|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1132-1209 |
1.00e-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: 116.15 E-value: 1.00e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412110 1132 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1209
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
949-1017 |
6.74e-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: 108.06 E-value: 6.74e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412110 949 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1017
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
582-658 |
2.93e-27 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 106.14 E-value: 2.93e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 582 EGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 658
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1255-1311 |
4.66e-16 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 73.69 E-value: 4.66e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 1255 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRR 1311
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-398 |
1.02e-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: 76.63 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 107 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQtlKSQAETIALEKEQKLQND 182
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEA--EVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 183 FAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 252
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 253 RAEVAQREAETLREQLSSANHSLqlaSQIQKAPDVLQvdgspssspraSAVSSLLcpsQEQAIEVLTRSSLEVELAAKER 332
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---EELEELIEELE-----------SELEALL---NERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412110 333 EIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKL--KGQADYEEVKKELNTLKS 398
Cdd:TIGR02168 902 ELRELESKRSELRRELEELRE----KLAQLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIED 965
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-393 |
1.22e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 58 EDLRKQVAPLLKsfQGEI----DALSKRSKEAEAAFLTVYKRLIDvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETL 133
Cdd:COG1196 196 GELERQLEPLER--QAEKaeryRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 134 EEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKEQKlqNDFAEKERKLQETQMSTTSKLEEAEHKLQ 209
Cdd:COG1196 263 AELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 210 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApdvlq 289
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 290 vdgSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAK 369
Cdd:COG1196 413 ---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340
....*....|....*....|....
gi 1720412110 370 NSTLKQLEEKLKGQADYEEVKKEL 393
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAA 513
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1255-1312 |
1.68e-13 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 66.50 E-value: 1.68e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412110 1255 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1312
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1255-1310 |
9.85e-13 |
|
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: 64.19 E-value: 9.85e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412110 1255 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIR 1310
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
11-396 |
6.00e-11 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 66.90 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 11 YWKRFDLQQLQRELD-ATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRK-----QVAPL--LKSFQGEIDA----- 77
Cdd:COG5185 130 IVALKDELIKVEKLDeIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFgltlgLLKGIseLKKAEPSGTVnsike 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 78 -------LSKRSKEAEAAFLTVYKRLIDVPDPVPALdvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT- 149
Cdd:COG5185 210 setgnlgSESTLLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANn 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 150 ----IKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDL 225
Cdd:COG5185 287 likqFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 226 KTKYD-EETTAKAD-----------EIEMIMTDLERANQraEVAQREAETLREQLSSANhslQLASQIQKAPDVLQVDGS 293
Cdd:COG5185 367 VGEVElSKSSEELDsfkdtiestkeSLDEIPQNQRGYAQ--EILATLEDTLKAADRQIE---ELQRQIEQATSSNEEVSK 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 294 PSSSPRASAV-----SSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNA 368
Cdd:COG5185 442 LLNELISELNkvmreADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
410 420
....*....|....*....|....*...
gi 1720412110 369 KNSTLKQLEeklkgQADYEEVKKELNTL 396
Cdd:COG5185 522 VAESLKDFM-----RARGYAHILALENL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-399 |
1.98e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 190 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 266 EQ---LSSANHSLQLASQIQKA---------------------------PDVLQV----------DGSPSSSPRASAVSS 305
Cdd:COG4717 227 EEleqLENELEAAALEERLKEArlllliaaallallglggsllsliltiAGVLFLvlgllallflLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 306 LLCPSQEQAIEVL----TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQ 375
Cdd:COG4717 307 LQALPALEELEEEeleeLLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEE 386
|
330 340
....*....|....*....|....
gi 1720412110 376 LEEKLKGQADYEEVKKELNTLKSM 399
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQ 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-353 |
7.60e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLTV 92
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 93 YKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKSQAEtiA 172
Cdd:COG1196 322 EEEL---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 173 LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQ 252
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 253 RAEVAQ--REAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAK 330
Cdd:COG1196 462 LELLAEllEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
330 340
....*....|....*....|...
gi 1720412110 331 EREIAQLVEDVQRLQASLTKLRE 353
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIE 564
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-435 |
2.82e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 123 ETENqKLRET---LEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTS 199
Cdd:TIGR02168 176 ETER-KLERTrenLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 200 KLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQ 276
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQL------EE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 277 LASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSA 356
Cdd:TIGR02168 328 LESKLDELAEELA--------------------ELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 357 SQISQLEQQLNAKNSTLKQLEEKLKGQAD-----YEEVKKELNTLKSMEFApsEGAGTQDSTKPLEVLLLEKNRSLQSEN 431
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEAL 463
|
....
gi 1720412110 432 ATLR 435
Cdd:TIGR02168 464 EELR 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-398 |
2.94e-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: 62.01 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 58 EDLRKQVAPLLK---SFQGEIDALSKRSKEAEAAFLTVYKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLE 134
Cdd:TIGR02169 684 EGLKRELSSLQSelrRIENRLDELSQELSDASRKIGEIEKEI---------EQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 135 EYNKEFAEVknqEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQ 212
Cdd:TIGR02169 755 NVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 213 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhslqlaSQIQKAPDVLQVDG 292
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 293 SPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVqrlqasltklrENSASqISQLEQQLNAKNST 372
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----------EEELS-LEDVQAELQRVEEE 966
|
330 340
....*....|....*....|....*..
gi 1720412110 373 LKQLEE-KLKGQADYEEVKKELNTLKS 398
Cdd:TIGR02169 967 IRALEPvNMLAIQEYEEVLKRLDELKE 993
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-398 |
5.63e-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: 61.24 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 112 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 192 ETQMSTTSKLEEAEHKLQTLQTALEK----TRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 268 LSSANHSL------------QLASQIQKAPDV---LQVDGSPSSSPRASAVSSLLcpSQEQAIEVLTR---------SSL 323
Cdd:TIGR02169 334 LLAEIEELereieeerkrrdKLTEEYAELKEEledLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRL 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412110 324 EVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKELNTLKS 398
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-231 |
5.94e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 93 ykrlidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412110 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDE 231
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
58-381 |
9.00e-09 |
|
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: 60.09 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 131
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 132 TLEEYNKEFAE--VKNQEVT-----IKALK----------EKIREYEQTLKSQaetialekEQKLQ--NDFAEKERKLQE 192
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKdemdilressDKVKKLEATVETY--------KKKLEdlGDLRRQVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 193 TQ---MSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---RE 266
Cdd:pfam05622 160 RNaeyMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 267 QLSSANHSLQlASQIQKApdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 346
Cdd:pfam05622 236 TLRETNEELR-CAQLQQA-------------------------ELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720412110 347 SLTKLRE----NSASQISQLEQQLNAKNSTLKQLEEKLK 381
Cdd:pfam05622 290 ENKMLRLgqegSYRERLTELQQLLEDANRRKNELETQNR 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-399 |
1.17e-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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 166 SQAETIA-LEKE-QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKtkydeettakaDEIEMI 243
Cdd:COG4942 17 AQADAAAeAEAElEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALE-----------QELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 244 MTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLcPSQEQAIEvltrssl 323
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAE------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 324 evELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSM 399
Cdd:COG4942 154 --ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-268 |
2.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflTVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 96 LIDVPDPVpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlksqaet 170
Cdd:PRK03918 534 LIKLKGEI------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP-------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 171 iALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEET--------TAKADEIEM 242
Cdd:PRK03918 600 -FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAG 677
|
250 260
....*....|....*....|....*.
gi 1720412110 243 IMTDLERANQRAEVAQREAETLREQL 268
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-400 |
2.74e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 19 QLQRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLT 91
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 92 VYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKSQAETi 171
Cdd:PRK03918 478 LRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 172 aLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDLKTKYDE---------ETTAKADEIE 241
Cdd:PRK03918 548 -LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEylelkdaekELEREEKELK 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 242 MIMTDLERANQRAEVAQREAETLREQLSSANHSLqlasqiqkapdvlqvdgspsssprasavssllcpSQEQAIEvltrs 321
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKY----------------------------------SEEEYEE----- 663
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412110 322 sLEVELAAKEREIAQLVEDVQRLQasltKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 400
Cdd:PRK03918 664 -LREEYLELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-398 |
3.53e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTI--------------KALKEKIREYEQTLKSQAETIAL 173
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslegskRKLEEKIRELEERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 174 EKEQ------------------KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTA---LEKTRTELFDLKTKYdEE 232
Cdd:PRK03918 278 LEEKvkelkelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRL-EE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 233 TTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-NHSLQLASQIQKAPDVL----QVDGSPSSSPRASAVSSL 306
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELeKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 307 LCP------SQEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLNAK 369
Cdd:PRK03918 437 KCPvcgrelTEEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKY 515
|
330 340
....*....|....*....|....*....
gi 1720412110 370 NstLKQLEEKLKgqaDYEEVKKELNTLKS 398
Cdd:PRK03918 516 N--LEELEKKAE---EYEKLKEKLIKLKG 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-394 |
5.10e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 185
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 186 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMI-----------------MTDLE 248
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenqsykqeiknlesqINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 249 RANQRAEVAQREAETLREQLSSANHSLQ-----LASQIQKAPDVLQvDGSPSSSPRASAVSSL--LCPSQEQAIEVLTRS 321
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIKNNSEIK-DLTNQDSVKELIIKNLdnTRESLETQLKVLSRS 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 322 ---------SLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS---QISQLEQQLNAKNSTLKQLEEKL---KGQADY 386
Cdd:TIGR04523 477 inkikqnleQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKEKESKISDLEDELnkdDFELKK 556
|
....*...
gi 1720412110 387 EEVKKELN 394
Cdd:TIGR04523 557 ENLEKEID 564
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
1.54e-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: 55.07 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720412110 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-435 |
1.67e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 17 LQQLQRELDATATVLANRQDESEQSRKRL---------IEQSREFKKNTPEDLRKQVapllksfqGEIDALSKRSKEaea 87
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKrkleekireLEERIEELKKEIEELEEKV--------KELKELKEKAEE--- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 88 afltvYKRLIDVpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsq 167
Cdd:PRK03918 295 -----YIKLSEF------------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 168 aetiALEKEQKLQNDFAEKERKLQETQMSTTSK-LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMtD 246
Cdd:PRK03918 356 ----ELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-E 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 247 LERANQRAEVAQRE----------AETLREQLSSANHSLQLASQIQKAPDVL-QVDGSPSSSPRASAVSSLLcpsqEQAI 315
Cdd:PRK03918 431 LKKAKGKCPVCGRElteehrkellEEYTAELKRIEKELKEIEEKERKLRKELrELEKVLKKESELIKLKELA----EQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 316 EVltRSSLEV----ELAAKEREIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKQLEEKLK---------G 382
Cdd:PRK03918 507 EL--EEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAellkeleelG 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 383 QADYEEVKKELNTLKSM--EF-----APSEGAGTQDSTKPLEVLLLEKNRSLQSENATLR 435
Cdd:PRK03918 584 FESVEELEERLKELEPFynEYlelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-374 |
1.80e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 206 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-----QLASQ 280
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 281 IQKAPDVLQVdgspsssprasavssllCPSQEQAIEVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 360
Cdd:COG4913 386 RAEAAALLEA-----------------LEEELEALEE-ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
250
....*....|....
gi 1720412110 361 QLEQQLNAKNSTLK 374
Cdd:COG4913 448 ALAEALGLDEAELP 461
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-259 |
1.87e-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: 53.78 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKE---QKLQNDFAEK 186
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEiesLKRRISDLED 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412110 187 E-RKLQEtqmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTdlERANQRAEVAQR 259
Cdd:COG1579 111 EiLELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
17-451 |
2.35e-07 |
|
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: 55.75 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 17 LQQLQRELDATATVLANRQDE---------SEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQ---------GEIDAL 78
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQslkereqqlQTKEQI 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 79 SKRSKEAEAAFLTVYKRLIDVPDPV--------PALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtI 150
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPCPLcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ---R 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 151 KALKEKIREYEQTLKSQAETIALEKE------------QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQT----- 213
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEdipnlqnitvrlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqqcs 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 214 ---ALEKTRTELFDLKTKYDEET---------------------TAKADEIEMIMTDLERANQRAEVAQREAETL----- 264
Cdd:TIGR00618 639 qelALKLTALHALQLTLTQERVRehalsirvlpkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeydr 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 265 -REQLSSANHSLQ--------LASQIQK-----APDVLQVDGSPSSSPRASAVSSLLCPSQEQAIE------VLTRSSLE 324
Cdd:TIGR00618 719 eFNEIENASSSLGsdlaaredALNQSLKelmhqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiqffNRLREEDT 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 325 VELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 392
Cdd:TIGR00618 799 HLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412110 393 LNTLKSMEFAPSEGAgtqdSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRD 451
Cdd:TIGR00618 878 LNGINQIKIQFDGDA----LIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
2.88e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 190 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 1720412110 270 S 270
Cdd:COG4913 430 S 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-358 |
3.13e-07 |
|
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: 54.38 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVD 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 292 GSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 358
Cdd:COG4942 176 LEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
36-268 |
3.49e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 36 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKE--AEAafltvyKRLIDVPDpvpalDVGQQL- 112
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKElrEEA------QELREKRD-----ELNEKVk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 113 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 193 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTK----------YDEETTAKADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqeLHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
....*.
gi 1720412110 263 TLREQL 268
Cdd:COG1340 227 ELHEEI 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-268 |
4.66e-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: 54.68 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 14 RFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 89 FLTVYKRlidvpdpvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFA----EVKNQEVTIKALKEKIREYEQTL 164
Cdd:TIGR02168 812 LTLLNEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 165 KSQAETIALEKE--QKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEM 242
Cdd:TIGR02168 883 ASLEEALALLRSelEELSEELRELESKRSELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEE 955
|
250 260
....*....|....*....|....*.
gi 1720412110 243 IMTDLERANQRAEVAQREAETLREQL 268
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI 981
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-398 |
9.77e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 58 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYN 137
Cdd:COG4717 74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 138 KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEK 217
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 218 TRTELFDLKtkyDEETTAKADEIEMIMT----------------------------------------------DLERAN 251
Cdd:COG4717 232 LENELEAAA---LEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllallflllarekaslgkEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 252 QRAEVAQREAETLREQLS--------SANHSLQLASQIQKAPDVL--------QVDGSPSSSPRASAVSSLLCPSQEQAI 315
Cdd:COG4717 309 ALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLreaeeleeELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 316 EVLTRS----SLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEK----------LK 381
Cdd:COG4717 389 AALEQAeeyqELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREElaeleaeleqLE 466
|
410
....*....|....*..
gi 1720412110 382 GQADYEEVKKELNTLKS 398
Cdd:COG4717 467 EDGELAELLQELEELKA 483
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
760-943 |
1.15e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 760 SASPMSTVSTYPPLAISLKKTPAAPETST--AALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMksELVRGSTWKDPW 837
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGVwgAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGAM--EVVSPLPRPRQH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 838 WSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERsqlqgpsasaeywKEWPSAESPYSQSSELSLTGASRSETPQ 917
Cdd:PHA03247 347 YPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRASLPTRKR-------------RSARHAATPFARGPGGDDQTRPAAPVPA 413
|
170 180
....*....|....*....|....*.
gi 1720412110 918 NSPLPSSPIVPMAKPAKPSVPPLTPE 943
Cdd:PHA03247 414 SVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-289 |
1.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALekeQKLQNDFAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 197 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170
....*....|....*..
gi 1720412110 273 HSLQLASQIQKAPDVLQ 289
Cdd:COG4913 763 VERELRENLEERIDALR 779
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-289 |
1.33e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 86 EAAFLTVYKRLIDVPDPvPALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARLKKLLNNIDLEEG-PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 166 S--------QAETIALEKEQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412110 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQ 289
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLE 1143
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-455 |
1.52e-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: 53.15 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLK-SQAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 202
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSdASRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 203 EAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 280
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 281 iqkapdvlqvdgspsssprasavssllcpsqeqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS--- 357
Cdd:TIGR02169 816 -----------------------------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiek 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 358 -------QISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsEGAGTQDSTkplevllLEKNRSLQS 429
Cdd:TIGR02169 855 eienlngKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELE-------RKIEELEAQ-------IEKKRKRLS 920
|
330 340
....*....|....*....|....*..
gi 1720412110 430 E-NATLRISNSDLSGSARRKGRDQPES 455
Cdd:TIGR02169 921 ElKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-397 |
1.80e-06 |
|
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: 52.90 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 119 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 188
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 189 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 266 EQLSSANHSLQ---------------LASQIQKAPDVLQVdgspsssprasavssllcpsQEQAIEVLTR--SSLEVELA 328
Cdd:pfam10174 352 LRLEEKESFLNkktkqlqdlteekstLAGEIRDLKDMLDV--------------------KERKINVLQKkiENLQEQLR 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412110 329 AKEREIAQLVEDVQRLQASLTklreNSASQISQLEQQLNAKNSTLKQLEEK--LKGQADYEEV---KKELNTLK 397
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSS----NTDTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-398 |
4.03e-06 |
|
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: 51.56 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 185
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 186 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 264 lrEQLSSANHSLqLASQIQKAPDVLQvdgspsssprasavssllcpsQEQAIEVLTRsslevELAAKEREIAQLVEDVQR 343
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQ---------------------KEKEKKDLIK-----EIEEKEKKISSLEKELEK 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412110 344 LQASLTKLrensASQISQLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKS 398
Cdd:TIGR04523 622 AKKENEKL----SSIIKNIKSKKNKLKQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-286 |
4.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykr 95
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 96 lidvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4913 688 --------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720412110 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAPD 286
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIR 860
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-400 |
5.65e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLtvykr 95
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL----- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 96 lidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtikALKEKIREYEqtLKSQAETIALEK 175
Cdd:pfam05483 445 ----------------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE-----LEKEKLKNIE--LTAHCDKLLLEN 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 176 eQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTaLEKTRTELFDLKTKYDEETTAKADEIE-----------MIM 244
Cdd:pfam05483 502 -KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN-LEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 245 TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSL---LCPSQEQAIEVLTRS 321
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLeleLASAKQKFEEIIDNY 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 322 SLEVELAAKEREiaQLVEDVQRLQASLtklrENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD--YEEVKKELNTLKSM 399
Cdd:pfam05483 660 QKEIEDKKISEE--KLLEEVEKAKAIA----DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDkiIEERDSELGLYKNK 733
|
.
gi 1720412110 400 E 400
Cdd:pfam05483 734 E 734
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-384 |
8.00e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 112 LEIKVQRLH--------DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ------ 177
Cdd:pfam12128 256 AELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealed 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 178 ---KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----R 249
Cdd:pfam12128 330 qhgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 250 ANQRAE---VAQREAETLREQLSSANHSL-----QLASQIQKAPdvLQVDGSPsssprasaVSSLLCPSQEQAIEVLTRS 321
Cdd:pfam12128 407 DRQLAVaedDLQALESELREQLEAGKLEFneeeyRLKSRLGELK--LRLNQAT--------ATPELLLQLENFDERIERA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412110 322 SLEVELAAKEreiaqlVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQA 384
Cdd:pfam12128 477 REEQEAANAE------VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
123-443 |
8.16e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 123 ETENQKLRETLEEYNKEFA---EVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQM 195
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYLLyldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEklaqVLKENKEEEKEKKLQEEEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 196 STTSKLEEAEHKlqtlQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQRAEVAQREAETLREQLSSANHS 274
Cdd:pfam02463 289 KLLAKEEEELKS----ELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 275 LQLASQIQKAPDVLQVDGSPSSSPRASAvssllcpsQEQAIEVLTRSSLEVELAAKEREiaQLVEDVQRLQASLTKLREn 354
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKL--------KEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEILE- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 355 sASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATL 434
Cdd:pfam02463 434 -EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
....*....
gi 1720412110 435 RISNSDLSG 443
Cdd:pfam02463 513 LALIKDGVG 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
142-398 |
8.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 142 EVKNQEVTIKALKEKIREYEQ------TLKSQAETiaLEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKLQTLQTA 214
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIEL--LEPIRELAERYAAARERLAELEyLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 215 LEKTRTELFDLKTKydeettakadeiemimtdLERANQRAEVAQREAETLREQLssanhslqlasqiqkapdvLQVDGsp 294
Cdd:COG4913 297 LEELRAELARLEAE------------------LERLEARLDALREELDELEAQI-------------------RGNGG-- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 295 sssprasavssllcpsqeQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL-------RENSASQISQLEQQLN 367
Cdd:COG4913 338 ------------------DRLE-----QLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLE 394
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720412110 368 AKNSTLKQLEEKL--------KGQADYEEVKKELNTLKS 398
Cdd:COG4913 395 ALEEELEALEEALaeaeaalrDLRRELRELEAEIASLER 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-567 |
8.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 196 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 276 QLASQIQKAPDVLqvdgspsssPRASAVSSLLcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRE 353
Cdd:COG3883 96 YRSGGSVSYLDVL---------LGSESFSDFL--DRLSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 354 NSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKEL-NTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENA 432
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAE---EAAAEAQLAELeAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 433 TLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGK 512
Cdd:COG3883 242 AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720412110 513 FALNSLLQRQLMQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGM 567
Cdd:COG3883 322 VVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYV 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
17-379 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 17 LQQLQRELDATATVLANRQDESEQSRkrlIEQSREFKKNTPEDLRKQVAPLlKSFQGEIDALSKRSKEAEAAfLTVYKRL 96
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEA---LEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEE-LEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 97 IDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNqEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 177 QKLQNDFAE------------------KERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL---FDLKTKYDEETTA 235
Cdd:COG4717 265 GGSLLSLILtiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 236 KADEIEMIMTDLERANQRAEVAQREAE----------TLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSS 305
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEiaallaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412110 306 LLCPSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsqISQLEQQLNAKNSTLKQLEEK 379
Cdd:COG4717 425 LDEEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
1.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 91 TVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 171 ---IALEKEQKLQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-385 |
1.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQL-----QAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 190 LQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4372 103 LESLQ-EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 270 SAnhslQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLT 349
Cdd:COG4372 182 EQ----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720412110 350 KLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQAD 385
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-358 |
1.62e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 105 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 182 DFAEKERKLQET-----QMSTTSKLEEAEHKLQTLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 257 AQREAETLREQLSSANHSLQLASQiqkapdvlqvdgspsssprasavssllcpSQEQAIEVLTR--SSLEVELAAKEREI 334
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKA-----------------------------ERQKLLARLEKelAELAAELAELQQEA 222
|
250 260
....*....|....*....|....
gi 1720412110 335 AQLVEDVQRLQASLTKLRENSASQ 358
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAA 246
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
123-388 |
1.78e-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: 49.79 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 123 ETENQKLRETLEEYNKEFAEV--KNQEVTikalKEKIREYEQTlksQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELekKHQQLC----EEKNALQEQL---QAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 201 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaevAQREAETLREQ 267
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK---LSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 268 LSsaNHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRsSLEVELAAKEREIAQLVEDVQRLQAS 347
Cdd:pfam01576 161 IS--EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQ 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720412110 348 LTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 388
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
105-396 |
1.79e-05 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 48.80 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 105 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 179
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 180 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 259
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 260 eaetLREQLSSANHSLQlaSQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSL----------EVELAA 329
Cdd:cd22654 155 ----LRTQIKTINDEIQ--EELTKILNRPIEVGDGSINIGKQVFTITITTATTKTVDVTSIGGLingignasddEVKEAA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 330 KerEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 396
Cdd:cd22654 229 N--KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-476 |
1.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKsfqgEIDALSKRSKEAEAAFLTVYKRlidvpdpvpALDVGQQ 111
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----KADAAKKKAEEAKKAAEAAKAE---------AEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 112 LEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikALKEKIREYeqtlKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD----EAKKKAEED----KKKADELKKAAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMTDLERANQ---RAEVAQREAETLREql 268
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAEEAKKADEakkKAEEAKKKADEAKK-- 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 269 ssANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVltRSSLEVELAAKEREIAQLVEDVQRLQASL 348
Cdd:PTZ00121 1505 --AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 349 TKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQadyEEVKKELNTLKSMEfapsEGAGTQDSTKPLEVLLLEKNRSLQ 428
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA---EEAKIKAEELKKAE----EEKKKVEQLKKKEAEEKKKAEELK 1653
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1720412110 429 SENATLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQ 476
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
199-394 |
1.98e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 199 SKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADeiemimTDLERANQRAEVAQREA--ETLREQLSSA--NHS 274
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED------LEKEIKRLELEIEEVEAriKKYEEQLGNVrnNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 275 LQ-LASQIQkapdvlqvdgspsssprasavssllcpSQEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL 351
Cdd:COG1579 91 YEaLQKEIE---------------------------SLKRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720412110 352 RENSASQISQLEQQLNAKNSTLKQLEEKLKGQ--ADYEEVKKELN 394
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-395 |
2.02e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 125 ENQKLRETLEeyNKEFAEVKNQEVTIKALKEKIREYEqtlksqaetiALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam02463 174 ALKKLIEETE--NLAELIIDLEELKLQELKLKEQAKK----------ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 205 EHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERanqRAEVAQREAETLREQLSSANHSLQLASQIQKa 284
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKLERRKVDDEEKLK- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 285 pdVLQVDGSPSSSPRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 364
Cdd:pfam02463 318 --ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270
....*....|....*....|....*....|.
gi 1720412110 365 QLNAKNSTLKQLEEKLKGQADYEEVKKELNT 395
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-392 |
2.25e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYE----------QTLKSQAETIALEKE-------------------- 176
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLEELEEERDdllaeaglddadaeavearr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 177 QKLQNDFAEKERKLQETQMSTTSKLEEAE-----------------HKLQTLQTALEKTRTELFDLKTK---YDEETTAK 236
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAEslredaddleeraeelrEEAAELESELEEAREAVEDRREEieeLEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 237 ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDvLQVDGSpsssprasavssllCPSQEQAI 315
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtARERVEEAEA-LLEAGK--------------CPECGQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 316 E----VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE--NSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEV 389
Cdd:PRK02224 462 EgsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
...
gi 1720412110 390 KKE 392
Cdd:PRK02224 542 LRE 544
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-399 |
2.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 187 ERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 262 ETLREQLSSanhSLQLASQIQKAPDVLQVDGSPSSsprasavssllcpsQEQAIEVLTRSSLE-----VELAAKEREI-A 335
Cdd:COG3206 243 AALRAQLGS---GPDALPELLQSPVIQQLRAQLAE--------------LEAELAELSARYTPnhpdvIALRAQIAALrA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412110 336 QLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSM 399
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-376 |
2.92e-05 |
|
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: 46.82 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 131 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKSQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 202
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 203 EAEHKLQTLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 275
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 276 QLASQIQkapdvlqvdgspsssprasavSSLLcpsqEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENS 355
Cdd:pfam13851 137 QQKTGLK---------------------NLLL----EKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDA 178
|
250 260
....*....|....*....|..
gi 1720412110 356 ASQISQ-LEQQLNAKNSTLKQL 376
Cdd:pfam13851 179 LQAVTEkLEDVLESKNQLIKDL 200
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
3.12e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.70 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720412110 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
13-384 |
3.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 13 KRFDLQQLQRELDATATVLAnrqdESEQSRKRLIEQSREfKKNTPEDLRKQVAPLLKSF---QGEIDALSKRSKEAEAAF 89
Cdd:PRK02224 249 RREELETLEAEIEDLRETIA----ETEREREELAEEVRD-LRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 90 LTVYKRLIDVPdpVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQT-- 163
Cdd:PRK02224 324 EELRDRLEECR--VAAQAHNEEAESLREDADDLEERAEELREEAAELESELeearEAVEDRREEIEELEEEIEELRERfg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 164 --------LKSQAETIALEKE-------------QKLQNDFAEKERKLQETQMST----------TSKLEEAEHKLQTLQ 212
Cdd:PRK02224 402 dapvdlgnAEDFLEELREERDelrereaeleatlRTARERVEEAEALLEAGKCPEcgqpvegsphVETIEEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 213 TALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQ-LASQIQKAPDVLQ 289
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAeLEAEAEEKREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 290 vDGSPSSSPRASAVSSLlcpSQEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASltklRENSASQISQLEQQLNAK 369
Cdd:PRK02224 562 -EAEEEAEEAREEVAEL---NSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREK----REALAELNDERRERLAEK 632
|
410
....*....|....*
gi 1720412110 370 NSTLKQLEEKLKGQA 384
Cdd:PRK02224 633 RERKRELEAEFDEAR 647
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
118-271 |
3.31e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 118 RLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIAlEKEQKLQnDFAEKERKLQETQMS- 196
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIK-RLELEIE-EVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412110 197 TTSK-LEEAEHKLQTL---QTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSA 271
Cdd:COG1579 86 RNNKeYEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-379 |
3.56e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 151 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 214 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSLqla 278
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSL--- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 279 SQIQKAPDVLQVdgspsssprasavssLLCPSQEQAIEVLTrssLEVELAAKEREIAQLVEDVQRLQASLTKL---RENS 355
Cdd:PHA02562 316 EKLDTAIDELEE---------------IMDEFNEQSKKLLE---LKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDN 377
|
250 260
....*....|....*....|....
gi 1720412110 356 ASQISQLEQQLNAKNSTLKQLEEK 379
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKE 401
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1255-1312 |
5.69e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.12 E-value: 5.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412110 1255 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRE 1312
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKK 109
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-434 |
6.54e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 210 TlqtalektrtelfdlktkydeETTAKADEIEMIMTDLERANQ-RAEVAQREAETLREQLSSA-------NHSLQLASQI 281
Cdd:TIGR00606 312 R---------------------TVREKERELVDCQRELEKLNKeRRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 282 QKAPDVLQVDGSPSSSPRASAVSSLLCPSQE-QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIS 360
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 361 QLEQQLNAKNSTLKQLEEKLKG--QADYEEVKKELNTLKSMEFAPSEGAGTQD-STKPLEVLLLEKNRSLQSENATL 434
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
9.66e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412110 181 NDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
702-967 |
1.05e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 702 EPVQTSSTSSSGNSDDairsILQQARREMEAQQAALDPALKPAPLSQPdltiltpkhLSASPMSTVSTYPPLAISLKKTP 781
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEP---------VAVAAAATTATQSWAAPVEPVTQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 782 AAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGvLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTA 861
Cdd:PRK10263 343 TPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEG-YPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYY 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 862 SGKERAGSSQPRAERSQLQGPSASA-------EYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAK 934
Cdd:PRK10263 422 APAPEQPAQQPYYAPAPEQPVAGNAwqaeeqqSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETK 500
|
250 260 270
....*....|....*....|....*....|...
gi 1720412110 935 PSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 967
Cdd:PRK10263 501 PARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
108-383 |
1.14e-04 |
|
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: 47.02 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 108 VGQQLEIKVQRLHDIETENQKLR--------------ETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL 173
Cdd:pfam05483 132 VSLKLEEEIQENKDLIKENNATRhlcnllketcarsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 174 EKEQKLQNDFAEKERKLQETQMSTTSK----------LEEAEHKLQTLQTALEKTRTELFDL--KTKYDEE----TTAKA 237
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLEEEYKKEINDKekqvsllliqITEKENKMKDLTFLLEESRDKANQLeeKTKLQDEnlkeLIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 238 DEIEMIMTDLERANQRAEVAQReaeTLREQLSSANHSLQLASQIQKApdvlQVDGSPSSSPRASAVSSLLcPSQEQAIEV 317
Cdd:pfam05483 292 DHLTKELEDIKMSLQRSMSTQK---ALEEDLQIATKTICQLTEEKEA----QMEELNKAKAAHSFVVTEF-EATTCSLEE 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412110 318 LTRSSLEvELAAKEREIAQLVEDVQRLQASL---TKLRENSASQISQL------EQQLNAKNSTLKQLEEKLKGQ 383
Cdd:pfam05483 364 LLRTEQQ-RLEKNEDQLKIITMELQKKSSELeemTKFKNNKEVELEELkkilaeDEKLLDEKKQFEKIAEELKGK 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-401 |
2.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 150 IKALKEKIREYEqTLKSQAETIALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY 229
Cdd:COG4717 48 LERLEKEADELF-KPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 230 D-EETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKApdvlqvdgspsssprasavssllc 308
Cdd:COG4717 126 QlLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------ELEAELAEL------------------------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 309 psQEQAIEVLTRSSLevelaAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKGQADYEE 388
Cdd:COG4717 176 --QEELEELLEQLSL-----ATEEELQDLAEELEELQQ-----------RLAELEEELEEAQEELEELEEELEQLENELE 237
|
250
....*....|...
gi 1720412110 389 VKKELNTLKSMEF 401
Cdd:COG4717 238 AAALEERLKEARL 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
60-266 |
2.89e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 60 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLTVYKR--LIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLR------- 130
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 131 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 204
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412110 205 EHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
743-943 |
3.23e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 743 PAPLSQPDLTILTPKhlSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRP 822
Cdd:PHA03247 2754 PARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 823 MKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEywkewPSAESPYSQS 902
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTE-----SFALPPDQPE 2906
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720412110 903 SELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSvPPLTPE 943
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ-PPLAPT 2946
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
303-454 |
3.46e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 303 VSSLLCPSQEQAIEVLTRSSLEVEL-AAKEREIAQlVED---VQRLQASLTKLrensaSQISQLEQQLNAKNSTLKQLEE 378
Cdd:PRK11281 21 CLSSAFARAASNGDLPTEADVQAQLdALNKQKLLE-AEDklvQQDLEQTLALL-----DKIDRQKEETEQLKQQLAQAPA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412110 379 KLKgqadyeEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSarrkgRDQPE 454
Cdd:PRK11281 95 KLR------QAQAELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL-----QTQPE 159
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-276 |
3.58e-04 |
|
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: 45.13 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 205 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ 276
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE 214
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
101-381 |
3.61e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 101 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 179
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 180 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 256
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 257 AQREAEtLREQLSSanhslqlaSQIQKAPdvlqvdgspsssprasavsslLCPSQEQAievltrssLEVELAAKEREIA- 335
Cdd:PRK11281 169 SQRLQQ-IRNLLKG--------GKVGGKA---------------------LRPSQRVL--------LQAEQALLNAQNDl 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720412110 336 --QLVEDVQRLQASLTKLRENSASQISQLEQQL-------NAKNstLKQLEEKLK 381
Cdd:PRK11281 211 qrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
131-391 |
3.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 131 ETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKER------------KLQETQMSTT 198
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDnradeateeafgKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 199 SKLEEAEHKLQTLQTALEKTRTELF---DLKTKYDEETTAKADEIEMIMTDLERAnQRAEVAQREAETLREQLSSANHSL 275
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 276 QLASQIQKAPDVLQVDgSPSSSPRASAVSSLLCPSQEQAIEVLTRssleVELAAKEREIAQLVEDVqRLQASLTKLRENS 355
Cdd:PTZ00121 1188 RKAEELRKAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKDAEEAKKAEEE-RNNEEIRKFEEAR 1261
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720412110 356 ASQISQLEQQLNA----KNSTLKQLEEKLKGQA--DYEEVKK 391
Cdd:PTZ00121 1262 MAHFARRQAAIKAeearKADELKKAEEKKKADEakKAEEKKK 1303
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-378 |
4.80e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 122 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 202 EEAEHKLQTLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHslQLASQI 281
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--QLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 282 QKAPDVLQVDgspsSSPRASAVSSLlcpsqEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQ 361
Cdd:COG3206 312 QRILASLEAE----LEALQAREASL-----QAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEE 376
|
250
....*....|....*..
gi 1720412110 362 LEQQLNAKNSTLKQLEE 378
Cdd:COG3206 377 ARLAEALTVGNVRVIDP 393
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-454 |
5.05e-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: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 254 AEVAQREAETLREQL----SSANHSLQLASQIQKAPDVLQVdgspssspRASAVSSLlcpsqEQAIEVLTRSSLEVELAA 329
Cdd:pfam05557 127 LQSTNSELEELQERLdllkAKASEAEQLRQNLEKQQSSLAE--------AEQRIKEL-----EFEIQSQEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 330 KERE-IAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMefaps 404
Cdd:pfam05557 194 SELArIPELEKELERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKL----- 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720412110 405 egAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPE 454
Cdd:pfam05557 268 --AQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
117-222 |
5.37e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 117 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIR--EYEQTLKSQaetiALEKEQKLQ 180
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKdlKWEHEVLEQ----RFEKVERER 122
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720412110 181 NDFAEK-ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTEL 222
Cdd:pfam13851 123 DELYDKfEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
68-270 |
5.60e-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: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 68 LKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQ-LEIKVQRLHDIET---ENQKLRETLEeyNKEFAEv 143
Cdd:pfam00261 17 LKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEE---ELERTEErLAEALEKLEEAEKaadESERGRKVLE--NRALKD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 144 knqevtikalKEKIREYEQTLKsQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKLQTLQTALEKTRT 220
Cdd:pfam00261 91 ----------EEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720412110 221 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-271 |
5.69e-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: 44.50 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 28 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTvykrlidvpdpvpALD 107
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ-------------SRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLKSQAETIalEKEQKLQNDFAEK 186
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAhEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 187 ERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQRE 260
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERK 252
|
250
....*....|.
gi 1720412110 261 AETLREQLSSA 271
Cdd:pfam07888 253 VEGLGEELSSM 263
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
110-273 |
7.03e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ-EVTIKALKEKIREYEQtLKSQAETIALEKE--QKLQNDFAEK 186
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEErDELNEKLNELREELDE-LRKELAELNKAGGsiDKLRKEIERL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 187 ERKLQETQMSTT------SKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTaKADEIEMIMTDL-ERANQ-RAEVAQ 258
Cdd:COG1340 122 EWRQQTEVLSPEeekelvEKIKELEKELEKAKKALEKNE-KLKELRAELKELRK-EAEEIHKKIKELaEEAQElHEEMIE 199
|
170
....*....|....*..
gi 1720412110 259 --REAETLREQLSSANH 273
Cdd:COG1340 200 lyKEADELRKEADELHK 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-397 |
8.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKR 95
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 96 LIDVPDPvpALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETiALEK 175
Cdd:COG1196 395 AAELAAQ--LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY------DEETTAKADEIEMIMTDLER 249
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 250 ANQRAEVAQREAETLREQL--------------SSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQAI 315
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKagratflpldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 316 E----------------------------VLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 367
Cdd:COG1196 632 LeaalrravtlagrlrevtlegeggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412110 368 AKNSTLKQLEEKLKGQ--------------------------------ADYEEVKKELNTLK 397
Cdd:COG1196 712 AEEERLEEELEEEALEeqleaereelleelleeeelleeealeelpepPDLEELERELERLE 773
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
108-248 |
8.69e-04 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 41.61 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 108 VGQQLEIKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQaetialekeQKLQNDFAEKE 187
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQ---------EKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412110 188 RKlqetqmsttsklEEAEHKLQTLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 248
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
18-445 |
8.76e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSrefkkntpedlrkqvapllksfqGEIDALSKRSKEAEAAFltvykrli 97
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQAN-----------------------GELEKASREETFARTAL-------- 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 98 dvpdpvpaldvgQQLEIKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIA 172
Cdd:pfam12128 649 ------------KNARLDLRRLFD---EKQSEKDKKNKALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 173 LEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKLQtlQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERA 250
Cdd:pfam12128 714 TEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERI 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 251 NQRAEVAQREAETLREQLSSANHSLQlasqiqkapdvlqvdgspsssprasavssllcpsqeqaievltrssleVELAAK 330
Cdd:pfam12128 788 AVRRQEVLRYFDWYQETWLQRRPRLA------------------------------------------------TQLSNI 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 331 EREIAQLVEDVQRLQASlTKLRensasqISQLEQQLNAKNSTLKQLEEKLKGQADYEEvkkELNTLKsmEFAPSEGAGTQ 410
Cdd:pfam12128 820 ERAISELQQQLARLIAD-TKLR------RAKLEMERKASEKQQVRLSENLRGLRCEMS---KLATLK--EDANSEQAQGS 887
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1720412110 411 DSTKP--LEVLLLEKNR---SLQSENATLRISNSDLSGSA 445
Cdd:pfam12128 888 IGERLaqLEDLKLKRDYlseSVKKYVEHFKNVIADHSGSG 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-406 |
1.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGEIDALSKRSKEAEAAfltvyKRLIDVP 100
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-----KKADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRET--LEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETI------- 171
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadeakk 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 172 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--R 249
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRAS--AVSSLLCPSQEQAIEVLTRSSLEVEL 327
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAEED 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 328 AAKEREIAQLVEDVQRLQASLTKLRENS--ASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSE 405
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
.
gi 1720412110 406 G 406
Cdd:PTZ00121 1754 E 1754
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
63-228 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 63 QVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldvgqQLEIKvqrlhDIETENQKLRETLEEYNKEFAE 142
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------EKEIK-----RLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 143 VKNQEVtIKALKEKIrEYEQTLKSQAETIALEKEQK---LQNDFAEKERKLQETQmsttsklEEAEHKLQTLQTALEKTR 219
Cdd:COG1579 85 VRNNKE-YEALQKEI-ESLKRRISDLEDEILELMERieeLEEELAELEAELAELE-------AELEEKKAELDEELAELE 155
|
....*....
gi 1720412110 220 TELFDLKTK 228
Cdd:COG1579 156 AELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
323-397 |
1.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 323 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LNAKNSTLKQLEEKL 380
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*...
gi 1720412110 381 KG-QADYEEVKKELNTLK 397
Cdd:COG4913 695 EElEAELEELEEELDELK 712
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
16-192 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLAN-------RQDESEQSRKRLIEQSREFkkntpEDLRKQvaplLKSFQGEIDALSKRSKEAEaa 88
Cdd:COG1579 11 DLQELDSELDRLEHRLKElpaelaeLEDELAALEARLEAAKTEL-----EDLEKE----IKRLELEIEEVEARIKKYE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 89 fltvyKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQA 168
Cdd:COG1579 80 -----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|....
gi 1720412110 169 ETIAlEKEQKLQNDFAEKERKLQE 192
Cdd:COG1579 152 AELE-AELEELEAEREELAAKIPP 174
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1274-1308 |
1.28e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 37.88 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|....*
gi 1720412110 1274 QQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSR 1308
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
16-269 |
1.49e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDeSEQSRkRLIEQSREFKKNTpEDLRKQV--AP-LLKSFQGEIDALSKRSKEaeaafltv 92
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQD-LEQTL-ALLDKIDRQKEET-EQLKQQLaqAPaKLRQAQAELEALKDDNDE-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 93 ykrliDVPDPVPALDVgQQLEikvQRLHDIETENQKLRETLEEYNKEFA---------------------EVKNQEVTIK 151
Cdd:PRK11281 113 -----ETRETLSTLSL-RQLE---SRLAQTLDQLQNAQNDLAEYNSQLVslqtqperaqaalyansqrlqQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 152 ALKEKIREYEQTLKsQAETIALEkeqkLQNDFAEKE----RKLQETQMS----TTSKLEEAEHKLQTLQTALEKTRTELF 223
Cdd:PRK11281 184 VGGKALRPSQRVLL-QAEQALLN----AQNDLQRKSlegnTQLQDLLQKqrdyLTARIQRLEHQLQLLQEAINSKRLTLS 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720412110 224 dlktkydEETTAKADEIEmimtDLERANQRAEVAQrEAETLReQLS 269
Cdd:PRK11281 259 -------EKTVQEAQSQD----EAARIQANPLVAQ-ELEINL-QLS 291
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
127-270 |
1.53e-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: 42.18 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 127 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYE---QTLKSQAETIALEKEQKLQNDFAEKERK-LQETQMSTTSKL 201
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELEQKL 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412110 202 EEAEHKLQTLQTALEKtrtelfdlktKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 270
Cdd:cd16269 229 EDQERSYEEHLRQLKE----------KMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
211-452 |
1.81e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 211 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPDVLQ 289
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 290 VdgspsssprasavssllcpSQEQAIEVLT-RSSLEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQ 365
Cdd:COG4372 84 E-------------------LNEQLQAAQAeLAQAQEELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 366 LNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsegagTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGS 444
Cdd:COG4372 145 IAEREEELKELEEQLESlQEELAALEQELQALS-----------EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
....*...
gi 1720412110 445 ARRKGRDQ 452
Cdd:COG4372 214 RELAEELL 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-206 |
1.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 12 WKRFDLQQLQRELDATATVLAN-------------RQDESEQSRKRLIEQSREFKKN--TPEDLRKQVAPLLKSFQGEID 76
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERldassddlaaleeQLEELEAELEELEEELDELKGEigRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 77 ALSKRSKEAEAAFLTvyKRLIDVPDPVPALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEF-AEVKNQEVTIKALk 154
Cdd:COG4913 738 AAEDLARLELRALLE--ERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWpAETADLDADLESL- 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720412110 155 ekiREYEQTLKSQAETIALEKEQKLqndfaeKERKLQETQMSTT---SKLEEAEH 206
Cdd:COG4913 815 ---PEYLALLDRLEEDGLPEYEERF------KELLNENSIEFVAdllSKLRRAIR 860
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
127-217 |
2.08e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 39.94 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 127 QKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETI--ALEK-EQKLQND----FAEKERKLQETQM 195
Cdd:smart00502 3 EALEELLTKLRKKAAELEDALKQLISiiqeVEENAADVEAQIKAAFDELrnALNKrKKQLLEDleeqKENKLKVLEQQLE 82
|
90 100
....*....|....*....|..
gi 1720412110 196 STTSKLEEAEHKLQTLQTALEK 217
Cdd:smart00502 83 SLTQKQEKLSHAINFTEEALNS 104
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-382 |
2.34e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 84 EAEAAFLTVYKRLIDVpdpVPALDVGQ----QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 160 YEQTLkSQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKLQTLQTALEKTRTeLFD 224
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQR-AER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 225 LKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDVLQVDgspssspr 299
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAWLAAQ-------- 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 300 aSAVSSLlcpsQEQAIEVLTRSslevelaakeREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN-------AKNST 372
Cdd:PRK04863 610 -DALARL----REQSGEEFEDS----------QDVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPR 674
|
410
....*....|
gi 1720412110 373 LKQLEEKLKG 382
Cdd:PRK04863 675 LNALAERFGG 684
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
184-423 |
2.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 184 AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 264 LREQLSSANHSLQlasQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVlTRSSLEVELAAKEREIAQLVEDVQR 343
Cdd:COG4372 106 LQEEAEELQEELE---ELQKERQDLE--------------------QQRKQLEA-QIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 344 LQASLTKLRENSA--------SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKP 415
Cdd:COG4372 162 LQEELAALEQELQalseaeaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
....*...
gi 1720412110 416 LEVLLLEK 423
Cdd:COG4372 242 LELEEDKE 249
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
2.46e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpaldVGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 112 L-EIKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-----VTIKALKEKIRE-YEQTLKSQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LaELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADeaqlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 181 NDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTAlektrtelfdlktkydeETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFLQDIKEKVEEERAGRLLKLN-----------------ELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 1720412110 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
115-379 |
3.05e-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: 42.25 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 115 KVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEK 186
Cdd:COG3096 348 KIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 187 ERKLQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLERAnQRAEVAQRE 260
Cdd:COG3096 426 RALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERS-QAWQTAREL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 261 AETLREQLSSANHSLQLASQIQKAPDVLQvdgspsssprasavssllcpSQEQAIEVLT----RSSLEVELAAK-EREIA 335
Cdd:COG3096 501 LRRYRSQQALAQRLQQLRAQLAELEQRLR--------------------QQQNAERLLEefcqRIGQQLDAAEElEELLA 560
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720412110 336 QLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEK 379
Cdd:COG3096 561 ELEAQLEELEEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-457 |
3.20e-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: 42.34 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 13 KRFD-LQQLQRELDATATVLANRQDESE-----QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSK 80
Cdd:TIGR00606 173 QKFDeIFSATRYIKALETLRQVRQTQGQkvqehQMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 81 RSKEAEAAFLTVYKrlidvpdpvpaldvgqqLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKE----K 156
Cdd:TIGR00606 253 RLKEIEHNLSKIMK-----------------LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ--LNDLYHnhqrT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 157 IREYEQTL-KSQAETIALEKEQKLQNdfaeKERKLQETQMSTTSkLEEAEHKLQTLQTALEK----TRTELFDLKTKYDE 231
Cdd:TIGR00606 314 VREKERELvDCQRELEKLNKERRLLN----QEKTELLVEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 232 ETTAK----------ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKApDVLQVDGSPSSSPRAS 301
Cdd:TIGR00606 389 ERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK-KQEELKFVIKELQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 302 AVSSLLCPSQEQaievLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKQLEEKLK 381
Cdd:TIGR00606 468 GSSDRILELDQE----LRKAERELSKAEKNSLTETLKKEVKSLQNEKADL-DRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412110 382 GQADYEEVKKELNTLKSMEFAPSegAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPESRR 457
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSL--LGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
111-385 |
3.75e-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: 41.82 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 111 QLEIKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKSQAETIALEKeQKLQNDFAEKER 188
Cdd:pfam15964 364 ELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 189 KLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR-------EA 261
Cdd:pfam15964 439 QLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarareEC 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 262 ETLREQLSSANHSLQLASQIQKAPDVLQVDGSPSSSPRASAVSSLLCPSQEQ--AIEVLTRSSLEVELAAKEREIAQLVE 339
Cdd:pfam15964 519 LKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQmeAQHDKTVNEQYSLLTSQNTFIAKLKE 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720412110 340 DVQRLQASLTKLRENSASQISQLEQQlnakNSTLKQLEEKLKGQAD 385
Cdd:pfam15964 599 ECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-394 |
3.94e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 110 QQLEIKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREY---------------------------- 160
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklkknkdkinklnsdlskinseiknd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 161 -EQTLKSQAETIALEKE----QKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTA 235
Cdd:TIGR04523 116 kEQKNKLEVELNKLEKQkkenKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID-KIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 236 KADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ-IQKAPDVLQvdgspSSSPRASAVSSllcpSQEQA 314
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQeINEKTTEIS-----NTQTQLNQLKD----EQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 315 IEVLTRSSLEVELAakEREIAQLVEDVQRLQASLTKLR----------------------ENSASQISQLEQQLNAKNST 372
Cdd:TIGR04523 266 KKQLSEKQKELEQN--NKKIKELEKQLNQLKSEISDLNnqkeqdwnkelkselknqekklEEIQNQISQNNKIISQLNEQ 343
|
330 340
....*....|....*....|...
gi 1720412110 373 LKQLEEKLKG-QADYEEVKKELN 394
Cdd:TIGR04523 344 ISQLKKELTNsESENSEKQRELE 366
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-173 |
4.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 17 LQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPL---LKSFQGEIDALSKRSKEAEAA--FLT 91
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELsreLAGLRAELEELEKRREEIKKTleKLK 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 92 VYKRLID-----VPDPVPALDVGQQLEIKVQRLHDIETEN--QKLRETLEEYNKEFAEVKNQEVTIKALKEKIR------ 158
Cdd:PRK03918 701 EELEEREkakkeLEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENKVKlfvvyq 780
|
170
....*....|....*..
gi 1720412110 159 --EYEQTLKSQAETIAL 173
Cdd:PRK03918 781 gkERPLTFLSGGERIAL 797
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
321-439 |
5.21e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.20 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 321 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLNAKNSTLKQLEEKLKgqADYEEVKKELNTLKsme 400
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720412110 401 FAPSEGAGTQdstkplevlLLEKNRSLQSENATLRISNS 439
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
727-938 |
6.02e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 727 RREMEAQQAALDPALKPAP----LSQPDLTILTPKHLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQ 802
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 803 DVPTLDPPGSADAAQGVLRPMKSELVRGSTwkdpwwspiqPERRNLTSSEETKADETTASGKERAGSSQPRAER--SQL- 879
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRV----------AVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSwaSSLa 3012
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412110 880 ----QGPSASAEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVP 938
Cdd:PHA03247 3013 lheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATP 3075
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
114-292 |
6.13e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 114 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 190 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttakadeiEMIMTDLERANQRAEVA 257
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL--------EEIMDEFNEQSKKLLEL 342
|
170 180 190
....*....|....*....|....*....|....*
gi 1720412110 258 QREAETLREQLSSANHSlqlASQIQKAPDVLQVDG 292
Cdd:PHA02562 343 KNKISTNKQSLITLVDK---AKKVKAAIEELQAEF 374
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-411 |
7.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETiALEKEQKLQNDFAEKERKLQETQM---STTSKLEEAEHKLQTLQTALEK 217
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRK-ALFELDKLQEELEQLREELEQAREeleQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 218 TRTELfdlkTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVLQvdgspsss 297
Cdd:COG4372 85 LNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK------QLEAQIAELQSEIA-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 298 prasavssllcpSQEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLqaSLTKLRENSASQISQLEQQLNAKNSTLKQLE 377
Cdd:COG4372 147 ------------EREEELK-----ELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
250 260 270
....*....|....*....|....*....|....
gi 1720412110 378 EKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQD 411
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-216 |
7.25e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.01 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 5 VGSMFQYWKRFDLQQLQRELDATATVlANRQDESEQSRKRLIEQSREFKKntpedLRKQVAPLLKSFQGEIDALSKRSke 84
Cdd:COG0610 690 LRALFPEGVDFSAFDPTEKLEALDEA-VERFLGDEEARKEFKKLFKELSR-----LYNLLSPDDEFGDLELEKYRDDV-- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 85 aeAAFLTVYKRLIDVPDPVPAldvgQQLEIKVQRLHD--IETENQKLRETLEE---YNKEFAE-VKNqevTIKALKEKIR 158
Cdd:COG0610 762 --SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQnpvQYRKFSElLEE---IIEEYNNGAL 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412110 159 EYEQTLKsqaETIALEKEQKLQNDFAEKErKLQETQMSTTSKLEEAEHKLQTLQTALE 216
Cdd:COG0610 833 DADEVLE---ELEELAKEVKEEEERAEEE-GLNEEELAFYDALAENLGDEKLKELAKE 886
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
117-278 |
7.64e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 117 QRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKSQAETIALEKEQKLQN-- 181
Cdd:COG3096 991 ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERARIRRDELHEel 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 182 -------DFAEKERKLQETQM-STTSKLEEAEHKLQTLQTALEktrtelfdlktkydeetTAKA---DEIEMIM-TDLER 249
Cdd:COG3096 1069 sqnrsrrSQLEKQLTRCEAEMdSLQKRLRKAERDYKQEREQVV-----------------QAKAgwcAVLRLARdNDVER 1131
|
170 180
....*....|....*....|....*....
gi 1720412110 250 ANQRAEVAQREAETLREQLSSANHSLQLA 278
Cdd:COG3096 1132 RLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
134-221 |
7.94e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 134 EEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHK-----L 208
Cdd:smart00935 21 KQLEKEFKKRQAE---LEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEelqkiL 97
|
90
....*....|...
gi 1720412110 209 QTLQTALEKTRTE 221
Cdd:smart00935 98 DKINKAIKEVAKK 110
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-392 |
8.12e-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: 40.72 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 49 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDpvpALDVGQQLEIKVQRLHDIETENQK 128
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 129 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKSQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKL 208
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 209 QTLQTALEKTRTELFDLKTKYDEEttakadeiemimtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVL 288
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQE---------------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 289 QVdgspssspRASAVSSLLCPSQEQAIEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQ 365
Cdd:TIGR00618 396 QS--------LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQS 467
|
330 340
....*....|....*....|....*..
gi 1720412110 366 LNAKNSTLKQLEEKLKgqaDYEEVKKE 392
Cdd:TIGR00618 468 LKEREQQLQTKEQIHL---QETRKKAV 491
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
122-253 |
9.20e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 38.74 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 122 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKSQAETIAlekeqKLQNDFAEKERKLQETQMsT 197
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412110 198 TSKLEEAEHKLqtlqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 253
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
320-397 |
9.77e-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: 39.52 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412110 320 RSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVK---KELNTL 396
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESL 101
|
.
gi 1720412110 397 K 397
Cdd:COG1579 102 K 102
|
|
| |
