|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
901-1150 |
3.20e-15 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 80.72 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 901 RRGGETESEWRRAPVERDWRRGEARDDERPfrrgddlPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDED 980
Cdd:PRK12678 58 ARGGGAAAAAATPAAPAAAARRAARAAAAA-------RQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARER 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 981 RPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRpprralDDDRPPRRALDDD 1060
Cdd:PRK12678 131 RERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG------RREERGRDGDDRD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1061 RPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRaaDDDRGPRRGLDDD 1140
Cdd:PRK12678 205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNE 282
|
250
....*....|
gi 2024509102 1141 RGPRRGLDDD 1150
Cdd:PRK12678 283 REPELREDDV 292
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
956-1156 |
3.98e-13 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 74.17 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 956 PAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRR 1035
Cdd:PRK12678 76 AARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1036 ALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRgswraaDDDRGPRRGLDDDRPPRRALDDDRPPRR 1115
Cdd:PRK12678 156 ARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD------DRDRRDRREQGDRREERGRRDGGDRRGR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024509102 1116 GLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRN 1156
Cdd:PRK12678 230 RRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
882-1110 |
1.35e-12 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 72.24 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 882 PFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDdlPRRGPAEEKE 961
Cdd:PRK12678 73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG--AARKAGEGGE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 962 RPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGswraaDDDRGPRRGMDDDRPPRRALDDDR 1041
Cdd:PRK12678 151 QPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD-----DRDRRDRREQGDRREERGRRDGGD 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 1042 PPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRaaDDDRGPRRGLDDDRPPRRALDDD 1110
Cdd:PRK12678 226 RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNEREPELREDDV 292
|
|
| PINT |
smart00088 |
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ... |
427-498 |
4.66e-12 |
|
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: 63.03 E-value: 4.66e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102 427 YVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFvDAFQLERSIVDAARHCDLQVRLDHTTRTLSFGSDLN 498
Cdd:smart00088 2 LVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-769 |
1.26e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALakalavikppHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREK 591
Cdd:COG1196 270 EELRLELEELELEL----------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELeeeleELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdfimA 671
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------L 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 672 KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQ----RVRDMELWEQQEEERITTLQLEREKALEHK 747
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEalleLLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260
....*....|....*....|..
gi 2024509102 748 NRLSRMLEDRDLFEARLKALRR 769
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALL 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
575-803 |
1.45e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 575 IEERKERLESLNIQREK--------EELEQREAELQ----KVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQ 642
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 643 ikktelgakAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIplikTAYEEQRVRDM 722
Cdd:COG1196 275 ---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAEL----EEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 723 ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
.
gi 2024509102 803 R 803
Cdd:COG1196 420 E 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
517-805 |
2.24e-10 |
|
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: 65.47 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALaviKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERleslnIQREKEELEQ 596
Cdd:TIGR02169 194 DEKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAELQKVRKAEEERLRQEAKERE---KERILQEHEQIK--KKTVRERLEQIKKTELG-AKAFKDID--IEDLEELDpdf 668
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIAslERSIAEKERELEDAEERlAKLEAEIDklLAEIEELE--- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 669 imaKQVEQLEKEKKELQERLKNQEKKIDYFERakRLEEIPL-IKTAYEEQRVRDMELWEQQEE---------ERITTLQL 738
Cdd:TIGR02169 343 ---REIEEERKRRDKLTEEYAELKEELEDLRA--ELEEVDKeFAETRDELKDYREKLEKLKREinelkreldRLQEELQR 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 739 EREKALEHKNRLSRMLEDRDLFEARLKALRRTVYED--KLKQFQERLAEERRNRLEERKKQRKEERRIT 805
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
530-782 |
6.88e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 530 LAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERK-ERLESLNIQREKEELEQREAElqKVRKAE 608
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE--EAKKAE 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 609 EERLRQEaKEREKERILQEHEQIKKKTVRE--RLEQIKKTELGAKAFKDIDIEDLEEldpDFIMAKQVEQLEKEKKELQE 686
Cdd:PTZ00121 1617 EAKIKAE-ELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 687 RLKNQEKKIDYFERAKRLEEIPL-----IKTAYEEQRVRDMELWEQQEEERITTLQLEREKalEHKNRLSRMLEDRDLFE 761
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKA 1770
|
250 260
....*....|....*....|.
gi 2024509102 762 ARLKALRRTVYEDKLKQFQER 782
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEK 1791
|
|
| PCI |
pfam01399 |
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ... |
405-494 |
9.33e-10 |
|
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15).
Pssm-ID: 460195 Cd Length: 105 Bit Score: 57.23 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 405 SRVSKVLNWVKDQAEKEPELQLYVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPfVDAFQLERSIVDAARHCDLQVRL 484
Cdd:pfam01399 16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLG-LSVDEVEKILAKLIRDGRIRAKI 94
|
90
....*....|
gi 2024509102 485 DHTTRTLSFG 494
Cdd:pfam01399 95 DQVNGIVVFS 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-800 |
1.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLA-VTAFLKNSRKEHQRILARRQTIEERKE--RLESLNIQREKEELEQRE-------AELQKVRKAEEER 611
Cdd:COG1196 231 LLKLRELEAELEeLEAELEELEAELEELEAELAELEAELEelRLELEELELELEEAQAEEyellaelARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 612 LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpdfimAKQVEQLEKEKKELQERLKNQ 691
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 692 EKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTV 771
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*....
gi 2024509102 772 YEDKLKQFQERLAEERRNRLEERKKQRKE 800
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-806 |
4.80e-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: 61.23 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 561 SRKEHQRILARRQTIEErkerleslnIQREKEELEQREAELQKVRKAEEERLRQ-----EAKEREKERILQEHEQIKKK- 634
Cdd:TIGR02168 665 SAKTNSSILERRREIEE---------LEEKIEELEEKIAELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDl 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 635 --------TVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQV-EQLEKEKKELQERLKNQEKKIDYFERAKRLE 705
Cdd:TIGR02168 736 arleaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 706 EiplIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKAlRRTVYEDKLKQFQERLAE 785
Cdd:TIGR02168 816 N---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALAL 891
|
250 260
....*....|....*....|.
gi 2024509102 786 ERRNRLEERKKQRKEERRITY 806
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSE 912
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
911-1215 |
7.48e-09 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 60.57 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 911 RRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRRegDEDRPPRREGDED 990
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST--PPAAASPRPPRRS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 991 RPLRRGLDEDRPprRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALddDRPPRRALDDDRPPRRAlddd 1070
Cdd:PHA03307 211 SPISASASSPAP--APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITL--PTRIWEASGWNGPSSRP---- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1071 rPPRRSLDDDRGSWRAADDDRGPRRGLDddrPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGldDD 1150
Cdd:PHA03307 283 -GPASSSSSPRERSPSPSPSSPGSGPAP---SSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS--RP 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1151 RGPwrntdddrlsrrDDDRGPWRSSEDSRPGPWRPFGKPGGWREREKAREDSWGPPRDSRPPGDR 1215
Cdd:PHA03307 357 PPP------------ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPA 409
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
560-804 |
1.62e-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: 59.31 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 560 NSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRqeAKEREKERILQEHEqikkkTVRER 639
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSL--QSELRRIENRLDELSQELSDASRKIG--EIEKEIEQLEQEEE-----KLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 640 LEQIKktelgakafkdidiEDLEELDPDFIMAKQ-VEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQR 718
Cdd:TIGR02169 739 LEELE--------------EDLSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 719 --VRDMELWEQQEEERITTLQLER---EKALEHKNRLSRMLEDR--------DLFEARLKALRRTV--YEDKLKQFQERL 783
Cdd:TIGR02169 805 eeVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQiksiekeiENLNGKKEELEEELeeLEAALRDLESRL 884
|
250 260
....*....|....*....|.
gi 2024509102 784 AEERRNRLEERKKQRKEERRI 804
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKI 905
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
540-802 |
2.18e-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: 59.21 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 540 PHLLQEKEEQHQLAVtafLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKER 619
Cdd:pfam02463 201 KLKEQAKKALEYYQL---KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 620 EKERILQEhEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAK------QVEQLEKEKKELQERLKNQEK 693
Cdd:pfam02463 278 EKEKKLQE-EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKElkkekeEIEELEKELKELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 694 KIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYE 773
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
250 260
....*....|....*....|....*....
gi 2024509102 774 DKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
519-770 |
2.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 519 IRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeslniqrekEELEQRE 598
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI---------EELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 599 AELQKVRKAEEERLRQeakEREKERILQEHEQIKKK--TVRERLEQIKKTelgakafkdidIEDLEEldpdfiMAKQVEQ 676
Cdd:PRK03918 283 KELKELKEKAEEYIKL---SEFYEEYLDELREIEKRlsRLEEEINGIEER-----------IKELEE------KEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 677 LEKEKKELQERLKNQEKKIDYFERAKRL-EEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
250
....*....|....*
gi 2024509102 756 DRDLFEARLKALRRT 770
Cdd:PRK03918 423 ELKKAIEELKKAKGK 437
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
880-1123 |
3.42e-08 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 58.26 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 880 DDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRS---DDLPRRGDDLPRRGP 956
Cdd:PHA03307 192 EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENecpLPRPAPITLPTRIWE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 957 AEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPL---RRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPP 1033
Cdd:PHA03307 272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPApssPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1034 RRAldddrPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRsldddRGSWRAADDDRGprrgldDDRPPRRalDDDRPP 1113
Cdd:PHA03307 352 SPS-----RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR-----RARAAVAGRARR------RDATGRF--PAGRPR 413
|
250
....*....|
gi 2024509102 1114 RRGLDDDRGS 1123
Cdd:PHA03307 414 PSPLDAGAAS 423
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
576-804 |
4.87e-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: 58.06 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 576 EERKERLESLNIQREKEELEQREAELQKVRKAEEERL-------RQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEL 648
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 649 GA-KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTayEEQRVRDMELWEQ 727
Cdd:pfam02463 233 KLnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE--LKSELLKLERRKV 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102 728 QEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERRI 804
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
542-803 |
8.08e-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: 57.29 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKERE- 620
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 621 ---KERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:pfam02463 309 kvdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE---EEEELEKLQEKLEQLEEELLAKKKLESER 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 698 FERAKRLEEIPLIKTAYEEQRVRDM-----------------ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLF 760
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLlelarqledllkeekkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024509102 761 EARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERR 803
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
424-811 |
9.02e-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: 56.90 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 424 LQLYVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFVDAFQLERS-IVDAARHCDLQVRLDHTTRTLSFGSDLNYSTR 502
Cdd:pfam02463 580 LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEgILKDTELTKLKESAKAKESGLRKGVSLEEGLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 503 EDAPLGPQLQSMPSEQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLK-------------NSRKEHQRIL 569
Cdd:pfam02463 660 EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKleaeelladrvqeAQDKINEELK 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 570 ARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE----ERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKK 645
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErektEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 646 TELGAKAFKDIDIEDLEELDPDFIMA-KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMEL 724
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEqKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 725 WEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARlkalRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERR- 803
Cdd:pfam02463 900 KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE----ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKv 975
|
....*....
gi 2024509102 804 -ITYYREKE 811
Cdd:pfam02463 976 nLMAIEEFE 984
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
542-683 |
9.54e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.32 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLavtaflknsRKEHQR-ILARRQTIEERKERLE--SLNIQREKEELEQREAELQKVRKAEEERLRQ-EAK 617
Cdd:PRK12704 59 LLEAKEEIHKL---------RNEFEKeLRERRNELQKLEKRLLqkEENLDRKLELLEKREEELEKKEKELEQKQQElEKK 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102 618 EREKERILQEHeqikkktvRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:PRK12704 130 EEELEELIEEQ--------LQELERI--SGLTAEEAKEILLEKVEeEARHE--AAVLIKEIEEEAKE 184
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
564-846 |
1.04e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 564 EHQRILARRQTiEERKERLESLNIQREKEELEQreaELQKVRKAEE-ERLRQEAKER------EKERILQEH----EQIK 632
Cdd:pfam17380 279 QHQKAVSERQQ-QEKFEKMEQERLRQEKEEKAR---EVERRRKLEEaEKARQAEMDRqaaiyaEQERMAMERerelERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 633 KKTVRERLEQIKKTELGAKAFKDIDIEDL--------EELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLqmerqqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 705 EEIPLIktayEEQRVRDMELWEQQEEERITTLQLEREKALEHK-NRLSRMLEDRDlfEARLKALRRTVYEDKLKQFQERL 783
Cdd:pfam17380 435 REVRRL----EEERAREMERVRLEEQERQQQVERLRQQEEERKrKKLELEKEKRD--RKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 784 AEERRNRLEERKKQrkEERRITYYREKEEEEQRLREEQLLKEreekerIEREKREQEQREYQE 846
Cdd:pfam17380 509 IEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
517-759 |
1.67e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEE--RKERLESLNIQREKEEl 594
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEqiRAEQEEARQREVRRLE- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 595 EQREAELQKVRKAEEER------LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdf 668
Cdd:pfam17380 442 EERAREMERVRLEEQERqqqverLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL---- 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 669 imakqveqLEKEKKELQERLKNQEKKidyferakrleeipliKTAYEEQRvrdmelwEQQEEERITTLQLEREKALEHKN 748
Cdd:pfam17380 518 --------LEKEMEERQKAIYEEERR----------------REAEEERR-------KQQEMEERRRIQEQMRKATEERS 566
|
250
....*....|.
gi 2024509102 749 RLSRMLEDRDL 759
Cdd:pfam17380 567 RLEAMEREREM 577
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-784 |
2.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 545 EKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKE------ELEQREAELQKVRKA----EEERLRQ 614
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineissELPELREELEKLEKEvkelEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 615 EAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDIdIEDLEELDPDfimAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEK-VKELKELKEK---AEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 695 IDYFER-----AKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKAL-EHKNRLSRMLEDRDL--FEARLKA 766
Cdd:PRK03918 316 LSRLEEeingiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPekLEKELEE 395
|
250 260
....*....|....*....|
gi 2024509102 767 L--RRTVYEDKLKQFQERLA 784
Cdd:PRK03918 396 LekAKEEIEEEISKITARIG 415
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
569-690 |
2.76e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 569 LARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEL 648
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2024509102 649 gakafKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKN 690
Cdd:COG1196 742 -----LEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
558-803 |
4.27e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK---VRKAEEERLRQEAKEREKER---ILQEHEQI 631
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeARKAEDARKAEEARKAEDAKrveIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 632 KKKTVRERLEQIKKTELGAKAfkdIDIEDLEELDP--DFIMAKQVEQLEKEKKELQERLKNQEKKIdyfERAKRLEEIPl 709
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKA---EEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAK- 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 710 iKTAYEEQR---VRDMELWEQQEEERITTLQLERE--KALEHK--NRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQER 782
Cdd:PTZ00121 1237 -KDAEEAKKaeeERNNEEIRKFEEARMAHFARRQAaiKAEEARkaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260
....*....|....*....|.
gi 2024509102 783 LAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKK 1336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-784 |
6.95e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLAVtafLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK-VRKAEEERLRQEAKERE 620
Cdd:COG4913 244 LEDAREQIELLEP---IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 621 KERILQEHEQIKKKTVRERLEQIKktelgakafkdidiedleeldpdfimaKQVEQLEKEKKELQERLKNQEkkidyfER 700
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLE---------------------------REIERLERELEERERRRARLE------AL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 701 AKRLE-EIPLIKTAYEEQRVRDMELWEQQEEERittlQLEREKALEHKNRLSRMLEDRDLFEARLKAL--RRTVYEDKLK 777
Cdd:COG4913 368 LAALGlPLPASAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLerRKSNIPARLL 443
|
....*..
gi 2024509102 778 QFQERLA 784
Cdd:COG4913 444 ALRDALA 450
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
908-1127 |
9.23e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 53.64 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 908 SEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDR--PPRR 985
Cdd:PHA03307 759 SNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESsgPARP 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 986 EGDEDRPlrrgldedrPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRA-LDDDRPPR 1064
Cdd:PHA03307 839 PGAAARP---------PPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGApAPRPRPAP 909
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102 1065 RALDDDRPPRRSldDDRGSWRaadddRGPRRGLDDDRPPRRALDDDRPPR---RGLDDDR--GSWRAA 1127
Cdd:PHA03307 910 RVKLGPMPPGGP--DPRGGFR-----RVPPGDLHTPAPSAAALAAYCPPEvvaELVDHPLfpEPWRPA 970
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
588-717 |
9.93e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 588 QREKEElEQREAELQKVRKAEEERLRQEAKEREKERilQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPD 667
Cdd:PRK09510 80 QRKKKE-QQQAEELQQKQAAEQERLKQLEKERLAAQ--EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2024509102 668 FIMAKQVEQlEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKTAYEEQ 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 ... |
479-758 |
1.19e-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: 53.19 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 479 DLQVRLDHTTrtlsfgSDLNYSTREDAPLGPQLQSmpsEQIRN-QLTAMSSALA---KALAVIKPPHLLQEKEEQHQLav 554
Cdd:pfam05483 454 DLEIQLTAIK------TSEEHYLKEVEDLKTELEK---EKLKNiELTAHCDKLLlenKELTQEASDMTLELKKHQEDI-- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 555 taflKNSRKEHQRILARRQTIEERKERLESlNIQREKEELEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQI-- 631
Cdd:pfam05483 523 ----INCKKQEERMLKQIENLEEKEMNLRD-ELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcn 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 632 -KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVE-QLEKEKKELQERLKNQEKKIDyferAKRLEEIPL 709
Cdd:pfam05483 598 nLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIE----DKKISEEKL 673
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024509102 710 IKTAYEEQRVRDMELWEQQEEERITTLQLEREKAL--EHKNRLSRMLEDRD 758
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmeKHKHQYDKIIEERD 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
564-745 |
1.21e-06 |
|
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: 51.08 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 564 EHQRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRlkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 642 QIKKtelgAKAFKDIdiedLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEipLIKTAYEEQRVRD 721
Cdd:COG1579 84 NVRN----NKEYEAL----QKEIE---SLKRRISDLEDEILELMERIEELEEELA--ELEAELAE--LEAELEEKKAELD 148
|
170 180
....*....|....*....|....
gi 2024509102 722 MELWEQQEEerITTLQLEREKALE 745
Cdd:COG1579 149 EELAELEAE--LEELEAEREELAA 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
572-707 |
1.45e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERLEslNIQREKEeLEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQikkkTVRERLEQIKKTElgak 651
Cdd:PRK12704 41 KRILEEAKKEAE--AIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE----NLDRKLELLEKRE---- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102 652 afkdidiedlEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEI 707
Cdd:PRK12704 110 ----------EELE------KKEKELEQKQQELEKKEEELEELIE--EQLQELERI 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-805 |
1.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR-ERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVE 675
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 676 QLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIK---TAYEEQRVRDMELWEQQEEERITTLQLEREK---ALEHKNR 749
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRaraALAAALA 593
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102 750 LSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERRIT 805
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
546-803 |
1.91e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 546 KEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERIL 625
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 626 QEHE------QIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFE 699
Cdd:PTZ00121 1336 KKAEeakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 700 RAKRLEEiplIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQF 779
Cdd:PTZ00121 1416 AKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
250 260
....*....|....*....|....
gi 2024509102 780 QERLAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAK 1516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
542-802 |
2.72e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLAVTAFLKNS---------RKEHQRILARRQT----IEERKERLESLniqreKEELEQREAELQKVRKAE 608
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSdasrkigeiEKEIEQLEQEEEKlkerLEELEEDLSSL-----EQEIENVKSELKELEARI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 609 EERLRQEAKEREKE-----RILQEHEQIKKKTVRERLEQIKKTElgaKAFKDIDiEDLEELDPDfimakqVEQLEKEKKE 683
Cdd:TIGR02169 768 EELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIE---ARLREIE-QKLNRLTLE------KEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 684 LQERLKNQEKKIDyfERAKRLEEIPLIKTAYEEQrVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLED--RDLFE 761
Cdd:TIGR02169 838 LQEQRIDLKEQIK--SIEKEIENLNGKKEELEEE-LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleAQIEK 914
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2024509102 762 ARLKALRRTV-----------YEDKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:TIGR02169 915 KRKRLSELKAklealeeelseIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
518-754 |
3.28e-06 |
|
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: 50.65 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 518 QIRNqltamSSALAKALAVIK---------PPHLLQEKEEQHQ----LAVTAFLKNSRK----EHQRILARrqTIEERKE 580
Cdd:cd16269 32 QIEN-----SAAVQKALAHYEeqmeqrvqlPTETLQELLDLHAacekEALEVFMKRSFKdedqKFQKKLME--QLEEKKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 581 RLESLNiqrEKEELEQREAELQKVRKAEEERLRQE--AKE-------REKERILQEHEQIKKKTVR--ERLE---QIKKT 646
Cdd:cd16269 105 EFCKQN---EEASSKRCQALLQELSAPLEEKISQGsySVPggyqlylEDREKLVEKYRQVPRKGVKaeEVLQeflQSKEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 647 ElgAKAFKDIDiEDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERakrleeipliktAYEEQrvrdMELW 725
Cdd:cd16269 182 E--AEAILQAD-QALTEKEKEIEAERaKAEAAEQERKLLEEQQRELEQKLEDQER------------SYEEH----LRQL 242
|
250 260
....*....|....*....|....*....
gi 2024509102 726 EQQEEERITTLQLEREKALEHKNRLSRML 754
Cdd:cd16269 243 KEKMEEERENLLKEQERALESKLKEQEAL 271
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1016-1226 |
3.31e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 51.44 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1016 AADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRsldDDRGSWRAADDDRGPRR 1095
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQAR---ERRERGEAARRGAARKA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1096 GLDDDRPPRRALDDDRPPRRGLDDDRgswRAADDDRGPRRglDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSS 1175
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEEERDE---RRRRGDREDRQ--AEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024509102 1176 EDSRPGPWRPFGKPGGWREREKAREDSWGPPRDSRPP-GDREWDRDKDRDDN 1226
Cdd:PRK12678 221 RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGrGGRRGRRFRDRDRR 272
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
573-784 |
3.59e-06 |
|
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: 50.34 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 573 QTIEERKERLESLNIQREKEE-LEQREAELQKVRKAEEERL-----RQEAKEREKERILQEHEqiKKKTVRERLE----- 641
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAaLCKKYAELLEEMKRLQKDLkklkkKQDQLQKEKDQLQSELS--KAILAKSKLEklcre 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 642 ---QIKKTELGAKAFKDIDIEDLEELDPDF------IMAKQVEQLEKEKK------ELQERLKN----QEKKIDYFERak 702
Cdd:pfam09728 79 lqkQNKKLKEESKKLAKEEEEKRKELSEKFqstlkdIQDKMEEKSEKNNKlreeneELREKLKSlieqYELRELHFEK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 703 rleeipLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDrdlfEARLKAlRRTVYEDKLKQFQER 782
Cdd:pfam09728 157 ------LLKTKELEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSET----EKELRE-QLNLYVEKFEEFQDT 225
|
..
gi 2024509102 783 LA 784
Cdd:pfam09728 226 LN 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
562-801 |
4.49e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQE-------------------------A 616
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldylklneeridllqellrdeQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 617 KEREKERILQEHEQIKKKTVRERLEQIKK-----TELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKekklqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 692 EKKIDYFERAKRLEEIPLIKTAYEEQRVRDM----ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEAR---L 764
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELeklqEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqlL 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024509102 765 KALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEE 801
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
984-1224 |
5.33e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 51.06 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 984 RREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPP 1063
Cdd:PRK12678 58 ARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1064 RRaldddRPPRRSLDDDRGSWRAADDDRGPRRglDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGP 1143
Cdd:PRK12678 138 RR-----GAARKAGEGGEQPATEARADAAERT--EEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1144 RRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSSEDSRPGPWRPFGKPGGWREREKAREDswgppRDSRppGDREWDRDKDR 1223
Cdd:PRK12678 211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD-----RDRR--GRRGGDGGNER 283
|
.
gi 2024509102 1224 D 1224
Cdd:PRK12678 284 E 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-780 |
5.98e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLAVTAfLKNSRKEHQRILARRQTIEERKERLEsLNIQREKEELEQREAELQKVRK--AEEERLRQEAKER 619
Cdd:TIGR02168 296 EISRLEQQKQILRER-LANLERQLEELEAQLEELESKLDELA-EELAELEEKLEELKEELESLEAelEELEAELEELESR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 620 EKEriLQEHEQIKKKTVRERLEQIKKTElgakafkdidiEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFE 699
Cdd:TIGR02168 374 LEE--LEEQLETLRSKVAQLELQIASLN-----------NEIERLE------ARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 700 RAKRLEEIPLIKTAYEE--QRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLK 777
Cdd:TIGR02168 435 LKELQAELEELEEELEElqEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
...
gi 2024509102 778 QFQ 780
Cdd:TIGR02168 515 QSG 517
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
950-1212 |
6.15e-06 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 50.73 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 950 DLPRRG-PAEEKERPSVESSEDRPP----RREGDEDRPPRREGDEDRPlrrglDEDRPPRRGLDDDRGswRAADDDRGPR 1024
Cdd:PHA03321 407 ELFRTGvPSEHYEASLRLLSSRQPPgapaPRRDNDPPPPPRARPGSTP-----ACARRARAQRARDAG--PEYVDPLGAL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1025 RGMDD--DRPPRRAldddRPPRRAL----DDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRR--- 1095
Cdd:PHA03321 480 RRLPAgaAPPPEPA----AAPSPATyytrMGGGPPRLPPRNRATETLRPDWGPPAAAPPEQMEDPYLEPDDDRFDRRdga 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1096 -GLDDDRPPRRALDDDRPPRRGLDDDRGswRAADDDRGPRRGLDDDRGPRRGLD---DDRGPWrntdddrlsrrdddrGP 1171
Cdd:PHA03321 556 aAAATSHPREAPAPDDDPIYEGVSDSEE--PVYEEIPTPRVYQNPLPRPMEGAGeppDLDAPT---------------SP 618
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024509102 1172 WRSSEDSRPGpWR--PFGKPggwreREKAREDSWGPPRDSRPP 1212
Cdd:PHA03321 619 WVEEENPIYG-WGdsPLFSP-----PPAARFPPPDPALSPEPP 655
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-1039 |
6.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREA-----ELQKvrKAEEERLRQEAK 617
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadAAKK--KAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 618 EREKERILQEHEQIKKKTVRERLEQIKKtelgakafKDIDIEDLEELDPDFIMAKQVEQLEK---EKKELQERLKNQEKK 694
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKK--------KAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAKKKAEEA 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 695 IDYFERAKRLEE---IPLIKTAYEEQRVRDMELwEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTV 771
Cdd:PTZ00121 1470 KKADEAKKKAEEakkADEAKKKAEEAKKKADEA-KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 772 yeDKLKQFQErlAEERRNRLEERKKQRKEERRITYYREKEEEEQRLREEQLLKEREEKERIEREKREQEQREYQ----ER 847
Cdd:PTZ00121 1549 --DELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 848 VKKLEELEKKKRQREMEIEERERRREEERRGLDDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDD 927
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 928 ERPFRRGDDLPRRSDDLprRGDDLPRRGPAEEKERpsvESSEDrppRREGDEDRppRREGDEDRPLRRGLDEDRPPRRGL 1007
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKK---EAEED---KKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIR 1774
|
490 500 510
....*....|....*....|....*....|..
gi 2024509102 1008 DDDRGSWRAADDDRGPRRGMDDDRPPRRALDD 1039
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
924-1307 |
8.02e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.55 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 924 ARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDrPPRREGDEDRPPRREGDEDRPLRRgldEDRPP 1003
Cdd:PHA03307 14 AAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAA-ACDRFEPPTGPPPGPGTEAPANES---RSTPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1004 RRGLDDDRGSWRAADDDRGPRRGMDDdrPPRRALDDDRPPRRALDDDRPPRRALD--DDRPPRRALDDDRPPRRSLDDDR 1081
Cdd:PHA03307 90 WSLSTLAPASPAREGSPTPPGPSSPD--PPPPTPPPASPPPSPAPDLSEMLRPVGspGPPPAASPPAAGASPAAVASDAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1082 GSWRAAD------------DDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDD 1149
Cdd:PHA03307 168 SSRQAALplsspeetarapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1150 DRGPWRNTDDDRLSRRDDDRGPWRSS----EDSRPGPWRPFGKPGGwREREKAREDSWGPPRDSRPPGDREWDRDKDRDD 1225
Cdd:PHA03307 248 GWGPENECPLPRPAPITLPTRIWEASgwngPSSRPGPASSSSSPRE-RSPSPSPSSPGSGPAPSSPRASSSSSSSRESSS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1226 NEkdrefdrerdfdrDDRFRRPRDDAGWRRGPAEETSswRDSSRREEWDRGGrdmrdrraddrePPLRRGPPLRSDREEP 1305
Cdd:PHA03307 327 SS-------------TSSSSESSRGAAVSPGPSPSRS--PSPSRPPPPADPS------------SPRKRPRPSRAPSSPA 379
|
..
gi 2024509102 1306 SS 1307
Cdd:PHA03307 380 AS 381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
503-745 |
8.28e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 503 EDAPLGPQLQSMPSEQIRNQLTAMSSA--LAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKE 580
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 581 RLESLNIQRE----------KEELEQREAELQKVRKAEEERLRQEAKEREKERILQEhEQIKKKTVRER--LEQIKKTEL 648
Cdd:PTZ00121 1676 KAEEAKKAEEdekkaaealkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKkkAEEAKKDEE 1754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 649 GAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRvRDMELWEQQ 728
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS-KEMEDSAIK 1833
|
250
....*....|....*..
gi 2024509102 729 EEERITTLQLEREKALE 745
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFE 1850
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
517-784 |
9.05e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLEslniqrekEELEQ 596
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ--------EKLEQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQ 676
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEE-LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 677 LEKEKKELQERLKNQEkkidyferakrleeipliktayEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLED 756
Cdd:pfam02463 450 KEELEKQELKLLKDEL----------------------ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
250 260
....*....|....*....|....*...
gi 2024509102 757 RdlfEARLKALRRTVYEDKLKQFQERLA 784
Cdd:pfam02463 508 G---LKVLLALIKDGVGGRIISAHGRLG 532
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
563-803 |
9.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 563 KEHQRILARRQTIEERK----ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERI--LQEHEQIKKKTV 636
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKaeeaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMahFARRQAAIKAEE 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 637 RERLEQIKKTELGAKA---FKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyfERAKRLEEiplIKTA 713
Cdd:PTZ00121 1277 ARKADELKKAEEKKKAdeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA---EEAKKAAE---AAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 714 YEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSrmlEDRDLFEARLKAlrrtvYEDKLKQFQERLAEERRNRLEE 793
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKA-----EEDKKKADELKKAAAAKKKADE 1422
|
250
....*....|
gi 2024509102 794 RKKQRKEERR 803
Cdd:PTZ00121 1423 AKKKAEEKKK 1432
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
874-1040 |
1.12e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.90 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 874 EerrglddpfsrkesrwGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPR 953
Cdd:PRK12678 142 A----------------RKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 954 RGPAEEKERPSVESSEDRPPRREGDEDRP--PRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRaaDDDRGPRRGMDDDR 1031
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRRGRRRRRDrrDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNER 283
|
....*....
gi 2024509102 1032 PPRRALDDD 1040
Cdd:PRK12678 284 EPELREDDV 292
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
566-685 |
1.19e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.73 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 566 QRILARRQTIEE---RKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEH-EQIKKKTVRERLE 641
Cdd:cd16269 173 QEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHlRQLKEKMEEEREN 252
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024509102 642 QIKKTELgAKAFKDIDIEDLEELDpdfiMAKQVEQLEKEKKELQ 685
Cdd:cd16269 253 LLKEQER-ALESKLKEQEALLEEG----FKEQAELLQEEIRSLK 291
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
562-684 |
1.60e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLE 641
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL-----LEELL 742
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024509102 642 QIKKTELGAKAFKDIDIEDLEELDpdfimaKQVEQLEKEKKEL 684
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELE------RELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-804 |
1.62e-05 |
|
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: 48.99 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 592 EELEQREAELQKVRKA-EEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDiDIEDLEeldpdfim 670
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEA-ELAELE-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 671 aKQVEQLEKEKKELQERLKNQekkIDYFERAKRLEEIPLIKTAYE-EQRVRDMELWEQQEEER----------ITTLQLE 739
Cdd:COG4942 90 -KEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaeelradLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 740 REKALEHKNRLSRMLEDRDLFEARLKALRRTVyEDKLKQFQERLAEERRNRLEERKKQRKEERRI 804
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
543-707 |
3.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVTAfLKNSRKEHQRIlarRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQ-------- 614
Cdd:COG4717 83 AEEKEEEYAELQEE-LEELEEELEEL---EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleel 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 615 EAKEREKERILQEHEQIKKKTVRERLEqikKTELGAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKK 694
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDL-AEELEELQ------QRLAELEEELEEAQEELEELEEE 228
|
170
....*....|...
gi 2024509102 695 IDYFERAKRLEEI 707
Cdd:COG4717 229 LEQLENELEAAAL 241
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
530-701 |
4.29e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 530 LAKALAVIKPPHLlQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLN--IQREKEELEQREAELQKVRKA 607
Cdd:COG2433 378 IEEALEELIEKEL-PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeLEEKDERIERLERELSEARSE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 608 EEERLRqeaKEREKERILQEHEQIKKK--TVRERLEQIKKTELGAKAFKDIDIEDleeldpDFIMAKQVEQLEKEK-KEL 684
Cdd:COG2433 457 ERREIR---KDREISRLDREIERLEREleEERERIEELKRKLERLKELWKLEHSG------ELVPVKVVEKFTKEAiRRL 527
|
170
....*....|....*..
gi 2024509102 685 QERLKNQEKKIDYFERA 701
Cdd:COG2433 528 EEEYGLKEGDVVYLRDA 544
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
525-803 |
4.32e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 525 AMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESlniQREKEELEQREAELQK- 603
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED---KKKADELKKAAAAKKKa 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 604 --VRKAEEE-RLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAfkdidiedlEELDPDFIMAKQVEQLEK- 679
Cdd:PTZ00121 1421 deAKKKAEEkKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---------DEAKKKAEEAKKADEAKKk 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 680 --EKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTlQLEREKALEHKNRLSRMLEDR 757
Cdd:PTZ00121 1492 aeEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAK 1570
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024509102 758 DLFEARLKALRRTvyeDKLKQFQERLAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121 1571 KAEEDKNMALRKA---EEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
558-772 |
5.01e-05 |
|
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: 47.81 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR 637
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 638 ERLEQIKKTELGAKAFKDidieDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEE 716
Cdd:pfam05557 94 EKESQLADAREVISCLKN----ELSELRRQIQRAElELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 717 QRVRDMELWEQQEE-------------ERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVY 772
Cdd:pfam05557 170 QRIKELEFEIQSQEqdseivknskselARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
575-694 |
5.34e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 575 IEERKErleslNIQREKEELEQ---------REAElQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKK 645
Cdd:PRK00409 504 IEEAKK-----LIGEDKEKLNEliasleeleRELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK-LLEEAEKEAQ 576
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2024509102 646 TELG-AKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK00409 577 QAIKeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-704 |
5.91e-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: 47.74 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 516 SEQIRNQLTAMSSALAKALAVIKPPH-LLQEKEEQHQLAVTAFLKNSRKEhQRILARRQTIEERKERLESlNIQREKEEL 594
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQI-ASLNNEIERLEARLERLED-RRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 595 EQREAELQKVRKAE-EERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKafkdidiEDLEELDPDF-IMAK 672
Cdd:TIGR02168 424 EELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLdSLER 496
|
170 180 190
....*....|....*....|....*....|..
gi 2024509102 673 QVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
552-769 |
6.17e-05 |
|
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: 47.07 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 552 LAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREKEELEQREAELQKVRKAEEERLRQEAKE----REKE 622
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALkkeekALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 623 RILQEHEQIKKKTVRERLEQIKKTE--------LGAKAFKDI--DIEDLEELDPDfiMAKQVEQLEKEKKELQERLKNQE 692
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplallLSPEDFLDAvrRLQYLKYLAPA--RREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102 693 KKidyferAKRLEEiplIKTAYEEQRVRdmelWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRR 769
Cdd:COG4942 171 AE------RAELEA---LLAELEEERAA----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4253 |
COG4253 |
Uncharacterized conserved protein, DUF2345 family [Function unknown]; |
878-1155 |
6.18e-05 |
|
Uncharacterized conserved protein, DUF2345 family [Function unknown];
Pssm-ID: 443395 [Multi-domain] Cd Length: 900 Bit Score: 47.73 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 878 GLDDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPA 957
Cdd:COG4253 197 AFADDRLTERRASAEAASRADAAALRDLRLALRLARRAATAADDAQTTDDARLTADDSAADAGSLSGSGGDGGAAGGSLA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 958 EEKERPSVESSeDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRAL 1037
Cdd:COG4253 277 EATSSLRVPAA-SVSLARYQRARRAAAAAAAADARAGGADAAGGVGTGGGRRLAAGLAGAAAEEEEAVGAEARARRRRLL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1038 DDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPP-------RRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDD 1110
Cdd:COG4253 356 RAARAAIRLLAAAALALLALGRGALAGRSPAAAAGPgivggtdRRARRRATAFVDRAAGPPPRTQRARRPLLPRPRGAGG 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2024509102 1111 RPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWR 1155
Cdd:COG4253 436 PPPRVVSTRAGDTPSADDDDGGRRVVRDDRRVAWVGGGESWGAGG 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
545-742 |
6.53e-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: 47.76 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 545 EKEEQHQLAVTAFLKNSRKEHQRILARRQT-IEERKERLESLNIQreKEELEQREAELQ--------KVRKAEEERLRQE 615
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGK--KEELEEELEELEaalrdlesRLGDLKKERDELE 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 616 AKEREKERILQEHE---QIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMakqvEQLEKEKKELQERLKNQE 692
Cdd:TIGR02169 896 AQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL----EDVQAELQRVEEEIRALE 971
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 693 ----KKIDYFER-AKRLEEipliktaYEEQRvrdMELWEQQEEERITTLQLEREK 742
Cdd:TIGR02169 972 pvnmLAIQEYEEvLKRLDE-------LKEKR---AKLEEERKAILERIEEYEKKK 1016
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-784 |
7.12e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK----KTVRERLEQIKKTELgakafkdiDIEDLEEldpdfIMAK 672
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefeKELRERRNELQKLEK--------RLLQKEE-----NLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 673 QVEQLEKEKKELQERLKNQEKKIDYFEraKRLEEiplIKTAYEEQRvrdmelweqQEEERITTLQLErekalEHKNRLSR 752
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELE--KKEEE---LEELIEEQL---------QELERISGLTAE-----EAKEILLE 161
|
170 180 190
....*....|....*....|....*....|...
gi 2024509102 753 MLEDrdlfEARLKALRRT-VYEDKLKQFQERLA 784
Cdd:PRK12704 162 KVEE----EARHEAAVLIkEIEEEAKEEADKKA 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
558-815 |
7.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQRILARRQT---IEERKERLESLNIqrekEELEQREAELQKVR------KAEEERLRQEAK---EREKERIL 625
Cdd:PRK03918 485 LEKVLKKESELIKLKELaeqLKELEEKLKKYNL----EELEKKAEEYEKLKekliklKGEIKSLKKELEkleELKKKLAE 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 626 QEHeqiKKKTVRERLEQIKK--TELGAKAFKDID--IEDLEELDPDFIMAKQVEqleKEKKELQERLKNQEKKIDyfera 701
Cdd:PRK03918 561 LEK---KLDELEEELAELLKelEELGFESVEELEerLKELEPFYNEYLELKDAE---KELEREEKELKKLEEELD----- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 702 KRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLqleREKALEHKNRLSRMledrdlfEARLKALRRTVyeDKLKQFQE 781
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEEL---REEYLELSRELAGL-------RAELEELEKRR--EEIKKTLE 697
|
250 260 270
....*....|....*....|....*....|....
gi 2024509102 782 RLaeerrnrleerkKQRKEERRityyrekeeeEQ 815
Cdd:PRK03918 698 KL------------KEELEERE----------KA 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-753 |
1.14e-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: 46.97 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKpphLLQEKEEQHQLAVTAF---LKNSRKEHQRILARRQTIEERKERLEslniqREKEE 593
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLE-----RRIAA 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 594 LEQREAELQKVRKAEEERLRQEAKEREKERILQE--HEQIKKKtvrerLEQIKKTELGAKAFKDidieDLEELDpdfima 671
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEelESELEAL-----LNERASLEEALALLRS----ELEELS------ 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 672 KQVEQLEKEKKELQERLKNQEKKIDYFERAK---RLEEIPLIKTAYEEQRVrDMELWEQQEEERITTLQLEREKALEHKN 748
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLeglEVRIDNLQERLSEEYSL-TLEEAEALENKIEDDEEEARRRLKRLEN 979
|
....*
gi 2024509102 749 RLSRM 753
Cdd:TIGR02168 980 KIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-804 |
1.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 575 IEERKERLESLNiQREKEELEQREAELQKVRKAEEERLRQ-----------------------------EAKEREKERIL 625
Cdd:TIGR04523 347 LKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqindleskiqnqeklnqqkdeqiKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 626 QEHEQIKKKTVRERlEQIKKTElGAKAFKDIDIEDLEELDPDFimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLE 705
Cdd:TIGR04523 426 KEIERLKETIIKNN-SEIKDLT-NQDSVKELIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKELK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 706 EIPLIKTAYEEQRVrdmELWEQQEEERITTLQLEREKaLEHKNRLSRMLEDRDLFEARLKalrRTVYEDKLKQFQERLAE 785
Cdd:TIGR04523 500 KLNEEKKELEEKVK---DLTKKISSLKEKIEKLESEK-KEKESKISDLEDELNKDDFELK---KENLEKEIDEKNKEIEE 572
|
250
....*....|....*....
gi 2024509102 786 ERRNRLEERKKQRKEERRI 804
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELI 591
|
|
| FadA |
pfam09403 |
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha ... |
593-704 |
1.32e-04 |
|
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha helices that form an intra-molecular coiled-coil arrangement.
Pssm-ID: 430587 [Multi-domain] Cd Length: 99 Bit Score: 42.27 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 593 ELEQREAELQKVRKAEEERL--RQEAKEREKERiLQEHEQIKKKtVRERLEQIKKTElGAKAFKDidieDLEELdpdfim 670
Cdd:pfam09403 1 RLSALEAELQKLENKEEQRFnkEKAKAEAAAAD-LAKNYELKAE-IEEKLAKLEADS-DVRFYKD----EYKEL------ 67
|
90 100 110
....*....|....*....|....*....|....
gi 2024509102 671 akqVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam09403 68 ---LKKYKDLLKELEKEIKEEEKIIDNFEALLSL 98
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
543-707 |
1.70e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 45.33 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVTAFLKNSRKEhqrILARRQTIEERKERLESLNIQ-REK-----EELEQREAELQKV-RKAEEERLRQE 615
Cdd:pfam09728 93 LAKEEEEKRKELSEKFQSTLKD---IQDKMEEKSEKNNKLREENEElREKlksliEQYELRELHFEKLlKTKELEVQLAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 616 AK----EREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpDFI----------------MAKQVE 675
Cdd:pfam09728 170 AKlqqaTEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQ-DTLnksnevfttfkkemekMSKKIK 248
|
170 180 190
....*....|....*....|....*....|....
gi 2024509102 676 QLEKEKKELQERLKNQEKKIDYF--ERAKRLEEI 707
Cdd:pfam09728 249 KLEKENLTWKRKWEKSNKALLEMaeERQKLKEEL 282
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
559-784 |
1.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 559 KNSRKEHQRILARRQTIEERKERLESLNIQREK------------EELEQREAELQKVrKAEEERLRQEAKEREKERILQ 626
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadevlEEHEERREELETL-EAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 627 EHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimakQVEQLEKEKKELQERLKNQ--------------- 691
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA---------RREELEDRDEELRDRLEECrvaaqahneeaeslr 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 692 EKKIDYFERAKRLEE--------IPLIKTAYEEQRVRDMELWEQQEE--ERITTLQLEREKALEHKNRLsrmLEDRDLFE 761
Cdd:PRK02224 349 EDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEEL---REERDELR 425
|
250 260
....*....|....*....|...
gi 2024509102 762 ARLKALRRTvyedkLKQFQERLA 784
Cdd:PRK02224 426 EREAELEAT-----LRTARERVE 443
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
970-1130 |
1.83e-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: 45.65 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 970 DRPPRREGDEDRPPRREGDEDRPLRRGLDEDRpprrglDDDRgswraadddrgPRRGMDddrppRRALDDDRPPRRALDD 1049
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR------FRDR-----------HRRSRE-----RSYREDSRPRDRRRYD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1050 DRPPRRALDDDRPPRRalddDRPPRRSLDDDRGSwraadddRGPRRGLddDRPPRRALDDDRPPRRGLDDDRGSWRAADD 1129
Cdd:TIGR01642 60 SRSPRSLRYSSVRRSR----DRPRRRSRSVRSIE-------QHRRRLR--DRSPSNQWRKDDKKRSLWDIKPPGYELVTA 126
|
.
gi 2024509102 1130 D 1130
Cdd:TIGR01642 127 D 127
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
542-643 |
1.85e-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: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQLAVTAflKNSRKEHQRILARRQT-IEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKERE 620
Cdd:pfam17380 497 LEKELEERKQAMIEE--ERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
90 100
....*....|....*....|...
gi 2024509102 621 KERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam17380 575 REMMRQIVESEKARAEYEATTPI 597
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
571-706 |
1.92e-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: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 571 RRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQeaKEREKERiLQEHEQIKKKTVRERLEQIKKTELGA 650
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR--LEEQVER-LEAEVEELEAELEEKDERIERLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102 651 KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEE 706
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
542-683 |
2.32e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 43.72 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 542 LLQEKEEQHQL--AVTAFLKNSRKEHQRiLARRqtIEERKERLEslniqREKEELEQREAELQKVRKAEEERLRQ-EAKE 618
Cdd:pfam12072 55 LLEAKEEIHKLraEAERELKERRNELQR-QERR--LLQKEETLD-----RKDESLEKKEESLEKKEKELEAQQQQlEEKE 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102 619 REKERILQEHeqikkktvRERLEQIKKteLGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:pfam12072 127 EELEELIEEQ--------RQELERISG--LTSEEAKEILLDEVEeELRHE--AAVMIKEIEEEAKE 180
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
563-783 |
2.34e-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: 45.58 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 563 KEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE-ERLRQEAKER----EKERILQEHEQIKKKTVR 637
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEaVRTNPEINDRirllEQEVARYKEESGKAQAEV 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 638 ERLEQIKKTELGAKAFKDIDIEDLEELDPdfimaKQVEqlEKEKKELQERLKNQEkkidyfERAKRLEEIpliktayEEQ 717
Cdd:pfam10174 582 ERLLGILREVENEKNDKDKKIAELESLTL-----RQMK--EQNKKVANIKHGQQE------MKKKGAQLL-------EEA 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 718 RVRDMELW----EQQEEERITTLQLEREKALEHKNRLS---RMLEDRDLFEARLKALRRTVYEDKLKQFQERL 783
Cdd:pfam10174 642 RRREDNLAdnsqQLQLEELMGALEKTRQELDATKARLSstqQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
572-681 |
2.86e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 44.33 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERLESlnIQREKEELEQREAELQKVRKA---EEERLRQEAKEREKERILQEHEQikkKTVRERLEQIKKTEL 648
Cdd:COG4026 134 REELLELKEKIDE--IAKEKEKLTKENEELESELEElreEYKKLREENSILEEEFDNIKSEY---SDLKSRFEELLKKRL 208
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024509102 649 gakaFKDIDIEDL------EELDPDFIMAKQVEQLEKEK 681
Cdd:COG4026 209 ----LEVFSLEELwkelfpEELPEEDFIYFATENLKPGK 243
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
572-706 |
3.08e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERLESLNIQREKE----ELEQREAELQKVRkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTE 647
Cdd:COG2268 213 EIAIAQANREAEEAELEQEREietaRIAEAEAELAKKK--AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERER 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 648 lgakafkdidiedleeldpdfimAKQVEQLEKEKKELQERlKNQEKKIDYfERAKRLEE 706
Cdd:COG2268 291 -----------------------EIELQEKEAEREEAELE-ADVRKPAEA-EKQAAEAE 324
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
572-781 |
3.20e-04 |
|
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: 44.95 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERLESlNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRERLEQI-----K 644
Cdd:COG5185 324 EQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIpqnqrG 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 645 KTELGAKAFKD---IDIEDLEELDPDFIMA-KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAyEEQRVR 720
Cdd:COG5185 403 YAQEILATLEDtlkAADRQIEELQRQIEQAtSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKE 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 721 DMELWEQQEEERITTLQLEREKALEHKNR-------------LSRMLEDRDLFEARLKALRRTVYEDKLKQFQE 781
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERqlegvrskldqvaESLKDFMRARGYAHILALENLIPASELIQASN 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-755 |
3.37e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQRILARRQT-IEERKERLESLNIQ-----REKEELEQREAELQK----VRKAEEERLRQEAKEREK-ERILQ 626
Cdd:TIGR02168 328 LESKLDELAEELAELEEkLEELKEELESLEAEleeleAELEELESRLEELEEqletLRSKVAQLELQIASLNNEiERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 627 EHEQIKKKtvRERLEQIKKTELGAKAFKDID--IEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168 408 RLERLEDR--RERLQQEIEELLKKLEEAELKelQAELEELE------EELEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024509102 705 EEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
559-778 |
3.59e-04 |
|
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: 45.00 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 559 KNSRKEhQRILARRQTIEERK---ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERIlqeheqikKKT 635
Cdd:NF033838 198 KEPRDE-EKIKQAKAKVESKKaeaTRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRA--------KRG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 636 VRERLEQIKKTELGAKAfKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQ--EKKIDYFERA-KRLEeiplIKT 712
Cdd:NF033838 269 VLGEPATPDKKENDAKS-SDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQkeEDRRNYPTNTyKTLE----LEI 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 713 AYEEQRVRDMELW-------EQQEEERITTLQLEREKALEHKNRLSRMLEDRDlfEARLKALRRTVYEDKLKQ 778
Cdd:NF033838 344 AESDVKVKEAELElvkeeakEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRK--KAEEEAKRKAAEEDKVKE 414
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
543-759 |
3.62e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNiqREKEELEQREAEL--------QKVRKAEEERLRQ 614
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELEEKVKDLtkkisslkEKIEKLESEKKEK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 615 EAKEREKERILQEHEQIKKKTV--------RERLEQIK--KTELGAKAF-KDIDIEDLEELDPDFI------------MA 671
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENlekeidekNKEIEELKqtQKSLKKKQEeKQELIDQKEKEKKDLIkeieekekkissLE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 672 KQVEQLEKEKKELQERLKNQEKKIDYFErakrlEEIPLIKTAYEEQRVRDMELWEQQEEERI-------TTLQLEREKAL 744
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLK-----QEVKQIKETIKEIRNKWPEIIKKIKESKTkiddiieLMKDWLKELSL 691
|
250
....*....|....*
gi 2024509102 745 EHKNRLSRMLEDRDL 759
Cdd:TIGR04523 692 HYKKYITRMIRIKDL 706
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
511-738 |
3.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 511 LQSMPSEQIRNQLTAMSSALAKalaviKPPHLLQEKEEQHQLavtafLKNSRKEHQRILARRQTIEERKERLESLniQRE 590
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGR-----KPELNLKELKELEEE-----LKEAEEKEEEYAELQEELEELEEELEEL--EAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 591 KEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLEQIKKTELGAKAFKDiDIEDLEE------L 664
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL-----EERLEELRELEEELEELEA-ELAELQEeleellE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 665 DPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyferaKRLEEIplIKTAYEEQRVRDMELWEQQEEERITTLQL 738
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEEL------EEAQEE--LEELEEELEQLENELEAAALEERLKEARL 250
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
952-1113 |
3.78e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.06 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 952 PRRGPAEEKERPSVESsedRPPRREGDEDRPPRREGDEDRPLRR---------GLDEDRPPRRGLDDDRGSW-RAADDDR 1021
Cdd:PHA03378 598 PVPHPSQTPEPPTTQS---HIPETSAPRQWPMPLRPIPMRPLRMqpitfnvlvFPTPHQPPQVEITPYKPTWtQIGHIPY 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1022 GPR-RGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDD 1100
Cdd:PHA03378 675 QPSpTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754
|
170
....*....|...
gi 2024509102 1101 RPPRRALDDDRPP 1113
Cdd:PHA03378 755 RPPAAAPGRARPP 767
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
936-1150 |
3.98e-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: 44.90 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 936 DLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWR 1015
Cdd:NF033609 629 DSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1016 AADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRR 1095
Cdd:NF033609 709 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1096 GLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609 789 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
562-705 |
4.19e-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: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 562 RKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAE--QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 642 QIKKTELGAKAFKDIDIEDLEEldpdfimAKQvEQLEKEKKELQERLKNQEKKidyfERAKRLE 705
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAE-------AKK-KAEEAKKKAEAEAKAKAEAE----AKAKAEE 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-689 |
5.28e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 566 QRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKktvreRLEQI 643
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALlkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE-AKKEADEIIK-----ELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2024509102 644 KKTELGAKAFKDIdIEDLEELDPdfiMAKQVEQLEKEKKELQERLK 689
Cdd:PRK00409 597 QKGGYASVKAHEL-IEARKRLNK---ANEKKEKKKKKQKEKQEELK 638
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
968-1081 |
5.72e-04 |
|
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: 44.14 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 968 SEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRraldddRPPRRAL 1047
Cdd:TIGR01622 2 YRDRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRPREK 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024509102 1048 DDDRPP-RRALDDDRPPRR--ALDDDRPPRRSLDDDR 1081
Cdd:TIGR01622 76 RRRRGDsYRRRRDDRRSRRekPRARDGTPEPLTEDER 112
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
919-1105 |
5.89e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 919 WRRGE---ARDDErpfrrGDDLPRRSDDLPRRGDD--LPRRGPAEEKERPSVESSEDRPprregdeDRPPRregdEDRPL 993
Cdd:PHA03247 2536 WIRGLeelASDDA-----GDPPPPLPPAAPPAAPDrsVPPPRPAPRPSEPAVTSRARRP-------DAPPQ----SARPR 2599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 994 RRGLDEDRPPRRGldddrGSWRAADDDRGPRRGMDDDRP----PRRALDDDRPPRRALDDDRPPRRAldddRPPRRALDD 1069
Cdd:PHA03247 2600 APVDDRGDPRGPA-----PPSPLPPDTHAPDPPPPSPSPaanePDPHPPPTVPPPERPRDDPAPGRV----SRPRRARRL 2670
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024509102 1070 DRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRR 1105
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
925-1051 |
5.92e-04 |
|
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: 44.14 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 925 RDDERPFRRGDDLPRRSDdlpRRGDDLPRRGPAEEKERPSvESSEDRPPRREGDEDRPPRREGDEDRPLRrgldedRPPR 1004
Cdd:TIGR01622 3 RDRERERLRDSSSAGDRD---RRRDKGRERSRDRSRDRER-SRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRP 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2024509102 1005 RGLDDDRG-SWRAADDDRGPRRgmDDDRPPRRALDDDRPPRRaldDDR 1051
Cdd:TIGR01622 73 REKRRRRGdSYRRRRDDRRSRR--EKPRARDGTPEPLTEDER---DRR 115
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
517-784 |
6.28e-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: 44.07 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKppHLLqEKEEQHQLAVTAFLKNSRKEHQRILARR----QTIEERKERLESL------- 585
Cdd:pfam06160 89 DEIEELLDDIEEDIKQILEELD--ELL-ESEEKNREEVEELKDKYRELRKTLLANRfsygPAIDELEKQLAEIeeefsqf 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 586 -----------------NIQREKEELEQR-------EAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRER 639
Cdd:pfam06160 166 eeltesgdylearevleKLEEETDALEELmedipplYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKeiQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 640 LEQ----IKKTELGAKAFKDIDIED-LEELdpdfimakqVEQLEKEKKELQERLKNQEKKIDYFERAKR-----LEEIPL 709
Cdd:pfam06160 246 LEEnlalLENLELDEAEEALEEIEErIDQL---------YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEqnkelKEELER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 710 IKTAY-----EEQRVRDmelWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALrrtvyEDKLKQFQERLA 784
Cdd:pfam06160 317 VQQSYtlnenELERVRG---LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI-----EEEQEEFKESLQ 388
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
1050-1157 |
7.46e-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: 43.73 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1050 DRPPRRALDDDRPPRRALDDDRPPRRSLDDDRgsWRAADDDRGPRRGLDDDRPPRRALDDDRPPRrgldDDRGSWRAADD 1129
Cdd:TIGR01642 2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDSRSPR----SLRYSSVRRSR 75
|
90 100
....*....|....*....|....*....
gi 2024509102 1130 DRGPRRGLDDDRGPR-RGLDDDRGPWRNT 1157
Cdd:TIGR01642 76 DRPRRRSRSVRSIEQhRRRLRDRSPSNQW 104
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
902-1120 |
7.99e-04 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 43.79 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 902 RGGETESEWRRAPVERDWRRGEARDDE----RPFRRGDD-------LPRRSDDLPRRGDDLPR---RGPAEEKERPSVES 967
Cdd:PHA03321 449 RPGSTPACARRARAQRARDAGPEYVDPlgalRRLPAGAApppepaaAPSPATYYTRMGGGPPRlppRNRATETLRPDWGP 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 968 SEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPrrgmDDDRPPRRALDDDRPPRRAL 1047
Cdd:PHA03321 529 PAAAPPEQMEDPYLEPDDDRFDRRDGAAAAATSHPREAPAPDDDPIYEGVSDSEEP----VYEEIPTPRVYQNPLPRPME 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 1048 DDDRPPrralDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDddrPPRRALDDDRPPRRGLDDD 1120
Cdd:PHA03321 605 GAGEPP----DLDAPTSPWVEEENPIYGWGDSPLFSPPPAARFPPPDPALS---PEPPALPAHRPRPGALAPD 670
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
949-1073 |
8.70e-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: 43.73 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 949 DDLPRRGPAEEKERpSVESSEDRPPRREGDEDRppRREGDEDRPLRRGLDEDRPPRRGLDDDrgswRAADDDRGPRRGMD 1028
Cdd:TIGR01642 2 DEEPDREREKSRGR-DRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDS----RSPRSLRYSSVRRS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2024509102 1029 DDRPPRRALDDDR--PPRRALDDDRPPRRALDDDRppRRALDDDRPP 1073
Cdd:TIGR01642 75 RDRPRRRSRSVRSieQHRRRLRDRSPSNQWRKDDK--KRSLWDIKPP 119
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
545-659 |
9.55e-04 |
|
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: 43.05 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 545 EKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKerleslNIQREKEELEQREAEL-QKVRKAEEERLRQEAKE-REKE 622
Cdd:pfam07767 212 LKEEEKLERVLEKIAESAATAEAREEKRKTKAQRN------KEKRRKEEEREAKEEKaLKKKLAQLERLKEIAKEiAEKE 285
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024509102 623 RILQEHEQIKKKTVRERLEQIKKTE---LGAKAFKDIDIE 659
Cdd:pfam07767 286 KEREEKAEARKREKRKKKKEEKKLRprkLGKHKVPEPDLE 325
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
545-749 |
9.78e-04 |
|
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: 43.40 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 545 EKEEQHQLAVTAFLKNSRKEH--------QRILARRQTIE-ERKERLESLNIQREKEELEQR---EAELQKVRKAEEERL 612
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKasrdrlraERAEMRRLEVErKRREQEEQRRLQQEQLERAEKmreELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 613 RQEAKEREKERilQEHEQIKK----KTVRERLEQiKKTELGAKAFKDIDIEDLEEldpdfimAKQVEQLEKEKKELQERL 688
Cdd:pfam15709 392 RKQRLEEERQR--QEEEERKQrlqlQAAQERARQ-QQEEFRRKLQELQRKKQQEE-------AERAEAEKQRQKELEMQL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024509102 689 KNQEKKIDYFERAKRLEEIPLiKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNR 749
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQ-KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
553-645 |
9.94e-04 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 41.77 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 553 AVTAFLKNsRKehQRILarrQTIEERKERLESLNiqrekEELEQREAELQKVrKAEEERLRQEA---KEREKERILQehe 629
Cdd:CHL00019 48 VLSDLLDN-RK--QTIL---NTIRNSEERREEAI-----EKLEKARARLRQA-ELEADEIRVNGyseIEREKENLIN--- 112
|
90
....*....|....*.
gi 2024509102 630 QIKKKTvrERLEQIKK 645
Cdd:CHL00019 113 QAKEDL--ERLENYKN 126
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
571-755 |
1.04e-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: 43.80 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 571 RRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQE-------AKEREKERILQEHEQIKKKtvRERLE 641
Cdd:TIGR00618 213 MPDTYHERKQVLEKElkHLREALQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELRAQEAVLEETQER--INRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 642 QIKKTELGAKAFKDIDiedleeLDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-----EEIPLIKTAYEE 716
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIE------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtlhsQEIHIRDAHEVA 364
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024509102 717 QRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:TIGR00618 365 TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
920-1123 |
1.14e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 920 RRGEARDDERPfrrgdDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRregdEDRPPRREGDEDRPLRRGLDE 999
Cdd:PHA03247 2879 ARPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ----PQPPPPPPPRPQPPLAPTTDP 2949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1000 D--RPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRA------LDDDRPPRRALDDDR 1071
Cdd:PHA03247 2950 AgaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWAsslalhEETDPPPVSLKQTLW 3029
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 1072 PPRRSLDDDRGSWRAADDDRGPRRGLD-DDRPPRRALDDDRPPRRGLDDDRGS 1123
Cdd:PHA03247 3030 PPDDTEDSDADSLFDSDSERSDLEALDpLPPEPHDPFAHEPDPATPEAGARES 3082
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
517-801 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTaflknsRKEHQRILARRQTIEERKERLESLniQREKEELEQ 596
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELA------ELQEELEELLEQLSLATEEELQDL--AEELEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMA----- 671
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgll 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 672 ---------------KQVEQLEK--EKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERIT 734
Cdd:COG4717 287 allflllarekaslgKEAEELQAlpALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102 735 TLQLEREKALEHKNrlsrmLEDRDLFEARLKALRRTV-YEDKLKQFQERLAEERRNRLEERKKQRKEE 801
Cdd:COG4717 367 ELEQEIAALLAEAG-----VEDEEELRAALEQAEEYQeLKEELEELEEQLEELLGELEELLEALDEEE 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
518-694 |
1.44e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 518 QIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQR 597
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 598 EAElqkvrkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKK--TELGA---KAfkdidIEDLEELDP--DFiM 670
Cdd:COG1196 734 REE-------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEReiEALGPvnlLA-----IEEYEELEEryDF-L 800
|
170 180
....*....|....*....|....*.
gi 2024509102 671 AKQVEQLEKEKKELQERLK--NQEKK 694
Cdd:COG1196 801 SEQREDLEEARETLEEAIEeiDRETR 826
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
544-783 |
1.56e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 544 QEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeSLNIQREKEELEQREAELQKVRKAEEERLrqeakEREKER 623
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQ-----QEKEEL 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 624 ILQEHEQikKKTVRERLEQIKKtELGAKAFKDIDIED-LEELDPDFIMAK---------QVEQLEKEKKELQERLKNQEK 693
Cdd:TIGR00606 929 ISSKETS--NKKAQDKVNDIKE-KVKNIHGYMKDIENkIQDGKDDYLKQKetelntvnaQLEECEKHQEKINEDMRLMRQ 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 694 KIDYFERAKRLEEIPLIKtayeeqRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLF--EARLKALRRTV 771
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTL------RKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIkrNHVLALGRQKG 1079
|
250
....*....|..
gi 2024509102 772 YEDKLKQFQERL 783
Cdd:TIGR00606 1080 YEKEIKHFKKEL 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
517-783 |
1.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 517 EQIRNQLTAMSSALAKALAVikpphlLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeslniQREKEELEQ 596
Cdd:COG4717 159 RELEEELEELEAELAELQEE------LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA-----QEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 597 REAEL--QKVRKAEEERLRQEA-------------------------------------------KEREKERILQEHEQI 631
Cdd:COG4717 228 ELEQLenELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 632 KKKTVRERLEQIKKTELgAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQE------------------- 692
Cdd:COG4717 308 QALPALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEleqeiaallaeagvedeee 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 693 --KKIDYFERAKRL-EEIPLIKTAYEEQRVRDMELWEQQEEERITT-LQLEREKALEHKNRLSRMLEDRDLFEARLKALR 768
Cdd:COG4717 387 lrAALEQAEEYQELkEELEELEEQLEELLGELEELLEALDEEELEEeLEELEEELEELEEELEELREELAELEAELEQLE 466
|
330
....*....|....*
gi 2024509102 769 RTVYEDKLKQFQERL 783
Cdd:COG4717 467 EDGELAELLQELEEL 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
558-755 |
2.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQRILARRQTIEER----KERLESLN--IQREKEELEQREAELQkvrKAEEERLRQEAKEREKERILQEH--E 629
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAEldalQAELEELNeeYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERarA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 630 QIKKKTVRERLEQIkkteLGAKAFKD-ID----IEDLEELDpdfimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRL 704
Cdd:COG3883 95 LYRSGGSVSYLDVL----LGSESFSDfLDrlsaLSKIADAD-----ADLLEELKADKAELEAKKAELEAKLA--ELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024509102 705 EEIpliktayeEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:COG3883 164 AEL--------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
926-1150 |
2.74e-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: 42.20 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 926 DDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRR 1005
Cdd:NF033609 623 DSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1006 GLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWR 1085
Cdd:NF033609 703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1086 AADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609 783 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 847
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
1040-1135 |
2.89e-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: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1040 DRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRraldddRPPRRGLDD 1119
Cdd:TIGR01622 4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRPREKRR 77
|
90
....*....|....*..
gi 2024509102 1120 DRG-SWRAADDDRGPRR 1135
Cdd:TIGR01622 78 RRGdSYRRRRDDRRSRR 94
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
543-784 |
3.18e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVTAFLKNSRKEHQRILARR----QTIEERKERLESLniqreKEELEQREAELQK--VRKAEEERLRQEA 616
Cdd:PRK04778 131 LLESEEKNREEVEQLKDLYRELRKSLLANRfsfgPALDELEKQLENL-----EEEFSQFVELTESgdYVEAREILDQLEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 617 KEREKERILQEHEQIKKKTVRERLEQIKKTELGAK-------AFKDIDIE---------------DLEELDPDfIMAKQV 674
Cdd:PRK04778 206 ELAALEQIMEEIPELLKELQTELPDQLQELKAGYRelveegyHLDHLDIEkeiqdlkeqidenlaLLEELDLD-EAEEKN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 675 EQLEKEKKEL-----------QERLKNQEKKIDYFERAKR-----LEEIPLIKTAY-----EEQRVRDmelWEQQEEERI 733
Cdd:PRK04778 285 EEIQERIDQLydilerevkarKYVEKNSDTLPDFLEHAKEqnkelKEEIDRVKQSYtlnesELESVRQ---LEKQLESLE 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024509102 734 TTLQLEREKALEHKNRLSrMLEDRdlFEARLKALrrTVYEDKLKQFQERLA 784
Cdd:PRK04778 362 KQYDEITERIAEQEIAYS-ELQEE--LEEILKQL--EEIEKEQEKLSEMLQ 407
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
543-691 |
3.54e-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: 41.28 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLAVtaflkNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam09787 77 LQELEAQQQEEA-----ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102 623 RilqehEQIKKKT--------VRERLEQIKKTELGAKAFkdidiedLEELDPDF-IMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam09787 152 R-----NQLTSKSqssssqseLENRLHQLTETLIQKQTM-------LEALSTEKnSLVLQLERMEQQIKELQGEGSNG 217
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
570-645 |
3.65e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 570 ARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAK------EREKERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam02841 201 AKEKAIEAERAKAEAA--EAEQELLREKQKEEEQMMEAQERSYQEHVKqliekmEAEREQLLAEQERMLEHKLQEQEELL 278
|
..
gi 2024509102 644 KK 645
Cdd:pfam02841 279 KE 280
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
967-1226 |
3.66e-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: 41.82 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 967 SSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRA 1046
Cdd:NF033609 620 SDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1047 LDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRA 1126
Cdd:NF033609 700 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1127 ADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDrgpwrSSEDSRPgpwrpfgkpggwrEREKAREDSWGPP 1206
Cdd:NF033609 780 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-----SDSDSDS-------------DSDSDSDSDSDSD 841
|
250 260
....*....|....*....|
gi 2024509102 1207 RDSRPPGDREWDRDKDRDDN 1226
Cdd:NF033609 842 SDSDSDSDSDSDSDSESDSN 861
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
608-776 |
4.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 608 EEERLRQEAKEREKERILQEHEQIKKKTVRERleqikktelgakafkdidIEDLEEldpdfimakQVEQLEKEKKELQER 687
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE------------------IRRLEE---------QVERLEAEVEELEAE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 688 LKNQEKKIDYFERakrleEIPLIKTAYEEQRVRDMELweQQEEERITTLQLEREKALEHKNRLSRMLEdrdlfeaRLKAL 767
Cdd:COG2433 436 LEEKDERIERLER-----ELSEARSEERREIRKDREI--SRLDREIERLERELEEERERIEELKRKLE-------RLKEL 501
|
....*....
gi 2024509102 768 RRTVYEDKL 776
Cdd:COG2433 502 WKLEHSGEL 510
|
|
| U2AF_lg |
TIGR01642 |
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ... |
958-1090 |
4.20e-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: 41.42 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 958 EEKERPSVESSEDRppRREGDEDRPPRREGDEDRplRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRal 1037
Cdd:TIGR01642 2 DEEPDREREKSRGR--DRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSR-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 1038 ddDRPPRRALDDDRPPR-RALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDD 1090
Cdd:TIGR01642 76 --DRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYELVTAD 127
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
572-693 |
4.55e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERLESLnIQREKEELEQREAELqkvrkaeeERLRQ--EAKEREKERILQEHEQIKkkTVRERLEQI-KKTEL 648
Cdd:PRK04778 305 RKYVEKNSDTLPDF-LEHAKEQNKELKEEI--------DRVKQsyTLNESELESVRQLEKQLE--SLEKQYDEItERIAE 373
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024509102 649 GAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEK 693
Cdd:PRK04778 374 QEIAYSEL-QEELEEIL------KQLEEIEKEQEKLSEMLQGLRK 411
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
572-635 |
4.73e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 4.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 572 RQTIEERKERLEslniqREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT 635
Cdd:PRK05035 452 KARFEARQARLE-----REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKA 510
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
562-758 |
5.20e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREaelqkvRKAEEERLRQEAKEREKERILQEHEQI---KKKTVRE 638
Cdd:PTZ00440 794 NKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEK------NDEELKQLLQKFPTEDENLNLKELEKEfneNNQIVDN 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 639 RLEQIKKTELGAKAFKDIDIEdleeLDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQR 718
Cdd:PTZ00440 868 IIKDIENMNKNINIIKTLNIA----INRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKE 943
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024509102 719 vrdmELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRD 758
Cdd:PTZ00440 944 ----KIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGND 979
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
588-766 |
5.28e-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: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 588 QREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKtelgakafkdidiedleeldpd 667
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA---------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 668 fimAKQVEQLEKEKKELQ---ERLKNQEKKidyfERAKRLEEIPLIKTAYEEQRvrdmelweQQEEERITTLQLERE-KA 743
Cdd:TIGR02794 104 ---AKQAEQAAKQAEEKQkqaEEAKAKQAA----EAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKkKA 168
|
170 180
....*....|....*....|...
gi 2024509102 744 LEHKNRLSRMLEDRDLFEARLKA 766
Cdd:TIGR02794 169 EEAKKKAEAEAKAKAEAEAKAKA 191
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
572-691 |
5.38e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.57 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 572 RQTIEERKERleslnIQREKEELEQREAELQKVRKAEEERLrQEAKErEKERILQEHEQIKKKTVRERLEQIKktelgak 651
Cdd:cd06503 25 LKALDEREEK-----IAESLEEAEKAKEEAEELLAEYEEKL-AEARA-EAQEIIEEARKEAEKIKEEILAEAK------- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024509102 652 afkdidiEDLEEldpdfIMAKQVEQLEKEKKELQERLKNQ 691
Cdd:cd06503 91 -------EEAER-----ILEQAKAEIEQEKEKALAELRKE 118
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
544-690 |
5.52e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 544 QEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL----EQREAELQKVRKAEEERLRQEAKER 619
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqkeEQLDARAEKLDNLENQLEEREKALS 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102 620 EKERILQEheqiKKKTVRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKELQERLKN 690
Cdd:PRK12705 116 ARELELEE----LEKQLDNELYRV--AGLTPEQARKLLLKLLDaELEEE--KAQRVKKIEEEADLEAERKAQ 179
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1032-1227 |
6.29e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1032 PPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRgldDDRPPRRALDDDR 1111
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQAR---ERRERGEAARRGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1112 PPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGpwrntdddrlsrrdddrgpwRSSEDSRPGPWRPFGKPGG 1191
Cdd:PRK12678 142 ARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQ--------------------AEAERGERGRREERGRDGD 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024509102 1192 WREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:PRK12678 202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRD 237
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
966-1181 |
7.32e-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: 41.05 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 966 ESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRR 1045
Cdd:NF033609 649 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1046 ALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWR 1125
Cdd:NF033609 729 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 1126 AADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSSE---DSRPG 1181
Cdd:NF033609 809 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDsnsDSESG 867
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
559-751 |
7.33e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 39.77 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 559 KNSRKEHQRILARRQTIEER--KERLESLNIQREKEELEQREAELQKVRKAEEE----------RLRQEAKEREKERILQ 626
Cdd:cd07647 18 KKMCKELEDFLKQRAKAEEDygKALLKLSKSAGPGDEIGTLKSSWDSLRKETENvanahiqlaqSLREEAEKLEEFREKQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 627 E-----HEQIKKKTVRERLEQIKKTeLGAKAFKDIDIEDLEELDPDF----IMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:cd07647 98 KeerkkTEDIMKRSQKNKKELYKKT-MKAKKSYEQKCREKDKAEQAYekssSGAQPKEAEKLKKKAAQCKTSAEEADSAY 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 698 FERAKRLEEiplIKTAYEEQRVRDMELWEQQEEERITTLqleREKALEHKNRLS 751
Cdd:cd07647 177 KSSIGCLED---ARVEWESEHATACQVFQNMEEERIKFL---RNALWVHCNLGS 224
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
543-652 |
8.82e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 543 LQEKEEQHQLavtaflKNSRKEHQRILARrqtiEERKERLEslniQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:PRK09510 92 LQQKQAAEQE------RLKQLEKERLAAQ----EQKKQAEE----AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110
....*....|....*....|....*....|
gi 2024509102 623 RILQEHEQIKKKtvRERLEQIKKTELGAKA 652
Cdd:PRK09510 158 AAAKKAAAEAKK--KAEAEAAKKAAAEAKK 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
499-756 |
9.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 499 YSTREDAPLGPQLQSMPSEQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEER 578
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 579 KERLESLNIQREKEELEQREAELQKVRKAEEERlrqeakeREKERILQEHEqikkKTVRERLEQIKKTELGAKafkdidI 658
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEEL-------EELEEQLEELL----GELEELLEALDEEELEEE------L 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 659 EDLEEldpdfimakQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEiplIKTAYEEQRVRdmelwEQQEEERITTLQ- 737
Cdd:COG4717 435 EELEE---------ELEELEEELEELREELAELEAELEQLEEDGELAE---LLQELEELKAE-----LRELAEEWAALKl 497
|
250 260
....*....|....*....|...
gi 2024509102 738 ----LEREKALEHKNRLSRMLED 756
Cdd:COG4717 498 alelLEEAREEYREERLPPVLER 520
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
1100-1227 |
9.50e-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: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1100 DRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDrlsrrdddrgpwRSSEDSR 1179
Cdd:TIGR01622 4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSR------------RPNRRYR 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2024509102 1180 PgpwrpfgkpggwREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:TIGR01622 72 P------------REKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPL 107
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
541-634 |
9.52e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.06 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 541 HLLQEKEEQHQlavtAFLKNSRKEHQRIlarRQTIEERKERLESLNIQREKE-----ELEQREAELQ-KVRKAEEE-RLR 613
Cdd:PRK11637 187 AELEEKQSQQK----TLLYEQQAQQQKL---EQARNERKKTLTGLESSLQKDqqqlsELRANESRLRdSIARAEREaKAR 259
|
90 100
....*....|....*....|.
gi 2024509102 614 QEAKEREKERILQEHEQIKKK 634
Cdd:PRK11637 260 AEREAREAARVRDKQKQAKRK 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
558-697 |
9.60e-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: 40.39 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 558 LKNSRKEHQrILARRQTIEERKERLESL-NIQREKEEL-EQREAELQKVRKAEEER-LRQEAKEREKERILQEHEQI--- 631
Cdd:TIGR04523 554 LKKENLEKE-IDEKNKEIEELKQTQKSLkKKQEEKQELiDQKEKEKKDLIKEIEEKeKKISSLEKELEKAKKENEKLssi 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 632 ------KKKTVRERLEQIKKTELGAKA-FKDID--IEDLEELDPDFIMA------------------------------- 671
Cdd:TIGR04523 633 ikniksKKNKLKQEVKQIKETIKEIRNkWPEIIkkIKESKTKIDDIIELmkdwlkelslhykkyitrmirikdlpkleek 712
|
170 180 190
....*....|....*....|....*....|.
gi 2024509102 672 -KQVEQ----LEKEKKELQERLKNQEKKIDY 697
Cdd:TIGR04523 713 yKEIEKelkkLDEFSKELENIIKNFNKKFDD 743
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
562-803 |
9.87e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 562 RKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERlRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG5022 761 RRRYLQALKRIKKIQVIQHGFRLR--RLVDYELKWRLFIKLQPLLSLLGS-RKEYRSYLACIIKLQKTIKREKKLRETEE 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 642 Q---IKKTELGAKAFKDI-DIEDLEELDPDFIMAKQVEQLEKEKKELQErLKNQEKKIDY-FERAKRLEEIPLiktayee 716
Cdd:COG5022 838 VefsLKAEVLIQKFGRSLkAKKRFSLLKKETIYLQSAQRVELAERQLQE-LKIDVKSISSlKLVNLELESEII------- 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 717 qrvrdmELWEQQEEERITTLQLErekaLEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKK 796
Cdd:COG5022 910 ------ELKKSLSSDLIENLEFK----TELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKK 979
|
....*..
gi 2024509102 797 QRKEERR 803
Cdd:COG5022 980 STILVRE 986
|
|
|