|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1028-1105 |
1.18e-30 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 115.77 E-value: 1.18e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 1028 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1105
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
845-913 |
7.85e-28 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 107.68 E-value: 7.85e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110835729 845 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 913
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
456-532 |
3.34e-27 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 106.14 E-value: 3.34e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 456 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 532
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1151-1207 |
6.36e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 73.30 E-value: 6.36e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 1151 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1207
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-364 |
4.15e-14 |
|
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: 77.79 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 18 QQLQRELDATATVLANRQD---ESEQSRKRLIEQSRE-----FKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDilnELERQLKSLERQAEKaerykELKAELRELELALLVLrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 89 FLTVYKRLidvpdpvpaldvgQQLEIKVQRLhdiETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTL 164
Cdd:TIGR02168 255 LEELTAEL-------------QELEEKLEEL---RLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 165 KSQAETIALEKEQK--LQNDFAEKERKLQETQMSTTS---KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD- 238
Cdd:TIGR02168 319 EELEAQLEELESKLdeLAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASl 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 239 --EIEMIMTDLERANQRAEVAQREAETLREQLSSANhslqlasqiqkapdveqaievltRSSLEVELAAKEREIAQLVED 316
Cdd:TIGR02168 399 nnEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----------------------LKELQAELEELEEELEELQEE 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 110835729 317 VQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 364
Cdd:TIGR02168 456 LERLEEALEELRE----ELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-377 |
1.69e-13 |
|
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: 75.86 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 107 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 182
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 183 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 252
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 253 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE--- 329
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRSele 897
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 330 -------NSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEF 377
Cdd:TIGR02168 898 elseelrELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1151-1208 |
2.14e-13 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 66.11 E-value: 2.14e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 1151 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1208
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-369 |
3.87e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsrefkkntpedlrkqvapllksfqgEIDALSKRSKEAEAAFltvykrli 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA-------------------------ELEELEAELEELEAEL-------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 98 dvpdpvpaldvgQQLEIKVQRLHD-IETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:COG1196 263 ------------AELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 177 QklQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 331 E--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 257 AQREAETLREQLSSANHSLQLASQIQkapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 336
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350
....*....|....*....|....*....|...
gi 110835729 337 QLEQQLNAKNSTLKQLEEKLKGQADYEEVKKEL 369
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1151-1206 |
1.17e-12 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 63.81 E-value: 1.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 1151 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1206
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-411 |
2.09e-11 |
|
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: 68.93 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 123 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 199
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 200 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 276
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 277 LASQIQKAPDVEQAIEVLTrSSLEVELAAKEREIAQLVEDVQ---RLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 353
Cdd:TIGR02168 328 LESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110835729 354 EKLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 411
Cdd:TIGR02168 407 ARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-374 |
5.06e-11 |
|
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: 67.79 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 58 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 134
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 135 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 212
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 213 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS-----ANHSLQLASQIQKAPDV 287
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkerDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 288 EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASltklRENSASqISQLEQQLNAKNSTLKQLEE-KLKGQADYEE 364
Cdd:TIGR02169 909 EAQIEKKRKrlSELKAKLEALEEELSEIEDPKGEDEEI----PEEELS-LEDVQAELQRVEEEIRALEPvNMLAIQEYEE 983
|
330
....*....|
gi 110835729 365 VKKELNTLKS 374
Cdd:TIGR02169 984 VLKRLDELKE 993
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-375 |
8.75e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 19 QLQRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLT 91
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 92 VYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKSQAETi 171
Cdd:PRK03918 478 LRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 172 aLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERA 250
Cdd:PRK03918 548 -LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LERE 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 251 NQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklren 330
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA-------- 680
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110835729 331 sasQISQLEQQLNAKNSTLKQLEEKLKgqaDYEEVKKELNTLKSM 375
Cdd:PRK03918 681 ---ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-370 |
9.14e-11 |
|
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: 66.52 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 82 SKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 157 IREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 236 KAD-----------EIEMIMTDLERANQraEVAQREAETLREQLS-SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 303
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRqIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 304 AAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQadYEEVKKELN 370
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ--LEGVRSKLD 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-299 |
2.60e-10 |
|
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: 65.46 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 93 ykrlidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 110835729 250 ANQRAEVAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 299
Cdd:TIGR02168 497 LQENLEGFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-322 |
3.12e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSfQGEIDALSKRSKEAEAAFLTVYKR 95
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARL-EQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 96 LidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiALEK 175
Cdd:COG1196 325 L---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEI-EMIMTDLERANQRA 254
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeEEEALLELLAELLE 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 255 EVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 322
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-374 |
3.60e-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: 65.09 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 112 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 192 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssA 271
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL--A 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 272 NHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKN 346
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreKLEKLKREINELK 405
|
250 260
....*....|....*....|....*....
gi 110835729 347 STLKQL-EEKLKGQADYEEVKKELNTLKS 374
Cdd:TIGR02169 406 RELDRLqEELQRLSEELADLNAAIAGIEA 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-353 |
5.79e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 206 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 286 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 353
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-334 |
1.02e-09 |
|
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: 62.09 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 105 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 182 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 257 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 334
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-374 |
1.66e-09 |
|
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: 62.35 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 185
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 186 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQREAETLR 265
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 266 EQLSSanhslqLASQIQKAPDVEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAK 345
Cdd:TIGR04523 391 SQIND------LESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNL 459
|
250 260
....*....|....*....|....*....
gi 110835729 346 NSTLKQLEEKLKgqadyeEVKKELNTLKS 374
Cdd:TIGR04523 460 DNTRESLETQLK------VLSRSINKIKQ 482
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-375 |
2.39e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 7 SMFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlrkqvapllksfQGEIDALSKRSKEAE 86
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL----------------QEELEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 87 AAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIKALKEKIREYEQTLKS 166
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 167 QAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMT- 245
Cdd:COG4717 182 LLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LEERLKEARLLLLIAAa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 246 ----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER 308
Cdd:COG4717 258 llallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110835729 309 EIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 375
Cdd:COG4717 338 ELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-372 |
5.24e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflTVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 96 LIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlksqaet 170
Cdd:PRK03918 534 LIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP-------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 171 iALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERA 250
Cdd:PRK03918 600 -FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSRE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 251 NQRAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKLRE 329
Cdd:PRK03918 675 LAGLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LLKE 739
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 110835729 330 NSASQISQLEQQL-----NAKNS--TLKQLEEKLKGQADYEEVKKELNTL 372
Cdd:PRK03918 740 RALSKVGEIASEIfeeltEGKYSgvRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-375 |
1.05e-08 |
|
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: 59.01 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 166 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTkydeettakadEIEMI 243
Cdd:COG4942 17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQ-----------ELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 244 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKERE 309
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 310 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSM 375
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-360 |
2.23e-08 |
|
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: 57.85 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 121 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERKLQETQMsttsK 200
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELEK----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 201 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQ 280
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA------ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 281 IQkapdvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 360
Cdd:COG4942 166 RA-----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-374 |
2.32e-08 |
|
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: 58.88 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 185
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 186 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 264 lrEQLSSANHSLqLASQIQKAPDVEQAIEvlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLN 343
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQKEK--EKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKN 641
|
250 260 270
....*....|....*....|....*....|..
gi 110835729 344 AKNSTLKQLEEKLKG-QADYEEVKKELNTLKS 374
Cdd:TIGR04523 642 KLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
106-375 |
3.19e-08 |
|
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: 58.44 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 106 LDVGQQLEIKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA----ETIA--LEKEQ 177
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 178 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 253
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 254 AEVAQREAETLREQLSsanhslQLASQI-QKAPDVEQAIEvltrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSA 332
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIgQEIPSDEDILN------LQCETLVQEEE------------QFLSRLEEKSA 842
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 110835729 333 SQIsQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 375
Cdd:TIGR00618 843 TLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-374 |
3.63e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 142 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 214
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 215 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLSSANHslqlasqiqkapdveQAIEvl 294
Cdd:COG4913 297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQIRGNGG---------------DRLE-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 295 trsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLNAKNSTLKQLEEKL--------KGQ 359
Cdd:COG4913 342 ---QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALaeaeaalrDLR 418
|
250
....*....|....*
gi 110835729 360 ADYEEVKKELNTLKS 374
Cdd:COG4913 419 RELRELEAEIASLER 433
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
36-357 |
6.16e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.07 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 36 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAA-FLTVYKRLIDvpdpvpaldvgQQL 112
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEAQeLREKRDELNE-----------KVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 113 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 193 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 272
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 273 HSLQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQL 352
Cdd:COG1340 216 KEIVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEI 272
|
....*
gi 110835729 353 EEKLK 357
Cdd:COG1340 273 FEKLK 277
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
19-356 |
7.18e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 19 QLQRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV---YKR 95
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYNR 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 96 LIdvpdpvpaLDVGQQLEIKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKSQAETIALE 174
Cdd:pfam12128 380 RR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKSR 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 175 -KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQR 253
Cdd:pfam12128 446 lGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASRR 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 254 AEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA- 322
Cdd:pfam12128 515 LEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDVp 593
|
330 340 350
....*....|....*....|....*....|....
gi 110835729 323 SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKL 356
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-559 |
8.37e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 86 EAAFLTVYKRLIDVPDPvPALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARLKKLLNNIDLEEG-PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 166 S--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQ----LASQIQKAPDVEQAIEV-------LT 295
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskfLSQLVNTLEPVFQKLSVlqleldgLF 1160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 296 RSSLEVELAAKEREIAqLVEDVQRLQASLTKLRENSASQISQLEQQLNAK------NSTLKQLEEKLKGQA-DYEEVKKE 368
Cdd:COG5022 1161 WEANLEALPSPPPFAA-LSEKRLYQSALYDEKSKLSSSEVNDLKNELIALfskifsGWPRGDKLKKLISEGwVPTEYSTS 1239
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 369 LNTLKSMEFAPSEGAGtQDSTKPLEVL-LLEKNRSLQSENATLriSNSDLSGPYSTNSISSPSPLqqSPDVNGMAPSPSQ 447
Cdd:COG5022 1240 LKGFNNLNKKFDTPAS-MSNEKLLSLLnSIDNLLSSYKLEEEV--LPATINSLLQYINVGLFNAL--RTKASSLRWKSAT 1314
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 448 SESAGSISEGEEIDTAEIARqVKEQLI------------KHNIGQ--RIFGhYVLGLSQGSVSEILARPKPWNKLTvrgk 513
Cdd:COG5022 1315 EVNYNSEELDDWCREFEISD-VDEELEeliqavkvlqllKDDLNKldELLD-ACYSLNPAEIQNLKSRYDPADKEN---- 1388
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 110835729 514 epfHKMKQFLsdeQNILALRSIQGRQRENPG-QSLNRLFQEVPKRRN 559
Cdd:COG5022 1389 ---NLPKEIL---KKIEALLIKQELQLSLEGkDETEVHLSEIFSEEK 1429
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-495 |
1.27e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 196 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 276 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 340
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 341 QLNAKNSTLKQLEEKLK-GQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 419
Cdd:COG3883 176 QQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 420 PYSTNSISSPSPLQQSPDVNGMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSV 495
Cdd:COG3883 256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGG 331
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
199-370 |
1.30e-07 |
|
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: 54.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 199 SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLREQLSSA--NHS 274
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEEQLGNVrnNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 275 LQ-LASQIQKApdvEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQ 351
Cdd:COG1579 91 YEaLQKEIESL---KRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
170 180
....*....|....*....|.
gi 110835729 352 LEEKLKGQ--ADYEEVKKELN 370
Cdd:COG1579 168 LAAKIPPEllALYERIRKRKN 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-361 |
1.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykr 95
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 96 lidvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4913 688 --------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAP-DVEQAIEVLTRSSLEVE--------LAAKEREiaqlVED 316
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIrEIKERIDPLNDSLKRIPfgpgrylrLEARPRP----DPE 895
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110835729 317 VQRLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQAD 361
Cdd:COG4913 896 VREFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEE 937
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-355 |
2.11e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.41 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 151 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 214 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 277
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 278 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQL 352
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 110835729 353 EEK 355
Cdd:PHA02562 399 VKE 401
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
2.18e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 54.30 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 110835729 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-374 |
2.38e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 173
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 174 EKEQ------------------KLQNDFAEKERKLQETQMSTT----------SKLEEAEHKLQTLQTALEKTRTELFDL 225
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 226 KTKYDEETTAKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP-- 285
Cdd:PRK03918 358 EERHELYEEAKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 286 --------DVEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLNAKN 346
Cdd:PRK03918 438 cpvcgrelTEEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN 516
|
330 340
....*....|....*....|....*...
gi 110835729 347 stLKQLEEKLKgqaDYEEVKKELNTLKS 374
Cdd:PRK03918 517 --LEELEKKAE---EYEKLKEKLIKLKG 539
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-352 |
3.23e-07 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 52.22 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 131 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 202
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 203 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 275
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 276 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLNAKNSTLKQL 352
Cdd:pfam13851 137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-360 |
3.49e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 13 KRFDLQQLQRELDATATVLAnrqdESEQSRKRLIEQSREfKKNTPEDLRKQVAPLLKSF---QGEIDALSKRSKEAEAAF 89
Cdd:PRK02224 249 RREELETLEAEIEDLRETIA----ETEREREELAEEVRD-LRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 90 LTVYKRLIDVPdpVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQT-- 163
Cdd:PRK02224 324 EELRDRLEECR--VAAQAHNEEAESLREDADDLEERAEELREEAAELESELeearEAVEDRREEIEELEEEIEELRERfg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 164 --------LKSQAETIALEKE-------------QKLQNDFAEKERKLQETQMST----------TSKLEEAEHKLQTLQ 212
Cdd:PRK02224 402 dapvdlgnAEDFLEELREERDelrereaeleatlRTARERVEEAEALLEAGKCPEcgqpvegsphVETIEEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 213 TALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQ 289
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAeLEAEAEEKREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 290 AIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQISQLEQQ--------------LNAKNSTLKQLE 353
Cdd:PRK02224 562 EAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKrealaelnderrerLAEKRERKRELE 640
|
....*..
gi 110835729 354 EKLKGQA 360
Cdd:PRK02224 641 AEFDEAR 647
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
31-376 |
3.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 31 LANRQDESEQSRKRLIEQSREF-----KKNTPEDLRKQVAPLlksfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPA 105
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakaKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 106 LD-VGQQLEIKVQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAET 170
Cdd:PRK03918 417 LKkEIKELKKAIEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEkerkLRKELRELEKVLKKESEL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 171 IALEK--------EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 225
Cdd:PRK03918 496 IKLKElaeqlkelEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 226 KTKYDEETTAKADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLT 295
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 296 RSSLEVELAAKEREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTL 372
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKY 733
|
....
gi 110835729 373 KSME 376
Cdd:PRK03918 734 KALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
3.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 190 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 110835729 270 S 270
Cdd:COG4913 430 S 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-359 |
4.15e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 197 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 273 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA-KNSTLKQ 351
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPE 831
|
....*...
gi 110835729 352 LEEKLKGQ 359
Cdd:COG4913 832 YEERFKEL 839
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-373 |
6.24e-07 |
|
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: 54.06 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 119 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 188
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 189 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 266 EQLSSANHSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASL 324
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 110835729 325 TklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 373
Cdd:pfam10174 432 S----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-375 |
6.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 187 ERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 262 ETLREQLSSANHSL----------QLASQIQkapDVEQAIEVLTRSSLE-----VELAAKEREI-AQLVEDVQRLQASLT 325
Cdd:COG3206 243 AALRAQLGSGPDALpellqspviqQLRAQLA---ELEAELAELSARYTPnhpdvIALRAQIAALrAQLQQEAQRILASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110835729 326 KLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSM 375
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-268 |
7.62e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 14 RFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 89 FLTVYKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02168 812 LTLLNEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 165 KSQAETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEM 242
Cdd:TIGR02168 883 ASLEEALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEE 955
|
250 260
....*....|....*....|....*.
gi 110835729 243 IMTDLERANQRAEVAQREAETLREQL 268
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI 981
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-383 |
8.84e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSrefkkntpedlrkqvapllksfqGEIDALSKRSKEAEAAFltvykrli 97
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQAN-----------------------GELEKASREETFARTAL-------- 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 98 dvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIA 172
Cdd:pfam12128 649 ------------KNARLDLRRLFD---EKQSEKDKKNKALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 173 LEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQtlQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERA 250
Cdd:pfam12128 714 TEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERI 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 251 NQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVEQAIEvltrsslevelaakereiaqlvedvqRLQASLTKLREN 330
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS--------------------------ELQQQLARLIAD 836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 110835729 331 SASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEvkkELNTLKsmEFAPSEGA 383
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS---KLATLK--EDANSEQA 884
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
656-839 |
1.38e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 656 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 733
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 734 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 813
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 110835729 814 NSPLPSSPIVPMAKPAKPSVPPLTPE 839
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-410 |
1.70e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRKRL------IEQSREFKKNTPEDLRKQVAPLLK---SFQG---EIDALSKRSKE 84
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLqntvheLEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGvlqEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 85 AEAAFLTVYKRLIDVP---------------DPVPALDVGQQLEIKVQrLHDIETENQKLRETLEEYNKEFAE--VKNQE 147
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHfrslgsaiskilrelDTEISYLKGRIFPVEDQ-LEALKSESQNKIELLLQQHQDRIEqlISEHE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 148 VTIKALKEKI---REYEQTLKSQAETIALEKEQK----------LQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA 214
Cdd:pfam15921 278 VEITGLTEKAssaRSQANSIQSQLEIIQEQARNQnsmymrqlsdLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 215 LEKTRTElfdlKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlssanhslqlasqiqkapDVEQAIevl 294
Cdd:pfam15921 358 LTEARTE----RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------------------DTGNSI--- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 295 TRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQ---LEEKLKGQADY-EEVKKELn 370
Cdd:pfam15921 413 TIDHLRRELDDRNME-------VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMlRKVVEEL- 484
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 110835729 371 TLKSMEFAPSEgagtqDSTKPLEVLLLEKNRSLQSENATL 410
Cdd:pfam15921 485 TAKKMTLESSE-----RTVSDLTASLQEKERAIEATNAEI 519
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-376 |
1.77e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykr 95
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL----- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 96 lidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEK 175
Cdd:pfam05483 445 ----------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 176 eQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIM 244
Cdd:pfam05483 502 -KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 245 TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDV 317
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNY 659
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 318 QRlQASLTKLRENS-----------ASQISQLEQQLNA----KNSTLKQLEEKLKGQAD--YEEVKKELNTLKSME 376
Cdd:pfam05483 660 QK-EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
26-364 |
1.93e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 26 ATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRLIDVPDPVpA 105
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEI-----EDLRETIAETER----EREELAEEVRDLRERLEELEEERDDLLAEA-G 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 106 LDVGQQlEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlksqaetialEKEQKLQNDFAE 185
Cdd:PRK02224 304 LDDADA-EAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 186 KERKLQETQMSTT---SKLEEAEHKLQTLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:PRK02224 368 LESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 263 TLRE--QLSSANHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQL 338
Cdd:PRK02224 447 ALLEagKCPECGQPVEGSPHVETIEEDRERVEELEaeLEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELI 525
|
330 340
....*....|....*....|....*.
gi 110835729 339 EQQLNAKNSTLKQLEEKLKGQADYEE 364
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEA 551
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-357 |
2.04e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 107 DVGQQLEIKVQ-----RLHDIETENQKLRETLEEY--NKEFAevknqEVTIKALKEKIREYEQTlksQAETIALEKE-QK 178
Cdd:PRK02224 191 QLKAQIEEKEEkdlheRLNGLESELAELDEEIERYeeQREQA-----RETRDEADEVLEEHEER---REELETLEAEiED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 179 LQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTE----------LFDLKTKYDEETTAKADEIEMIMTDLE 248
Cdd:PRK02224 263 LRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 249 RANQRAEVAQREAETLREQLSSANhslqlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL- 327
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELR---------EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDAp 404
|
250 260 270
....*....|....*....|....*....|..
gi 110835729 328 --RENSASQISQLEQQLNAKNSTLKQLEEKLK 357
Cdd:PRK02224 405 vdLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
101-357 |
2.14e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 101 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 179
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 180 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 256
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 257 AQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAAKEREIA---QLVEDVQRLQASLTKLRENSAS 333
Cdd:PRK11281 169 SQRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQALLNAQNDlqrKSLEGNTQLQDLLQKQRDYLTA 234
|
250 260 270
....*....|....*....|....*....|.
gi 110835729 334 QISQLEQQL-------NAKNstLKQLEEKLK 357
Cdd:PRK11281 235 RIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
105-372 |
2.27e-06 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 51.50 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 105 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 179
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 180 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 259
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 260 eaetLREQLSSANHSLQ----------------------LASQIQKAPDVEQAIEVLTRSSL----------EVELAAKe 307
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinigkQVFTITITTATTKTVDVTSIGGLingignasddEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 308 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 372
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-371 |
2.75e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 125 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 202 EEAEhKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 279
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 280 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 357
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250
....*....|....
gi 110835729 358 GQADYEEVKKELNT 371
Cdd:pfam02463 413 LARQLEDLLKEEKK 426
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
113-426 |
3.20e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 113 EIKVQRLHDIETENQKLRE-TLEEYNKEFAEVK-----------NQEVTIKALKEKIREYEQT---LKSQA------ETI 171
Cdd:PRK01156 383 SKNIERMSAFISEILKIQEiDPDAIKKELNEINvklqdisskvsSLNQRIRALRENLDELSRNmemLNGQSvcpvcgTTL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 172 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAn 251
Cdd:PRK01156 463 GEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINEL- 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 252 qraevaqREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVltRSSLEVE-LAAKEREIAQLVEDV----QRLQASLTK 326
Cdd:PRK01156 542 -------KDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAV--ISLIDIEtNRSRSNEIKKQLNDLesrlQEIEIGFPD 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 327 LRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSMEfapSEGAGTQDSTKPLEVLLLEKNRSLQSE 406
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNNKYNEIQEN---KILIEKLRGKIDNYKKQI---AEIDSIIPDLKEITSRINDIEDNLKKS 686
|
330 340
....*....|....*....|
gi 110835729 407 NATLRISNSDLSGPYSTNSI 426
Cdd:PRK01156 687 RKALDDAKANRARLESTIEI 706
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
198-424 |
4.50e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 198 TSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlsSANHSLQL 277
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK--SENYIDEI 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 278 ASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQLNAKNSTLK 350
Cdd:TIGR01612 1149 KAQINDLEDV--ADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVKGINLSYGK 1221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110835729 351 QLEEKLKGQADyEEVKKELNTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGPYSTN 424
Cdd:TIGR01612 1222 NLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIIS 1293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-374 |
4.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 177 QKLQNDFAEKERKLQ-----------ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMT 245
Cdd:COG4717 265 GGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 246 DLERANQ-RAEVAQREAETLREQLSSANHSL----------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLV 314
Cdd:COG4717 345 RIEELQElLREAEELEEELQLEELEQEIAALlaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110835729 315 EDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEklkgQADYEEVKKELNTLKS 374
Cdd:COG4717 425 LDEEELEEELEELEEELEEleeELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
114-327 |
4.97e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 114 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 190 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlERANQRAEvA 257
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EIMDEFNE-Q 335
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 258 QREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 327
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-630 |
5.92e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 112 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 177
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 178 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 249
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 250 ANQRAE---VAQREAETLREQLSSANHSL------------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL- 313
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyrlksrlgELKLRLNQATATPELLLQLENFDERIERAREEQEAANAe 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 314 VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQAdyeevkkelNTLksMEFAPSEGAGTQDST-KPL 392
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA---------GTL--LHFLRKEAPDWEQSIgKVI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 393 EVLLL-------EKNRSLQSENATLRISNSDLSGPYSTNSISSPSPLQQSPDVngmAPSPSQSESAgSISEGEEiDTAEI 465
Cdd:pfam12128 556 SPELLhrtdldpEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDK---AEEALQSARE-KQAAAEE-QLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 466 ARQVKEQLIKHNIGQRIFGHYVLGLSQGSVS-EILARPKpwNKLTVRGKEPFHKMKQFLSDEQNIL------ALRSIQGR 538
Cdd:pfam12128 631 NGELEKASREETFARTALKNARLDLRRLFDEkQSEKDKK--NKALAERKDSANERLNSLEAQLKQLdkkhqaWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 539 QRENPGQSLNRLfQEVPKRRNGSEGNITTRIRASETGSDEAIKSILEQAKRELqvqKTAEPVQTSSTSSSGNSDDAIRSI 618
Cdd:pfam12128 709 KREARTEKQAYW-QVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL---ASLGVDPDVIAKLKREIRTLERKI 784
|
570
....*....|..
gi 110835729 619 LQQARREMEAQQ 630
Cdd:pfam12128 785 ERIAVRRQEVLR 796
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
108-369 |
8.17e-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: 50.49 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 108 VGQQLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 173
Cdd:pfam05483 132 VSLKLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 174 EKEQKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKA 237
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 238 DEIEMIMTDLERANQRAEVAQReaeTLREQLSSANHSLQLASQiQKAPDVEQAIEVLTRSSLEV-ELAAKEREIAQLVE- 315
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQK---ALEEDLQIATKTICQLTE-EKEAQMEELNKAKAAHSFVVtEFEATTCSLEELLRt 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 316 DVQRLqasltklrENSASQISQLEQQLNAKNSTLKQLEE-KLKGQADYEEVKKEL 369
Cdd:pfam05483 368 EQQRL--------EKNEDQLKIITMELQKKSSELEEMTKfKNNKEVELEELKKIL 414
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
184-399 |
8.26e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 184 AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---EETTAKADEIEMIMTDLERANQRAEVAQRE 260
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEqleEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 261 AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ-ISQLE 339
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaLDELL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 340 QQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEK 399
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-358 |
1.23e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 84 EAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 160 YEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQTALEKTRTeLFD 224
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQR-AER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 225 LKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDVEQAIEVLTRSSL 299
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAWLAAQDALARLRE 617
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 300 EVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNSTLKQLEEKLKG 358
Cdd:PRK04863 618 QSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-353 |
1.34e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 205 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 276
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 277 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLNAKNSTLKQL 352
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 110835729 353 E 353
Cdd:pfam07111 297 E 297
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-419 |
1.60e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTL--KSQAETIALEKEQKLQN---DFAEKERKLQETQMSTT---- 198
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEeelKLLAKEEEELKSELLKLerrk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 199 ----SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImTDLERANQRAEVAQREAETLREQLSSANHS 274
Cdd:pfam02463 310 vddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-EELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 275 LQLASQIQKAPDVEQAIEVltrsSLEVELAAKEREIAQLvedvqrlqASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 354
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEA----QLLLELARQLEDLLKE--------EKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 355 KLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 419
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-373 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEA-AARLLLL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaEVKNQEVTIKALKEKIREYEQTLksqAETIALEKE 176
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-----EAALEAALAAALQNIVVEDDEVA---AAAIEYLKA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 177 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 257 AQREAETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE 329
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110835729 330 NSASQISQ-LEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 373
Cdd:COG1196 729 QLEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
69-374 |
1.73e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 69 KSFQGEIDAlSKRSKEAEAAFLTVYKRLIDVpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV 148
Cdd:TIGR01612 1496 KGCKDEADK-NAKAIEKNKELFEQYKKDVTE-----LLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 149 TIKALK-EKIR---EYEQTLKSQAETIALEKE-QKLQNDFAE------------KERKLQETQMSTTS------KLEEAE 205
Cdd:TIGR01612 1570 KIKEIKkEKFRiedDAAKNDKSNKAAIDIQLSlENFENKFLKisdikkkindclKETESIEKKISSFSidsqdtELKENG 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 206 HKLQTLQTALEKTRTE---LFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQRE-----AETLREQLSSANHSLQl 277
Cdd:TIGR01612 1650 DNLNSLQEFLESLKDQkknIEDKKKELDELDS----EIEKIEIDVDQHKKNYEIGIIEkikeiAIANKEEIESIKELIE- 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 278 asqiqkaPDVEQAIEVLTRSSLE-----VELAAKEREIAQLVEDVQRLQASLTK-LRENSASQISQLE---QQLNAKNST 348
Cdd:TIGR01612 1725 -------PTIENLISSFNTNDLEgidpnEKLEEYNTEIGDIYEEFIELYNIIAGcLETVSKEPITYDEiknTRINAQNEF 1797
|
330 340 350
....*....|....*....|....*....|.
gi 110835729 349 LKQLEEKLKGQA-----DYEEVKKELNTLKS 374
Cdd:TIGR01612 1798 LKIIEIEKKSKSylddiEAKEFDRIINHFKK 1828
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
1.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 91 TVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 171 ---IALEKEQKLQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-354 |
2.75e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 122 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 202 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 264
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 265 REQLSsanhslQLASQIQKAPDVEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNA 344
Cdd:COG3206 316 ASLEA------ELEALQAREASLQAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEAL 383
|
250
....*....|
gi 110835729 345 KNSTLKQLEE 354
Cdd:COG3206 384 TVGNVRVIDP 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
211-357 |
2.77e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 211 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 288
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 289 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKLK 357
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
117-370 |
2.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlKSQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN--LVQTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 197 T---TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 259
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 260 EAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVElaakeREIAQlvedvQRLQASLTKLRE--NSASQISQ 337
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEVS-----RSEAW-----DVARELLRRLREqrHLAEQLQQ 517
|
250 260 270
....*....|....*....|....*....|...
gi 110835729 338 LEQQLNAknstlkqLEEKLKGQADYEEVKKELN 370
Cdd:PRK04863 518 LRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-355 |
3.84e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 115 KVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEK 186
Cdd:COG3096 348 KIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 187 ERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE--- 255
Cdd:COG3096 426 RALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARell 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 256 --------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTK 326
Cdd:COG3096 502 rryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAE 575
|
250 260
....*....|....*....|....*....
gi 110835729 327 LREnsasQISQLEQQLNAKNSTLKQLEEK 355
Cdd:COG3096 576 AVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
3.96e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 110835729 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-376 |
4.07e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQL-----QAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 190 LQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4372 103 LESLQ-EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 270 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 349
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260
....*....|....*....|....*..
gi 110835729 350 KQLEEKLKGQADYEEVKKELNTLKSME 376
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEAL 288
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-410 |
4.09e-05 |
|
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: 48.50 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 210 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLASQ 280
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 281 IQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK 357
Cdd:TIGR00606 392 IKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 358 G--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 410
Cdd:TIGR00606 472 RilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-376 |
5.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 119 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKlqndfAEKERKLQEtqmstt 198
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 199 skLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 278
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 279 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLNAKNSTLKQLEEKLK 357
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEK 352
|
250
....*....|....*....
gi 110835729 358 GQADYEEVKKELNTLKSME 376
Cdd:PRK03918 353 RLEELEERHELYEEAKAKK 371
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1151-1208 |
5.81e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 44.73 E-value: 5.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 1151 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1208
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-378 |
6.23e-05 |
|
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: 47.51 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 119 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KSQAETIALE-KEQKLQNDFAEKERKLQE 192
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 193 TQMSTTSKleeaEHKLQTLQTALEKTRTEL------FDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:pfam10174 329 LKESLTAK----EQRAAILQTEVDALRLRLeekesfLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 263 TLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQI 335
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKV 484
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 110835729 336 SQLEQQLNAKNSTLKQLEEKLKGQADyEEVKKElNTLKSMEFA 378
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-368 |
6.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLIDVP 100
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI------- 171
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadeakk 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 172 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--R 249
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRE 329
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
330 340 350
....*....|....*....|....*....|....*....
gi 110835729 330 NSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 368
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-374 |
7.21e-05 |
|
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: 47.32 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKSQaETIALEKEQKLQND--FAEK 186
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 187 ERKLQETQMSTT----SKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 258
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEkqkkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 259 REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 335
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 110835729 336 SQLE---QQLNAKNSTLKQLEEKLKgqadyeEVKKELNTLKS 374
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-376 |
8.05e-05 |
|
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: 47.35 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 13 KRFD-LQQLQRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSK 80
Cdd:TIGR00606 173 QKFDeIFSATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 81 RSKEAEAAFLTVYKrlidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----K 156
Cdd:TIGR00606 253 RLKEIEHNLSKIMK-----------------LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 157 IREYEQTL-KSQAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDE 231
Cdd:TIGR00606 314 VREKERELvDCQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 232 ETTAK----------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEV 301
Cdd:TIGR00606 389 ERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKEL 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 302 E-LAAKEREIAQLVEDVQRLQASLTKLRENSASQiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 376
Cdd:TIGR00606 464 QqLEGSSDRILELDQELRKAERELSKAEKNSLTE-TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-259 |
9.74e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 186
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110835729 187 E-RKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTdlERANQRAEVAQR 259
Cdd:COG1579 111 EiLELMERIEELEEELAELEAELAELEAELEEKKAEL-------DEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-376 |
9.91e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMSTTSKLEEAEH 206
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKLRSRVDL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 207 KLQTLQtALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQ------------RAEVAQREAETLREQLSSA 271
Cdd:pfam15921 529 KLQELQ-HLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 272 NHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER---------EIAQLVEDVQRLQASLTKLRENsasqISQLEQQL 342
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlravkdikqERDQLLNEVKTSRNELNSLSED----YEVLKRNF 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 110835729 343 NAKNSTLKQLEEKLKGQ--ADYEEVKKELNTLKSME 376
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQlkSAQSELEQTRNTLKSME 719
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
113-264 |
1.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 113 EIKVQRLHDIETENQKLRETLE-EYNKEFAEVKNQEvtikalkEKIREYEQTLKSQAETIALEKEQ---------KLQND 182
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEElekkekeleQKQQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 183 FAEKERKLQETQMSTTSKLEEA------EHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDlerANQR-- 253
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERIsgltaeEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADkKAKEILAQ---AIQRca 202
|
170
....*....|.
gi 110835729 254 AEVAqreAETL 264
Cdd:PRK12704 203 ADHV---AETT 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-376 |
1.19e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRlidvpdpvpALDVGQQ 111
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----KADAAKKKAEEAKKAAEAAKAE---------AEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 112 LEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikALKEKIREYeqtlKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD----EAKKKAEED----KKKADELKKAAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMTDLERANQ---RAEVAQREAETLREQL 268
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAEEAKKADEakkKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 269 SSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR 328
Cdd:PTZ00121 1507 EAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 110835729 329 ENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD----YEEVKKELNTLKSME 376
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVE 1636
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
154-354 |
1.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 154 KEKIREYEQTLKSQAETIA----LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALektrtelfdlktKY 229
Cdd:PRK04863 279 NERRVHLEEALELRRELYTsrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL------------RQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 230 DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHS-LQLASQIQkapDVEQAIEVLTRSSLE----VELA 304
Cdd:PRK04863 347 QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEvDELKSQLA---DYQQALDVQQTRAIQyqqaVQAL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110835729 305 AKEREIAQL----VEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEE 354
Cdd:PRK04863 424 ERAKQLCGLpdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
618-863 |
1.23e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 618 ILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEA 697
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 698 QDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQG 777
Cdd:PRK10263 363 VPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 778 PSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLtpeqyevYMYQEVD 850
Cdd:PRK10263 442 VAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL-------YYFEEVE 513
|
250
....*....|...
gi 110835729 851 tiELTRQVKEKLA 863
Cdd:PRK10263 514 --EKRAREREQLA 524
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
221-373 |
1.30e-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: 46.39 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 297
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 298 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 373
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
19-405 |
1.69e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 19 QLQRELDATatvlanrQDESEQSrkrliEQSREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAafltvYKRLID 98
Cdd:pfam05622 63 LLQKQLEQL-------QEENFRL-----ETARDDYRIKCEELEKEVLEL----QHRNEELTSLAEEAQA-----LKDEMD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 99 V----PDPVPALDvgQQLEIKVQRLHDIETENQKLReTLEEYNKEFAEVKNQevtikaLKEKIREYeQTLKSQAETIale 174
Cdd:pfam05622 122 IlresSDKVKKLE--ATVETYKKKLEDLGDLRRQVK-LLEERNAEYMQRTLQ------LEEELKKA-NALRGQLETY--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 175 kEQKLQndfaEKERKLQEtQMSTTSKLE----EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD---- 246
Cdd:pfam05622 189 -KRQVQ----ELHGKLSE-ESKKADKLEfeykKLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQADalls 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 247 ------------------------LERANQRAEVAQREAE-----TLREQLSSANHSL-----QLASQIQKAPDVEQAIE 292
Cdd:pfam05622 263 pssdpgdnlaaeimpaeireklirLQHENKMLRLGQEGSYrerltELQQLLEDANRRKneletQNRLANQRILELQQQVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 293 VLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLNAKNSTLKQLEEKL 356
Cdd:pfam05622 343 ELQKALQEQgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEqieelepkqdsNLAQKIDELQEALRKKDEDMKAMEERY 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 110835729 357 KgqadyEEVKKELNTLKSMEfaPSEGAGTQDSTKPLEVLLLEKNRSLQS 405
Cdd:pfam05622 423 K-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
1.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 181 NDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
164-368 |
2.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 164 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 242
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 243 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQA 322
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-------------EEELE-----KKEKELEQKQQELEKKEEELEELIE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110835729 323 SLTKLRENsasqISQLEQQlNAKNSTLKQLEEKLKGQA-----DYEEVKKE 368
Cdd:PRK12704 139 EQLQELER----ISGLTAE-EAKEILLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-364 |
2.98e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 123 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 201 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 267
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 268 LSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--- 328
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaql 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110835729 329 ----ENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 364
Cdd:pfam01576 239 akkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
639-839 |
3.47e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 639 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 718
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 719 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 798
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110835729 799 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 839
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-417 |
3.64e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 254 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDV 317
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 318 QRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefapsegAGTQDSTKPLE 393
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL-------AQDTGLNLRSP 278
|
250 260
....*....|....*....|....
gi 110835729 394 VLLLEKNRSLQSENATLRISNSDL 417
Cdd:pfam05557 279 EDLSRRIEQLQQREIVLKEENSSL 302
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
111-361 |
4.00e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 111 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 188
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 189 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 261
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 262 ETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQLVE 315
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 110835729 316 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 361
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
110-368 |
4.31e-04 |
|
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: 44.96 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERK 189
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 190 LQETQmSTTSKLEEAEHKLQTLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TL 264
Cdd:TIGR00618 313 HTELQ-SKMRSRAKLLMKRAAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 265 REQLSSANHSLQLASQIQKAPDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE- 339
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEs 464
|
250 260 270
....*....|....*....|....*....|
gi 110835729 340 -QQLNAKNSTLKQLEEKLKgqaDYEEVKKE 368
Cdd:TIGR00618 465 aQSLKEREQQLQTKEQIHL---QETRKKAV 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-266 |
4.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 60 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 130
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 131 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 204
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110835729 205 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-232 |
4.97e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLA---------NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKE 84
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSriearlreiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 85 AEAAFLTVYKRLIDVPDPVPALDvgQQLEIKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELE--AQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPK 940
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 165 KS----QAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQ---TALEKTRTELFDLKTKYDEE 232
Cdd:TIGR02169 941 GEdeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
141-359 |
5.74e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.06 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETialekeqklqNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRT 220
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 221 ELFD------LKTKYDEETTAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEV 293
Cdd:pfam12795 73 EILAslsleeLEQRLLQTSAQLQELQN----QLAQLNSQLIELQTRPERAQQQLSEARQRLQqIRNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110835729 294 LTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 359
Cdd:pfam12795 149 AQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
118-464 |
6.08e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQmST 197
Cdd:PTZ00108 1047 RFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLK-NT 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 198 TSK---LEEaehkLQTLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVAQREAETLREQLS 269
Cdd:PTZ00108 1125 TPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKKKKKSSADKSKKA 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 270 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTL 349
Cdd:PTZ00108 1193 SVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPK 1272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 350 KQLEEKLKGQADYEEVKKELNTLKSmeFAPSEGAGTQDST-KPLEVLLLEKNRSLQSENATLRISNSDlsgpysTNSISS 428
Cdd:PTZ00108 1273 NAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKVkKRLEGSLAALKKKKKSEKKTARKKKSK------TRVKQA 1344
|
330 340 350
....*....|....*....|....*....|....*.
gi 110835729 429 PSPLQQSPdvngmAPSPSQSESAGSISEGEEIDTAE 464
Cdd:PTZ00108 1345 SASQSSRL-----LRRPRKKKSDSSSEDDDDSEVDD 1375
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
29-419 |
6.86e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 29 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDvpdpvpaldv 108
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 109 gqqleikvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKER 188
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 189 KLQETQMSTTSKLEEAEHKLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 256
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 257 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 320
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 321 QASLTKLREnSASQISQLEQQLN-----------------AKNSTLKQLEEKLKGQA-DYEEVKKELNTLK---SMEFAP 379
Cdd:PRK10929 282 DLIASQQRQ-AASQTLQVRQALNtlreqsqwlgvsnalgeALRAQVARLPEMPKPQQlDTEMAQLRVQRLRyedLLNKQP 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 110835729 380 SEGAGTQDSTKPLEVlllEKNRSLQSENATLR-ISNSDLSG 419
Cdd:PRK10929 361 QLRQIRQADGQPLTA---EQNRILDAQLRTQReLLNSLLSG 398
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-354 |
7.67e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 28 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 107
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 186
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 187 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 260
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 261 AETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ 321
Cdd:pfam07888 253 VEGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
|
330 340 350
....*....|....*....|....*....|....
gi 110835729 322 ASLTKLRensaSQISQLEQQL-NAKNSTLKQLEE 354
Cdd:pfam07888 332 ERLQEER----MEREKLEVELgREKDCNRVQLSE 361
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-373 |
7.90e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 54 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLTVYKRLIDVPDPVPAL----DVG 109
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQ----RLHDIETENQKLRETLEEYNK--------------EFAEVKNQEVT----IKALKEKIREYEQTLKSq 167
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiindpvyknrnyinDYFKYKNDIENkkqiLSNIDAEINKYHAIIKK- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 168 aetiaLEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDL 247
Cdd:PRK01156 331 -----LSVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 248 ERANQRAEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT--------------------------- 295
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynek 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 296 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKE 368
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNR 554
|
....*
gi 110835729 369 LNTLK 373
Cdd:PRK01156 555 YKSLK 559
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
22-361 |
7.97e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 22 RELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF--- 89
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqst 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 90 ---LTVYKRLIDVPDP--VPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKIR 158
Cdd:pfam05557 131 nseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 159 EYEQTLKSQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKLQTLQTALEKTRTELfdlktkYDEETTAKAD 238
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQDT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 239 EIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVEDV 317
Cdd:pfam05557 272 GLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRRL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 110835729 318 QRLQASLTKLRENSASQISQLEQQLNAKNSTlKQLEEKLKGQAD 361
Cdd:pfam05557 345 QRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAED 387
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
17-423 |
8.55e-04 |
|
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: 43.88 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlrkQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRL 96
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE---ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREyeqtLKSQAETIALEKE 176
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----------IQHLKSKTNE----LKSEKLQIGTNLQ 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 177 QKLQndFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 246
Cdd:TIGR00606 882 RRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 247 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 312
Cdd:TIGR00606 960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 313 LvedvqrlqasLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNT-LKSMEFAPSEgagtqdstk 390
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIKHFKKeLREPQFRDAE--------- 1100
|
410 420 430
....*....|....*....|....*....|...
gi 110835729 391 plevlllEKNRSLQSENATLRISNSDLSGPYST 423
Cdd:TIGR00606 1101 -------EKYREMMIVMRTTELVNKDLDIYYKT 1126
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
121-383 |
8.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 121 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKSQAETIALEKEQKLqndfAEKERKLQETQMSTTS 199
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 200 KLEEAEHKLQTLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 279
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 280 QIQKAPDVEQAIEVltRSSLEVELAakereiaqlvEDVQRLQASLTKLRENSASQISQLEQQLNAKnsTLKQLEEKLKGQ 359
Cdd:PTZ00121 1174 DAKKAEAARKAEEV--RKAEELRKA----------EDARKAEAARKAEEERKAEEARKAEDAKKAE--AVKKAEEAKKDA 1239
|
250 260
....*....|....*....|....
gi 110835729 360 ADYEEVKKELNTLKSMEFAPSEGA 383
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMA 1263
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
117-222 |
9.25e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 117 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 180
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110835729 181 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 222
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-191 |
9.60e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVY- 93
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINe 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 94 -KRLIDvpdpvPALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI 171
Cdd:TIGR02169 404 lKRELD-----RLQEELQRLSEELADLNaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
170 180
....*....|....*....|..
gi 110835729 172 A-LEKEQ-KLQNDFAEKERKLQ 191
Cdd:TIGR02169 479 DrVEKELsKLQRELAEAEAQAR 500
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
16-358 |
1.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKkntpeDLRKQVApllkSFQGEIDALSKRSKEAEAAF--LTVY 93
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVD-----SLKSQLA----DYQQALDVQQTRAIQYQQAVqaLEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 94 KRLIDVPDPVPALDVGQQLEIKV-------------QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKAlKEKIREY 160
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAkeqqateevleleQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTA-RELLRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 161 --EQTLKSQAETIAL---EKEQKLQNDfAEKERKLQETQMSTTSKLEEAEhKLQTLQTALEKTRTELFDLKTKYDEETTA 235
Cdd:COG3096 505 rsQQALAQRLQQLRAqlaELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 236 KADEIEMIMTDLERANQRAEV---AQREAETLREQLSsanhsLQLASqiqkAPDVEQAIEvltrsslevELAAKEREIAQ 312
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAwlaAQDALERLREQSG-----EALAD----SQEVTAAMQ---------QLLEREREATV 644
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 110835729 313 LVEDVQRLQASLtklrensASQISQLEQQLNAKNSTLKQLEEKLKG 358
Cdd:COG3096 645 ERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
152-353 |
1.20e-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: 42.82 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 152 ALKEKIREYEQ----TLKSQAETIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 227
Cdd:pfam09787 4 SAKQELADYKQkaarILQSKEKLIASLKEGSGVEGL--------DSSTALTLELEELRQERDLLREEIQKLRGQIQQLRT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 228 KydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIEVLTR--SSLEVELaa 305
Cdd:pfam09787 76 E---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELERLQEelRYLEEEL-- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110835729 306 kEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQLNA------------------KNSTLKQLE 353
Cdd:pfam09787 131 -RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLHQltetliqkqtmlealsteKNSLVLQLE 201
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
129-357 |
1.20e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 42.76 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 129 LRETLEEYNKEFAEVknqevtIKALKEKIREYEQTLKSQAETIAL------EKEQKLQNDFAEkERKLQETQMSTTSKLE 202
Cdd:pfam04108 54 LEKVLNELKKDFKQL------LKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLLDFID-EDSVEILRDALKELID 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 203 EAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEAETLREQLssANHsLQLASQIQ 282
Cdd:pfam04108 127 ELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EMASLLESL--TNH-YDQCVTAV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 283 KAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQL 352
Cdd:pfam04108 199 KLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALKEF 278
|
....*
gi 110835729 353 EEKLK 357
Cdd:pfam04108 279 EERWE 283
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1170-1204 |
1.23e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 37.88 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....*
gi 110835729 1170 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1204
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-373 |
1.27e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 115 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ 177
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 178 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKLQTLQT------ALEKTRTELFDLKTKYDEETTA---------- 235
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 236 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 305
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 306 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTL 372
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQVVQA 1113
|
.
gi 110835729 373 K 373
Cdd:COG3096 1114 K 1114
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
108-248 |
1.33e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 41.22 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 108 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQaetialekeQKLQNDFAEKE 187
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQ---------EKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 188 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 248
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
299-373 |
1.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 299 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 356
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 110835729 357 KG-QADYEEVKKELNTLK 373
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
34-374 |
1.51e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 34 RQDESEQSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQ------GEIDALSKRSKEAEAAFLTVYKRLIDVPdPVP 104
Cdd:pfam05667 241 RKRKRTKLLKRIAEQLRSAALAGTEatsGASRSAQDLAELLSsfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAAT-SSP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 105 ALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQ-KLQNDF 183
Cdd:pfam05667 320 PTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTlDLLPDA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 184 AEKERKLQetqmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqraevaqreaet 263
Cdd:pfam05667 400 EENIAKLQ-------ALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKE-------------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 264 LREQLssanhslqlasqiqkapdvEQAIEvltrsslevELAAKEREIAQLVEDVQRLQasltklRENSASQISQ--LEQQ 341
Cdd:pfam05667 459 LREKI-------------------KEVAE---------EAKQKEELYKQLVAEYERLP------KDVSRSAYTRriLEIV 504
|
330 340 350
....*....|....*....|....*....|...
gi 110835729 342 LNAKnstlKQLEEKLKGQADYEEVKKELNTLKS 374
Cdd:pfam05667 505 KNIK----KQKEEITKILSDTKSLQKEINSLTG 533
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
23-373 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 23 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLR----------KQVAPLLKSFQGEIDALSKRSKE---AEAAF 89
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELVDCQRELEKLNKERRLlnqEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 90 LTVYKRLIDVPDPVPALDVGQQLEIKVQRLH------------DIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKE 155
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfsERQIKNfhTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 156 K-IREYEQTLKSQAETIALEKE--QKLQNDFAEKERKLQ--ETQMSTTSKLEEAEHK-LQTLQTALEKTRTElfdlkTKY 229
Cdd:TIGR00606 426 EqADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQqlEGSSDRILELDQELRKaERELSKAEKNSLTE-----TLK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 230 DEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSSLEVEL 303
Cdd:TIGR00606 501 KEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQLEDWL 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 304 AAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLK 373
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
112-376 |
1.89e-03 |
|
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: 42.89 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 112 LEIKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKSQAETIALEKEQkLQNDFAEKERK-- 189
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKin 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 190 --------LQETQMSTTSKLEEAEHKLQTLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQ--RAEVAQ- 258
Cdd:pfam10174 398 vlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEQREREDRerLEELESl 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 259 -REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLRENS---- 331
Cdd:pfam10174 474 kKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAEeavr 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 110835729 332 -----ASQISQLEQQLNAKNstlkqlEEKLKGQAdyeEVKKELNTLKSME 376
Cdd:pfam10174 552 tnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE 592
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
23-361 |
1.92e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 23 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVP 100
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 101 DPVPalDVGQQLEIKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 173
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 174 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 240
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 241 EMIMTDLERANQRAEVAQREAETlreqlssanHSLQLASQIQKAPDVEQAIEVLTRSsleveLAAKEREIAQLVEDVQRL 320
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKET---------RALSLARALEEALEAKEELERTNKQ-----LRAEMEDLVSSKDDVGKN 679
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 110835729 321 QASLTKLREnsasqisQLEQQLNAKNSTLKQLEEKLKGQAD 361
Cdd:pfam01576 680 VHELERSKR-------ALEQQVEEMKTQLEELEDELQATED 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-357 |
1.99e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 103 VPALDVGQQLEIKVQRLHDIET-ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQn 181
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 182 dfAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----------TKYDEETTAKADEIEMIMTDLERAN 251
Cdd:TIGR00618 513 --PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERkqraslkeqmQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 252 QRAEVAQREAET---LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR 328
Cdd:TIGR00618 591 NITVRLQDLTEKlseAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL 670
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 110835729 329 ENSASQISQLEQQ---------------LNAKNSTLKQLEEKLK 357
Cdd:TIGR00618 671 PKELLASRQLALQkmqsekeqltywkemLAQCQTLLRELETHIE 714
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
68-270 |
2.00e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 68 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 143
Cdd:pfam00261 17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 144 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 220
Cdd:pfam00261 91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110835729 221 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-376 |
2.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDVPDPVPALDVGQQL 112
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA--EEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 113 EIKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALK----EKIREYEQTLKSQAETIALEKEQKLQN-DF 183
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEvrkaEELRKAEDARKAEAARKAEEerkaEEARKAEDAKKAEAVKKAEEAKKDAEEaKK 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 184 AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ--RAEVAQREA 261
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 262 ETLREQLSSANHSlqlASQIQKAPDVEQAIEvlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 341
Cdd:PTZ00121 1325 EEAKKKADAAKKK---AEEAKKAAEAAKAEA--EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350
....*....|....*....|....*....|....*
gi 110835729 342 LNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 376
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-206 |
2.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 12 WKRFDLQQLQRELDATATVLAN-------------RQDESEQSRKRLIEQSREFKKN--TPEDLRKQVAPLLKSFQGEID 76
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERldassddlaaleeQLEELEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 77 ALSKRSKEAEAAFLTvyKRLIDVPDPVPALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEF-AEVKNQEVTIKALk 154
Cdd:COG4913 738 AAEDLARLELRALLE--ERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWpAETADLDADLESL- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 155 ekiREYEQTLKSQAETIALEKEQKLqndfaeKERKLQETQMSTT---SKLEEAEH 206
Cdd:COG4913 815 ---PEYLALLDRLEEDGLPEYEERF------KELLNENSIEFVAdllSKLRRAIR 860
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
8-374 |
2.25e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 8 MFQYWKRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQsREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEA 87
Cdd:COG5185 1 AVQRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVF-ITILFFPLGISRDSLRVTLRSVINVLDGLNYQNDVKKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 88 AFLTVYKRLIDVPDPVPalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKSQ 167
Cdd:COG5185 80 ESSVKARKFLKEKKLDT--KILQEYVNSLIKLPNYEWSADILISLLYLYKSE----IVALKDELIKVEKLDEIADIEASY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 168 AETIALEK-------EQKL-QNDFAEKERKLQETQMSTTSKLEEAEH-----------------KLQTLQTALEKTRTE- 221
Cdd:COG5185 154 GEVETGIIkdifgklTQELnQNLKKLEIFGLTLGLLKGISELKKAEPsgtvnsikesetgnlgsESTLLEKAKEIINIEe 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 222 ---LFDLKTKYDEETTAKADEIEMIMTD-----LERANQRAEVAQR---EAETLREQLSSANHSLQ-LASQIQKAPDVEQ 289
Cdd:COG5185 234 alkGFQDPESELEDLAQTSDKLEKLVEQntdlrLEKLGENAESSKRlneNANNLIKQFENTKEKIAeYTKSIDIKKATES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 290 AIEVLTRSSLEVELAAKEREIAqlvEDVQRLQASLTKLREnsasqisQLEQQLNAKNSTLKQLEeklkGQADYEEVKKEL 369
Cdd:COG5185 314 LEEQLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQE-------SLTENLEAIKEEIENIV----GEVELSKSSEEL 379
|
....*
gi 110835729 370 NTLKS 374
Cdd:COG5185 380 DSFKD 384
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
2.39e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 127 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 201
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110835729 202 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 270
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
127-217 |
2.79e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.17 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 127 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 195
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 110835729 196 STTSKLEEAEHKLQTLQTALEK 217
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
63-228 |
2.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 63 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldvgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 142
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 143 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 219
Cdd:COG1579 85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155
|
....*....
gi 110835729 220 TELFDLKTK 228
Cdd:COG1579 156 AELEELEAE 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
16-192 |
2.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 16 DLQQLQRELDATATVLAN-------RQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaa 88
Cdd:COG1579 11 DLQELDSELDRLEHRLKElpaelaeLEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 89 fltvyKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQA 168
Cdd:COG1579 80 -----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|....
gi 110835729 169 ETIAlEKEQKLQNDFAEKERKLQE 192
Cdd:COG1579 152 AELE-AELEELEAEREELAAKIPP 174
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
111-411 |
2.91e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 41.51 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 111 QLEIKVQRLhDIET-ENQKLRETlEEYNKEfaevknqevtIKALKEKIREYEQTLKSQAETIA---LEKEQKLQNDFAEK 186
Cdd:pfam14915 5 QDEIAMLRL-EIDTiKNQNQEKE-KKYLED----------IEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 187 ERklqetqmsTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLRE 266
Cdd:pfam14915 73 TM--------LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 267 QLSSANHSLQLASQI--QKAPDVEQAIevltrSSLEVEL---AAKEREIAQLVEDVQRlqasltklrensasQISQLEQQ 341
Cdd:pfam14915 134 KMNFDVSNLRDENEIlsQQLSKAESKA-----NSLENELhrtRDALREKTLLLESVQR--------------DLSQAQCQ 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 342 lnaknstLKQLEEKLkgQADYEEVKKELNTLKSMEfapsegagtqdstkplevlllEKNRSLQSENATLR 411
Cdd:pfam14915 195 -------KKELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
277-419 |
3.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 277 LASQIQKAPDVEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQL 352
Cdd:PRK11281 19 LLCLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 353 EEKLKgqadyeEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSG 419
Cdd:PRK11281 93 PAKLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
17-288 |
3.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATA----TVLANRQDESEQSRKRLIEQSREFKKNTPE-DLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLT 91
Cdd:PRK04863 874 LSALNRLLPRLNlladETLADRVEEIREQLDEAEEAKRFVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRD 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 92 VYKRLIDVP------------DPVPALDVGQQLEIKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKEKIR 158
Cdd:PRK04863 954 AKQQAFALTevvqrrahfsyeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKSSYD 1030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 159 EYEQTLKsqaetialEKEQKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKLQTLQTALEKTRTELfdlktkydeet 233
Cdd:PRK04863 1031 AKRQMLQ--------ELKQELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC----------- 1086
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 110835729 234 takadEIEMimtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 288
Cdd:PRK04863 1087 -----EAEM-----DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-369 |
3.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE--QKLQNDFAEKE 187
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEAQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 188 RKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllkeANRNAEKEEELAEAEKLIESLPRELAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 264 LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 343
Cdd:COG4372 219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLL 298
|
250 260
....*....|....*....|....*.
gi 110835729 344 AKNSTLKQLEEKLKGQADYEEVKKEL 369
Cdd:COG4372 299 ALLLNLAALSLIGALEDALLAALLEL 324
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
252-381 |
3.91e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 252 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 317
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 318 QRLQASLTKLRENS------------------ASQISQLEQQLNAKNS----------TLKQLEEKLKG----------- 358
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180
....*....|....*....|...
gi 110835729 359 QADYEEVKKELNTLKSMEFAPSE 381
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSE 962
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
4.30e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 112 L-EIKVQRLHDIETENQKLRETLE----------EYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELDklaeelsarlEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 181 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 110835729 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-361 |
4.76e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 235 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 314
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 110835729 315 edvqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 361
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
141-310 |
5.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKLQTLQTALEKtRT 220
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 221 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 297
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 110835729 298 SLEVELAAKEREI 310
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
221-373 |
5.67e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANhslqlaSQIQkapDVEQAIEVLtrs 297
Cdd:PRK04778 64 EKFEeWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFrkAKHEINEIESLLDLIE------EDIE---QILEELQEL--- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 298 sleVELAAKER-EIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 373
Cdd:PRK04778 132 ---LESEEKNReEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESGDYVEAREILDQLE 204
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
107-369 |
5.87e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 107 DVGQQLEIKVQRLHDIETENQKLREtleeynkefAEVKNQEVtIKALKEKIREYEQTLKSQA----ETIA-LEKE-QKLQ 180
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQELLE---------SEEKNREE-VEQLKDLYRELRKSLLANRfsfgPALDeLEKQlENLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 181 NDFAEKERKLQETQMSTTSK-LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLERANQRAEVAQ- 258
Cdd:PRK04778 179 EEFSQFVELTESGDYVEAREiLDQLEEELAALEQIMEEIPELLKELQTELPDQL----QELKAGYRELVEEGYHLDHLDi 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 259 -REAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTrSSLEVELAAK---EREIAQLVEDVQRLQASLTKLREns 331
Cdd:PRK04778 255 eKEIQDLKEQIDENLallEELDLDEAEEKNEEIQERIDQLY-DILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKE-- 331
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 110835729 332 asQISQLEQ--QLNAKN-STLKQLEEKLKG-QADYEEVKKEL 369
Cdd:PRK04778 332 --EIDRVKQsyTLNESElESVRQLEKQLESlEKQYDEITERI 371
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
155-407 |
5.97e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 155 EKIREYEQTLKSQAEtialEKEQKLQND--FAEKERK-LQETQMSTTS---KLEEAEHKLQTLQTALEKTR--TELFDLK 226
Cdd:pfam05483 88 EKIKKWKVSIEAELK----QKENKLQENrkIIEAQRKaIQELQFENEKvslKLEEEIQENKDLIKENNATRhlCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 227 TKYDEETTAK----ADEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSLQLASQIQKAPDVEQAIEvltrSSLEVE 302
Cdd:pfam05483 164 CARSAEKTKKyeyeREETRQVYMDL---NNNIEKMILAFEELRVQ--AENARLEMHFKLKEDHEKIQHLE----EEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 303 LAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNtlKSMEF 377
Cdd:pfam05483 235 INDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHlTKELEDIKMSLQ--RSMST 311
|
250 260 270
....*....|....*....|....*....|
gi 110835729 378 APSEGAGTQDSTKPLEVLLLEKNRSLQSEN 407
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
623-834 |
6.58e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 623 RREMEAQQAALDPALKPAP----LSQPDLTILTPKHLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQ 698
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 699 DVPTLDPPGSADAAQGVLRPMKSELVRGSTwkdpwwspiqPERRNLTSSEETKADETTASGKERAGSSQPRAER--SQL- 775
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRV----------AVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwaSSLa 3012
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110835729 776 ----QGPSASAEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVP 834
Cdd:PHA03247 3013 lheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATP 3075
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-216 |
6.70e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.01 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 5 VGSMFQYWKRFDLQQLQRELDATATVlANRQDESEQSRKRLIEQSREFKKntpedLRKQVAPLLKSFQGEIDALSKRSke 84
Cdd:COG0610 690 LRALFPEGVDFSAFDPTEKLEALDEA-VERFLGDEEARKEFKKLFKELSR-----LYNLLSPDDEFGDLELEKYRDDV-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 85 aeAAFLTVYKRLIDVPDPVPAldvgQQLEIKVQRLHD--IETENQKLRETLEE---YNKEFAE-VKNqevTIKALKEKIR 158
Cdd:COG0610 762 --SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQnpvQYRKFSElLEE---IIEEYNNGAL 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110835729 159 EYEQTLKsqaETIALEKEQKLQNDFAEKErKLQETQMSTTSKLEEAEHKLQTLQTALE 216
Cdd:COG0610 833 DADEVLE---ELEELAKEVKEEEERAEEE-GLNEEELAFYDALAENLGDEKLKELAKE 886
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
297-415 |
7.40e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 38.82 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 297 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 376
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 110835729 377 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 415
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-278 |
9.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 117 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 181
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 182 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 249
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 110835729 250 ANQRAEVAQREAETLREQLSSANHSLQLA 278
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
17-356 |
9.38e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 17 LQQLQRELDATATVLANRQDESEQSRKRlIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlTVYK 94
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREE-VEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 95 RLIDVPDPVPALDVGQQLEIKV------------------------------------------------QRLHDIETEN 126
Cdd:PRK04778 186 ELTESGDYVEAREILDQLEEELaaleqimeeipellkelqtelpdqlqelkagyrelveegyhldhldieKEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 127 QKLRETLEEYNKEFAEVKNQEvtikaLKEKIRE-YEQtlksqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAE 205
Cdd:PRK04778 266 DENLALLEELDLDEAEEKNEE-----IQERIDQlYDI----------LEREVKARK---------------------YVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 206 HKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQ 282
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EIT 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835729 283 KAPDvEQAIevlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLnaknSTLKQLEEKL 356
Cdd:PRK04778 369 ERIA-EQEI---AYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
277-368 |
9.47e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835729 277 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKL 356
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
|
90
....*....|....
gi 110835729 357 K--GQADYEEVKKE 368
Cdd:COG2433 451 SeaRSEERREIRKD 464
|
|
| |
