:pfam05557 245 EEAATLELEKEKLEQE 260
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
542-683 |
4.06e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 42.95 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 542 ILQEKEEQHQL--AVNAYLKNSRKEHQRiLARRqtIEERKERLEslniqREKEELEQREAELQKVRKAEEERLRQ-EAKE 618
Cdd:pfam12072 55 LLEAKEEIHKLraEAERELKERRNELQR-QERR--LLQKEETLD-----RKDESLEKKEESLEKKEKELEAQQQQlEEKE 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146219837 619 REKERILQEHeqikkktvRERLEQIKKteLGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:pfam12072 127 EELEELIEEQ--------RQELERISG--LTSEEAKEILLDEVEeELRHE--AAVMIKEIEEEAKE 180
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
536-705 |
4.54e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 536 VIRPAHILQEKEEQHQLAVNAylknSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQE 615
Cdd:TIGR02794 42 LVDPGAVAQQANRIQQQKKPA----AKKEQERQKKLEQQAEEAEKQRAAE--QARQKELEQRAAAEKAAKQAEQAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 616 AKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimAKQvEQLEKEKKELQERLKNQEKKi 695
Cdd:TIGR02794 116 EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE-------AKK-KAEEAKKKAEAEAKAKAEAE- 186
|
170
....*....|
gi 146219837 696 dyfERAKRLE 705
Cdd:TIGR02794 187 ---AKAKAEE 193
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
517-803 |
4.90e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIrpaHILQEKEEQHQLAVNAYLKNSRKEHQRILARR----QTIEERKERLESL------- 585
Cdd:pfam06160 89 DEIEELLDDIEEDIKQILEEL---DELLESEEKNREEVEELKDKYRELRKTLLANRfsygPAIDELEKQLAEIeeefsqf 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 586 -----------------NIQREKEELEQR-------EAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRER 639
Cdd:pfam06160 166 eeltesgdylearevleKLEEETDALEELmedipplYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKeiQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 640 LEQ----IKKTELGAKAFKDIDIED-LEELdpdfimakqVEQLEKEKKELQERLKNQEKKIDYFERAKR-----LEEIPL 709
Cdd:pfam06160 246 LEEnlalLENLELDEAEEALEEIEErIDQL---------YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEqnkelKEELER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 710 IKSAYeeqrvkdmdlweqqeeeRITTMQLEREKALEhkNRMSRMLEDRDLFVMRLKAARQ--SVYEEKLKQFEERLA--E 785
Cdd:pfam06160 317 VQQSY-----------------TLNENELERVRGLE--KQLEELEKRYDEIVERLEEKEVaySELQEELEEILEQLEeiE 377
|
330
....*....|....*....
gi 146219837 786 ERHSRLEDRKRQ-RKEERK 803
Cdd:pfam06160 378 EEQEEFKESLQSlRKDELE 396
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
518-803 |
5.72e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 518 QIRNQLTAMSSVLAKALEVIrpaHILQEKEEQHQLAVNAYLKNSRKEHQRILARR----QTIEERKERLESLniqreKEE 593
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEEL---QELLESEEKNREEVEQLKDLYRELRKSLLANRfsfgPALDELEKQLENL-----EEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 594 LEQREAELQK--VRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAK-------AFKDIDIED-LEE 663
Cdd:PRK04778 181 FSQFVELTESgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRelveegyHLDHLDIEKeIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 664 LDpdfimaKQVEQLEKEKKELQ-----ERLKNQEKKIDY----FER---AKR--LEEIPLIKSAYEEQRVKDMDLWEQ-- 727
Cdd:PRK04778 261 LK------EQIDENLALLEELDldeaeEKNEEIQERIDQlydiLERevkARKyvEKNSDTLPDFLEHAKEQNKELKEEid 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 728 --QEEERITTMQLEREKALEhkNRMSRMLEDRDLFVMRL--KAARQSVYEEKLKQFEERLA--EERHSRL-EDRKRQRKE 800
Cdd:PRK04778 335 rvKQSYTLNESELESVRQLE--KQLESLEKQYDEITERIaeQEIAYSELQEELEEILKQLEeiEKEQEKLsEMLQGLRKD 412
|
...
gi 146219837 801 ERK 803
Cdd:PRK04778 413 ELE 415
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
572-681 |
6.43e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 43.18 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 572 RQTIEERKERLESlnIQREKEELEQREAELQKVRKA---EEERLRQEAKEREKERILQEHEQikkKTVRERLEQIKKTEL 648
Cdd:COG4026 134 REELLELKEKIDE--IAKEKEKLTKENEELESELEElreEYKKLREENSILEEEFDNIKSEY---SDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....*....
gi 146219837 649 gakaFKDIDIEDL------EELDPDFIMAKQVEQLEKEK 681
Cdd:COG4026 209 ----LEVFSLEELwkelfpEELPEEDFIYFATENLKPGK 243
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
572-686 |
6.58e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 572 RQTIEERKERLESLNIQREKE----ELEQREAELQKVRkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTE 647
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREietaRIAEAEAELAKKK--AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERER 290
|
90 100 110
....*....|....*....|....*....|....*....
gi 146219837 648 LGAKAFKDIDiEDLEELDPDFIMAKQVEQLEKEKKELQE 686
Cdd:COG2268 291 EIELQEKEAE-REEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-855 |
7.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKEHQRILARRQT--------IEERKERLESLNIQRE--------KEELEQREAELQKVRK--AEEERLRQEAKER 619
Cdd:TIGR02168 170 YKERRKETERKLERTREnldrlediLNELERQLKSLERQAEkaerykelKAELRELELALLVLRLeeLREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 620 EKERILQEHEQiKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdfimAKQVEQLEKEKKELQERLKNQEKKIDYFE 699
Cdd:TIGR02168 250 EAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 700 RAKRLEEIPLIKSAYEEQRVKDMdlwEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQF 779
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEK---LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146219837 780 EE-RLAEERHSRLEDRKRQRKEERKityyrekeeeeqrraeeqmlkerEERERAERAKREEELREYQERVKKLEEVE 855
Cdd:TIGR02168 400 NEiERLEARLERLEDRRERLQQEIE-----------------------ELLKKLEEAELKELQAELEELEEELEELQ 453
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
530-796 |
7.31e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 530 LAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRIlarRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE 609
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA---RTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 610 ERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDL-EELDPDFIMAK-QVEQLEKE-KKELQ- 685
Cdd:pfam12128 683 RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLkAAIAARRSGAKaELKALETWyKRDLAs 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 686 -----ERLKNQEKKIDYFERakRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLF 760
Cdd:pfam12128 763 lgvdpDVIAKLKREIRTLER--KIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
250 260 270
....*....|....*....|....*....|....*.
gi 146219837 761 VMRLKAARQSvyEEKLkqfeERLAEERHSRLEDRKR 796
Cdd:pfam12128 841 RAKLEMERKA--SEKQ----QVRLSENLRGLRCEMS 870
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-689 |
7.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 566 QRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKktvreRLEQI 643
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALlkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE-AKKEADEIIK-----ELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 146219837 644 KKTELGAKAFKDIdIEDLEELDPdfiMAKQVEQLEKEKKELQERLK 689
Cdd:PRK00409 597 QKGGYASVKAHEL-IEARKRLNK---ANEKKEKKKKKQKEKQEELK 638
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
943-1181 |
7.77e-04 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 44.13 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 943 DEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGL 1022
Cdd:NF033609 627 DSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1023 DDERGSWRTADEDRGPRRGMDDDRGPRRGGADDERS-SWRNADDDRGPRRGMDDDRGPRRGLDDDRGPWRNAAEDRISRR 1101
Cdd:NF033609 707 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1102 GADDDRGPWRNMDDDRVPRRGDDARPgpwrpfvKPGGWREKEKAREESWGPPRESRPSEEREWDRDKEKDRDNQDREEND 1181
Cdd:NF033609 787 DSDSDSDSDSDSDSDSDSDSDSDSDS-------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
563-783 |
8.89e-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: 43.66 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 563 KEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE-ERLRQEAKER----EKERILQEHEQIKKKTVR 637
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEaVRTNPEINDRirllEQEVARYKEESGKAQAEV 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 638 ERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKkidyFERAKRLEEIPLIKSAyeeq 717
Cdd:pfam10174 582 ERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQL----LEEARRREDNLADNSQ---- 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146219837 718 rvkdmdlwEQQEEERITTMQLEREKALEHKNRMS---RMLEDRDLFVMRLKAARQSVYEEKLKQFEERL 783
Cdd:pfam10174 654 --------QLQLEELMGALEKTRQELDATKARLSstqQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
566-804 |
8.90e-04 |
|
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: 43.90 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 566 QRILARRQTIEERKERLES----LNIQREKEELEQREAE-----------------LQKVRKAEEERLRQEA----KERE 620
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLiideKRQQLERLRREREKAEryqallkekreyegyelLKEKEALERQKEAIERqlasLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 621 KERILQEHEQIKKKTV--RERLEQI-----KKTELGAKAFKDiDIEDLE---ELDPDFIMAK--QVEQLEKEKKELQERL 688
Cdd:TIGR02169 253 LEKLTEEISELEKRLEeiEQLLEELnkkikDLGEEEQLRVKE-KIGELEaeiASLERSIAEKerELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 689 KNQEKKIDYFERA---KRLEEIPLiKSAYEEQRVKDMDLWEQQEEE-------RITTMQLEREK-ALEHKNRMSRMLEDR 757
Cdd:TIGR02169 332 DKLLAEIEELEREieeERKRRDKL-TEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLeKLKREINELKRELDR 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 146219837 758 DLFVMRLKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEERKI 804
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
955-1067 |
9.17e-04 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 43.34 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 955 DRIPRRGLDDDRGPRRGPDEDRFSRRGTDDDRpsWRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGLDDERGSWRtade 1034
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSR---- 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 146219837 1035 DRGPRRGMDDDRGP--RRGGADDERS-SWRNADDDR 1067
Cdd:TIGR01642 76 DRPRRRSRSVRSIEqhRRRLRDRSPSnQWRKDDKKR 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-857 |
1.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 564 EHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEE--RLRQEAKE-REKERILQEH--EQIKKKTvrE 638
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQlKELEEKLKKYnlEELEKKA--E 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 639 RLEQIKKTELGAKAFKDIDIEDLEELDPdfiMAKQVEQLEKEKKELQERLKNQEKKIDY--FERAKRLEE-IPLIKSAYE 715
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEE---LKKKLAELEKKLDELEEELAELLKELEElgFESVEELEErLKELEPFYN 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 716 EQ-RVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDlfvMRLKAARQSVYEEKLKQFEERLAE--ERHSRLE 792
Cdd:PRK03918 603 EYlELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR---KELEELEKKYSEEEYEELREEYLElsRELAGLR 679
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146219837 793 DRKRQRKEERKityyrekeeeeqrraEEQMLKEREERERAERAKREEELREYQERVKKLEEVERK 857
Cdd:PRK03918 680 AELEELEKRRE---------------EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
532-803 |
1.24e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESlniQREKE------------ELEQREA 599
Cdd:NF033838 105 NVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKD---QKEEDrrnyptntyktlELEIAES 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 600 ELqKVRKAEEERLRQEAKE-REKERILQEHEQIK-KKTVRERLEQIK----KTELGAKAFKDIDIEDLEELDPDfimAKQ 673
Cdd:NF033838 182 DV-EVKKAELELVKEEAKEpRDEEKIKQAKAKVEsKKAEATRLEKIKtdreKAEEEAKRRADAKLKEAVEKNVA---TSE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 674 VEQLEKEKKE--LQERLKNQEKKIDYFERAKRLEE--------IPLIKSAYEEQRVKDMD--LWEQQEEER-----ITTM 736
Cdd:NF033838 258 QDKPKRRAKRgvLGEPATPDKKENDAKSSDSSVGEetlpspslKPEKKVAEAEKKVEEAKkkAKDQKEEDRrnyptNTYK 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 146219837 737 QLEREKALEHKNRMSRMLEdrdlfvMRLKAARQSVYEEKLKQ----FEERLAEErhSRLEDRKRQRKEERK 803
Cdd:NF033838 338 TLELEIAESDVKVKEAELE------LVKEEAKEPRNEEKIKQakakVESKKAEA--TRLEKIKTDRKKAEE 400
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
879-1025 |
1.29e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.97 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 879 GDDPLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIP 958
Cdd:PRK12678 149 GEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRG 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146219837 959 RRGlDDDRGPRRGPDEDRFSRRGTDDDrpswRNADDDRPPRRIGDDDRGSWRHTD--DDRPPRRGLDDE 1025
Cdd:PRK12678 229 RRR-RRDRRDARGDDNREDRGDRDGDD----GEGRGGRRGRRFRDRDRRGRRGGDggNEREPELREDDV 292
|
|
| CCDC50_N |
pfam15295 |
Coiled-coil domain-containing protein 50 N-terminus; |
540-634 |
1.33e-03 |
|
Coiled-coil domain-containing protein 50 N-terminus;
Pssm-ID: 464621 [Multi-domain] Cd Length: 126 Bit Score: 40.09 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 540 AHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAEL--QKVRKAEEERLRQEAK 617
Cdd:pfam15295 27 AHNLQEQEIEHHYATNIQRNQLVQNDIRVAKQLQEEEELQAQTLFQRRLAQLEEQDEEIAKEiqEELQREAEERRRREEE 106
|
90
....*....|....*..
gi 146219837 618 EREKERILQEHEQIKKK 634
Cdd:pfam15295 107 DEEIARQLQERERERER 123
|
|
| FadA |
pfam09403 |
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha ... |
593-704 |
1.48e-03 |
|
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha helices that form an intra-molecular coiled-coil arrangement.
Pssm-ID: 430587 [Multi-domain] Cd Length: 99 Bit Score: 39.19 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 593 ELEQREAELQKVRKAEEERL--RQEAKEREKERiLQEHEQIKKKtVRERLEQI---KKTELGAKAFKDIdiedleeldpd 667
Cdd:pfam09403 1 RLSALEAELQKLENKEEQRFnkEKAKAEAAAAD-LAKNYELKAE-IEEKLAKLeadSDVRFYKDEYKEL----------- 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 146219837 668 fimakqVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam09403 68 ------LKKYKDLLKELEKEIKEEEKIIDNFEALLSL 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
558-857 |
1.72e-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: 43.03 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKEHQRILARRQTIEERKERLE------SLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQI 631
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 632 KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDF-IMAKQVEQLEKEKKELQERlKNQEKKIDYFERAKRLEEIPLI 710
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQC 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 711 KSAYEEQRVKDMDLWEQQEE------ERITTMQLERE------KALEHKNR---MSRMLEDRDLF---VMRLKAARQSVY 772
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEienassSLGSDLAAREDalnqslKELMHQARtvlKARTEAHFNNNeevTAALQTGAELSH 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 773 EEKLKQFEERLAEERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLE 852
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*
gi 146219837 853 EVERK 857
Cdd:TIGR00618 863 QLTQE 867
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
943-1181 |
1.78e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 42.97 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 943 DEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGL 1022
Cdd:NF033609 621 DSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1023 DDERGSWRTADEDRGPRRGMDDDrgprrGGADDERSSWRNADDDRGPRRGMDDDRGPRRGLDDDRGPWRNAAEDRISRRG 1102
Cdd:NF033609 701 DSDSDSDSDSDSDSDSDSDSDSD-----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146219837 1103 ADDDRGPWRNMDDDRVPRRGDDArpgpwrpfvKPGGWREKEKAREESWGPPRESRPSEEREWDRDKEKDRDNQDREEND 1181
Cdd:NF033609 776 SDSDSDSDSDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 845
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
559-787 |
2.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 559 KNSRKEHQRILARRQTIEERKERLESLNIQREK------------EELEQREAELQKVrKAEEERLRQEAKEREKERILQ 626
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadevlEEHEERREELETL-EAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 627 EHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimakQVEQLEKEKKELQERLKNQ--------------- 691
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA---------RREELEDRDEELRDRLEECrvaaqahneeaeslr 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 692 EKKIDYFERAKRLEE--------IPLIKSAYEEQRVKDMDLWEQQEE--ERITTMQLEREKALEHKnrmSRMLEDRDLFV 761
Cdd:PRK02224 349 EDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFL---EELREERDELR 425
|
250 260
....*....|....*....|....*.
gi 146219837 762 MRLKAARQSvyeekLKQFEERLAEER 787
Cdd:PRK02224 426 EREAELEAT-----LRTARERVEEAE 446
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
941-1138 |
2.34e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 941 GDDEERESSLRPD-DDRIPRRGLDDDRGPRRGPD-----EDRFSRRGTDDDRPSWRNADDDRPPRR---IGDDDRGSWRH 1011
Cdd:PHA03307 204 PRPPRRSSPISASaSSPAPAPGRSAADDAGASSSdssssESSGCGWGPENECPLPRPAPITLPTRIweaSGWNGPSSRPG 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1012 TDDDRPPRRGLDDERGSWRTADEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRGPRRGMDDDRGPRRGldDDRGPwr 1091
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS--RPPPP-- 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 146219837 1092 nAAEDRISRRGADDDRGPWRNMDD-DRVPRRGDDARPGPWR----PFVKPGG 1138
Cdd:PHA03307 360 -ADPSSPRKRPRPSRAPSSPAASAgRPTRRRARAAVAGRARrrdaTGRFPAG 410
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
543-707 |
2.34e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.48 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEhqrILARRQTIEERKERLESLNIQ-REK-----EELEQREAELQKV-RKAEEERLRQE 615
Cdd:pfam09728 93 LAKEEEEKRKELSEKFQSTLKD---IQDKMEEKSEKNNKLREENEElREKlksliEQYELRELHFEKLlKTKELEVQLAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 616 AK----EREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFI---------------MAKQVEQ 676
Cdd:pfam09728 170 AKlqqaTEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNksnevfttfkkemekMSKKIKK 249
|
170 180 190
....*....|....*....|....*....|...
gi 146219837 677 LEKEKKELQERLKNQEKKIDYF--ERAKRLEEI 707
Cdd:pfam09728 250 LEKENLTWKRKWEKSNKALLEMaeERQKLKEEL 282
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-698 |
2.81e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIR----PAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKE 592
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 593 E------LEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTvRERLEQIKKTELGAKAFKDIDIEDLEE--- 663
Cdd:TIGR02168 872 EselealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-REKLAQLELRLEGLEVRIDNLQERLSEeys 950
|
170 180 190
....*....|....*....|....*....|....*
gi 146219837 664 LDPDFIMAKQVEqLEKEKKELQERLKNQEKKIDYF 698
Cdd:TIGR02168 951 LTLEEAEALENK-IEDDEEEARRRLKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
543-783 |
2.88e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNiqREKEELEQREAEL--------QKVRKAEEERLRQ 614
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELEEKVKDLtkkisslkEKIEKLESEKKEK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 615 EAKEREKERILQEHEQIKKKTV--------RERLEQIK--KTELGAKAF-KDIDIEDLEELDPDFI------------MA 671
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENlekeidekNKEIEELKqtQKSLKKKQEeKQELIDQKEKEKKDLIkeieekekkissLE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 672 KQVEQLEKEKKELQERLKNQEKKIDYFErakrlEEIPLIKSAYEEQRVKDMDLWEQQEE------ERITTM-QLEREKAL 744
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLK-----QEVKQIKETIKEIRNKWPEIIKKIKEsktkidDIIELMkDWLKELSL 691
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 146219837 745 EHKNRMSRMLEDRDLfvMRLKAARQSVYEE--KLKQFEERL 783
Cdd:TIGR04523 692 HYKKYITRMIRIKDL--PKLEEKYKEIEKElkKLDEFSKEL 730
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
985-1071 |
2.94e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 41.83 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 985 DRPSWRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGLDDERGSWRTADEDRGPRRGMDDDRGPR----RGGADDERSSW 1060
Cdd:TIGR01622 4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRryrpREKRRRRGDSY 83
|
90
....*....|.
gi 146219837 1061 RNADDDRGPRR 1071
Cdd:TIGR01622 84 RRRRDDRRSRR 94
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
558-738 |
3.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvR 637
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL-----E 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 638 ERLEQIKKTELGAKAFKDiDIEDLEE------LDPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyferaKRLEEIplIK 711
Cdd:COG4717 153 ERLEELRELEEELEELEA-ELAELQEeleellEQLSLATEEELQDLAEELEELQQRLAELEEEL------EEAQEE--LE 223
|
170 180
....*....|....*....|....*..
gi 146219837 712 SAYEEQRVKDMDLWEQQEEERITTMQL 738
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARL 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
566-801 |
3.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 566 QRILARRQTIEERKERLESLN-----IQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK-----KT 635
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEerleaLEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 636 VRERLEQIKKTELGAKafkdidiEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYE 715
Cdd:COG4913 690 LEEQLEELEAELEELE-------EELDELK------GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 716 E----QRVKDMDLWEQQEEERITTMQLEREKALEhkNRMSRMLEDRDLFVMRLKAARQSV--YEEKLKQFEERLAEERHS 789
Cdd:COG4913 757 AalgdAVERELRENLEERIDALRARLNRAEEELE--RAMRAFNREWPAETADLDADLESLpeYLALLDRLEEDGLPEYEE 834
|
250
....*....|..
gi 146219837 790 RLEDRKRQRKEE 801
Cdd:COG4913 835 RFKELLNENSIE 846
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
539-635 |
3.43e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.86 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 539 PAHI-L-----QEKEEQHQLAvnaylknsRKEHQRILARrQTIEERKERLEslniqREKEELEQREAELQKVRKAEEERL 612
Cdd:PRK05035 422 PSNIpLvqyyrQAKAEIRAIE--------QEKKKAEEAK-ARFEARQARLE-----REKAAREARHKKAAEARAAKDKDA 487
|
90 100
....*....|....*....|...
gi 146219837 613 RQEAKEREKERILQEHEQIKKKT 635
Cdd:PRK05035 488 VAAALARVKAKKAAATQPIVIKA 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
505-747 |
3.93e-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: 41.29 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 505 APVGPHLQSMPSEQIRNQLTAMSSVLAKALEVIrpahilqEKEEQHQLAVNAYLKNSRkehQRILARRQTIEERKERLES 584
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALE---RRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 585 LniQREKEELEQREAELQKVRKAEEERLRQEAkerekeRILQEHEQIKKKTVRERLEQIKKTELGAKAFKDI---DIEDL 661
Cdd:COG4942 81 L--EAELAELEKEIAELRAELEAQKEELAELL------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLapaRREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 662 EELDPDFI-MAKQVEQLEKEKKELQERLKNQEKKIDYFERAK--RLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQL 738
Cdd:COG4942 153 EELRADLAeLAALRAELEAERAELEALLAELEEERAALEALKaeRQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*....
gi 146219837 739 EREKALEHK 747
Cdd:COG4942 233 EAEAAAAAE 241
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
532-811 |
4.17e-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: 41.06 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKA-EEE 610
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIqEED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 611 RLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpdfIMAKQVEQLEKEKKELQERLKN 690
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREE---EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 691 QEKKIDYFERAKRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRML--EDRDLFVMRLKAAR 768
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEaeREEEEFERMLRKQA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 146219837 769 QSVYEEKLKQFEERLAEERHSR-----LEDRKRQRKEERK------ITYYREKE 811
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRelekqIEEREEQRAAEREeeleegERLREEEA 325
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
545-857 |
4.33e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 545 EKEEQHQLAVNAYLKNSRKEHQRILarRQTIEERKERLESL-NIQREKEELEQREAELQKVRKAEEERLRQeaKEREKER 623
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEI--EKLKKENQSYKQEIkNLESQINDLESKIQNQEKLNQQKDEQIKK--LQQEKEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 624 ILQEHEQIKKKTVRERlEQIKKTElGAKAFKDIDIEDLEELDPDFimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKR 703
Cdd:TIGR04523 424 LEKEIERLKETIIKNN-SEIKDLT-NQDSVKELIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 704 LEEIPLIKSAYEEQrVKDmdLWEQQEEERITTMQLEREKA---LEHKNRMSRMLEDRDlfvmRLKaarQSVYEEKLKQFE 780
Cdd:TIGR04523 498 LKKLNEEKKELEEK-VKD--LTKKISSLKEKIEKLESEKKekeSKISDLEDELNKDDF----ELK---KENLEKEIDEKN 567
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 146219837 781 ERLAEERHSRLEDRKRQRKEERKITYYREKEEEeqrraeeqmLKEREERERAERAKREEELREYQERVKKLEEVERK 857
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD---------LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
543-691 |
4.53e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLniqreKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam09787 77 LQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERL-----QEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146219837 623 RilqehEQIKKKT--------VRERLEQIKKTELGAKAFkdidiedLEELDPDF-IMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam09787 152 R-----NQLTSKSqssssqseLENRLHQLTETLIQKQTM-------LEALSTEKnSLVLQLERMEQQIKELQGEGSNG 217
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
543-801 |
4.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLN-----IQREKEELEQREAELQKVRKAEEERLRQ--- 614
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQkerqdLEQQRKQLEAQIAELQSEIAEREEELKElee 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 615 --EAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERL---- 688
Cdd:COG4372 158 qlESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLalsa 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 689 -----KNQEKKIDYFERAKRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMR 763
Cdd:COG4372 238 lldalELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
250 260 270
....*....|....*....|....*....|....*...
gi 146219837 764 LKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEE 801
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
573-784 |
4.57e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 40.71 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 573 QTIEERKERLESLNIQREKEE-LEQREAELQKVRKAEEERL-----RQEAKEREKERILQEHEqiKKKTVRERLE----- 641
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAaLCKKYAELLEEMKRLQKDLkklkkKQDQLQKEKDQLQSELS--KAILAKSKLEklcre 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 642 ---QIKKTELGAKAFKDIDIEDLEELDPDF------IMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEI--PLI 710
Cdd:pfam09728 79 lqkQNKKLKEESKKLAKEEEEKRKELSEKFqstlkdIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHfeKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146219837 711 KSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLkaarqSVYEEKLKQFEERLA 784
Cdd:pfam09728 159 KTKELEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQL-----NLYVEKFEEFQDTLN 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-743 |
4.79e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 575 IEERKERLESLNiQREKEELEQREAELQKVRKAEEERLRQ-----------------------------EAKEREKERIL 625
Cdd:TIGR04523 347 LKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqindleskiqnqeklnqqkdeqiKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 626 QEHEQIKKKTVRERlEQIKKTElGAKAFKDIDIEDLEELDPDFimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLE 705
Cdd:TIGR04523 426 KEIERLKETIIKNN-SEIKDLT-NQDSVKELIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKELK 499
|
170 180 190
....*....|....*....|....*....|....*...
gi 146219837 706 EIPLIKSAYEEQrVKdmDLWEQQEEERITTMQLEREKA 743
Cdd:TIGR04523 500 KLNEEKKELEEK-VK--DLTKKISSLKEKIEKLESEKK 534
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
545-659 |
5.03e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 40.74 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 545 EKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKerleslNIQREKEELEQREAEL-QKVRKAEEERLRQEAKE-REKE 622
Cdd:pfam07767 212 LKEEEKLERVLEKIAESAATAEAREEKRKTKAQRN------KEKRRKEEEREAKEEKaLKKKLAQLERLKEIAKEiAEKE 285
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 146219837 623 RILQEHEQIKKKTVRERLEQIKKTE---LGAKAFKDIDIE 659
Cdd:pfam07767 286 KEREEKAEARKREKRKKKKEEKKLRprkLGKHKVPEPDLE 325
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
558-645 |
5.08e-03 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 39.46 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 558 LKNSRKehQRILarrQTIEERKERLESLNiqrekEELEQREAELQKVrKAEEERLRQEA---KEREKERILQeheQIKKK 634
Cdd:CHL00019 52 LLDNRK--QTIL---NTIRNSEERREEAI-----EKLEKARARLRQA-ELEADEIRVNGyseIEREKENLIN---QAKED 117
|
90
....*....|.
gi 146219837 635 TvrERLEQIKK 645
Cdd:CHL00019 118 L--ERLENYKN 126
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
531-652 |
5.11e-03 |
|
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: 40.60 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 531 AKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKvRKAEEE 610
Cdd:TIGR02794 77 AEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAA-KQAEEE 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 146219837 611 RLRQEAKEREKE----RILQEHEQIKKKtvrERLEQIKKTELGAKA 652
Cdd:TIGR02794 156 AKAKAAAEAKKKaeeaKKKAEAEAKAKA---EAEAKAKAEEAKAKA 198
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
1015-1139 |
5.12e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 41.03 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1015 DRPPRRGLDDERGSWRTADEDRGPRRGMDDDRGPRRggaDDERSSWRNADDDRGPRRGMDDDRGPRrgldDDRGPWRNAA 1094
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDR---HRRSRERSYREDSRPRDRRRYDSRSPR----SLRYSSVRRS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 146219837 1095 EDRISRRGADDDRGPW-RNMDDDRVPR---RGDDARPGPWRpfVKPGGW 1139
Cdd:TIGR01642 75 RDRPRRRSRSVRSIEQhRRRLRDRSPSnqwRKDDKKRSLWD--IKPPGY 121
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
539-749 |
5.19e-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: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 539 PAHILQEKEEQHQlAVNAYLKNSRKEHQRILARRQtieeRKERLESLNIQREKEELEQR---EAELQKVRKAEEERLRQE 615
Cdd:pfam15709 320 PSKALLEKREQEK-ASRDRLRAERAEMRRLEVERK----RREQEEQRRLQQEQLERAEKmreELELEQQRRFEEIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 616 AKEREKERilQEHEQIKK----KTVRERLEQiKKTELGAKAFKDIDIEDLEEldpdfimAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam15709 395 RLEEERQR--QEEEERKQrlqlQAAQERARQ-QQEEFRRKLQELQRKKQQEE-------AERAEAEKQRQKELEMQLAEE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 146219837 692 EKKIDYFERAKRLEEIPLiKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNR 749
Cdd:pfam15709 465 QKRLMEMAEEERLEYQRQ-KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
572-804 |
5.62e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 572 RQTIEERKERLESLNIQREKEELEqREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTElgak 651
Cdd:COG5185 207 IKESETGNLGSESTLLEKAKEIIN-IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLN---- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 652 afkdidiEDLEELdpdfimAKQVEQLekeKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRVKDMDLWEQQEEe 731
Cdd:COG5185 282 -------ENANNL------IKQFENT---KEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAE- 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146219837 732 rittMQLEREKALEhknRMSRMLEDRDLFVmrlKAARQSVYEEKLKQFEERLAEERHSRLEDRKRQRKEERKI 804
Cdd:COG5185 345 ----IEQGQESLTE---NLEAIKEEIENIV---GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEI 407
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
576-889 |
5.63e-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: 41.11 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 576 EERKERLESLNIQREKEELEQREAELQKVRKAEEERL-------RQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEL 648
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 649 GAKAFKdidIEDLEEldpdfimaKQVEQLEKEKKELQERLKNQEKKidyferAKRLEEIPLIKSAYEEQRVKDMDLWEQQ 728
Cdd:pfam02463 233 KLNEER---IDLLQE--------LLRDEQEEIESSKQEIEKEEEKL------AQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 729 EEERITTMQLEREKALEHKnrmsrmledrdlfvmrlkaaRQSVYEEKLKQFEERLAEERHSRLEDRKRqrKEERKITYYR 808
Cdd:pfam02463 296 EELKSELLKLERRKVDDEE--------------------KLKESEKEKKKAEKELKKEKEEIEELEKE--LKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 809 EKEEEEQrraeeqMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGDDPLSRKDS 888
Cdd:pfam02463 354 EEEEEEE------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKE 427
|
.
gi 146219837 889 R 889
Cdd:pfam02463 428 E 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
500-694 |
5.93e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 500 ATREDAPVGPHLQSMPSEQIRNQLTAMSSVLAKALEVIRPAHILQEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERK 579
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 580 ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEheqikkktvRERLEQIkktELGAkafkdidIE 659
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE---------IEALGPV---NLLA-------IE 788
|
170 180 190
....*....|....*....|....*....|....*....
gi 146219837 660 DLEELDP--DFiMAKQVEQLEKEKKELQERLK--NQEKK 694
Cdd:COG1196 789 EYEELEEryDF-LSEQREDLEEARETLEEAIEeiDRETR 826
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
517-701 |
5.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 517 EQIRNQLTAMSSVLAKALEVIRPAHILQE--KEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLN--IQREKE 592
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 593 ELEQREAELQKVRKAEEERLRQEAK-EREKERILQEHEQikkktVRERLEQikktelgakAFKDIDIEDLEELDPDFIMA 671
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRlEKELEQAEEELDE-----LQDRLEA---------AEDLARLELRALLEERFAAA 758
|
170 180 190
....*....|....*....|....*....|
gi 146219837 672 KQVEQLEKEKKELQERLKNQEKKIDYFERA 701
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
545-858 |
6.45e-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: 40.86 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 545 EKEEQHQLAVNAYLknsRKEHQRILARRQTIEERKERLESLNIQREK-----EELEQREAELQKVRKAEEE--RLRQEAK 617
Cdd:pfam05483 88 EKIKKWKVSIEAEL---KQKENKLQENRKIIEAQRKAIQELQFENEKvslklEEEIQENKDLIKENNATRHlcNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 618 EREKERIlQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIE-DLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKID 696
Cdd:pfam05483 165 ARSAEKT-KKYEYEREETRQVYMDLNNNIEKMILAFEELRVQaENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 697 YFerakrleeipLIKSAYEEQRVKDMDLWEQQEEERI------TTMQLEREKAL-EHKNRMSRMLEDRDLFVMRlKAARQ 769
Cdd:pfam05483 244 LL----------LIQITEKENKMKDLTFLLEESRDKAnqleekTKLQDENLKELiEKKDHLTKELEDIKMSLQR-SMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 770 SVYEEKLKQFEE---RLAEERHSRLEDRKRQRKEERKITyyreKEEEEQRRAEEQMLKEREERERAERAKREEELREYQE 846
Cdd:pfam05483 313 KALEEDLQIATKticQLTEEKEAQMEELNKAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330
....*....|..
gi 146219837 847 RVKKLEEVERKK 858
Cdd:pfam05483 389 KSSELEEMTKFK 400
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
553-803 |
6.49e-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: 40.29 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 553 AVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQE----- 627
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYeeklq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 628 -----HEQIKKKTVRERLEQIKKTELGAKAFKDIDI------------EDLEELDPDFIMAKQVEQLEKEKKELQERLKN 690
Cdd:pfam13868 99 ereqmDEIVERIQEEDQAEAEEKLEKQRQLREEIDEfneeqaewkeleKEEEREEDERILEYLKEKAEREEEREAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 691 QEKKIDYFER-AKRLEEIPLIKSAYEEQRVKdmdlwEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFvMRLKAARQ 769
Cdd:pfam13868 179 EEEKEREIARlRAQQEKAQDEKAERDELRAK-----LYQEEQERKERQKEREEAEKKARQRQELQQAREEQ-IELKERRL 252
|
250 260 270
....*....|....*....|....*....|....
gi 146219837 770 SVYEEKLKQFEERLaeERHSRLEDRKRQRKEERK 803
Cdd:pfam13868 253 AEEAEREEEEFERM--LRKQAEDEEIEQEEAEKR 284
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
532-778 |
6.58e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 532 KALEVIRPAHILQEKEEQHQLaVNAYLKNSRKEhQRILARRQTIEERK---ERLESLNIQREKEELEQREAELQKVRKAE 608
Cdd:NF033838 172 KTLELEIAESDVEVKKAELEL-VKEEAKEPRDE-EKIKQAKAKVESKKaeaTRLEKIKTDREKAEEEAKRRADAKLKEAV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 609 EERLRQEAKEREKERIlqeheqikKKTVRERLEQIKKTELGAKAfKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERL 688
Cdd:NF033838 250 EKNVATSEQDKPKRRA--------KRGVLGEPATPDKKENDAKS-SDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 689 KNQ--EKKIDYFERAKRLEEIPLIKSayeEQRVKDMDLW-------EQQEEERITTMQLEREKALEHKNRMSRMLEDRDl 759
Cdd:NF033838 321 KDQkeEDRRNYPTNTYKTLELEIAES---DVKVKEAELElvkeeakEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRK- 396
|
250
....*....|....*....
gi 146219837 760 fVMRLKAARQSVYEEKLKQ 778
Cdd:NF033838 397 -KAEEEAKRKAAEEDKVKE 414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
589-805 |
6.93e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 589 REKEELEQREAELQKVRKaeeerlRQEAKEREKERILQEHEQI--KKKTVRERLEqiKKTELGAKAFK-----DIDIEDL 661
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKE------RQQKAESELKELEKKHQQLceEKNALQEQLQ--AETELCAEAEEmrarlAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 662 EELDPDfiMAKQVE-------QLEKEKKELQERLKNQEKKIDYFERAKR---LEEIPLiksayeEQRVKDMDLWEQQEEE 731
Cdd:pfam01576 74 EEILHE--LESRLEeeeersqQLQNEKKKMQQHIQDLEEQLDEEEAARQklqLEKVTT------EAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146219837 732 RITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSvYEEKLKQFEERLAEERHSRLEDRKRQRKEERKIT 805
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK-HEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
535-659 |
7.07e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 535 EVIRPAHI---LQEKEEQHQLAvnayLKNSRKEHQRILARRQTieERKERLESLNIQREKEELEQREAELQKVRKAEEER 611
Cdd:COG2268 196 EIIRDARIaeaEAERETEIAIA----QANREAEEAELEQEREI--ETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 146219837 612 LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIE 659
Cdd:COG2268 270 IAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE 317
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
668-853 |
7.09e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 668 FIMAKQVEQLEKEKKELQErlKNQEKKIDYFERAKRLEEipLIKSAYEEQRVKDMDLWEQQE-EERITTMQLEREKALEH 746
Cdd:COG4717 42 FIRAMLLERLEKEADELFK--PQGRKPELNLKELKELEE--ELKEAEEKEEEYAELQEELEElEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 747 KNRMSRMLEDRDLFVMRLKAARQ-SVYEEKLKQFEERLAE--ERHSRLEDRKRQRKEERKITYYREKEEEEQRRAEEQML 823
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEElrELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190
....*....|....*....|....*....|
gi 146219837 824 KEREERERAERAKREEELREYQERVKKLEE 853
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEE 227
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
543-754 |
7.47e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 543 LQEKEEQHQ----LAVNAYLKNSRK----EHQRILARrqTIEERKERLESLNiqrEKEELEQREAELQKVRKAEEERLRQ 614
Cdd:cd16269 61 LQELLDLHAacekEALEVFMKRSFKdedqKFQKKLME--QLEEKKEEFCKQN---EEASSKRCQALLQELSAPLEEKISQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 615 E--AKE-------REKERILQEHEQIKKKTVR--ERLE---QIKKTElgAKAFKDIDiEDLEELDPDFIMAK-QVEQLEK 679
Cdd:cd16269 136 GsySVPggyqlylEDREKLVEKYRQVPRKGVKaeEVLQeflQSKEAE--AEAILQAD-QALTEKEKEIEAERaKAEAAEQ 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146219837 680 EKKELQERLKNQEKKIDYFERakrleeipliksAYEEQrvkdMDLWEQQEEERITTMQLEREKALEHKNRMSRML 754
Cdd:cd16269 213 ERKLLEEQQRELEQKLEDQER------------SYEEH----LRQLKEKMEEERENLLKEQERALESKLKEQEAL 271
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
564-858 |
7.97e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 564 EHQRILARRQtieERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEqikKKTVRERLEQ- 642
Cdd:pfam05667 211 RNAAELAAAQ---EWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRS---AQDLAELLSSf 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 643 IKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIPLIKSAYEEQRvKDM 722
Cdd:pfam05667 285 SGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELE--ELQEQLEDLESSIQELEKEI-KKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 723 DLWEQQEEERITTMQL---EREKALEHKNRMSRMLEDRDLFVMRLKAARQSVyEEKL----KQFEERLAE--ERHSRLED 793
Cdd:pfam05667 362 ESSIKQVEEELEELKEqneELEKQYKVKKKTLDLLPDAEENIAKLQALVDAS-AQRLvelaGQWEKHRVPliEEYRALKE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146219837 794 RKRQRKEERKityyrekeeeeqrraeEQMlkereereraerakreEELREYQERVKKLEEVERKK 858
Cdd:pfam05667 441 AKSNKEDESQ----------------RKL----------------EEIKELREKIKEVAEEAKQK 473
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
544-690 |
7.98e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 544 QEKEEQHQLAVNAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL----EQREAELQKVRKAEEERLRQEAKER 619
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqkeEQLDARAEKLDNLENQLEEREKALS 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146219837 620 EKERILQEheqiKKKTVRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKELQERLKN 690
Cdd:PRK12705 116 ARELELEE----LEKQLDNELYRV--AGLTPEQARKLLLKLLDaELEEE--KAQRVKKIEEEADLEAERKAQ 179
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
570-645 |
9.46e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 570 ARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAK------EREKERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam02841 201 AKEKAIEAERAKAEAA--EAEQELLREKQKEEEQMMEAQERSYQEHVKqliekmEAEREQLLAEQERMLEHKLQEQEELL 278
|
..
gi 146219837 644 KK 645
Cdd:pfam02841 279 KE 280
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
975-1104 |
9.57e-03 |
|
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.
Pssm-ID: 273727 [Multi-domain] Cd Length: 509 Bit Score: 40.26 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 975 DRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHtdddrppRRGLDDERgswRTADEDRGPRRgmDDDRGPRrggad 1054
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRH-------RRSRERSY---REDSRPRDRRR--YDSRSPR----- 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 146219837 1055 DERSSWRNADDDRGPRRGMDDDRGPR-RGLDDDRGPWRNAAEDRISRRGAD 1104
Cdd:TIGR01642 65 SLRYSSVRRSRDRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWD 115
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
1056-1182 |
9.60e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 40.29 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146219837 1056 ERSSWRNADDDRGPRRGMDDDRGPRRGLDDDRgpwrnaaeDRISRRGADDDRGPWRNMDDDRVPRRGDDARPGPWRPfvk 1135
Cdd:TIGR01622 4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSR--------DRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRRYRP--- 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 146219837 1136 pggwREKEKAREESWGPPRESRpSEEREWDRDKEKDRDNQDREENDK 1182
Cdd:TIGR01622 73 ----REKRRRRGDSYRRRRDDR-RSRREKPRARDGTPEPLTEDERDR 114
|
|
| |
