|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1122-1199 |
1.15e-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: 1.15e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 1122 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1199
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
939-1007 |
7.82e-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: 7.82e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 939 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1007
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
547-623 |
1.96e-26 |
|
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: 103.83 E-value: 1.96e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 547 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 623
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1245-1301 |
1.39e-15 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 72.15 E-value: 1.39e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 1245 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1301
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-400 |
3.57e-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: 78.17 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 96 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 171
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 172 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 241
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 242 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 318
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 319 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 398
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
..
gi 148277064 399 LR 400
Cdd:TIGR02168 977 LE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-352 |
1.48e-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: 76.25 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 22 NRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEaaflnvykRLIDvpdpvpalDLGQQ 100
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKE-LKAELRELELALLVLrLEELREELEELQEELKEAE--------EELE--------ELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAETIALEKEQK--LQNDFAE 174
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLdeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 KERKLQETQMSTTS---KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQR 248
Cdd:TIGR02168 342 LEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 249 EAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLR------ 317
Cdd:TIGR02168 422 EIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEalEELREELEEAEQALDAAERELAQLQARLDSLErlqenl 501
|
330 340 350
....*....|....*....|....*....|....*
gi 148277064 318 ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 352
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1245-1302 |
8.28e-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: 64.57 E-value: 8.28e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 1245 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1302
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
71-397 |
1.55e-12 |
|
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: 72.30 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 71 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 145
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 146 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 224
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 225 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 280
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 281 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 356
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 148277064 357 ELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENA 397
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-418 |
3.64e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 100 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 179
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 180 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 259
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 260 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---ASLTKLRENSASQISQLEQQLSAKNS 336
Cdd:COG1196 363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEeaeEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 337 TLKQLEEKLKgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD---LSGSARRK 413
Cdd:COG1196 436 EEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegfLEGVKAAL 514
|
....*
gi 148277064 414 GKDQP 418
Cdd:COG1196 515 LLAGL 519
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1245-1300 |
4.49e-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: 62.27 E-value: 4.49e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 1245 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1300
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
94-323 |
2.23e-10 |
|
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: 64.40 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 94 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 170
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 171 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 245
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 246 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 323
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-364 |
2.24e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 8 RLKRELDAtatvLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQV----------------------APLLKSFQGEID 65
Cdd:PRK03918 388 KLEKELEE----LEKAKEEIEEEISKITARIGELKKEI-KELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 66 ALSKRSKEAEAAFLNVYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEK 145
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 146 IREYEQTLKNQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTA 224
Cdd:PRK03918 534 LIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 225 KADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVE 304
Cdd:PRK03918 608 KDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSR 673
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 305 DVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 364
Cdd:PRK03918 674 ELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-363 |
2.41e-10 |
|
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: 65.43 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 22 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 96
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 174
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQRE 249
Cdd:TIGR04523 317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 250 AETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQ 329
Cdd:TIGR04523 386 IKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLTN 447
|
330 340 350
....*....|....*....|....*....|....*
gi 148277064 330 QLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 363
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-401 |
4.46e-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: 64.69 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 112 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 188
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 189 KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 265
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 266 LASQIQKAPDVEQAIEVLTrSSLEVELAAKEREIAQLVEDVQ---RLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 342
Cdd:TIGR02168 328 LESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 343 EKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRI 401
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-342 |
1.12e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 116 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 194
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 195 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 274
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 275 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 342
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
61-400 |
1.40e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 61 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 140
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 141 ALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDE 220
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 221 ETTAKADEIEMIMT-----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVEQAIEV 282
Cdd:COG4717 243 ERLKEARLLLLIAAallallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 283 LTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEVKK 356
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 148277064 357 ELNILKSmEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALR 400
Cdd:COG4717 403 ELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-272 |
1.95e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 178
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 179 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 254
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 148277064 255 EQLSSANHSLQLASQIQK 272
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-361 |
2.39e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGE-----IDALSKRSKEAEaaflNV 81
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYE----KL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 82 YKRLIDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlk 154
Cdd:PRK03918 531 KEKLIKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP--- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 155 nqaetiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMT 234
Cdd:PRK03918 600 ------FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 235 DLERANQRAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsl 313
Cdd:PRK03918 670 ELSRELAGLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA-- 735
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148277064 314 tKLRENSASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 361
Cdd:PRK03918 736 -LLKERALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-349 |
3.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSfQGEIDALSKRSKEAEAAFLNVYKRLi 86
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARL-EQDIARLEERRRELEERLEELEEEL- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 87 dvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKNQAEtiALEKEQ 166
Cdd:COG1196 326 --------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 167 KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRAEVA 246
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 247 Q--REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASq 323
Cdd:COG1196 467 EllEEAALLEAALAELLEELaEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA- 545
|
330 340
....*....|....*....|....*.
gi 148277064 324 iSQLEQQLSAKNSTLKQLEEKLKGQA 349
Cdd:COG1196 546 -AALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-363 |
8.72e-09 |
|
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: 60.47 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ----- 180
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEkltee 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 181 ---------------------------ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK---TKYDEETTAKADEIE 230
Cdd:TIGR02169 260 iselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 231 MIMTDLERANQR-----AEVAQREAE--TLREQLSSANHSLQLASQIQKapDVEQAIEVLTR---------SSLEVELAA 294
Cdd:TIGR02169 340 ELEREIEEERKRrdkltEEYAELKEEleDLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRLQEELQR 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148277064 295 KEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKELNILKS 363
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-427 |
9.73e-09 |
|
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: 60.47 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 117 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKN-QAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 191
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSDaSRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 192 EAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 269
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 270 iqkapdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLK 339
Cdd:TIGR02169 816 -----------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 340 QLEEKLKG-QADYEEVKKELNILKsmefapsEGAGTQDAAkplevllLEKNRSLQSE-NAALRISNSDLSGSARRKGKDQ 417
Cdd:TIGR02169 879 DLESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLSElKAKLEALEEELSEIEDPKGEDE 944
|
330
....*....|
gi 148277064 418 PESRRPGSLP 427
Cdd:TIGR02169 945 EIPEEELSLE 954
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
130-371 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 130 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 207
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 208 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVEQAI 280
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAE------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 281 EVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNI 360
Cdd:COG4942 170 EA-ERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAER 242
|
250
....*....|.
gi 148277064 361 LKSMEFAPSEG 371
Cdd:COG4942 243 TPAAGFAALKG 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
25-346 |
1.34e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 25 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEaeaaFLNVYKRLIDVPDpvpalDLGQQLQ-L 103
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKE----LREEAQELREKRD-----ELNEKVKeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 104 KVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQ 183
Cdd:COG1340 77 KEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 184 msttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSANHS 263
Cdd:COG1340 154 -----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELHKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 264 LQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLSAKNSTLKQLEE 343
Cdd:COG1340 218 IVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 148277064 344 KLK 346
Cdd:COG1340 275 KLK 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-344 |
1.60e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLNVYKRLI 86
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 87 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTL------------- 153
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLliaaallallglg 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 154 ------------------------------------KNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAE--- 194
Cdd:COG4717 266 gsllsliltiagvlflvlgllallflllarekaslgKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLell 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 195 HKVQSLQTALEKTRTELFDLKTKYDEE------TTAKADEIEMIMTDLERANQRAEvAQREAETLREQLSSANHSLQLAS 268
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQeiaallAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 269 QIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLSAKNSTLKQLEEK 344
Cdd:COG4717 423 EALDEEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-357 |
2.04e-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: 58.24 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 161 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 240
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 306
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148277064 307 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 357
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
7-345 |
3.05e-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: 58.70 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNV---YK 83
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 84 RLIdvpdpvpaLDLGQQLQLKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKNQAETIAL 162
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 241
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 242 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA 311
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDV 592
|
330 340 350
....*....|....*....|....*....|....*
gi 148277064 312 -SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 345
Cdd:pfam12128 593 pEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-288 |
4.36e-08 |
|
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: 58.14 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnvykr 84
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 85 lidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEK 164
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 165 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 241
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148277064 242 RAEVAQREAETLREQLSSANHSLQLASQ-IQKAPDVEQAIEVLTRSSL 288
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSElISVDEGYEAAIEAALGGRL 547
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
45-410 |
5.79e-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: 57.93 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 45 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaLDLGQQLQLKVQRlhDIETENQKLRETLEE 124
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL------FDEKQSEKDKKNK--ALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 125 YNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTAL 204
Cdd:pfam12128 687 LEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 205 EKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVEQAIEv 282
Cdd:pfam12128 753 ETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS- 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 283 ltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 362
Cdd:pfam12128 825 -------------------------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA 879
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 148277064 363 SMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSA 410
Cdd:pfam12128 880 NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSG 927
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
140-413 |
6.76e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 140 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 218
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 219 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 298
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 299 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 378
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260 270
....*....|....*....|....*....|....*
gi 148277064 379 KPLEVLLLEKNRSLQSENAALRISNSDLSGSARRK 413
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
120-341 |
7.56e-08 |
|
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: 54.14 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 120 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 191
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 192 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 264
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 265 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 341
Cdd:pfam13851 137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-349 |
9.25e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 14 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 87
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 88 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIAlEKEQK 167
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 168 LQ-NDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 244
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 245 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 321
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 148277064 322 SQISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 349
Cdd:PRK02224 606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
106-253 |
9.25e-08 |
|
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: 54.55 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 178
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 179 LQETqmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 253
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-362 |
1.25e-07 |
|
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: 56.57 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 26 ESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLK---SFQGEIDALsKRSKEAEAAFLNVYKRLIDVPDPvPALDLGQQLQ 102
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsVKELIIKNL-DNTRESLETQLKVLSRSINKIKQ-NLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 103 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQKLQNDFAEKErkLQET 182
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKE--IDEK 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 183 QmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ----LS 258
Cdd:TIGR04523 567 N----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIikniKS 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 259 SANHSLQLASQIQ--------KAPDVEQAIEvltrsslevELAAKEREIAQLVEDvqRLQASLTKLRENSASQIsqleqq 330
Cdd:TIGR04523 639 KKNKLKQEVKQIKetikeirnKWPEIIKKIK---------ESKTKIDDIIELMKD--WLKELSLHYKKYITRMI------ 701
|
330 340 350
....*....|....*....|....*....|..
gi 148277064 331 lsaKNSTLKQLEEKlkgqadYEEVKKELNILK 362
Cdd:TIGR04523 702 ---RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
108-362 |
1.68e-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: 55.98 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 108 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 184
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 185 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 261
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 262 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 320
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 148277064 321 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 362
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-259 |
2.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 178
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 179 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 258
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 148277064 259 S 259
Cdd:COG4913 430 S 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
95-316 |
2.65e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 95 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 170
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 171 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 238
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 239 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 316
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
161-359 |
3.02e-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: 53.00 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 161 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 240
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVEQAievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRE 318
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILE--------LMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148277064 319 NSASQISQLEQQLSAKNSTLKQLEEKLKGQ--ADYEEVKKELN 359
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
85-364 |
3.41e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 85 LIDVPDPVPALDLGQQLQLKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKN 155
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 156 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLk 215
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 216 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA-- 293
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAel 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 294 ------------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKE 357
Cdd:COG3206 283 sarytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLERE 359
|
....*..
gi 148277064 358 LNILKSM 364
Cdd:COG3206 360 VEVAREL 366
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
47-239 |
4.33e-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: 53.53 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 47 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDI-ETENQKL-RETLEE 124
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEKDQ--------TALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 125 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 203
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 148277064 204 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 239
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
140-344 |
4.50e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 140 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 202
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 203 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 266
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 267 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 341
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 148277064 342 EEK 344
Cdd:PHA02562 399 VKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-365 |
4.60e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 25 DESEQSRKRLIEQSREFKKNTPEDLRKqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldLGQQLQLK 104
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEK-----------ELEELEKAKEEIEEEISKITARIGELKK------EIKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 105 VQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKNQAETIALEK------ 164
Cdd:PRK03918 428 IEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEKERKLRkelrELEKVLKKESELIKLKElaeqlk 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 165 --EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK 225
Cdd:PRK03918 507 elEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 226 ADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEVELAAK 295
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELEKKYSEEEYEEL 664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148277064 296 EREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 365
Cdd:PRK03918 665 REEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-403 |
5.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 221 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 296
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 297 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLK---------------GQAD 350
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRArleallaalglplpaSAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 351 YEEVKKELNILKsmEFAPSEGAGTQDAAKPLEVLLLEKNR---SLQSENAAL--RISN 403
Cdd:COG4913 382 FAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRelrELEAEIASLerRKSN 437
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
114-403 |
7.33e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 114 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 190
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 191 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 268
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 269 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKN------STLKQ 340
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaQLLLE 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 341 LEEKLKGQADYE---EVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSL-QSENAALRISN 403
Cdd:pfam02463 413 LARQLEDLLKEEkkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELkKSEDLLKETQL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-359 |
7.52e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 151 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSL----------------------------Q 201
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKEleelsrqisalrkdlarleaeveqleerI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 202 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIE 281
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 282 VLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 359
Cdd:TIGR02168 828 SLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
185-455 |
1.03e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 185 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 264
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 265 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 329
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 330 QLSAKNSTLKQLEEKLKgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGS 409
Cdd:COG3883 176 QQAEQEALLAQLSAEEA-AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148277064 410 ARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 455
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-346 |
1.17e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 98 GQQLQLKVQrlhdIE-TENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAE 174
Cdd:PRK02224 187 GSLDQLKAQ----IEeKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY-----DEETTAK-----ADEIEMIMTDLERANQRAE 244
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddaDAEAVEArreelEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 245 VAQREAETLRE---QLSSANHSLQlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL---RE 318
Cdd:PRK02224 339 AHNEEAESLREdadDLEERAEELR-----EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDApvdLG 408
|
250 260
....*....|....*....|....*...
gi 148277064 319 NSASQISQLEQQLSAKNSTLKQLEEKLK 346
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLR 436
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
112-408 |
1.34e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 112 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 190
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 191 EEaehkVQSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTD-LERANQRAEV-AQREAETLREQLSSAN--HSLQ 265
Cdd:pfam02463 295 EE----ELKSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEiEELEKELKELeIKREAEEEEEEELEKLqeKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 266 LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE--IAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 337
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148277064 338 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSG 408
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-363 |
1.51e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 26 ESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflNVYKRLIDVpdpvpaldlGQQLQLKV 105
Cdd:PRK03918 142 ESDESREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEK---------EKELEEVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKNQAETIALEKEQ----- 166
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEELEEKvkelk 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 167 -------------KLQNDFAEKERKLQETQMSTT----------SKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT 223
Cdd:PRK03918 287 elkekaeeyiklsEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 224 AKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP----------D 275
Cdd:PRK03918 367 AKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgkcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 276 VEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLSAKNstLKQLEEK 344
Cdd:PRK03918 447 EEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN--LEELEKK 523
|
410
....*....|....*....
gi 148277064 345 LKgqaDYEEVKKELNILKS 363
Cdd:PRK03918 524 AE---EYEKLKEKLIKLKG 539
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
160-401 |
1.91e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 160 IALEKEQKLQNDFAEKERKLQETQmsTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkydEETTAKADEIEMIMTDLERA 239
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 240 NQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 319
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA-------ELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 320 -----SASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQS 394
Cdd:COG4372 173 lqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
....*..
gi 148277064 395 ENAALRI 401
Cdd:COG4372 253 EEVILKE 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-313 |
2.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPED---LRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLN 80
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELeaeIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 81 VYKRLIDVPDPVPALDlGQQLQLKVQRlHDIETENQKLREtleEYNKEFAEVKNQEVTIKALKEKIREYEQtlknqaeti 160
Cdd:TIGR02169 327 LEAEIDKLLAEIEELE-REIEEERKRR-DKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYRE--------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 161 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlkTKYDEETTAKADEIEMIMTDLERAN 240
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKER------EIAQLVEDVQRLQASL 313
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgTVAQLGSVGERYATAI 541
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-308 |
3.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmS 185
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 186 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 261
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148277064 262 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 308
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-257 |
4.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNV 81
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 82 YKRLIDVPDPVPalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE-VKNQEVTIKALKEKIREYEQtlKNQAETI 160
Cdd:TIGR02168 816 NEEAANLRERLE--SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEElEELIEELESELEALLNERAS--LEEALAL 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 161 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLERAN 240
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKIE 964
|
250
....*....|....*..
gi 148277064 241 QRAEVAQREAETLREQL 257
Cdd:TIGR02168 965 DDEEEARRRLKRLENKI 981
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
3-347 |
4.95e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 3 CVAGARLKRELDATATVLANRQDESEQSRKRlieQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaAFLNVY 82
Cdd:COG5022 830 KKLRETEEVEFSLKAEVLIQKFGRSLKAKKR---FSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKL-VNLELE 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 83 KRLIDV-----PDPVPALDLGQQLQLKVQRLHD-IETENQKLRetleEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQ 156
Cdd:COG5022 906 SEIIELkkslsSDLIENLEFKTELIARLKKLLNnIDLEEGPSI----EYVKLPELNKLHEV-ESKLKETSEEYEDLLKKS 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 157 AETI-----ALEKEQKLQNDFAEKeRKLQETQMSTTSKLEEAEHKVQSLQTALEktrtelfdlktKYDEETTAKAdeIEM 231
Cdd:COG5022 981 TILVregnkANSELKNFKKELAEL-SKQYGALQESTKQLKELPVEVAELQSASK-----------IISSESTELS--ILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 232 IMTDLERANQrAEVAQREAETLREQL---SSANHSLQLaSQIQKAPDVEQAIEVLTRSSLEVELAAKEReiaqlVEDVQR 308
Cdd:COG5022 1047 PLQKLKGLLL-LENNQLQARYKALKLrreNSLLDDKQL-YQLESTENLLKTINVKDLEVTNRNLVKPAN-----VLQFIV 1119
|
330 340 350
....*....|....*....|....*....|....*....
gi 148277064 309 LQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG 347
Cdd:COG5022 1120 AQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDG 1158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
106-353 |
5.65e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEqtlknqaetialEKEQKLQNDFAEKERKLQETQMS 185
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLE------------ERAEELREEAAELESELEEAREA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 186 TT---SKLEEAEHKVQSLQTALEKTRTELFDLKTkYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE--QLSSA 260
Cdd:PRK02224 379 VEdrrEEIEELEEEIEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVEEAEALLEagKCPEC 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 261 NHSLQLASQIQKAPDVEQAIEVLT--RSSLEVELAAKEREIAQLvEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 338
Cdd:PRK02224 458 GQPVEGSPHVETIEEDRERVEELEaeLEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
250
....*....|....*
gi 148277064 339 KQLEEKLKGQADYEE 353
Cdd:PRK02224 537 ERAEELRERAAELEA 551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-350 |
6.30e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAflnvykrli 86
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDAS--------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 87 dvpdpvpALDLgQQLQlkvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQ 166
Cdd:COG4913 684 -------SDDL-AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 167 KLQNDFAEKERKLQETQMSttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RAEV 245
Cdd:COG4913 750 LLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLALL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 246 AQREAETL-------REQLSSANHS--LQLASQIQKAP-DVEQAIEVLTRSSLEVE--------LAAKEREiaqlVEDVQ 307
Cdd:COG4913 822 DRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIrEIKERIDPLNDSLKRIPfgpgrylrLEARPRP----DPEVR 897
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 148277064 308 RLQASLTKLRENSASQISQLEQqlsAKNSTLKQLEEKLKGQAD 350
Cdd:COG4913 898 EFRQELRAVTSGASLFDEELSE---ARFAALKRLIERLRSEEE 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-357 |
6.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGE---IDALSKRSKEAEAAflNVYK 83
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAkkkADEAKKKAEEKKKA--DEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 84 RLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIA 161
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 162 LEKEQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--R 238
Cdd:PTZ00121 1518 AEEAKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 239 ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRE 318
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
330 340 350
....*....|....*....|....*....|....*....
gi 148277064 319 NSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 357
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-363 |
6.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 47 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYN 126
Cdd:COG4717 74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 127 KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEK 206
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 207 TRTELFDL-------------------------------------------------------KTKYDEETTAKADEIEM 231
Cdd:COG4717 232 LENELEAAaleerlkearlllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 232 IMTDLERANQRAEVAQ-------------------REAETLREQLSSANHSLQLASQIQK---------APDVEQAIEVL 283
Cdd:COG4717 312 ALEELEEEELEELLAAlglppdlspeellelldriEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 284 TRSSLEVELAAKEREI--------------------AQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 343
Cdd:COG4717 392 EQAEEYQELKEELEELeeqleellgeleellealdeEELEEELEELEEELEELEE----ELEELREELAELEAELEQLEE 467
|
410 420
....*....|....*....|
gi 148277064 344 klkgQADYEEVKKELNILKS 363
Cdd:COG4717 468 ----DGELAELLQELEELKA 483
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
108-405 |
7.36e-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: 51.21 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 108 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 179
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 180 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 258
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 259 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 334
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148277064 335 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD 405
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
12-365 |
7.40e-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: 50.88 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 12 ELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLnvykrlidvpdp 91
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL------------ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 92 vpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKNQAETIAL 162
Cdd:pfam05483 445 ---------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 EKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELF----DLKTKYDE-ETTAKADEIEMImtdl 236
Cdd:pfam05483 516 KKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEYEVL---- 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 237 eRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRl 309
Cdd:pfam05483 584 -KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK- 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148277064 310 QASLTKLRENS-----------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 365
Cdd:pfam05483 662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-362 |
9.16e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLI 86
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 87 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknqeVTIKALKEKIREYEQTLknqAETIALEKEQ 166
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA------------ALAAALQNIVVEDDEVA---AAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 167 KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 246
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 247 QREAETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 319
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 148277064 320 SASQISQ-LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 362
Cdd:COG1196 730 LEAEREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
35-343 |
1.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 35 IEQSREFKKntpEDLRKQvaplLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETE 114
Cdd:COG3206 162 LEQNLELRR---EEARKA----LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 115 NQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAE 194
Cdd:COG3206 228 LAEARAELAE----------AEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 195 HKVQSLQTALEKTRTELfdlktkydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAP 274
Cdd:COG3206 291 PDVIALRAQIAALRAQL--------------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 275 dveqaievltrsslevelaAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 343
Cdd:COG3206 348 -------------------ELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTVGNVRVIDP 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
200-346 |
1.08e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 200 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 277
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 278 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKLK 346
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
94-359 |
1.30e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 94 ALDLGQQLQLKVQRLHDIEtenqklrETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFA 173
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQ-------YRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 174 EKERKLQETQMST---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------- 241
Cdd:PRK04863 359 ELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdlta 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 242 -----RAEVAQREAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKL 316
Cdd:PRK04863 438 dnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRL 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148277064 317 RE--NSASQISQLEQQLSAknstlkqLEEKLKGQADYEEVKKELN 359
Cdd:PRK04863 506 REqrHLAEQLQQLRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
101-416 |
1.38e-05 |
|
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: 49.97 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 180
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 181 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAkadeiemIMTDLERANQRAEVAQREAETLREQLSSA 260
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEIENASSSLGSDLAAREDAL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 261 NHSLQLASQIQK------APDVEQAIEVLT----------------------RSSLEVELAAKEREIAQLVED------- 305
Cdd:TIGR00618 742 NQSLKELMHQARtvlkarTEAHFNNNEEVTaalqtgaelshlaaeiqffnrlREEDTHLLKTLEAEIGQEIPSdedilnl 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 306 -----VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKp 380
Cdd:TIGR00618 822 qcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE- 899
|
330 340 350
....*....|....*....|....*....|....*.
gi 148277064 381 levLLLEKNRSLQSENAALRISNSDLSGSARRKGKD 416
Cdd:TIGR00618 900 ---ITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
61-357 |
1.46e-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: 49.82 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 61 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 135
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 136 evtIKALKEKIREYEQTLKNQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF 212
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 213 DLKtkydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANhslQLASQIQKAPDVEQAIevltrSSLEVEL 292
Cdd:pfam10174 500 DLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH---NAEEAVRTNPEINDRI-----RLLEQEV 567
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 293 AAKEREIAQLVEDVQRLQASLtKLRENSAS----QISQLE---------QQLSAKNSTLKQLEEKLKGQADYEEVKKE 357
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGIL-REVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRR 644
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
55-360 |
1.62e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 55 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 134
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 135 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 214
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 215 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 294
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 295 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 355
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 148277064 356 KELNI 360
Cdd:PRK11281 282 QELEI 286
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
97-434 |
1.66e-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: 49.44 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 LGQQLQLKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKNQAETIALEKEQkLQNDFAEKE 176
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 177 RK----------LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQ--RAE 244
Cdd:pfam10174 394 RKinvlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEQREREDRerLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 245 VAQ--REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLRENS 320
Cdd:pfam10174 470 LESlkKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 321 ---------ASQISQLEQQLSAKNstlkqlEEKLKGQAdyeEVKKELNILKSMEfapsegagTQDAAKPLEVLLLEKNRS 391
Cdd:pfam10174 548 eavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NEKNDKDKKIAELESLTL 610
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 148277064 392 LQSENAALRISN-SDLSGSARRKGKDQ-PESRRPGSLPAPPPSQL 434
Cdd:pfam10174 611 RQMKEQNKKVANiKHGQQEMKKKGAQLlEEARRREDNLADNSQQL 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
42-349 |
1.75e-05 |
|
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: 49.84 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 42 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 109
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 110 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 177
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 178 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 249
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 250 AETLREQLSSANHSL------------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKL 316
Cdd:pfam12128 421 ESELREQLEAGKLEFneeeyrlksrlgELKLRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKR 500
|
330 340 350
....*....|....*....|....*....|...
gi 148277064 317 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 349
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-235 |
3.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 10 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 89
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 90 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 169
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 170 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 235
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
20-226 |
3.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 20 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL 95
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 96 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDF 172
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148277064 173 AEKERKLQETQmSTTSKLEEAEHKVQSLQTALEktrtelfDLKTKYDEETTAKA 226
Cdd:COG3206 337 AQLEARLAELP-ELEAELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-346 |
3.21e-05 |
|
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: 48.63 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 12 ELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP 89
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 90 DPVPalDLGQQLQLKVQ-------RLHDIETENQKLRETLEEynkEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL 162
Cdd:pfam01576 468 SQLQ--DTQELLQEETRqklnlstRLRQLEDERNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 EKEQKlqndfaekeRKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD---------EETTAKAD----EI 229
Cdd:pfam01576 543 LEEGK---------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlEKKQKKFDqmlaEE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 230 EMIMTDLERANQRAEVAQREAET--------------LREQLSSANHSLQ--LASQIQKAPDVEQAIEVLTRS--SLEVE 291
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKETralslaraleealeAKEELERTNKQLRaeMEDLVSSKDDVGKNVHELERSkrALEQQ 693
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148277064 292 LAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNstlKQLEEKLK 346
Cdd:pfam01576 694 VEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARD---EQGEEKRR 745
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
108-367 |
3.48e-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: 48.66 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 108 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 181
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 182 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 254
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 255 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 327
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148277064 328 EQQLSAKNSTLKQLEEKLKGQADyEEVKKElNILKSMEFA 367
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
115-342 |
3.52e-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: 48.59 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 115 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 193
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 194 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 265
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 266 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 341
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 148277064 342 E 342
Cdd:pfam07111 297 E 297
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1245-1330 |
3.72e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 1245 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1324
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 148277064 1325 RSGRAA 1330
Cdd:COG5576 121 EEADLA 126
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
99-353 |
4.06e-05 |
|
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: 48.25 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 178
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 179 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 245
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 246 AQREAETLREQLSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRL 309
Cdd:pfam01576 150 LSKERKLLEERIS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148277064 310 QASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEE 353
Cdd:pfam01576 228 QAQIAELRaqlakkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
119-399 |
5.03e-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: 48.12 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 119 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 197
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 198 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 268
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 269 QIQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 345
Cdd:TIGR00606 391 QIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 346 KG--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLLEKNRSLQSENAAL 399
Cdd:TIGR00606 471 DRilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
61-347 |
5.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 61 QGEIDALSKRSKEAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 136
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 137 vtiKALKEKIREYEQTLkNQAETIALEKEQKLQ-----NDFAEKERKlQETQMSTTSKLEEAEHKVQSLQTAlektRTEL 211
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiAGEVSRSEA-WDVARELLRRLREQRHLAEQLQQL----RMRL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 212 FDLKTKYDEETTAKA-------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----A 273
Cdd:PRK04863 523 SELEQRLRQQQRAERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 274 PDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKL 345
Cdd:PRK04863 603 PAWLAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERF 682
|
..
gi 148277064 346 KG 347
Cdd:PRK04863 683 GG 684
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
163-419 |
5.66e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 242
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 243 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDV 306
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 307 QRLQASLTKLRENSASqISQLEQQLSAKNSTLKQlEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPleVLLL 386
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP--EDLS 282
|
250 260 270
....*....|....*....|....*....|...
gi 148277064 387 EKNRSLQSENAALRISNSDLSGSARRKGKDQPE 419
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
110-422 |
5.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 110 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKNQAETIALEKEQKLqndfAEKERKLQETQMSTTS 188
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 189 KLEEAEHKVQSLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 268
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 269 QIQKAPDVEQAIEVltRSSLEVELAAKEREI--AQLVEDVQRLQASLTKLRENSASQISQLEQqlsaknsTLKQLEEKLK 346
Cdd:PTZ00121 1174 DAKKAEAARKAEEV--RKAEELRKAEDARKAeaARKAEEERKAEEARKAEDAKKAEAVKKAEE-------AKKDAEEAKK 1244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 347 GqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRR 422
Cdd:PTZ00121 1245 A----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
107-216 |
7.73e-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: 46.55 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 107 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 180
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 148277064 181 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 216
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
97-346 |
8.90e-05 |
|
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: 46.61 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 LGQQLQLkvqrLHDIETENQKLRETLEEYNKEfaevknqevTIKALKEKIREYEQTLKNQAETIAL------EKEQKLQN 170
Cdd:pfam04108 40 LSVQLAN----LEKVREGLEKVLNELKKDFKQ---------LLKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 171 DFAEkERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEA 250
Cdd:pfam04108 107 DFID-EDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 251 ETLREQLssANHsLQLASQIQKAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS- 322
Cdd:pfam04108 181 ASLLESL--TNH-YDQCVTAVKLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSa 257
|
250 260
....*....|....*....|....*.
gi 148277064 323 --QISQLEQQLSAKNSTLKQLEEKLK 346
Cdd:pfam04108 258 lqLIAEIQSRLPEYLAALKEFEERWE 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-455 |
8.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 188 SKLEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL--- 264
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 265 -----QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 339
Cdd:COG3883 85 reelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 340 QLEEKLKG----QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGSARRKGK 415
Cdd:COG3883 165 ELEAAKAEleaqQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148277064 416 DQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAG 455
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
98-344 |
1.06e-04 |
|
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: 47.25 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 98 GQQLQLKVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQaETIALEKEQKLQ 169
Cdd:COG3096 342 ALRQQEKIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 170 NdFAEKERKLQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQ 241
Cdd:COG3096 421 A-LEKARALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 242 RAE-----------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRL 309
Cdd:COG3096 496 TARellrryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEEL 569
|
250 260 270
....*....|....*....|....*....|....*
gi 148277064 310 QASLTKLREnsasQISQLEQQLSAKNSTLKQLEEK 344
Cdd:COG3096 570 EEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
747-933 |
1.08e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 747 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 822
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 823 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 902
Cdd:PHA03247 347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
|
170 180 190
....*....|....*....|....*....|.
gi 148277064 903 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 933
Cdd:PHA03247 409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
49-255 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 49 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKR--LIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLR------- 119
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 120 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 193
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148277064 194 EHKVQSLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 255
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
43-362 |
1.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 43 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLNVYKRLIDVPDPVPAL----DLG 98
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQ----RLHDIETENQKLRETLEEYNK--EFAEVKNQEVTIKALKEK--IREYEQTLKNQAETIA--------L 162
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKYKndIENKKQILSNIDAEINkyhaiikkL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 EKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR 242
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEILKIQEID 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 243 AEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT---------------------------RSSLEV 290
Cdd:PRK01156 404 PDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynekKSRLEE 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 291 ELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILK 362
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
47-394 |
1.37e-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: 46.22 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 47 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAaflnvykrlIDVPDPVPALDLgQQLQLKVQRLHD----IETENQKLR 119
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGKKY-LLLQKQLEQLQEenfrLETARDDYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 120 ETLEEYNKEFAE--VKNQEVT-----IKALKEKIREYEQTLK--NQAETIALEKEQKLQ--NDFAEKERKLQETQ---MS 185
Cdd:pfam05622 87 IKCEELEKEVLElqHRNEELTslaeeAQALKDEMDILRESSDkvKKLEATVETYKKKLEdlGDLRRQVKLLEERNaeyMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 186 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---REQLSSANH 262
Cdd:pfam05622 167 RTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRDTLRETNE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 263 SL-----------------------------------------------------QLASQIQKAPDVEQAIE--VLTRSS 287
Cdd:pfam05622 243 ELrcaqlqqaelsqadallspssdpgdnlaaeimpaeireklirlqhenkmlrlgQEGSYRERLTELQQLLEdaNRRKNE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 288 LEVEL-AAKER--EIAQLVEDVQR----------------------------LQASLTKLRE-----------NSASQIS 325
Cdd:pfam05622 323 LETQNrLANQRilELQQQVEELQKalqeqgskaedssllkqkleehleklheAQSELQKKKEqieelepkqdsNLAQKID 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 326 QLEQQLSAKNSTLKQLEEKLKgqadyEEVKKELNILKSMEfaPSEGAGTQDAAKPLEVLLLEKNRSLQS 394
Cdd:pfam05622 403 ELQEALRKKDEDMKAMEERYK-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
99-363 |
1.53e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEK 175
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 176 ERKLQETQMSTT----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 247
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 248 REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 324
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148277064 325 SQLE---QQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKS 363
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-365 |
1.72e-04 |
|
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: 46.26 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 96 DLGQQLQ---------------------LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 154
Cdd:pfam15921 500 DLTASLQekeraieatnaeitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 155 NQAET---IALEKEQkLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQtaLEKTR-----TELFDLKTKYDEETT 223
Cdd:pfam15921 580 QHGRTagaMQVEKAQ-LEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLE--LEKVKlvnagSERLRAVKDIKQERD 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 224 AKADEIEMIMTDLERANQRAEVAQR-------EAET----LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 292
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRnfrnkseEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148277064 293 AAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLEEKLKGqadyeevkkELNILKSME 365
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAG---------ELEVLRSQE 799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-399 |
1.89e-04 |
|
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: 46.26 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 107 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQ 180
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 181 ETQMSTTSKLEEA----EHKVQSLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETL 253
Cdd:pfam15921 324 STVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 254 REQlssanhslqlasqiqkapDVEQAIevlTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSAsqiSQLEQQLSA 333
Cdd:pfam15921 404 WDR------------------DTGNSI---TIDHLRRELDDRNME-------VQRLEALLKAMKSECQ---GQMERQMAA 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 334 KNSTLKQLEEKLKGQADYEEVKKEL-NILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAL 399
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
210-362 |
1.98e-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: 46.00 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 210 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 286
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 287 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 362
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-379 |
2.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 114 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 189
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 190 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEmimTDLERANQRAEVAQREAEtlrEQLSSANHSLQLASQ 269
Cdd:PTZ00121 1642 EAEEKKKAEELK---------------KAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 270 IQKAPDVEQAIEVLTRSSLEVELAAKEREI----AQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEK 344
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAV 1780
|
250 260 270
....*....|....*....|....*....|....*
gi 148277064 345 LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAK 379
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
111-365 |
2.56e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 111 IETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIRE-----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMS 185
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEI--SRMRElerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 186 TTSKLEEAEHKVQSLQTALEKTRtelfdlktkydeettakADEIEMI-MTDLERANQRAEVAQREAETLREQLssanhsl 264
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEER-----------------AREMERVrLEEQERQQQVERLRQQEEERKRKKL------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 265 qlasQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQlvedVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ--LE 342
Cdd:pfam17380 478 ----ELEKEKRDRKRAEEQRRKILEKELEERKQAMIE----EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqeME 549
|
250 260
....*....|....*....|...
gi 148277064 343 EKLKGQADYEEVKKELNILKSME 365
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAME 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-357 |
2.90e-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: 45.73 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 38 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpALDLGQQLQLKVQRLHDIETENQK 117
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 118 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKNQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKV 197
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 198 QSLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLSSANHSLQLASQIQK 272
Cdd:TIGR00618 331 AAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 273 APDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQLSAKNSTLKQLEEKLK 346
Cdd:TIGR00618 404 ILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHL 483
|
330
....*....|.
gi 148277064 347 gqaDYEEVKKE 357
Cdd:TIGR00618 484 ---QETRKKAV 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-365 |
3.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 108 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQAETIALEKEQKlqndfAEKERKLQEtqmstt 187
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 188 skLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 267
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 268 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLSAKNSTLKQLEEKLK 346
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEK 352
|
250
....*....|....*....
gi 148277064 347 GQADYEEVKKELNILKSME 365
Cdd:PRK03918 353 RLEELEERHELYEEAKAKK 371
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
21-266 |
3.90e-04 |
|
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: 45.13 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 21 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 100
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQ-LKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKNQAETIALEKEQKLQ 169
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 170 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 246
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 148277064 247 QREAETLREQLSSANHSLQL 266
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
10-383 |
5.21e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 10 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 78
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 79 ----LNVYKRLIDVPDP--VPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 146
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 147 REYEQTLKNQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKVQSLQTALEKTRTELfdlktkYDEETTAKA 226
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 227 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVED 305
Cdd:pfam05557 271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 306 VQRLQASLTKLRENSASQISQLEQQLSAKNSTlKQLEEKLKGQADY-EEVKKELNILK-SMEFAPSEGAGTQDAAKPLEV 383
Cdd:pfam05557 344 LQRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
111-342 |
6.39e-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: 44.40 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 111 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAE-------------TIALEKEQKLQNDFA 173
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKAQFERDLQARDEQGEekrrqlvkqvrelEAELEDERKQRAQAV 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 174 EKERKLQ------ETQMSTTSK-LEEAEHKVQSLQTALEKTRTELFDLKTKYDE------ETTAKADEIEMIMTDLERAN 240
Cdd:pfam01576 770 AAKKKLEldlkelEAQIDAANKgREEAVKQLKKLQAQMKDLQRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEVAQREAETLREQLSSanhslQLASQIQKapdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-- 318
Cdd:pfam01576 850 AASERARRQAQQERDELAD-----EIASGASG------------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDrl 912
|
250 260
....*....|....*....|....*
gi 148277064 319 -NSASQISQLEQQLSAKNSTLKQLE 342
Cdd:pfam01576 913 rKSTLQVEQLTTELAAERSTSQKSE 937
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
57-259 |
7.03e-04 |
|
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: 43.09 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 57 LKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE----V 132
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALN--RRIQLLEEELERTEERLAEALEKLEEAEKAADEsergR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 133 KNQEVTIKALKEKIREYEQTLKnQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRT 209
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148277064 210 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 259
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
12-362 |
7.88e-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: 44.27 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 12 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvaplLKSFQGEidalSKRSKEAEAA-------FLNVYKR 84
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND-----LYHNHQR----TVREKERELVdcqreleKLNKERR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 85 LIDVPDPVPALDLGqQLQLKVQRLH------DIETENQKLRETLEEYNKEF---AEVKN-QEVTIKALKEKIREYEQTLK 154
Cdd:TIGR00606 337 LLNQEKTELLVEQG-RLQLQADRHQehirarDSLIQSLATRLELDGFERGPfseRQIKNfHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 155 NQAETIALEKEQ--KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQT-------------ALEKTRTELFDL----- 214
Cdd:TIGR00606 416 DLQSKERLKQEQadEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdrileldqELRKAERELSKAeknsl 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 215 -KTKYDEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSS 287
Cdd:TIGR00606 496 tETLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQ 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148277064 288 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 362
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
17-343 |
8.08e-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: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 17 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpald 96
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 lgQQLQLKVQRLHDIETENQklRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalEKEQKLQNDFAEKE 176
Cdd:pfam07888 100 --EEKYKELSASSEELSEEK--DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 177 RKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQREA 250
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 251 ETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 311
Cdd:pfam07888 254 EGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350
....*....|....*....|....*....|...
gi 148277064 312 SLTKLRensaSQISQLEQQLS-AKNSTLKQLEE 343
Cdd:pfam07888 333 RLQEER----MEREKLEVELGrEKDCNRVQLSE 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
114-211 |
8.46e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 114 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETiaLEKeqklqndfaeKERKLQETQMSTTSKLEEA 193
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLEL--LEK----------REEELEKKEKELEQKQQEL 126
|
90
....*....|....*...
gi 148277064 194 EHKVQSLQTALEKTRTEL 211
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-400 |
8.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 127 KEFAEVKNQEVTIKALKEKIREYEQTLKNQAEtialekEQKLQNDFAEKERKlqetqmSTTSKLEEAEHKVQSLQTALEK 206
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAE------AAADEAEAAEEKAEAAEKKKEE 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 207 TRTELFDLKTKYDE-----ETTAKADEIEMIMTDL---ERANQRAEVAQREAETLR--EQLSSANHSLQLASQIQKAPDV 276
Cdd:PTZ00121 1376 AKKKADAAKKKAEEkkkadEAKKKAEEDKKKADELkkaAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 277 EQAIEVLTRSSLE----------VELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLK 346
Cdd:PTZ00121 1456 AKKAEEAKKKAEEakkadeakkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148277064 347 GqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEvlllEKNRSLQSENAALR 400
Cdd:PTZ00121 1536 A----DEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALR 1581
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-398 |
9.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 9 LKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLNVYKRLID 87
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAEE 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 88 VPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQK 167
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 168 lqndfAEKERKLQETQmsttSKLEEAEHKVQSLQTALE-KTRTElfdlKTKYDEETTAKADEiemimtdleraNQRAEVA 246
Cdd:PTZ00121 1407 -----ADELKKAAAAK----KKADEAKKKAEEKKKADEaKKKAE----EAKKADEAKKKAEE-----------AKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 247 QREAETLREqlssANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKER---EIAQLVEDVQRLQASLTKLRENSASQ 323
Cdd:PTZ00121 1463 KKKAEEAKK----ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 324 ISQLEQQLSA----KNSTLKQLEEKLKG-QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 398
Cdd:PTZ00121 1539 AKKAEEKKKAdelkKAEELKKAEEKKKAeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
99-407 |
1.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 99 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAEtiALEKEQKLQNDFAEKERK 178
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNE--QLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 179 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 258
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 259 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 338
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 339 KQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLS 407
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
122-342 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 122 LEEYNKEFAEVKNQEVTIKALKEKIreyeqtlknqaetIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKVQSLQ 201
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKL-------------IASLKEGSGVEGL--------DSSTALTLELEELRQERDLLR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 202 TALEKTRTELFDLKTKydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIE 281
Cdd:pfam09787 61 EEIQKLRGQIQQLRTE---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 282 VLTR--SSLEVELaakEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQL------------------SAKN 335
Cdd:pfam09787 118 RLQEelRYLEEEL---RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLhqltetliqkqtmlealsTEKN 194
|
....*..
gi 148277064 336 STLKQLE 342
Cdd:pfam09787 195 SLVLQLE 201
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
116-347 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 116 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 194
Cdd:COG3096 495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 195 HKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSsanhsLQLASqiq 271
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSG-----EALAD--- 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148277064 272 kAPDVEQAIEvltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLSAKNSTLKQLEEKLKG 347
Cdd:COG3096 625 -SQEVTAAMQ---------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-256 |
1.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 32 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 109
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 110 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 186
Cdd:PTZ00121 1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148277064 187 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 256
Cdd:PTZ00121 1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
687-928 |
1.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 687 TAEPAQPSSASGSGNSDDAIRSILQQA---RREMEAQQAALDPA---------LKQAPLSQSDITILTPKLlSTSPMPTv 754
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAaparppvrrLARPAVSRSTESFALPPD-QPERPPQ- 2910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 755 ssyPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAAdcaqgvlrqvknevGRSGAWKDHWWSAVQPERRN 834
Cdd:PHA03247 2911 ---PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG--------------EPSGAVPQPWLGALVPGRVA 2973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 835 A--------ASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETP 906
Cdd:PHA03247 2974 VprfrvpqpAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE 3053
|
250 260
....*....|....*....|..
gi 148277064 907 QNSPLPSSPIVPMSKPTKPSVP 928
Cdd:PHA03247 3054 ALDPLPPEPHDPFAHEPDPATP 3075
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
241-400 |
1.13e-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: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 306
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 307 QRLQASLTKLRENS------------------ASQISQLEQQLSAKNS----------TLKQLEEKLKG----------- 347
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 348 QADYEEVKKELNILKSMEFAPSEGA------GTQDAAKplevlLLEKNRSLqseNAALR 400
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSEVVqrrphfSYEDAVG-----LLGENSDL---NEKLR 990
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
96-345 |
1.19e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 96 DLGQQLQLKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQtlKNQAEtiaLEKEQKLQNDFAE 174
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQ--KYEDE---LNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 KERKLQETQMSTTskleEAEHKVQSLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 253
Cdd:pfam00038 108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 254 REQLSS-ANHSLQLASQIQKApDVEQAIEVLTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 329
Cdd:pfam00038 176 RAQYEEiAAKNREEAEEWYQS-KLEELQQAAARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
|
250 260
....*....|....*....|
gi 148277064 330 QLSAK----NSTLKQLEEKL 345
Cdd:pfam00038 253 RYELQladyQELISELEAEL 272
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
52-217 |
1.22e-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: 42.22 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 52 QVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLKVQRLhdiETENQKLRETLEEYNKEFAE 131
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------EDLEKEIKRL---ELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 132 VKNQ-EVT-----IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttsklEEAEHKVQSLQTALE 205
Cdd:COG1579 85 VRNNkEYEalqkeIESLKRRISDLEDEILE-----LMERIEELEEELAELEAELAELE-------AELEEKKAELDEELA 152
|
170
....*....|..
gi 148277064 206 KTRTELFDLKTK 217
Cdd:COG1579 153 ELEAELEELEAE 164
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
12-261 |
1.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 12 ELDATATVLANRQD-----ESEQSRKRLIEQSREFKKNTPEDLRKQVAPL--LKSFQGEIDALSKR-SKEAEAAflnvyk 83
Cdd:pfam17380 328 EMDRQAAIYAEQERmamerERELERIRQEERKRELERIRQEEIAMEISRMreLERLQMERQQKNERvRQELEAA------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 84 RLIDVPDPVPALDLGQQLQLKVQ-RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaeTIAL 162
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK--KLEL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 163 EKEQKLQNDFAEKERKLQETQM-STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTAKADEIE--------MI 232
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEKELeERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREaEEERRKQQEMEerrriqeqMR 559
|
250 260
....*....|....*....|....*....
gi 148277064 233 MTDLERAnqRAEVAQREAETLREQLSSAN 261
Cdd:pfam17380 560 KATEERS--RLEAMEREREMMRQIVESEK 586
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
106-211 |
1.55e-03 |
|
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: 41.43 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 106 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIREyeqtLKNQAEtIALEKEQKLQND 171
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKD----LKWEHE-VLEQRFEKVERE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 148277064 172 FAEKERK----LQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 211
Cdd:pfam13851 122 RDELYDKfeaaIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-365 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 22 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLNVYKRLIDVPDP 91
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 92 VPALDLGQQLQLKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKNQAETIALE 163
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 164 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTE----------LFDLKTKYDE-----ETTAKADE 228
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADeakkaeekkkADEAKKKAEEakkadEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 229 I----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV----ELAAKEREIA 300
Cdd:PTZ00121 1327 AkkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDK 1404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148277064 301 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSME 365
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
689-957 |
1.62e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.15 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 689 EPAQPSSASGSGNSDDairsILQQARREMEAQQAALDPALKQAPLSQ---SDITILTPKLLSTSPMPTVSSYPPLAiSLK 765
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEpvaVAAAATTATQSWAAPVEPVTQTPPVA-SVD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 766 KPSAAPEAGASALPNPPAlkKEAQDAPglDPQGAADCAQGVLRQVknevgrsgAWKDHWWSAVQPERRNAASSEEAKAEE 845
Cdd:PRK10263 351 VPPAQPTVAWQPVPGPQT--GEPVIAP--APEGYPQQSQYAQPAV--------QYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 846 TGGGKEKGSGGSGGGSQPRAER----SQLQGPSSSEYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSK 921
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQpvagNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVE 497
|
250 260 270
....*....|....*....|....*....|....*.
gi 148277064 922 PTKPSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 957
Cdd:PRK10263 498 ETKPARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
96-423 |
1.72e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 96 DLGQQLQ-LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKNQAETIALEKEQKLQNDFAE 174
Cdd:PTZ00108 1035 DLVKELKkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEK 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 KERKLQETQmSTTSK---LEEaehkVQSLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVA 246
Cdd:PTZ00108 1114 KEKELEKLK-NTTPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKK 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 247 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 326
Cdd:PTZ00108 1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 327 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmeFAPSEGAGTQDA-AKPLEVLLLEKNRSLQSENAALRISNSD 405
Cdd:PTZ00108 1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKvKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
|
330
....*....|....*...
gi 148277064 406 lSGSARRKGKDQPESRRP 423
Cdd:PTZ00108 1339 -TRVKQASASQSSRLLRR 1355
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
130-348 |
1.78e-03 |
|
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: 41.90 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 130 AEVKNQEVTIKALKEKIREYEQTLKNQAETialekeqklqNDFAEKERKLQEtqmsttsKLEEAEHKVQSLQTALEKTRT 209
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQK-------ALDDAPAELRELRQELAALQA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 210 ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA---------ETLREQLSSANHSLQ-LASQIQKAPDVEQA 279
Cdd:pfam12795 66 KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSqlielqtrpERAQQQLSEARQRLQqIRNRLNGPAPPGEP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 280 IEVLTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQ 348
Cdd:pfam12795 146 LSEAQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
29-365 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 29 QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLNVYKrlidVPDPVPALDlgqqlQ 102
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALK-----S 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 103 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalKEKIREYEQTLKN-QAETIALEKEQKLQNdfaeKERKLQE 181
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDcQRELEKLNKERRLLN----QEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 182 TQMSTTSkLEEAEHKVQSLQTALEK----TRTELFDLKTKYDEETTAK----------ADEIEMIMTDLERANQRAEVAQ 247
Cdd:TIGR00606 347 VEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 248 REAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LAAKEREIAQLVEDVQRLQASLTKLRENSASQiSQ 326
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLEGSSDRILELDQELRKAERELSKAEKNSLTE-TL 499
|
330 340 350
....*....|....*....|....*....|....*....
gi 148277064 327 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 365
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
114-262 |
2.20e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.02 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 114 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 193
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148277064 194 EHKVQSLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 262
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1314-1387 |
2.30e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 1314 GQAGASDSPSARSGRAAPSSEGD-----SCDGVEATEGPGSADTEEPKSQGEAEREEVPRPAEQTEPPPSGTPGPDDAR 1387
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSgpapsSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD 361
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
108-398 |
2.35e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 108 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKNQAETIALEKE--QKLQNDFAEKERKLQEtQM 184
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEE-EI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 185 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSL 264
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER----EETRQVYMDL---NNNIEKMILAFEELRVQ--AENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 265 QLASQIQKAPDVEQAIEvltrSSLEVELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLSAKNSTLKQ 340
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLE----EEYKKEINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKE 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 341 LEEKLKG-QADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAA 398
Cdd:pfam05483 287 LIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-358 |
2.59e-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: 42.63 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 104 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 166
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 167 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKVQSLQT------ALEKTRTELFDLKTKYDEETTA---------- 224
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 225 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 294
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 295 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 358
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
104-342 |
2.68e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 104 KVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIreyeqtlkNQAEtialekeqklqnDFAEKER--KLQ 180
Cdd:pfam06160 33 KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELL--------FEAE------------ELNDKYRfkKAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 181 ETQMSTTSKLEEAEHKVQSLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevAQREA--- 250
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------ANRFSygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 251 --ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLRE------ 318
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELKEgyreme 224
|
250 260 270
....*....|....*....|....*....|...
gi 148277064 319 ---------NSASQISQLEQQLSAKNSTLKQLE 342
Cdd:pfam06160 225 eegyalehlNVDKEIQQLEEQLEENLALLENLE 257
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
20-277 |
2.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 20 LANRQDESEQSRKRLIEQSREFKKNTPE-DLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP--------- 89
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTevvqrrahf 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 90 ---DPVPALDLGQQLQLKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKEKIREYEQTLKnqaetialEKE 165
Cdd:PRK04863 972 syeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKSSYDAKRQMLQ--------ELK 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 166 QKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKVQSLQTALEKTRTELfdlktkydeettakadEIEMimtdlERAN 240
Cdd:PRK04863 1041 QELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC----------------EAEM-----DNLT 1094
|
250 260 270
....*....|....*....|....*....|....*..
gi 148277064 241 QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 277
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
101-280 |
3.04e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQLKVQR---LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQ---TLKNQAETIALEKEQ---KLQND 171
Cdd:pfam17078 20 LQLTVQSqnlLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDqlsELKNSYEELTESNKQlkkRLENS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 172 FAEKERKLQETQMSTT-------SKLEEAEH---KVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ 241
Cdd:pfam17078 100 SASETTLEAELERLQIqydalvdSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148277064 242 RAEVAQREAET-LREQLSSANHSLQLASQIQKAPDVEQAI 280
Cdd:pfam17078 180 NLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
29-365 |
3.07e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 29 QSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQGEIdaLSKRSKEAEAAFLNVYKRLIDVPDPVPALD-----LGQQ 100
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKqqsSIEEQRRLLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQqqkttLTQK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 180
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 181 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS- 259
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSe 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 260 ANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelaakerEIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 339
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
330 340
....*....|....*....|....*.
gi 148277064 340 QLEEKLKGQADYEEVKKELNILKSME 365
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQ 652
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
97-350 |
3.08e-03 |
|
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: 42.20 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 LGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKNQAETIALEKeQKLQNDFAE 174
Cdd:pfam15964 361 LKSELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 175 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR------ 248
Cdd:pfam15964 436 AQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarar 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 249 -EAETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQ 301
Cdd:pfam15964 516 eECLKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAK 595
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 148277064 302 LVEDVQRLQASLTKLRENSASQISQLEQQlsakNSTLKQLEEKLKGQAD 350
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
18-333 |
3.20e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 18 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpaldl 97
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 98 gqqlqlkvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKER 177
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 178 KLQETQMSTTSKLEEAEHKVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 245
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 246 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 309
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
|
330 340
....*....|....*....|....
gi 148277064 310 QASLTKLREnSASQISQLEQQLSA 333
Cdd:PRK10929 282 DLIASQQRQ-AASQTLQVRQALNT 304
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1305-1394 |
3.30e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.81 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 1305 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEVPRPAEQTEPPPSG 1379
Cdd:PRK12678 55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
|
90
....*....|....*
gi 148277064 1380 TPGPDDARDDDHEGG 1394
Cdd:PRK12678 135 EAARRGAARKAGEGG 149
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
116-313 |
3.31e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 116 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 194
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 195 HKVQSLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 268
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148277064 269 -----QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 313
Cdd:COG1842 169 rmeekIEEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
101-211 |
3.76e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 101 LQLKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVTI-KALKEKIREYEQT---LKNQAETIALE-KEQKLQNDFAEK 175
Cdd:pfam15294 131 LHMEIERLKE---ENEKLKERLKTLESQATQALDEKSKLeKALKDLQKEQGAKkdvKSNLKEISDLEeKMAALKSDLEKT 207
|
90 100 110
....*....|....*....|....*....|....*.
gi 148277064 176 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 211
Cdd:pfam15294 208 LNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-221 |
4.18e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 21 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVpaLDL 97
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKER--DEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 98 GQQLQLKVQRLHDIETENQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKN----QAETIALEKEQKLQNDFA 173
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSE----------LKAKLEALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRVE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148277064 174 EKERKLQETQMSTTSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEE 221
Cdd:TIGR02169 965 EEIRALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILERIEEYEKK 1015
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
224-350 |
4.36e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 224 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 303
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 148277064 304 edvqrlqasLTKLRENSAsQISQLEQQLSAKNSTLKQLEEKLKGQAD 350
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
97-237 |
4.48e-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: 39.68 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 97 LGQQLQLKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlknQAETialekEQKLQNDFAEKE 176
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 177 RKlqetqmsttsklEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 237
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-362 |
4.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 200 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQ 278
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 279 AIEVL-TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsQISQLEQQL-SAKNSTLKQLEEKLKGQA-DYEEVK 355
Cdd:COG4717 127 LLPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELeELLEQLSLATEEELQDLAeELEELQ 205
|
....*..
gi 148277064 356 KELNILK 362
Cdd:COG4717 206 QRLAELE 212
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
11-358 |
4.58e-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: 41.70 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 11 RELDATATVLANRQDESEQSRKR-------LIEQSREFKKNTPEDLR--KQVAPLLKSFQGEIDALSKRSKEAEAAflnv 81
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEAKRNverqlstLQAQLSDMKKKLEEDAGtlEALEEGKKRLQRELEALTQQLEEKAAA---- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 82 YKRLidvpdpvpaldlgqqlqlkvqrlhdiETENQKLRETLEEYnkeFAEVKNQEVTIKALKEKIREYEQTLknqAETIA 161
Cdd:pfam01576 568 YDKL--------------------------EKTKNRLQQELDDL---LVDLDHQRQLVSNLEKKQKKFDQML---AEEKA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 162 LEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKVQSLQTALEKTRTELFDLktkydeetTAKADEIEMIMTDLERAN 240
Cdd:pfam01576 616 ISARYAEERDRAEAEAREKETRaLSLARALEEALEAKEELERTNKQLRAEMEDL--------VSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 241 QRAEvaqREAETLREQLSsanhslQLASQIQKAPDVEQAIEVLT---RSSLEVELAAK----EREIAQLVEDVQRLQASL 313
Cdd:pfam01576 688 RALE---QQVEEMKTQLE------ELEDELQATEDAKLRLEVNMqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAEL 758
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 148277064 314 TKLRENSASQIS----------QLEQQLSAKN----STLKQLEeklKGQADYEEVKKEL 358
Cdd:pfam01576 759 EDERKQRAQAVAakkkleldlkELEAQIDAANkgreEAVKQLK---KLQAQMKDLQREL 814
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
56-358 |
4.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 56 LLKSFQGEIDALSKRSKEAEA-------------AFLNVYKRLIDVPDPVPAL-DLGQQLQLKVQRLHDIETENQKLRET 121
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELrQLNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 122 L----------------------EEYNKEFAEVKNQEVTIKALKEKIREYEQTLkNQAETIAlekeQKLQNDfaekerkl 179
Cdd:PRK04863 867 LeqakeglsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIV----SVLQSD-------- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 180 qetqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKT--------KYDEETTAKADEIEMImtdlERANQRAEVAQREAE 251
Cdd:PRK04863 934 -------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLN----EKLRQRLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 252 TLREQLSSANHSLQLASQIQkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRL----------QASLTK------ 315
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVL--------------ASLKSSYDAKRQMLQELKQELQDLgvpadsgaeeRARARRdelhar 1068
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 148277064 316 LRENSaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 358
Cdd:PRK04863 1069 LSANR-SRRNQLEKQLTFCEAEMDNLTKKLrKLERDYHEMREQV 1111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
288-359 |
4.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 288 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LSAKNSTLKQLEEKL 345
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*
gi 148277064 346 KG-QADYEEVKKELN 359
Cdd:COG4913 695 EElEAELEELEEELD 709
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
116-259 |
5.80e-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: 40.64 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 116 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKE-----QKLQNDFAEKERK-LQETQMSTTS 188
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEAIL--QADQALTEKEkeieaERAKAEAAEQERKlLEEQQRELEQ 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148277064 189 KLEEAEHkvqSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 259
Cdd:cd16269 227 KLEDQER---SYEEHLRQ-------LKEKMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7-181 |
6.40e-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: 39.91 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 7 ARLKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaaflnvyKRLI 86
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-------EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 87 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIAlEKEQ 166
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELE-AELE 159
|
170
....*....|....*
gi 148277064 167 KLQNDFAEKERKLQE 181
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
130-299 |
6.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 130 AEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKVQSLQTALEKtRT 209
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 210 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 286
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 148277064 287 SLEVELAAKEREI 299
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
266-362 |
6.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 266 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKL 345
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
|
90 100
....*....|....*....|.
gi 148277064 346 K--GQADYEEVKK--ELNILK 362
Cdd:COG2433 451 SeaRSEERREIRKdrEISRLD 471
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
26-345 |
6.96e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 26 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlNVYKRLIDVPDPV----------- 92
Cdd:PRK04778 133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVeareildqlee 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 93 ------------PAL------DLGQQL--------QLKVQ-----------RLHDIETENQKLRETLEEYNKEFAEVKNQ 135
Cdd:PRK04778 206 elaaleqimeeiPELlkelqtELPDQLqelkagyrELVEEgyhldhldiekEIQDLKEQIDENLALLEELDLDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 136 EvtikaLKEKIRE-YEQtlknqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKVQSLQTALEKTRTELFDL 214
Cdd:PRK04778 286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 215 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQKAPDvEQAIevlTRSSLEVE 291
Cdd:PRK04778 330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EITERIA-EQEI---AYSELQEE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148277064 292 LAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLsaknSTLKQLEEKL 345
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1264-1298 |
8.32e-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: 35.57 E-value: 8.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 148277064 1264 QQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSR 1298
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
114-370 |
9.13e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 114 ENQK--LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaetialekeqkLQNDFAEKE--RKLQETQMS-TTS 188
Cdd:pfam15921 102 EKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ-----------LQNTVHELEaaKCLKEDMLEdSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 189 KLEEAEHKVQSLQTALEKTRTELFDL-----KTKYDEET----------TAKADEIEMIMTDLERANQRAEVAQREAETL 253
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFeeasgKKIYEHDSmstmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 254 ReqlSSANHSLQLASQiQKAPDVEQAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 333
Cdd:pfam15921 251 K---SESQNKIELLLQ-QHQDRIEQLI-----SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270
....*....|....*....|....*....|....*...
gi 148277064 334 KNSTLKQLEEKLK-GQADYEEVKKELNilKSMEFAPSE 370
Cdd:pfam15921 322 LESTVSQLRSELReAKRMYEDKIEELE--KQLVLANSE 357
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
104-422 |
9.45e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 104 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 183
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 184 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 250
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 251 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 330
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 331 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAlRISNSDlsgsa 410
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEE----- 541
|
330
....*....|..
gi 148277064 411 RRKGKDQPESRR 422
Cdd:pfam17380 542 RRKQQEMEERRR 553
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
8-356 |
9.82e-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: 40.80 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 8 RLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlrkQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLID 87
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE---ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 88 VPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlknqaetiALEKEQK 167
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT------------NLQRRQQ 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 168 LQNDFAEKERKLQETqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTDLE 237
Cdd:TIGR00606 886 FEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKDIE 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148277064 238 RANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQLv 303
Cdd:TIGR00606 962 NKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQH- 1040
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 148277064 304 edvqrlqasLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKK 356
Cdd:TIGR00606 1041 ---------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIK 1085
|
|
| |
