|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
617-879 |
1.64e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 617 RISDIMDVYEMKLSTLAsKESR-------LQDLLETK-----ALALAQADRLIAQHRCQRTQAETEARTLASMLREVERK 684
Cdd:COG1196 190 RLEDILGELERQLEPLE-RQAEkaeryreLKEELKELeaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 685 NEELSVLLKAQQVESERAQsdiEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKL 764
Cdd:COG1196 269 LEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 765 NESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKE 844
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 578807635 845 LSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-865 |
4.39e-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: 73.55 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 626 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLR--------------EVERKNEELSVL 691
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskelteleaeieELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 692 LKAQQVESERAQSDI----EHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNES 767
Cdd:TIGR02168 777 LAEAEAEIEELEAQIeqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 768 LKEQNEKSIAQLIEKEEQRKEVQNQLvdrehklanlhqktKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSI 847
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNER--------------ASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
250
....*....|....*...
gi 578807635 848 KASSLEVQKAQLEGRLEE 865
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
628-877 |
9.24e-13 |
|
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: 72.41 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 628 KLSTLASKESRLQDLLETK--------ALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVES 699
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKreyegyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 700 ERAQSDIEHLFQhnRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQL 779
Cdd:TIGR02169 282 KDLGEEEQLRVK--EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 780 IEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 859
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
250
....*....|....*...
gi 578807635 860 EGRLEEKESLVKLQQEEL 877
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKL 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
622-878 |
7.03e-12 |
|
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: 69.70 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 622 MDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEAR-------TLASMLREVERKNEELSVLLKA 694
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 695 QQVESERAQSDIEHLFQHN----RKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKE 770
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLdelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 771 Q----------NEKSIAQLIEKEEQRKEVQNQLVDR--EHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRT 838
Cdd:TIGR02168 394 QiaslnneierLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 578807635 839 EQIRKELSIKASSLEVQKAQLEGRLEEKESL------VKLQQEELN 878
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFsegvkaLLKNQSGLS 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
640-851 |
3.24e-11 |
|
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: 65.94 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 640 QDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLE-S 718
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 719 VAEEHEILTK-----------SYMELLQRNESTEKKNKDLQI----------TCDSLNKQIETVKKLNESLKEQNEKSIA 777
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 778 QLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASS 851
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
650-882 |
3.82e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 650 LAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEhlfQHNRKLESVAEEHEILTKS 729
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE---QLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 730 YMELLQRNESTEKKNKDLQITCDSLNKQIEtvkKLNESLKEQNEKSIAQLIEKEEQRKEVQNQlvdrEHKLANLHQKTKV 809
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANL----RERLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807635 810 QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSH 882
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-877 |
1.67e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 625 YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSvLLKAQQVESERAQS 704
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-EAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEhlfqhnRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQitcdslnKQIETVKKLNESLKEQNEKSIAQLIEKEE 784
Cdd:COG1196 369 EAE------AELAEAEEELEELAEELLEALRAAAELAAQLEELE-------EAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 785 QRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQirkelsiKASSLEVQKAQLEGRLE 864
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLE 508
|
250
....*....|...
gi 578807635 865 EKESLVKLQQEEL 877
Cdd:COG1196 509 GVKAALLLAGLRG 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
630-834 |
1.73e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 630 STLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHL 709
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 710 FQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDlqitcdsLNKQIETVK-KLNEsLKEQNEKSIAQLIEKEEQRKE 788
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD-------LNAAIAGIEaKINE-LEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578807635 789 VQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 834
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
623-868 |
2.10e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 623 DVYEMK--LSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESE 700
Cdd:TIGR02169 682 RLEGLKreLSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 701 RAQSDIEHLfqhNRKLESVAEEheiltksyMELLQRNESTEKknkdLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 780
Cdd:TIGR02169 762 ELEARIEEL---EEDLHKLEEA--------LNDLEARLSHSR----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 781 EKEEQRKEVQNQLVDREH-----------------KLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRK 843
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDlkeqiksiekeienlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|....*
gi 578807635 844 ELSIKASSLEVQKAQLEGRLEEKES 868
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
638-880 |
2.79e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 638 RLQDLL-ETKAlalaQADRLIAQHRC----QRTQAETEARTLASMLREVERKNEELSvllkAQQVESERAQSDIEhlfQH 712
Cdd:TIGR02168 190 RLEDILnELER----QLKSLERQAEKaeryKELKAELRELELALLVLRLEELREELE----ELQEELKEAEEELE---EL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 713 NRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQ 792
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 793 LVDREHKLANLHQKTKVQEEKIKTLQKERE-------DKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEE 865
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEelesrleELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250
....*....|....*
gi 578807635 866 KESLVKLQQEELNKH 880
Cdd:TIGR02168 419 LQQEIEELLKKLEEA 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
596-889 |
1.05e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.44 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSGMVVKDQICDVRISDIMDVYEMKLS---TLASKESRLQDLLETKALALAQADRLIAQHrcqrtqAETEAR 672
Cdd:pfam15921 147 LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLShegVLQEIRSILVDFEEASGKKIYEHDSMSTMH------FRSLGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 673 TLASMLREVERKNEELS--VLLKAQQVESERAQSD--IEHLFQ-HNRKLESVAEEHEI----LT-------------KSY 730
Cdd:pfam15921 221 AISKILRELDTEISYLKgrIFPVEDQLEALKSESQnkIELLLQqHQDRIEQLISEHEVeitgLTekassarsqansiQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 731 MELLQ---RNEST--EKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSI----AQLIEKEEQRKEVQNQ---LVDREH 798
Cdd:pfam15921 301 LEIIQeqaRNQNSmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQEsgnLDDQLQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 799 K-LANLHQKTK---VQEEKIKTLQKEREDKEETIDILRKEL-SRTEQIRKELSIkassLEVQKAQLEGRLEEKESLVKLQ 873
Cdd:pfam15921 381 KlLADLHKREKelsLEKEQNKRLWDRDTGNSITIDHLRRELdDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGK 456
|
330
....*....|....*.
gi 578807635 874 QEELNKHSHMIAMIHS 889
Cdd:pfam15921 457 NESLEKVSSLTAQLES 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-899 |
1.05e-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: 62.38 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 711 QHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQ 790
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 791 NQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKE-SL 869
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRL 840
|
170 180 190
....*....|....*....|....*....|
gi 578807635 870 VKLQQEELNKHSHMIAMIHSLSGGKINPET 899
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
679-889 |
1.77e-09 |
|
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: 61.66 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 679 REVERKNEELSVLLkAQQVESERAQSDIEHLFQHNR-KLESVAEEHEILTKSYMELLQRNESTEKKNKDLQItcdSLNKQ 757
Cdd:pfam05483 233 KEINDKEKQVSLLL-IQITEKENKMKDLTFLLEESRdKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM---SLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 758 IETVKKLNESLKEQNeKSIAQLIE-KEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELS 836
Cdd:pfam05483 309 MSTQKALEEDLQIAT-KTICQLTEeKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 837 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLV-------KLQQEELNKHSHMIAMIHS 889
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdekkqfeKIAEELKGKEQELIFLLQA 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
636-882 |
2.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 636 ESRLQDLLETKALALAQADRLIAQHRcqRTQAETEARTLASMLREVERKNEELsvllkaqqveSERAQSDIEHLFQHNRK 715
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEEL----------EEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 716 LESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVD 795
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 796 REHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQE 875
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
....*..
gi 578807635 876 ELNKHSH 882
Cdd:COG1196 499 AEADYEG 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-874 |
3.18e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 633 ASKESRLQDLLETKALALAQADRLIAQHRCQRTQA--ETEARTLASMLREVE--RKNEEL---SVLLKAQQV-ESERAQS 704
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEekKKADELkkaEELKKAEEKkKAEEAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEHLFQHNRKLESV--AEEHEI--LTKSYMELLQRNESTEKKNKDLQITCDSLNKQiETVKKLNESLKEQneksiaqli 780
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAkkAEEARIeeVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKK--------- 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 781 EKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT--LQKEREDKEETIDILRK---ELSRTEQIRKElsikaSSLEVQ 855
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaeEAKKAEELKKK-----EAEEKK 1716
|
250
....*....|....*....
gi 578807635 856 KAQlEGRLEEKESLVKLQQ 874
Cdd:PTZ00121 1717 KAE-ELKKAEEENKIKAEE 1734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
668-880 |
4.27e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 668 ETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDL 747
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---RKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 748 QITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEET 827
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578807635 828 IDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
634-886 |
7.61e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 634 SKESRLQDLLEtKALALAQADRLiaqHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 713
Cdd:PTZ00121 1530 AEEAKKADEAK-KAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 R-KLESVAEEHEILTKSymELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESL---------KEQNEKSIAQLIEK- 782
Cdd:PTZ00121 1606 KmKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikaaeeakKAEEDKKKAEEAKKa 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 783 EEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT---LQKEREDKEETIDILRKELS----RTEQIRKELSIKASSLEVQ 855
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEedkkKAEEAKKDEEEKKKIAHLK 1763
|
250 260 270
....*....|....*....|....*....|.
gi 578807635 856 KAQLEGRLEEKESLVKLQQEELNKHSHMIAM 886
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
595-875 |
7.87e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 595 NIEELIEKLQSGMVVKDQICDVRISDIMDVyEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTL 674
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQL-KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 675 ASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEheiltksymeLLQRNESTEKKNKDLQITCDSL 754
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----------LTNQDSVKELIIKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 755 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 834
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578807635 835 LSRTEQIRKELSIKASSLEVQKaQLEGRLEEKESLVKLQQE 875
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNK-EIEELKQTQKSLKKKQEE 586
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
634-879 |
8.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 634 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAE-----TEARTLASMLR---EVERKNEELSvllkaQQVESERAQSD 705
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaAAAKKKADEAKkkaEEKKKADEAK-----KKAEEAKKADE 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 706 IEHLFQHNRKLESVAEEHEILTKS-----YMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 780
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 781 EKEEQRKEVQNQLVDREHKLANLHQKTKVQ--EEKIKTLQKEREDKEETIDILRKELSR-TEQIRKELSIKASSLEVQKA 857
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMK 1608
|
250 260
....*....|....*....|..
gi 578807635 858 QLEGRLEEKEslvKLQQEELNK 879
Cdd:PTZ00121 1609 AEEAKKAEEA---KIKAEELKK 1627
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
628-875 |
2.77e-08 |
|
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: 57.81 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 628 KLSTLASKESRLQDLLETKALALAQADRLIaqhRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIE 707
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 708 HLFQHNRKLE--SVAEEHEI------LTKSYMELlqrnESTEKKNKDLqitCDSLNKQIETVKKLNESLKEQNEKSIAQL 779
Cdd:pfam05483 612 ELHQENKALKkkGSAENKQLnayeikVNKLELEL----ASAKQKFEEI---IDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 780 IEKEEQRKEVQNQLvdrEHKLANL--------HQKTKVQEEKIKT--LQKEREDKEETIDI-LRKELSrteqirkelSIK 848
Cdd:pfam05483 685 DEAVKLQKEIDKRC---QHKIAEMvalmekhkHQYDKIIEERDSElgLYKNKEQEQSSAKAaLEIELS---------NIK 752
|
250 260
....*....|....*....|....*..
gi 578807635 849 ASSLEVQKaQLEGRLEEKESLVKLQQE 875
Cdd:pfam05483 753 AELLSLKK-QLEIEKEEKEKLKMEAKE 778
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
766-895 |
3.35e-08 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 57.17 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 766 ESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREhkLANLHQKTKVQEEKIKTLQKERED-------KEETIDILRKELSRT 838
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERE--LTEEEEEIRRLEEQVERLEAEVEEleaeleeKDERIERLERELSEA 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 839 -EQIRKEL--SIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHslSGGKI 895
Cdd:COG2433 454 rSEERREIrkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH--SGELV 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
634-879 |
6.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 634 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL-LKAQQVESERA---------Q 703
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELeKELESLEGSKRkleekirelE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 704 SDIEHLFQHNRKLESVAEEHEIL---TKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiaqLI 780
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 781 EKEEQRKEVQNQLVDREhKLANLHQKTKVQEEKIKTLQKERedKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLE 860
Cdd:PRK03918 342 ELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|....*....
gi 578807635 861 GRLEEKESLVklqqEELNK 879
Cdd:PRK03918 419 KEIKELKKAI----EELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
626-879 |
1.03e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 626 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASmlreveRKNEELSVLLKAQQVESERAQSD 705
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNKELKSELKNQEKKLEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 706 IE-HLFQHNRKLESVAEEHEILTKSYMELLQRNES-----TEKKN----------------KDLQITCDSLNKQIETVKK 763
Cdd:TIGR04523 326 IQnQISQNNKIISQLNEQISQLKKELTNSESENSEkqrelEEKQNeieklkkenqsykqeiKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 764 LNESLKEQ--NEKSIAQLIEKEEQR------------KEVQNQLVDREHKLANLHQKTKVQEEKIKTL------------ 817
Cdd:TIGR04523 406 LNQQKDEQikKLQQEKELLEKEIERlketiiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsinkikqnle 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 818 --QKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:TIGR04523 486 qkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
683-877 |
1.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 683 RKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEK--KNKDLQITCDSLNKQIET 760
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 761 VKKLNESLKEQneksIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEK-IKTLQKEREDKEETIDILRKELSRTE 839
Cdd:COG4717 144 LPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 578807635 840 QirkelsiKASSLEVQKAQLEGRLEEKESLVKLQQEEL 877
Cdd:COG4717 220 E-------ELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
752-877 |
1.63e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 752 DSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDIL 831
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578807635 832 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 877
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
632-875 |
1.81e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 632 LASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTlasmlREVER-KNEELSVL------LKAQQVESERAQS 704
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK-----RELERiRQEEIAMEisrmreLERLQMERQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEHLFQHNRKLESVAEEHEILTKSYMELLQ--RNESTEKKNKDLQITCDSLNKQIETVKKlnESLKEQNEKSIAQLIEK 782
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEqiRAEQEEARQREVRRLEEERAREMERVRL--EEQERQQQVERLRQQEE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 783 EEQRKEVQNQLVDREHKLANlHQKTKV--------------QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIK 848
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAE-EQRRKIlekeleerkqamieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
250 260
....*....|....*....|....*..
gi 578807635 849 ASSlEVQKaQLEGRLEEKESLVKLQQE 875
Cdd:pfam17380 550 ERR-RIQE-QMRKATEERSRLEAMERE 574
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
746-879 |
2.13e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 746 DLQItcDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKERE--- 822
Cdd:COG1579 16 DSEL--DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyea 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578807635 823 -DKEetIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:COG1579 94 lQKE--IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
678-843 |
2.19e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 678 LREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNE---STEKKNKDLQitcdSL 754
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlGNVRNNKEYE----AL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 755 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDRE----HKLANLHQKTKVQEEKIKTLQKEREDKEETIDi 830
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaeleEKKAELDEELAELEAELEELEAEREELAAKIP- 173
|
170
....*....|...
gi 578807635 831 lRKELSRTEQIRK 843
Cdd:COG1579 174 -PELLALYERIRK 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-879 |
2.39e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 668 ETEARTLASMLREVERKNEELSVLLKA--------QQVESERAQ---------SDIEHLFQHNRKLESVAEEHEILTKSY 730
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRtenieeliKEKEKELEEvlreineisSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 731 MELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQnEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ 810
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578807635 811 EEKIKTLQ---KEREDKEETIDILRKELsrtEQIRKELS-IKASSLEVQKA-QLEGRLEE-KESLVKLQQEELNK 879
Cdd:PRK03918 320 EEEINGIEeriKELEEKEERLEELKKKL---KELEKRLEeLEERHELYEEAkAKKEELERlKKRLTGLTPEKLEK 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
628-869 |
2.67e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 628 KLSTLASKESRLQDLLETKALAlaqaDRLIAQHRcqrtqAETEARTLAsmlreVERKNEELSVLLKAQQVESERAQsdie 707
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDL----EELIAERR-----ETIEEKRER-----AEELRERAAELEAEAEEKREAAA---- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 708 hlfqhnrKLESVAEEHeiltksymelLQRNESTEKKNKDLQITCDSLNK---QIETVKKLNESLKEQNEKSiAQLIEKEE 784
Cdd:PRK02224 562 -------EAEEEAEEA----------REEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKR-EALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 785 QRKEVQNQLVDREHKLANlhqktKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLE 864
Cdd:PRK02224 624 ERRERLAEKRERKRELEA-----EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
....*
gi 578807635 865 EKESL 869
Cdd:PRK02224 699 RREAL 703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
626-885 |
3.39e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 626 EMKLSTLASKESRLQDLLETKALALA----QADRL---IAQHRCQRTQAETEARTLASML----REVERKNEELSVLLKA 694
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQahneEAESLredADDLEERAEELREEAAELESELeearEAVEDRREEIEELEEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 695 QQVESER---AQSDIEHLFQHnrkLESVAEEHEILTKSYMEL---LQRNESTEKKNKDLQI-----TCDSLNKQIETVKK 763
Cdd:PRK02224 393 IEELRERfgdAPVDLGNAEDF---LEELREERDELREREAELeatLRTARERVEEAEALLEagkcpECGQPVEGSPHVET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 764 LNESlKEQNEKSIAQLIEKEEQRKEVQNQLvDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDilrkelsrteqirk 843
Cdd:PRK02224 470 IEED-RERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIE-------------- 533
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 578807635 844 ELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIA 885
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
634-880 |
3.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 634 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 713
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 RKLESVAEEHEILTKSyMELLQRNESTEKKNKDLQIT------CDSLNKQIETVKKLNESLKEQNEKSIA-QLIEKEEQR 786
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAaaakkkADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEA 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 787 KEVQNQLVDREHKLANLHQKTKVQE-EKIKTLQKEREDKEETIDILRK---------ELSRTEQIRK-------ELSIKA 849
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKaaeakkkadEAKKAEEAKKadeakkaEEAKKA 1536
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578807635 850 SSL----------EVQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:PTZ00121 1537 DEAkkaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
609-869 |
4.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 609 VKDQICDVRISDIMDV---YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAET---EARTLASMLREVE 682
Cdd:PRK02224 192 LKAQIEEKEEKDLHERlngLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 683 RKNEELSVLLKAQQVESERAQSDIEHLFQhnrKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVK 762
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLA---EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 763 KLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIR 842
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260
....*....|....*....|....*..
gi 578807635 843 KELSIKASSlevqkaqLEGRLEEKESL 869
Cdd:PRK02224 429 AELEATLRT-------ARERVEEAEAL 448
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
756-883 |
4.15e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 756 KQIETVKKLNESLKEQNEKsiaqliEKEEQRKEVQNQLVDREHKLAN-LHQKTKVQEEKIKTLQKEREDKEETIDilrKE 834
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKK------EAEAIKKEALLEAKEEIHKLRNeFEKELRERRNELQKLEKRLLQKEENLD---RK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578807635 835 LSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHM 883
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
595-880 |
4.19e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 595 NIEELIEKLQSGMVVKDQicdvRISDIMDVYEMKLSTLASKESRLQDLLETKALalaqadrlIAQHRCQRTQAETEARTL 674
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKELEELKEE--------IEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 675 ASMLREVERKNEELsvllKAQQVESERAQSDIEhlfqhnrKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSL 754
Cdd:PRK03918 258 EEKIRELEERIEEL----KKEIEELEEKVKELK-------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 755 NKQI-----------ETVKKLNESLKEQN-------------------------------EKSIAQLIEKEEQRKEVQNQ 792
Cdd:PRK03918 327 EERIkeleekeerleELKKKLKELEKRLEeleerhelyeeakakkeelerlkkrltgltpEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 793 LVDREHKLANLHQKTKVQEEKIKTLQKER------------EDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLE 860
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340
....*....|....*....|....*....
gi 578807635 861 GRLEEKESLVKLQQ---------EELNKH 880
Cdd:PRK03918 487 KVLKKESELIKLKElaeqlkeleEKLKKY 515
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
595-867 |
4.37e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 595 NIEELIEKLQSGMVVKDQICDVRISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEA--- 671
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 672 -RTLASMLREVERKNEELSVLLKAQQVESERAQSD---IEHLFQH--NRKLE---------SVAEEHEILTKSYMELLQ- 735
Cdd:pfam15921 376 dDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNsitIDHLRREldDRNMEvqrleallkAMKSECQGQMERQMAAIQg 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 736 RNESTEKKNK---DLQITCDSLNKQIE--TVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDR-----EHKLANLhQ 805
Cdd:pfam15921 456 KNESLEKVSSltaQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvDLKLQEL-Q 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 806 KTKVQEEKIKTLQKERE-------DKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG-----RLEEKE 867
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEalklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeindrRLELQE 608
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
666-879 |
4.85e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 666 QAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNK 745
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 746 DLQITCDSLNKQiETVKKLNESLKEQNEKSIAQLIEK--EEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKERED 823
Cdd:PTZ00121 1287 EEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 824 KEETidilrkELSRTEQIRKELSIKASSLEVQKAQlegRLEEKESLVKLQQEELNK 879
Cdd:PTZ00121 1366 AEAA------EKKKEEAKKKADAAKKKAEEKKKAD---EAKKKAEEDKKKADELKK 1412
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
626-873 |
9.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 626 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLL-KAQQVESE--RA 702
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKeKLIKLKGEikSL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 703 QSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNEST--------EKKNKDLQ------ITCDSLNKQIETVKKLNESL 768
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEpfyneyLELKDAEKELEREEKELKKL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 769 KEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLAnlhqktkvqEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELsik 848
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEI--- 692
|
250 260
....*....|....*....|....*
gi 578807635 849 ASSLEVQKAQLEGRLEEKESLVKLQ 873
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLE 717
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
670-879 |
1.00e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 670 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNE--------STE 741
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllqellrDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 742 KKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKER 821
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578807635 822 EDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
649-858 |
1.05e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 649 ALAQADRLIAQHRCQRTQAETEART----LASMLREVERKNEELSVL---LKAQQVESERAQSDIEhlfqhnRKLESVAE 721
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAaqaeLDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIA------EAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 722 EHEILTK------------SYMELLQRNESTEkknkDL--------QITcDSLNKQIETVKklneSLKEQNEKSIAQLIE 781
Cdd:COG3883 84 RREELGEraralyrsggsvSYLDVLLGSESFS----DFldrlsalsKIA-DADADLLEELK----ADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578807635 782 KEEQRKEVQNQLvdrEHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQ 858
Cdd:COG3883 155 KLAELEALKAEL---EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
688-879 |
1.25e-06 |
|
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: 51.69 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 688 LSVLLKAQQVESERAQSDIEhlfQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIetvKKLNES 767
Cdd:COG4942 11 LALAAAAQADAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 768 LKEqNEKSIAQL-IEKEEQRKEVQNQLV---------------------DREHKLANLHQKTKVQEEKIKTLQKEREDKE 825
Cdd:COG4942 85 LAE-LEKEIAELrAELEAQKEELAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578807635 826 ETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
692-877 |
1.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 692 LKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQI----ETVKKLNES 767
Cdd:COG3883 18 IQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerrEELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 768 LKEQ-----------NEKSIAQLIekeeQRKEVQNQLVDREHKLANLHQKTKvqeEKIKTLQKEREDKEETIDILRKELs 836
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFL----DRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAEL- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578807635 837 rtEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 877
Cdd:COG3883 167 --EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
634-826 |
1.57e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 634 SKESRLQDLLETKALALAQADRLIAQHRCQRtqaeteartlasmLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 713
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMR-------------RLEVERKRREQEEQRRLQQEQLERAEKMREELELEQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 RKlesVAEEHEILTKSYMELLQRNESTEKKNK-DLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQR-KEVQN 791
Cdd:pfam15709 383 QR---RFEEIRLRKQRLEEERQRQEEEERKQRlQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRqKELEM 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578807635 792 QLVDREHKLANLHQKTKV------QEEKIKTLQ--KEREDKEE 826
Cdd:pfam15709 460 QLAEEQKRLMEMAEEERLeyqrqkQEAEEKARLeaEERRQKEE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-876 |
1.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 668 ETEARTLASMLREVERKNEELSVLLKA-QQVESERAQ--SDIEHL-FQHNRKLESVAEEHEILTKSYMELL---QRNEST 740
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKlDELEEELAEllKELEELgFESVEELEERLKELEPFYNEYLELKdaeKELERE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 741 EKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQK- 819
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKt 695
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578807635 820 ---------EREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRL---------EEKESLVKLQQEE 876
Cdd:PRK03918 696 leklkeeleEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIaseifeeltEGKYSGVRVKAEE 770
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
635-879 |
2.15e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 635 KESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASmlrEVERKNEELsvllkaQQVESERAQSDIEhLFQHNR 714
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL------EQLEEELEQARSE-LEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 715 KLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLV 794
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 795 DREHKLANLHQKTKVQ-----EEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESL 869
Cdd:COG4372 161 SLQEELAALEQELQALseaeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250
....*....|
gi 578807635 870 VKLQQEELNK 879
Cdd:COG4372 241 ALELEEDKEE 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
669-879 |
3.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 669 TEARTLASMLreVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQ 748
Cdd:COG4717 38 TLLAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 749 ITCDSLNKQIetvkklneslkeQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQktkvQEEKIKTLQKEREDKEETI 828
Cdd:COG4717 116 EELEKLEKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578807635 829 DILRKELS-RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:COG4717 180 EELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
595-878 |
3.62e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 595 NIEELIEKlqsgmvvKDQICDvRISDIMDVYEMKLSTLASKESRLQ-------DLLETKALALAQADRLIAQHRCQRTQA 667
Cdd:pfam05483 283 NLKELIEK-------KDHLTK-ELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEF 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 668 ETEARTLASMLR------------------EVERKN---EELSVLLKAQQVESERAQS---DIEHLFQHNRKLESVAEEH 723
Cdd:pfam05483 355 EATTCSLEELLRteqqrleknedqlkiitmELQKKSselEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 724 EILTKSYMELLQRNEStEKKNKDLQITCDSLNKQ--IETVKKLNESLKEQNEKSI-------AQLIEKEEQRKEVQNQLV 794
Cdd:pfam05483 435 KGKEQELIFLLQAREK-EIHDLEIQLTAIKTSEEhyLKEVEDLKTELEKEKLKNIeltahcdKLLLENKELTQEASDMTL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 795 DREHKLANLHQKTKVQE---EKIKTLQKEREDKEETIDILRKELsrtEQIRKELSIKASSLEVQKAQLEGRLEEKESLVK 871
Cdd:pfam05483 514 ELKKHQEDIINCKKQEErmlKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
....*..
gi 578807635 872 LQQEELN 878
Cdd:pfam05483 591 ILENKCN 597
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
685-868 |
5.88e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 685 NEELSVLLKAQQVESEraqsdiehLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKkl 764
Cdd:COG1579 3 PEDLRALLDLQELDSE--------LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 765 neslkeqneksiaQLIEKEEQR-KEVQN--QLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELsrtEQI 841
Cdd:COG1579 73 -------------ARIKKYEEQlGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AEL 136
|
170 180
....*....|....*....|....*..
gi 578807635 842 RKELSIKASSLEVQKAQLEGRLEEKES 868
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEELEA 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
642-880 |
6.50e-06 |
|
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: 50.34 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 642 LLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL--------LKAQQVESERAQSDIEHLFQHN 713
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLadetladrLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 RKLESVA----------EEHEILTKSYMELLQRNestekknKDLQITCDSLNKQIETV---------------KKLNESL 768
Cdd:COG3096 917 KALAQLEplvavlqsdpEQFEQLQADYLQAKEQQ-------RRLKQQIFALSEVVQRRphfsyedavgllgenSDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 769 KEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDI------------LRKELS 836
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeaeerarirrdeLHEELS 1069
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578807635 837 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
663-821 |
9.86e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 663 QRTQAETEARTLASMLREVERKNEELsvlLKAQQVESERAQsdiehlfqhNRKLESVAEEHEILTKSYMELLQRNESTEK 742
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAA---LLEAKELLLRER---------NQQRQEARREREELQREEERLVQKEEQLDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 743 KNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKT---KVQEEKIKTLQK 819
Cdd:PRK12705 96 RAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAqrvKKIEEEADLEAE 175
|
..
gi 578807635 820 ER 821
Cdd:PRK12705 176 RK 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
630-828 |
1.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 630 STLASKESRLQDLLETKALALAQADRLIAQHrcQRTQAETEA---------RTLASMLREVERKNEELSVLLKAQQvESE 700
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEY--NELQAELEAlqaeidklqAEIAEAEAEIEERREELGERARALY-RSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 701 RAQSDIEHLFQhnrklesvaeeheilTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 780
Cdd:COG3883 100 GSVSYLDVLLG---------------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578807635 781 EKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETI 828
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
646-862 |
1.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 646 KALAL---AQA-------DRLIAQHRCQRTQAETEAR-------TLASMLREVERKNEELSVL--LKAQQVESERAQSDI 706
Cdd:COG4913 192 KALRLlhkTQSfkpigdlDDFVREYMLEEPDTFEAADalvehfdDLERAHEALEDAREQIELLepIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 707 EHL---------FQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETV--KKLnESLKEQneks 775
Cdd:COG4913 272 AELeylraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRL-EQLERE---- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 776 IAQLiekEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKE----REDKEETIDILRKELSRTEQIRKELSIKASS 851
Cdd:COG4913 347 IERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
250
....*....|.
gi 578807635 852 LEVQKAQLEGR 862
Cdd:COG4913 424 LEAEIASLERR 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
637-845 |
1.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 637 SRLQDLLETkalALAQADRL--IAQHRCQRTQAETEA---RTLASMLR--EVERKNEELSVLLKAQQVESERAQSDIEhl 709
Cdd:COG4913 238 ERAHEALED---AREQIELLepIRELAERYAAARERLaelEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELE-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 710 fQHNRKLESVAEEHEILTKSYMEL-LQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKE 788
Cdd:COG4913 313 -RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578807635 789 VQNQLVDREHKLANLHQKTKVQEEKiktLQKEREDKEETIDILRKELS----RTEQIRKEL 845
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSnipaRLLALRDAL 449
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
754-876 |
2.05e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 754 LNKQIETVKKLNESLKE-QNEKSIAQLIEKEE---QRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETID 829
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEaEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578807635 830 ILRKELSRTEQirkELSIKASSLEVQKAQLEGRLEEkesLVKLQQEE 876
Cdd:PRK12704 114 KKEKELEQKQQ---ELEKKEEELEELIEEQLQELER---ISGLTAEE 154
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
596-875 |
2.76e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSgmvVKDQIcdVRISDIMDVYEMKLSTLASKESRLQDLL------ETKALALAQADRLIAQhRCQRTQAET 669
Cdd:TIGR00606 746 IPELRNKLQK---VNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQ-QAAKLQGSD 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 670 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQI 749
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 750 TCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT-LQKEREDKEETI 828
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETEL 979
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578807635 829 DILRKELS----RTEQIRKELSIKASSLEVQKAQlEGRLEEKESLVKLQQE 875
Cdd:TIGR00606 980 NTVNAQLEecekHQEKINEDMRLMRQDIDTQKIQ-ERWLQDNLTLRKRENE 1029
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
600-875 |
2.85e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 600 IEKLQSGMVVKDQICDV---RISDIMDVYEMKLSTLASKESRLQDL----------LETKALALAQADRLIAQHRCQRtq 666
Cdd:pfam10174 382 IRDLKDMLDVKERKINVlqkKIENLQEQLRDKDKQLAGLKERVKSLqtdssntdtaLTTLEEALSEKERIIERLKEQR-- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 667 aETEARTLASMLREVERKNEELSVLLKAQQVE-SERAQSDIE------HLFQHNRKLESVAEEHEILTKSYMELLQRNES 739
Cdd:pfam10174 460 -EREDRERLEELESLKKENKDLKEKVSALQPElTEKESSLIDlkehasSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 740 TEKKNKDLQI---TCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ------ 810
Cdd:pfam10174 539 QLKKAHNAEEavrTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQmkeqnk 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 811 -EEKIKTLQKE--REDKEETIDILRKELSRT--------EQIRKELSIKASSLEVQKAQL---EGRLEEKES-LVKLQQE 875
Cdd:pfam10174 619 kVANIKHGQQEmkKKGAQLLEEARRREDNLAdnsqqlqlEELMGALEKTRQELDATKARLsstQQSLAEKDGhLTNLRAE 698
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
769-879 |
3.18e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 44.14 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 769 KEQNEKsiaQLIEKEEQRKEVQNQLVDREHKLANlhqktkvQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIK 848
Cdd:pfam20492 1 REEAER---EKQELEERLKQYEEETKKAQEELEE-------SEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100 110
....*....|....*....|....*....|.
gi 578807635 849 ASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVER 101
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
586-866 |
3.26e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 586 HLKDGVPGL-NIEELIEKLQSGMVVKDQICDVRISDIMDvyemkLSTLASKESRLQDLLETKAlalAQADRLIAQHRCQR 664
Cdd:pfam15921 535 HLKNEGDHLrNVQTECEALKLQMAEKDKVIEILRQQIEN-----MTQLVGQHGRTAGAMQVEK---AQLEKEINDRRLEL 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 665 TQAETEARTLASMLREVERKNEELS---VLLKAQQVESERAQSDIEH--------LFQHNRKLESVAEEHEILTKSYmel 733
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKDIKQerdqllneVKTSRNELNSLSEDYEVLKRNF--- 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 734 lqRNESTEkknkdLQITCDSLNKQIETVkklnESLKEQNEKSIAQLIEKEEQRKEV----QNQLVDREHKLANLHQKTKV 809
Cdd:pfam15921 684 --RNKSEE-----METTTNKLKMQLKSA----QSELEQTRNTLKSMEGSDGHAMKVamgmQKQITAKRGQIDALQSKIQF 752
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 578807635 810 QEEKIKTLQKEREDKEETIDILRKELSrteQIRKELSIKASSLEVQKAQlEGRLEEK 866
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELS---TVATEKNKMAGELEVLRSQ-ERRLKEK 805
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
625-877 |
3.68e-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: 47.86 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 625 YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELsvllkaqQVESERAQS 704
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL-------QNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEHLfqhnrklesvaEEHeiltksymelLQRNESTEKKNKDLQITCDSlnkqieTVKKLNES---LKEQNEKSIAQLIE 781
Cdd:pfam01576 104 HIQDL-----------EEQ----------LDEEEAARQKLQLEKVTTEA------KIKKLEEDillLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 782 KEEQRKEVQNQLVDREHKLANLhQKTKVQEEKIKTLQKEREDKEETidiLRKELsrtEQIRKELSIKASSLEVQKAQLEG 861
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSL-SKLKNKHEAMISDLEERLKKEEK---GRQEL---EKAKRKLEGESTDLQEQIAELQA 229
|
250
....*....|....*.
gi 578807635 862 RLEEKESLVKLQQEEL 877
Cdd:pfam01576 230 QIAELRAQLAKKEEEL 245
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
662-879 |
4.12e-05 |
|
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: 47.20 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 662 CQRTQAE-TEARTLASMLREVERKN-----EELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEE----HEILTKSYM 731
Cdd:pfam07888 39 CLQERAElLQAQEAANRQREKEKERykrdrEQWERQRRELESRVAELKEELRQSREKHEELEEKYKElsasSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 732 ELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKV-- 809
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElr 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807635 810 --QEEKIKTLQKEREDKEETIDIL----RKELsRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQ---QEELNK 879
Cdd:pfam07888 199 nsLAQRDTQVLQLQDTITTLTQKLttahRKEA-ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRdrtQAELHQ 276
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
654-870 |
4.24e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 654 DRLIAQHRCQRTQAETEARTLASMLREVERKNEELSvlLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSyMEL 733
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELE--EKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKE-LRQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 734 LQRNESTEKKNKDLqitcdslnkqIETVKKLNESLKEQNEKsiaqLIEKEEQRKEVQnqlVDREHKLANLHQKTKVQEek 813
Cdd:PRK00409 596 LQKGGYASVKAHEL----------IEARKRLNKANEKKEKK----KKKQKEKQEELK---VGDEVKYLSLGQKGEVLS-- 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807635 814 iktlQKEREDKEETIDILR-----KELSRTEQIRKEL--SIKASSLEVQKAQLE----G-RLEEKESLV 870
Cdd:PRK00409 657 ----IPDDKEAIVQAGIMKmkvplSDLEKIQKPKKKKkkKPKTVKPKPRTVSLEldlrGmRYEEALERL 721
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
700-843 |
4.48e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 700 ERAQSDIEHLfQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLkEQNEKSIAQL 779
Cdd:PRK12704 45 EEAKKEAEAI-KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL-EKKEKELEQK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 780 IEKEEQRKEvqnqlvdrehKLANLHQKTKVQEEKIKTLQKErEDKEETIDILRKELSR--TEQIRK 843
Cdd:PRK12704 123 QQELEKKEE----------ELEELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHeaAVLIKE 177
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
714-892 |
5.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 RKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQitcDSLNKQIETVKKLNESLKEQNEKsIAQLIEKEEQRKEVQNQL 793
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 794 VDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRK------ELSIKASSLEVQKAQLEGRLEEKE 867
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEkaeeyiKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180
....*....|....*....|....*
gi 578807635 868 SLVKLQQEELNKHSHMIAMIHSLSG 892
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKK 345
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
596-879 |
6.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSGMVVKDQicDVRISDIMDVYEMKLSTLA------------------SKESRLQDLLETKALALAQADRLI 657
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEK--DIIDEDIDGNHEGKAEAKAhvgqdeglkpsykdfdfdAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 658 AQHRCQRTQAETEARTLASMLREVE--RKNEELSVLLKAQQVESERAqsdiehlFQHNRKLESvAEEHEILTKSymellQ 735
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEeaRKAEDARKAEEARKAEDAKR-------VEIARKAED-ARKAEEARKA-----E 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 736 RNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLAnlHQKTKVQEEKIK 815
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA--EEAKKAEEERNN 1251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 816 TLQKEREDKEETIDILRKELSRTEQIRKELSIKASSlEVQKAQLEGRLEEKESL--VKLQQEELNK 879
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADEAKKAEEKKKAdeAKKKAEEAKK 1316
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
699-887 |
1.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 699 SERAQSDIEHLFQHNRKLESVAEEHEILTKsymELLQRNESTEKKNKDLQitcdSLNKQIETVKKLNESLKEQNEKSIAQ 778
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQARE---ELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 779 LIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQ 858
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180
....*....|....*....|....*....
gi 578807635 859 LEGRLEEKESLVKLQQEELNKHSHMIAMI 887
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIES 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
686-894 |
1.50e-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: 45.48 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 686 EELSVLLKAQQVESERAQSDIE-HLFQHNRKLESVAEEH--EILTKSYMELLQRNESTEKKNKDLQITC------DSLNK 756
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYkkEINDKEKQVSLLLIQITEKENKMKDLTFlleesrDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 757 QIETVKKLNESLKEQNEKsiaqlieKEEQRKEVQNQLVDREHKLANlhQKTKVQEEKI--KTLQKEREDKEETIDILRKE 834
Cdd:pfam05483 273 LEEKTKLQDENLKELIEK-------KDHLTKELEDIKMSLQRSMST--QKALEEDLQIatKTICQLTEEKEAQMEELNKA 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 835 LSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHSLSGGK 894
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
643-880 |
1.50e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 643 LETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL--------LKAQQVESERAQSDIEHLFQHNR 714
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLadetladrVEEIREQLDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 715 ---KLESVA-------EEHEILTKSYMELLQRNESTEKKNKDL------------QITCDSLNKQIEtvkkLNESLKEQN 772
Cdd:PRK04863 919 alaQLEPIVsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALtevvqrrahfsyEDAAEMLAKNSD----LNEKLRQRL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 773 EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKE----------------REDKEEtidiLRKELS 836
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsgaeeraRARRDE----LHARLS 1070
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 578807635 837 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
632-890 |
1.92e-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: 45.10 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 632 LASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELS-----VLLKAQQVESERAQSDI 706
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcdkLLLENKELTQEASDMTL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 707 EhLFQHNRKLESVAEEHEILTKSyMELLQRNESTEKKnkDLQITCDSLNKQIETVK-KLNESlkEQNEKSIA-QLIEKEE 784
Cdd:pfam05483 514 E-LKKHQEDIINCKKQEERMLKQ-IENLEEKEMNLRD--ELESVREEFIQKGDEVKcKLDKS--EENARSIEyEVLKKEK 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 785 QRKEVQN-------QLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQ--------IRKELSIKA 849
Cdd:pfam05483 588 QMKILENkcnnlkkQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeeiidnYQKEIEDKK 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578807635 850 SSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHSL 890
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL 708
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
781-866 |
2.18e-04 |
|
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Pssm-ID: 461615 [Multi-domain] Cd Length: 173 Bit Score: 42.76 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 781 EKEEQRKEVQNQLVDREHKlanlhQKTKVQEEKIKTLQKEREDKEETID--ILRKELS------RTEQIRKELSIKASSL 852
Cdd:pfam05300 59 DEEELRKKIKEELYKRLEQ-----EQAKVQEELARLAEREREAAQESLTraILRERAStederlKAQQLAKQLEEKEAEL 133
|
90
....*....|....*...
gi 578807635 853 EVQ----KAQLeGRLEEK 866
Cdd:pfam05300 134 KKQdafyKEQL-ARLEEK 150
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
766-880 |
2.33e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 44.21 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 766 ESLKEQNEKSIAqliEKEEQRKEVQNQLVDREHKlanlhQKTKVQEEKIKtLQKEREDKEETIDILRK---ELSRTEQIR 842
Cdd:pfam07767 208 EKKRLKEEEKLE---RVLEKIAESAATAEAREEK-----RKTKAQRNKEK-RRKEEEREAKEEKALKKklaQLERLKEIA 278
|
90 100 110
....*....|....*....|....*....|....*....
gi 578807635 843 KELSIKASSLEVQKAQLE-GRLEEKESLVKLQQEELNKH 880
Cdd:pfam07767 279 KEIAEKEKEREEKAEARKrEKRKKKKEEKKLRPRKLGKH 317
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
596-849 |
2.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSgmvvkdqiCDVRISDimdvYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAE-----TE 670
Cdd:TIGR02169 739 LEELEEDLSS--------LEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 671 ARTLASMLREVERKNEELSvlLKAQQVESERA----------------QSDIEHLFQHNRKLESVAEEHEI----LTKSY 730
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLT--LEKEYLEKEIQelqeqridlkeqiksiEKEIENLNGKKEELEEELEELEAalrdLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 731 MELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQL----------------------IEKEEQRKE 788
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiedpkgedeeipeeelsledVQAELQRVE 964
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578807635 789 VQ-------NQLVDREHKLANLHQKTkvQEEKIKTLQKEREDKEETIDilrkelsRTEQIRKELSIKA 849
Cdd:TIGR02169 965 EEiralepvNMLAIQEYEEVLKRLDE--LKEKRAKLEEERKAILERIE-------EYEKKKREVFMEA 1023
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
587-879 |
2.70e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 587 LKDGVPGLNIEELIEKLQSGMVVKDQIcdvrisdimdvyEMKLSTLASKESRLQDLLETKALALAQADRliAQHRC---- 662
Cdd:PRK03918 377 LKKRLTGLTPEKLEKELEELEKAKEEI------------EEEISKITARIGELKKEIKELKKAIEELKK--AKGKCpvcg 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 663 QRTQAETEARTLASMLREVERKNEELSVL------LKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQR 736
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELKEIeekerkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 737 NESTEKKNKDLQITcdsLNKQIETVKKLNESLKEQNEKsiaqLIEKEEQRKEVQNQLVDREHKLANLHQKT-KVQEEKIK 815
Cdd:PRK03918 523 KAEEYEKLKEKLIK---LKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESvEELEERLK 595
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 816 TLQKEREDKEETIDIlRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESlvklQQEELNK 879
Cdd:PRK03918 596 ELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK----ELEELEK 654
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
661-886 |
3.51e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 661 RCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNEST 740
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 741 EKKnkdlqitcdslnKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEvQNQLVDREhKLANLHQKTKVQEEKIKTLQKE 820
Cdd:pfam13868 113 EDQ------------AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE-EEREEDER-ILEYLKEKAEREEEREAEREEI 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 821 REDKEETIDILRKELSRTEQIRKEL----------SIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAM 886
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQDEKAERdelraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
635-882 |
3.65e-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: 44.35 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 635 KESRLQDLLETKalaLAQADRLiaqhRCQRTQAETEARTLASMLREVERKNEELSVL-------------LKAQQVESER 701
Cdd:pfam05557 95 KESQLADAREVI---SCLKNEL----SELRRQIQRAELELQSTNSELEELQERLDLLkakaseaeqlrqnLEKQQSSLAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 702 AQSDIEHLFQHNRKLESVAEEheilTKSYMELLQRNESTEKKNKDLQitcdSLNKQIETVKKLNESLKEQNEKSIAQLIE 781
Cdd:pfam05557 168 AEQRIKELEFEIQSQEQDSEI----VKNSKSELARIPELEKELERLR----EHNKHLNENIENKLLLKEEVEDLKRKLER 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 782 KEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRkelSIKASSLEVQKAQLEG 861
Cdd:pfam05557 240 EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENS---SLTSSARQLEKARREL 316
|
250 260
....*....|....*....|.
gi 578807635 862 RLEEKESLVKLQQEELNKHSH 882
Cdd:pfam05557 317 EQELAQYLKKIEDLNKKLKRH 337
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
778-863 |
3.67e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 778 QLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQirkelsikasSLEVQKA 857
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----------EIEERRE 86
|
....*.
gi 578807635 858 QLEGRL 863
Cdd:COG3883 87 ELGERA 92
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-845 |
3.80e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 645 TKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHE 724
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 725 ILTKSYMELLQR----NESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKL 800
Cdd:COG1196 655 GGSAGGSLTGGSrrelLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578807635 801 ANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKEL 845
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
674-875 |
4.57e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 674 LASMLREVERKN----EELSVLLKAQQVESER-AQSDIEHLFQHNRKlesvAEEHEILTksymELLQRNESTEKKNKDLQ 748
Cdd:pfam01576 24 AESELKELEKKHqqlcEEKNALQEQLQAETELcAEAEEMRARLAARK----QELEEILH----ELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 749 ITcdslnkqietVKKLNESLKEQNEksiaQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETI 828
Cdd:pfam01576 96 NE----------KKKMQQHIQDLEE----QLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578807635 829 DILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKEslvKLQQE 875
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE---KGRQE 205
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
661-881 |
4.74e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 661 RCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESeRAQSDIEHLFQHNRKLESVAEEHEILTKSYME-----LLQ 735
Cdd:pfam10174 45 RALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDEL-RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEenfrrLQS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 736 RNESTEKKNKDLQITCDSLNKQIET-----------VKKLNESL--KEQNEKSI-------AQLIEKEEQRKEVQNQLVD 795
Cdd:pfam10174 124 EHERQAKELFLLRKTLEEMELRIETqkqtlgardesIKKLLEMLqsKGLPKKSGeedwertRRIAEAEMQLGHLEVLLDQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 796 RE----HKLANLHQKTKVQEE--KIKTLQKEREDKEETIDILrkelsrteqirkELSIKASSLEVQKAQLEGRL--EEKE 867
Cdd:pfam10174 204 KEkeniHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSL------------ERNIRDLEDEVQMLKTNGLLhtEDRE 271
|
250
....*....|....
gi 578807635 868 SLVKlQQEELNKHS 881
Cdd:pfam10174 272 EEIK-QMEVYKSHS 284
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
670-877 |
5.05e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 670 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIE----HLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNK 745
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 746 DLQITCDSLNKQIETVKKLNESLKE---QNEKSIAQLIEKEEQRKEVQNQLVD-----REHKL------ANLHQKTKVQE 811
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSmaaQRDRTQAELHQARLQAAQLTLQLADaslalREGRArwaqerETLQQSAEADK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578807635 812 EKIKTLQKEREDKEETidiLRKELSRTEQIRKELSIKASSLEVQ-----------KAQLEGRLEEKESLVKLQQEEL 877
Cdd:pfam07888 318 DRIEKLSAELQRLEER---LQEERMEREKLEVELGREKDCNRVQlsesrrelqelKASLRVAQKEKEQLQAEKQELL 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
596-841 |
5.52e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSGMVVKDQICDV--RISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEART 673
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLeeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 674 LASMLREVERKNEELSVL--LKAQQVESERAQSDIEHLfqhNRKLESVAEeheiltksyMELLQRNESTEKKNKDLQITC 751
Cdd:PRK02224 574 VAELNSKLAELKERIESLerIRTLLAAIADAEDEIERL---REKREALAE---------LNDERRERLAEKRERKRELEA 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 752 DSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLhqktkvqeekiKTLQKEREDKEETIDIL 831
Cdd:PRK02224 642 EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL-----------EELRERREALENRVEAL 710
|
250
....*....|
gi 578807635 832 RKELSRTEQI 841
Cdd:PRK02224 711 EALYDEAEEL 720
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
667-894 |
5.88e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 667 AETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKD 746
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKV 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 747 LQitcdslnKQIETVKKLNESLKEqNEKSIAQLIEK----------EEQRKEVQ---------------NQLVDREHKLA 801
Cdd:TIGR00606 787 CL-------TDVTIMERFQMELKD-VERKIAQQAAKlqgsdldrtvQQVNQEKQekqheldtvvskielNRKLIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 802 NLHQKTKVQEEKIKTLQ-----KEREDKEETIDILRKEL----SRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKL 872
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQigtnlQRRQQFEEQLVELSTEVqsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
250 260 270
....*....|....*....|....*....|
gi 578807635 873 QQEEL--------NKHSHMIAMIHSLSGGK 894
Cdd:TIGR00606 939 AQDKVndikekvkNIHGYMKDIENKIQDGK 968
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
638-875 |
6.14e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 638 RLQDLLET-KALALAQADRLIAQHRCQRTQAETEARTLASM--LREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN- 713
Cdd:pfam15921 430 RLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKe 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 714 RKLESVAEEHEILtKSYMEL----LQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiaqliekeeqrkev 789
Cdd:pfam15921 510 RAIEATNAEITKL-RSRVDLklqeLQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN--------------- 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 790 QNQLVDREHKLANLHQKTKVQeekiktLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESL 869
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQ------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA 647
|
....*..
gi 578807635 870 VK-LQQE 875
Cdd:pfam15921 648 VKdIKQE 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
752-880 |
6.23e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 752 DSLNKQIETVKK---LNESLKE-QNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEET 827
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578807635 828 IDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKEslvkLQQEELNKH 880
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEE 331
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-845 |
7.16e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 679 REVERKNEELSvLLKAQQVESERAQSD----IEHLFQHNRKLESVAEEHEILTKSYMELLQRNEsTEKKNKDLQITCDSL 754
Cdd:TIGR04523 489 KELKSKEKELK-KLNEEKKELEEKVKDltkkISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 755 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 834
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
170
....*....|.
gi 578807635 835 LsrtEQIRKEL 845
Cdd:TIGR04523 647 V---KQIKETI 654
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
626-880 |
7.21e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 626 EMKLSTLASKESRLQDLlETKALALAQADRLIAQHRCQ-RTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQS 704
Cdd:TIGR00618 392 TQKLQSLCKELDILQRE-QATIDTRTSAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEHLFQHNRKLESVAEEHEILTKsYMELLQRNE-----STEKKNKDLQ------ITCDSLNKQIETVKKLNESLkeqnE 773
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPcplcgSCIHPNPARQdidnpgPLTRRMQRGEQTYAQLETSE----E 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 774 KSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDilrKELSRTEQIRKELSIKASSLE 853
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---KLSEAEDMLACEQHALLRKLQ 622
|
250 260
....*....|....*....|....*..
gi 578807635 854 VQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
735-876 |
7.53e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 735 QRNESTEKKNKDLQITCDSLNKQIETVK-KLNE-------------SLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKL 800
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQqEINEktteisntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 801 ANLHQKTKV-----QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG-------RLEEKES 868
Cdd:TIGR04523 291 NQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESensekqrELEEKQN 370
|
....*...
gi 578807635 869 LVKLQQEE 876
Cdd:TIGR04523 371 EIEKLKKE 378
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
746-879 |
9.62e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 746 DLQITCD--SLNKQIETVKKLNESLKEQNEKSIAQ-LIEKEEQRKEVQNQLVDR--EHKLANLHQKTKVQEE--KIKTLQ 818
Cdd:pfam15709 288 ESQVSIDgrSSPTQTFVVTGNMESEEERSEEDPSKaLLEKREQEKASRDRLRAEraEMRRLEVERKRREQEEqrRLQQEQ 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807635 819 KEREDK-EETIDI----------LRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKL-------QQEELNK 879
Cdd:pfam15709 368 LERAEKmREELELeqqrrfeeirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLqelqrkkQQEEAER 446
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
639-879 |
1.08e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 639 LQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVE--------RKNEELSVLLKAQQV--ESERAQSDIEh 708
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEeelerteeRLAEALEKLEEAEKAadESERGRKVLE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 709 lfqhNRKLESvAEEHEILTKSYMELLQRNESTEKKnkdlqitCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKE 788
Cdd:pfam00261 85 ----NRALKD-EEKMEILEAQLKEAKEIAEEADRK-------YEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 789 VQNQLvdrehklanlhQKTKVQEEKikTLQKErEDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKES 868
Cdd:pfam00261 153 VGNNL-----------KSLEASEEK--ASERE-DKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|.
gi 578807635 869 LVKLQQEELNK 879
Cdd:pfam00261 219 KYKAISEELDQ 229
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
657-876 |
1.13e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 657 IAQHRCQRTQAETEARTLASMLREVERKNEELSvllkAQQVESERAQSDIEHLF--QHNRKLeSVAEEHEILTKS--YME 732
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRKELAELN----KAGGSIDKLRKEIERLEwrQQTEVL-SPEEEKELVEKIkeLEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 733 LLQRNESTEKKNKDLQitcdslnkqiETVKKLNEsLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEE 812
Cdd:COG1340 148 ELEKAKKALEKNEKLK----------ELRAELKE-LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 813 KIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEE 876
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGE 280
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
757-881 |
1.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 757 QIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELS 836
Cdd:PRK12705 43 QKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578807635 837 -RTEQIRKELSIKAS-SLEVQKAQLEGRL-----EEKESLVKLQQEELNKHS 881
Cdd:PRK12705 123 eLEKQLDNELYRVAGlTPEQARKLLLKLLdaeleEEKAQRVKKIEEEADLEA 174
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
738-826 |
1.32e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 39.49 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 738 ESTEKKNKDLQITCDSLNkQIE-----TVKKLNESLKEQN--EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ 810
Cdd:pfam18595 12 AELERKARELQAKIDALQ-VVEkdlrsCIKLLEEIEAELAklEEAKKKLKELRDALEEKEIELRELERREERLQRQLENA 90
|
90
....*....|....*.
gi 578807635 811 EEKIKTLQKEREDKEE 826
Cdd:pfam18595 91 QEKLERLREQAEEKRE 106
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
684-845 |
1.37e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 42.30 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 684 KNEELSVLLKAQQVESERAQsdIEHL-FQHNRKLESVaEEHEILTKSYMELLQRNESTEKKNKdlqITCDSlnkqietvk 762
Cdd:pfam03999 132 LPLLIDPLPSLEELESFRKH--LENLrNEKERRLEEV-NELKKQIKLLMEELDLVPGTDFEED---LLCES--------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 763 KLNESLKEQNEKSIAQLIEK-EEQRKEVQNQLVDREHKLANLHQKTKV-QEEKIKTLQKEREDKEETIDILRKELSRTEQ 840
Cdd:pfam03999 197 EDNFCLSRENIDKLRKLIKQlEEQKAEREEKIDDLREKILELWNRLQVpQEEQESFVRENNSLSQDTIDALREELQRLEE 276
|
....*
gi 578807635 841 IRKEL 845
Cdd:pfam03999 277 LKKKN 281
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
681-879 |
1.44e-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: 42.31 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 681 VERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKsyMELLQRNESTekKNKDLQITCDSLNKQIET 760
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNK--IKILEQQIKD--LNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 761 VKKLNESLK---EQNEKSIAQLIEKEEQRKEV--------------QNQLVDREHKLANLHQKTKVQEEKIKTLQKERED 823
Cdd:TIGR04523 105 LSKINSEIKndkEQKNKLEVELNKLEKQKKENkknidkflteikkkEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 824 KEETIDILRKELSRTEQI----------RKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLlsnlkkkiqkNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
743-859 |
1.45e-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: 40.67 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 743 KNKDLQITCDSLNKQIETVKKLNESLK----EQNEKSIAQLIEKEEQRKEVQNQLVDRE----HKLANLHQKTKVQEEKI 814
Cdd:pfam13870 14 ELITLKHTLAKIQEKLEQKEELGEGLTmidfLQLQIENQALNEKIEERNKELKRLKLKVtntvHALTHLKEKLHFLSAEL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578807635 815 KTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 859
Cdd:pfam13870 94 SRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGLL 138
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
628-879 |
1.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 628 KLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLAsmlREVERKNEELSVL---LKAQQVESERAQS 704
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAqeeLESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 705 DIEHLFQHNRKLEsvaEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEE 784
Cdd:COG4372 116 ELEELQKERQDLE---QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 785 QRKEVQNQLVDREHKLAN---LHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG 861
Cdd:COG4372 193 NRNAEKEEELAEAEKLIEslpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*...
gi 578807635 862 RLEEKESLVKLQQEELNK 879
Cdd:COG4372 273 TEEEELEIAALELEALEE 290
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
773-876 |
1.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 773 EKSIAQLIEKEEQRKEVQNQLVDREHKLANL-HQKTKVQEEKIKTLQKEREDKEETIDILRKELS------RTEQIRKEL 845
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELeEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|.
gi 578807635 846 SIKASSLEVQKAQLEGRLEEKESLVKLQQEE 876
Cdd:PRK00409 603 SVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
638-902 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 638 RLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLA---SMLREVERKNEELSVLLK--AQQVESERAQSDIEHLFQH 712
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqklSVADAARRQFEKAYELVCkiAGEVERSQAWQTARELLRR 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 713 NRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQneksiaqliekEEQRKEVQNQ 792
Cdd:COG3096 504 YRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL-----------EAQLEELEEQ 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 793 LVDREHKLANLHQktkvQEEKIKTLQKEREDKEEtidILRKELSRTEQIRKELSIK-ASSLEVQKA-----QLEGRLEEK 866
Cdd:COG3096 573 AAEAVEQRSELRQ----QLEQLRARIKELAARAP---AWLAAQDALERLREQSGEAlADSQEVTAAmqqllEREREATVE 645
|
250 260 270
....*....|....*....|....*....|....*...
gi 578807635 867 ESLVKLQQEELNKHshmiamIHSLS--GGKINPETVNL 902
Cdd:COG3096 646 RDELAARKQALESQ------IERLSqpGGAEDPRLLAL 677
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
768-876 |
1.75e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 768 LKEQNEKSIAQlIEKEEQRKEVQNqlvDREHKLANLHQKTKVQEEKI----KTLQKEREDKEETID---ILRKELSRTEQ 840
Cdd:COG2268 197 IIRDARIAEAE-AERETEIAIAQA---NREAEEAELEQEREIETARIaeaeAELAKKKAEERREAEtarAEAEAAYEIAE 272
|
90 100 110
....*....|....*....|....*....|....*.
gi 578807635 841 IRKELSIKAsSLEVQKAQLEGRLEEKESLVKLQQEE 876
Cdd:COG2268 273 ANAEREVQR-QLEIAEREREIELQEKEAEREEAELE 307
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
776-899 |
1.75e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 776 IAQLIEKEEQRKEvqnQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEEtIDILRKELSRTEQirKELSIKASSLEVQ 855
Cdd:TIGR02169 165 VAEFDRKKEKALE---ELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEG--YELLKEKEALERQ 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578807635 856 KAQLEGRLEEKE-SLVKLQQE--ELNKHSHMIAMIHSLSGGKINPET 899
Cdd:TIGR02169 239 KEAIERQLASLEeELEKLTEEisELEKRLEEIEQLLEELNKKIKDLG 285
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
670-887 |
1.83e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 670 EARTLASMLREVERKNEELSV----LLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMEllQRNESTEKKNK 745
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLD--SKRTSWLNALA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 746 DLQ-ITCDSLNKQIETV-KKLNESLKEQNEKsiaqLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKiktlQKERED 823
Cdd:PRK01156 576 VISlIDIETNRSRSNEIkKQLNDLESRLQEI----EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN----KILIEK 647
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 824 KEETIDILRKELSRTEQI---RKELSIKASSLEVQKAQLEGRLE-------EKESLVKLQQEELNKHSHMIAMI 887
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIipdLKEITSRINDIEDNLKKSRKALDdakanraRLESTIEILRTRINELSDRINDI 721
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
647-875 |
2.15e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 647 ALALAQADRLIAQHRcQRTQAETE-ARTLASMLREVERKNEELsvLLKAQQVESERAQSDIEHLfqhnrkLESVAEEHEI 725
Cdd:NF041483 181 AAARAEAERLAEEAR-QRLGSEAEsARAEAEAILRRARKDAER--LLNAASTQAQEATDHAEQL------RSSTAAESDQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 726 LTKSYMELL----QRNESTEKKNKDLQITCDSL--------NKQIETVKKLNESLKEQNEKSIAQLI-----EKEEQRKE 788
Cdd:NF041483 252 ARRQAAELSraaeQRMQEAEEALREARAEAEKVvaeakeaaAKQLASAESANEQRTRTAKEEIARLVgeatkEAEALKAE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 789 VQNQLVDR----EHKLANLHQK--TKVQEEKIKTLQKEREDKEETIDILRKELSRT--------EQIRKELSIKASSLEV 854
Cdd:NF041483 332 AEQALADAraeaEKLVAEAAEKarTVAAEDTAAQLAKAARTAEEVLTKASEDAKATtraaaeeaERIRREAEAEADRLRG 411
|
250 260 270
....*....|....*....|....*....|
gi 578807635 855 QKA----QLEGRL-----EEKESLVKLQQE 875
Cdd:NF041483 412 EAAdqaeQLKGAAkddtkEYRAKTVELQEE 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
628-845 |
2.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 628 KLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELsvllkaqqvESERAQSDIE 707
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---------EELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 708 HLFQHNRKL--ESVAEEHEILTKSYmELLQRNESTEKKNKDLQITCDSLNKQIETVKKLN--ESLKEQNEKSIAQLIEKE 783
Cdd:COG4717 367 ELEQEIAALlaEAGVEDEEELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 784 EQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRT--EQIRKEL 845
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEllEEAREEY 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
672-875 |
2.39e-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: 41.88 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 672 RTLASMLREVERKNEELSVLLKAQ-----QVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKd 746
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRsqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 747 LQITCDSLNKQIETVKKLNESLKEQNEK------------SIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTkvqeeki 814
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERinrarkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR------- 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578807635 815 KTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEvqkaQLEGRLEEKESLVKLQQE 875
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE----ISCQQHTLTQHIHTLQQQ 387
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
806-880 |
2.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578807635 806 KTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 880
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
681-884 |
2.86e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 41.26 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 681 VERKNEELSVLLKAQQVESEraqsdiEHLFQHNRKLESVAEEHEiltKSYMELLQRNESTEKKNKDLQ-------ITCDS 753
Cdd:COG5059 348 SSREIEEIKFDLSEDRSEIE------ILVFREQSQLSQSSLSGI---FAYMQSLKKETETLKSRIDLImksiisgTFERK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 754 LNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKER--EDKEETIDIL 831
Cdd:COG5059 419 KLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKasKLRSSASTKL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578807635 832 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMI 884
Cdd:COG5059 499 NLRSSRSHSKFRDHLNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSL 551
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
596-876 |
2.99e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 596 IEELIEKLQSGMVVKDQICDV-----RISDI-MDVYEMKlSTLASKESRLQDLLETkalalaqadrLIAQHRCQRTQAET 669
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDwertrRIAEAeMQLGHLE-VLLDQKEKENIHLREE----------LHRRNQLQPDPAKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 670 EA-RTLASM----LREVERKNEELSvllkaQQVESERAQSDIeHLFQHNRKLES--VAEEHEILTKSYMELLQRNES-TE 741
Cdd:pfam10174 229 KAlQTVIEMkdtkISSLERNIRDLE-----DEVQMLKTNGLL-HTEDREEEIKQmeVYKSHSKFMKNKIDQLKQELSkKE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 742 KKNKDLQITCDSLNKQIETVKK----LNESL--KEQnEKSIAQ---------LIEKEEQRKEVQNQLVDRE-------HK 799
Cdd:pfam10174 303 SELLALQTKLETLTNQNSDCKQhievLKESLtaKEQ-RAAILQtevdalrlrLEEKESFLNKKTKQLQDLTeekstlaGE 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578807635 800 LANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEE 876
Cdd:pfam10174 382 IRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ 458
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
752-868 |
3.19e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.77 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 752 DSLNKQIETVKKLNESLKEQNEKSIAQLiekEEQRKEVQNQLVDREHKLANlhqktkvQEEKIKTLQKEREDKEETIDIL 831
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDL---EKQAEIAREAQQNYERELVL-------HAEDIKALQALREELNELKAEI 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 578807635 832 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKES 868
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
773-878 |
3.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 773 EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQ------KTKVQEEKIKTLQKEREDKEET---IDILRKELSRTEQIRK 843
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASsddLAALEEQLEELEAELE 702
|
90 100 110
....*....|....*....|....*....|....*
gi 578807635 844 ELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELN 878
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
723-877 |
3.42e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 723 HEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEK------EEQRK--EVQNQLV 794
Cdd:pfam08614 2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQlreelaELYRSrgELAQRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 795 DREHKLANLHQKTKVQEEKIKTLQKERedkeetidilrkelsrteqirkelsikaSSLEVQKAQLEGRLEEKESLVKLQQ 874
Cdd:pfam08614 82 DLNEELQELEKKLREDERRLAALEAER----------------------------AQLEEKLKDREEELREKRKLNQDLQ 133
|
...
gi 578807635 875 EEL 877
Cdd:pfam08614 134 DEL 136
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
721-901 |
3.48e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 721 EEHEILTK--SYMELLQRNESTEKKN-KDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDRE 797
Cdd:pfam10174 356 EKESFLNKktKQLQDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 798 HKLANLHQKTKVQEEKIKTL--QKEREDKE----------------ETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 859
Cdd:pfam10174 436 TALTTLEEALSEKERIIERLkeQREREDRErleeleslkkenkdlkEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578807635 860 EGRLEEKESLVKLQQEELNKHSHMIAMIHSL-SGGKINPETVN 901
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAeEAVRTNPEIND 558
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
600-867 |
4.71e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 600 IEKLQSG-MVVKDQICDVR--ISDIMDVYE---MKLSTLASKESRLQDLLETKALALAQADRLIAQHRC---QRTQAETE 670
Cdd:PRK01156 161 INSLERNyDKLKDVIDMLRaeISNIDYLEEklkSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 671 ARTLASMLREVERKNEELSvllkaqqveseRAQSDIEHLFQHNRKLESVAEEHEILTKSYMeLLQRNE---------STE 741
Cdd:PRK01156 241 LNELSSLEDMKNRYESEIK-----------TAESDLSMELEKNNYYKELEERHMKIINDPV-YKNRNYindyfkyknDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 742 KKNKDLQITCDSLNKQIETVKKLNESLKEQNeksiaQLIEKEEQRKEVQNQLVDrehkLANLHQKTKVQEEKIKTLQKER 821
Cdd:PRK01156 309 NKKQILSNIDAEINKYHAIIKKLSVLQKDYN-----DYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIESLKKKI 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578807635 822 EDKEETIDILRKELSRT---------------EQIRKEL---SIKASSLEVQKAQLEGRLEEKE 867
Cdd:PRK01156 380 EEYSKNIERMSAFISEIlkiqeidpdaikkelNEINVKLqdiSSKVSSLNQRIRALRENLDELS 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-877 |
4.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 747 LQITCDSLNKQIETVKKLNESLKEQNE--KSIAQLIEKEEQRKEVQNQLVDREHKLANLhQKTKVQeekIKTLQKEREDK 824
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDD---LAALEEQLEEL 697
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578807635 825 EETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 877
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
616-879 |
5.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 616 VRISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLiaqhrcqrtqaETEARTLASMLREVERKNEEL------- 688
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELeerhely 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 689 ----SVLLKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKL 764
Cdd:PRK03918 365 eeakAKKEELERLKKRLTGLTPEKL---EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 765 NESLKEQNEKSI------------AQLIEKEEQRKEVQNQLVDREHKLANlhQKTKVQEEKIKTLQKEREDKEETIDIlr 832
Cdd:PRK03918 442 GRELTEEHRKELleeytaelkrieKELKEIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKELEEKLKKYNL-- 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578807635 833 KELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKlQQEELNK 879
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK-KLAELEK 563
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
673-830 |
5.41e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.03 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 673 TLASMLREVERKNEELSVLLKAQQveseRAQSDIEHLFQHNRkleSVAEEHEiltKSYMELLQRNESTEKKNKDLQITCD 752
Cdd:smart00435 232 TLQEQLKELTAKDGNVAEKILAYN----RANREVAILCNHQR---TVSKTHE---KSMEKLQEKIKALKYQLKRLKKMIL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 753 SLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQnqlvdrehklanlhqKTKVQ----EEKIKTLQKEREDKEETI 828
Cdd:smart00435 302 LFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEE---------------KKKKQierlEERIEKLEVQATDKEENK 366
|
..
gi 578807635 829 DI 830
Cdd:smart00435 367 TV 368
|
|
| COG5134 |
COG5134 |
Uncharacterized conserved protein [Function unknown]; |
738-859 |
6.29e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227463 Cd Length: 272 Bit Score: 39.68 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 738 ESTEKKNKDLQITCDSLNKQiETVKKLNESL-KEQNEKSIAQlIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT 816
Cdd:COG5134 103 ESGGRRKIEPQDINEDPAKA-ENVEKVPESDaIEALEKQLTQ-QKSEKHNSSAINFIDELNKRLWSDPFVSSQRLRKQFR 180
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578807635 817 LQKEREDKEETidilrKELSRTEQIRKELSIKASSLEVQKAQL 859
Cdd:COG5134 181 ERKKIEKKQEA-----KDLSLKNRAALDIDILPSSSDKDKALL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
799-885 |
7.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 799 KLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELN 878
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
....*..
gi 578807635 879 KHSHMIA 885
Cdd:COG4942 101 AQKEELA 107
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
716-832 |
7.20e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.58 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 716 LESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQ---IETVKKLNESLKEQNEKS----IAQLIEKEEQRKE 788
Cdd:pfam02841 178 LQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEqelLREKQKEEEQMMEAQERSyqehVKQLIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578807635 789 VQNQLVDREhklanLHQKTKVQEEKIKT-LQKEREDKEETIDILR 832
Cdd:pfam02841 258 QLLAEQERM-----LEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
748-879 |
7.32e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 38.13 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 748 QITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQ---RKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDK 824
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKerlKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578807635 825 EETIDILRKELSRTEQIRkelSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 879
Cdd:pfam11600 81 EKAEKLRLKEEKRKEKQE---ALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
810-885 |
8.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578807635 810 QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIA 885
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
612-796 |
9.25e-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: 38.75 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 612 QICDVRISDImdvyEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEartlasmLREVERKNEELSVL 691
Cdd:COG1579 13 QELDSELDRL----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-------IEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807635 692 LKaqQVESERAQSDIEHLFQHNRKLESVAEEHEIltksymELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQ 771
Cdd:COG1579 82 LG--NVRNNKEYEALQKEIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....*.
gi 578807635 772 NEKSIAQLIEK-EEQRKEVQNQLVDR 796
Cdd:COG1579 154 LEAELEELEAErEELAAKIPPELLAL 179
|
|
| |
