|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
618-880 |
1.68e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 618 RISDIMDVYEMKLSTLAsKESR-------LQDLLETK-----ALALAQADRLIAQHRCQRTQAETEARTLASMLREVERK 685
Cdd:COG1196 190 RLEDILGELERQLEPLE-RQAEkaeryreLKEELKELeaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 686 NEELSVLLKAQQVESERAQsdiEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKL 765
Cdd:COG1196 269 LEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 766 NESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKE 845
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 147647143 846 LSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
627-866 |
4.47e-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: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 627 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLR--------------EVERKNEELSVL 692
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskelteleaeieELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 693 LKAQQVESERAQSDI----EHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNES 768
Cdd:TIGR02168 777 LAEAEAEIEELEAQIeqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 769 LKEQNEKSIAQLIEKEEQRKEVQNQLvdrehklanlhqktKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSI 848
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNER--------------ASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
250
....*....|....*...
gi 147647143 849 KASSLEVQKAQLEGRLEE 866
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
629-878 |
9.26e-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: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 629 KLSTLASKESRLQDLLETK--------ALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVES 700
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKreyegyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 701 ERAQSDIEHLFQhnRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQL 780
Cdd:TIGR02169 282 KDLGEEEQLRVK--EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 781 IEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 860
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
250
....*....|....*...
gi 147647143 861 EGRLEEKESLVKLQQEEL 878
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKL 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-879 |
7.28e-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: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 623 MDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEAR-------TLASMLREVERKNEELSVLLKA 695
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 696 QQVESERAQSDIEHLFQHN----RKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKE 771
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLdelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 772 Q----------NEKSIAQLIEKEEQRKEVQNQLVDR--EHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRT 839
Cdd:TIGR02168 394 QiaslnneierLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 147647143 840 EQIRKELSIKASSLEVQKAQLEGRLEEKESL------VKLQQEELN 879
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFsegvkaLLKNQSGLS 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
641-852 |
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 147647143 641 QDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLE-S 719
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 720 VAEEHEILTK-----------SYMELLQRNESTEKKNKDLQI----------TCDSLNKQIETVKKLNESLKEQNEKSIA 778
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 779 QLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASS 852
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-883 |
3.79e-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: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 651 LAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEhlfQHNRKLESVAEEHEILTKS 730
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE---QLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 731 YMELLQRNESTEKKNKDLQITCDSLNKQIEtvkKLNESLKEQNEKSIAQLIEKEEQRKEVQNQlvdrEHKLANLHQKTKV 810
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANL----RERLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147647143 811 QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSH 883
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
631-835 |
1.75e-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: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 631 STLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHL 710
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 711 FQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDlqitcdsLNKQIETVK-KLNEsLKEQNEKSIAQLIEKEEQRKE 789
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD-------LNAAIAGIEaKINE-LEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 147647143 790 VQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 835
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
626-878 |
1.76e-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: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 626 YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSvLLKAQQVESERAQS 705
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-EAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEhlfqhnRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQitcdslnKQIETVKKLNESLKEQNEKSIAQLIEKEE 785
Cdd:COG1196 369 EAE------AELAEAEEELEELAEELLEALRAAAELAAQLEELE-------EAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 786 QRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQirkelsiKASSLEVQKAQLEGRLE 865
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLE 508
|
250
....*....|...
gi 147647143 866 EKESLVKLQQEEL 878
Cdd:COG1196 509 GVKAALLLAGLRG 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
624-869 |
2.12e-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: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 624 DVYEMK--LSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESE 701
Cdd:TIGR02169 682 RLEGLKreLSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 702 RAQSDIEHLfqhNRKLESVAEEheiltksyMELLQRNESTEKknkdLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 781
Cdd:TIGR02169 762 ELEARIEEL---EEDLHKLEEA--------LNDLEARLSHSR----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 782 EKEEQRKEVQNQLVDREH-----------------KLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRK 844
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDlkeqiksiekeienlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|....*
gi 147647143 845 ELSIKASSLEVQKAQLEGRLEEKES 869
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
639-881 |
2.82e-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: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 639 RLQDLL-ETKAlalaQADRLIAQHRC----QRTQAETEARTLASMLREVERKNEELSvllkAQQVESERAQSDIEhlfQH 713
Cdd:TIGR02168 190 RLEDILnELER----QLKSLERQAEKaeryKELKAELRELELALLVLRLEELREELE----ELQEELKEAEEELE---EL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 714 NRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQ 793
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 794 LVDREHKLANLHQKTKVQEEKIKTLQKERE-------DKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEE 866
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEelesrleELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250
....*....|....*
gi 147647143 867 KESLVKLQQEELNKH 881
Cdd:TIGR02168 419 LQQEIEELLKKLEEA 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
597-890 |
1.04e-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: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSGMVVKDQICDVRISDIMDVYEMKLS---TLASKESRLQDLLETKALALAQADRLIAQHrcqrtqAETEAR 673
Cdd:pfam15921 147 LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLShegVLQEIRSILVDFEEASGKKIYEHDSMSTMH------FRSLGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 674 TLASMLREVERKNEELS--VLLKAQQVESERAQSD--IEHLFQ-HNRKLESVAEEHEI----LT-------------KSY 731
Cdd:pfam15921 221 AISKILRELDTEISYLKgrIFPVEDQLEALKSESQnkIELLLQqHQDRIEQLISEHEVeitgLTekassarsqansiQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 732 MELLQ---RNEST--EKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSI----AQLIEKEEQRKEVQNQ---LVDREH 799
Cdd:pfam15921 301 LEIIQeqaRNQNSmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQEsgnLDDQLQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 800 K-LANLHQKTK---VQEEKIKTLQKEREDKEETIDILRKEL-SRTEQIRKELSIkassLEVQKAQLEGRLEEKESLVKLQ 874
Cdd:pfam15921 381 KlLADLHKREKelsLEKEQNKRLWDRDTGNSITIDHLRRELdDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGK 456
|
330
....*....|....*.
gi 147647143 875 QEELNKHSHMIAMIHS 890
Cdd:pfam15921 457 NESLEKVSSLTAQLES 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
712-900 |
1.07e-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: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 712 QHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQ 791
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 792 NQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKE-SL 870
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRL 840
|
170 180 190
....*....|....*....|....*....|
gi 147647143 871 VKLQQEELNKHSHMIAMIHSLSGGKINPET 900
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
680-890 |
1.78e-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: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 680 REVERKNEELSVLLkAQQVESERAQSDIEHLFQHNR-KLESVAEEHEILTKSYMELLQRNESTEKKNKDLQItcdSLNKQ 758
Cdd:pfam05483 233 KEINDKEKQVSLLL-IQITEKENKMKDLTFLLEESRdKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM---SLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 759 IETVKKLNESLKEQNeKSIAQLIE-KEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELS 837
Cdd:pfam05483 309 MSTQKALEEDLQIAT-KTICQLTEeKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 838 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLV-------KLQQEELNKHSHMIAMIHS 890
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLdekkqfeKIAEELKGKEQELIFLLQA 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-883 |
2.40e-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: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 637 ESRLQDLLETKALALAQADRLIAQHRcqRTQAETEARTLASMLREVERKNEELsvllkaqqveSERAQSDIEHLFQHNRK 716
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEEL----------EEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 717 LESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVD 796
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 797 REHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQE 876
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
....*..
gi 147647143 877 ELNKHSH 883
Cdd:COG1196 499 AEADYEG 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
634-875 |
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 147647143 634 ASKESRLQDLLETKALALAQADRLIAQHRCQRTQA--ETEARTLASMLREVE--RKNEEL---SVLLKAQQV-ESERAQS 705
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEekKKADELkkaEELKKAEEKkKAEEAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEHLFQHNRKLESV--AEEHEI--LTKSYMELLQRNESTEKKNKDLQITCDSLNKQiETVKKLNESLKEQneksiaqli 781
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAkkAEEARIeeVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKK--------- 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 782 EKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT--LQKEREDKEETIDILRK---ELSRTEQIRKElsikaSSLEVQ 856
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaeEAKKAEELKKK-----EAEEKK 1716
|
250
....*....|....*....
gi 147647143 857 KAQlEGRLEEKESLVKLQQ 875
Cdd:PTZ00121 1717 KAE-ELKKAEEENKIKAEE 1734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
669-881 |
4.24e-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: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 669 ETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDL 748
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL---RKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 749 QITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEET 828
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 147647143 829 IDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
596-876 |
7.11e-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: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 596 NIEELIEKLQSGMVVKDQICDVRISDIMDVyEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTL 675
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQL-KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 676 ASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEheiltksymeLLQRNESTEKKNKDLQITCDSL 755
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----------LTNQDSVKELIIKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 756 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 835
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 147647143 836 LSRTEQIRKELSIKASSLEVQKaQLEGRLEEKESLVKLQQE 876
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNK-EIEELKQTQKSLKKKQEE 586
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
635-887 |
7.62e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 635 SKESRLQDLLEtKALALAQADRLiaqHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 714
Cdd:PTZ00121 1530 AEEAKKADEAK-KAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 R-KLESVAEEHEILTKSymELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESL---------KEQNEKSIAQLIEK- 783
Cdd:PTZ00121 1606 KmKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENkikaaeeakKAEEDKKKAEEAKKa 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 784 EEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT---LQKEREDKEETIDILRKELS----RTEQIRKELSIKASSLEVQ 856
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEedkkKAEEAKKDEEEKKKIAHLK 1763
|
250 260 270
....*....|....*....|....*....|.
gi 147647143 857 KAQLEGRLEEKESLVKLQQEELNKHSHMIAM 887
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
635-880 |
8.15e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 635 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAE-----TEARTLASMLR---EVERKNEELSvllkaQQVESERAQSD 706
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaAAAKKKADEAKkkaEEKKKADEAK-----KKAEEAKKADE 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 707 IEHLFQHNRKLESVAEEHEILTKS-----YMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 781
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 782 EKEEQRKEVQNQLVDREHKLANLHQKTKVQ--EEKIKTLQKEREDKEETIDILRKELSR-TEQIRKELSIKASSLEVQKA 858
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMK 1608
|
250 260
....*....|....*....|..
gi 147647143 859 QLEGRLEEKEslvKLQQEELNK 880
Cdd:PTZ00121 1609 AEEAKKAEEA---KIKAEELKK 1627
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
629-876 |
2.75e-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: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 629 KLSTLASKESRLQDLLETKALALAQADRLIaqhRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIE 708
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGDEV---KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 709 HLFQHNRKLE--SVAEEHEI------LTKSYMELlqrnESTEKKNKDLqitCDSLNKQIETVKKLNESLKEQNEKSIAQL 780
Cdd:pfam05483 612 ELHQENKALKkkGSAENKQLnayeikVNKLELEL----ASAKQKFEEI---IDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 781 IEKEEQRKEVQNQLvdrEHKLANL--------HQKTKVQEEKIKT--LQKEREDKEETIDI-LRKELSrteqirkelSIK 849
Cdd:pfam05483 685 DEAVKLQKEIDKRC---QHKIAEMvalmekhkHQYDKIIEERDSElgLYKNKEQEQSSAKAaLEIELS---------NIK 752
|
250 260
....*....|....*....|....*..
gi 147647143 850 ASSLEVQKaQLEGRLEEKESLVKLQQE 876
Cdd:pfam05483 753 AELLSLKK-QLEIEKEEKEKLKMEAKE 778
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
767-896 |
3.44e-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: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 767 ESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREhkLANLHQKTKVQEEKIKTLQKERED-------KEETIDILRKELSRT 839
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERE--LTEEEEEIRRLEEQVERLEAEVEEleaeleeKDERIERLERELSEA 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 840 -EQIRKEL--SIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHslSGGKI 896
Cdd:COG2433 454 rSEERREIrkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH--SGELV 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
635-880 |
6.34e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 635 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL-LKAQQVESERA---------Q 704
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELeKELESLEGSKRkleekirelE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 705 SDIEHLFQHNRKLESVAEEHEIL---TKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiaqLI 781
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 782 EKEEQRKEVQNQLVDREhKLANLHQKTKVQEEKIKTLQKERedKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLE 861
Cdd:PRK03918 342 ELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|....*....
gi 147647143 862 GRLEEKESLVklqqEELNK 880
Cdd:PRK03918 419 KEIKELKKAI----EELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
627-880 |
9.55e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 627 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASmlreveRKNEELSVLLKAQQVESERAQSD 706
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNKELKSELKNQEKKLEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 707 IE-HLFQHNRKLESVAEEHEILTKSYMELLQRNES-----TEKKN----------------KDLQITCDSLNKQIETVKK 764
Cdd:TIGR04523 326 IQnQISQNNKIISQLNEQISQLKKELTNSESENSEkqrelEEKQNeieklkkenqsykqeiKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 765 LNESLKEQ--NEKSIAQLIEKEEQR------------KEVQNQLVDREHKLANLHQKTKVQEEKIKTL------------ 818
Cdd:TIGR04523 406 LNQQKDEQikKLQQEKELLEKEIERlketiiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsinkikqnle 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 819 --QKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:TIGR04523 486 qkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
684-878 |
1.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 684 RKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEK--KNKDLQITCDSLNKQIET 761
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 762 VKKLNESLKEQneksIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEK-IKTLQKEREDKEETIDILRKELSRTE 840
Cdd:COG4717 144 LPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 147647143 841 QirkelsiKASSLEVQKAQLEGRLEEKESLVKLQQEEL 878
Cdd:COG4717 220 E-------ELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
753-878 |
1.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 753 DSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDIL 832
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 147647143 833 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 878
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
633-876 |
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 147647143 633 LASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTlasmlREVER-KNEELSVL------LKAQQVESERAQS 705
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK-----RELERiRQEEIAMEisrmreLERLQMERQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEHLFQHNRKLESVAEEHEILTKSYMELLQ--RNESTEKKNKDLQITCDSLNKQIETVKKlnESLKEQNEKSIAQLIEK 783
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEqiRAEQEEARQREVRRLEEERAREMERVRL--EEQERQQQVERLRQQEE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 784 EEQRKEVQNQLVDREHKLANlHQKTKV--------------QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIK 849
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAE-EQRRKIlekeleerkqamieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
250 260
....*....|....*....|....*..
gi 147647143 850 ASSlEVQKaQLEGRLEEKESLVKLQQE 876
Cdd:pfam17380 550 ERR-RIQE-QMRKATEERSRLEAMERE 574
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
747-880 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 747 DLQItcDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKERE--- 823
Cdd:COG1579 16 DSEL--DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyea 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 147647143 824 -DKEetIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:COG1579 94 lQKE--IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-844 |
2.31e-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: 52.62 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 679 LREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNE---STEKKNKDLQitcdSL 755
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlGNVRNNKEYE----AL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 756 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDRE----HKLANLHQKTKVQEEKIKTLQKEREDKEETIDi 831
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaeleEKKAELDEELAELEAELEELEAEREELAAKIP- 173
|
170
....*....|...
gi 147647143 832 lRKELSRTEQIRK 844
Cdd:COG1579 174 -PELLALYERIRK 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
669-880 |
2.37e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 669 ETEARTLASMLREVERKNEELSVLLKA--------QQVESERAQ---------SDIEHLFQHNRKLESVAEEHEILTKSY 731
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRtenieeliKEKEKELEEvlreineisSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 732 MELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQnEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ 811
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147647143 812 EEKIKTLQ---KEREDKEETIDILRKELsrtEQIRKELS-IKASSLEVQKA-QLEGRLEE-KESLVKLQQEELNK 880
Cdd:PRK03918 320 EEEINGIEeriKELEEKEERLEELKKKL---KELEKRLEeLEERHELYEEAkAKKEELERlKKRLTGLTPEKLEK 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
629-870 |
2.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 629 KLSTLASKESRLQDLLETKALAlaqaDRLIAQHRcqrtqAETEARTLAsmlreVERKNEELSVLLKAQQVESERAQsdie 708
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDL----EELIAERR-----ETIEEKRER-----AEELRERAAELEAEAEEKREAAA---- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 709 hlfqhnrKLESVAEEHeiltksymelLQRNESTEKKNKDLQITCDSLNK---QIETVKKLNESLKEQNEKSiAQLIEKEE 785
Cdd:PRK02224 562 -------EAEEEAEEA----------REEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKR-EALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 786 QRKEVQNQLVDREHKLANlhqktKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLE 865
Cdd:PRK02224 624 ERRERLAEKRERKRELEA-----EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
....*
gi 147647143 866 EKESL 870
Cdd:PRK02224 699 RREAL 703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
627-886 |
3.36e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 627 EMKLSTLASKESRLQDLLETKALALA----QADRL---IAQHRCQRTQAETEARTLASML----REVERKNEELSVLLKA 695
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQahneEAESLredADDLEERAEELREEAAELESELeearEAVEDRREEIEELEEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 696 QQVESER---AQSDIEHLFQHnrkLESVAEEHEILTKSYMEL---LQRNESTEKKNKDLQI-----TCDSLNKQIETVKK 764
Cdd:PRK02224 393 IEELRERfgdAPVDLGNAEDF---LEELREERDELREREAELeatLRTARERVEEAEALLEagkcpECGQPVEGSPHVET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 765 LNESlKEQNEKSIAQLIEKEEQRKEVQNQLvDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDilrkelsrteqirk 844
Cdd:PRK02224 470 IEED-RERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIE-------------- 533
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 147647143 845 ELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIA 886
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
635-881 |
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 147647143 635 SKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 714
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 RKLESVAEEHEILTKSyMELLQRNESTEKKNKDLQIT------CDSLNKQIETVKKLNESLKEQNEKSIA-QLIEKEEQR 787
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAaaakkkADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEA 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 788 KEVQNQLVDREHKLANLHQKTKVQE-EKIKTLQKEREDKEETIDILRK---------ELSRTEQIRK-------ELSIKA 850
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKaaeakkkadEAKKAEEAKKadeakkaEEAKKA 1536
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 147647143 851 SSL----------EVQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:PTZ00121 1537 DEAkkaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
596-881 |
3.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 596 NIEELIEKLQSGMVVKDQicdvRISDIMDVYEMKLSTLASKESRLQDLLETKALalaqadrlIAQHRCQRTQAETEARTL 675
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKELEELKEE--------IEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 676 ASMLREVERKNEELsvllKAQQVESERAQSDIEhlfqhnrKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSL 755
Cdd:PRK03918 258 EEKIRELEERIEEL----KKEIEELEEKVKELK-------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 756 NKQI-----------ETVKKLNESLKEQN-------------------------------EKSIAQLIEKEEQRKEVQNQ 793
Cdd:PRK03918 327 EERIkeleekeerleELKKKLKELEKRLEeleerhelyeeakakkeelerlkkrltgltpEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 794 LVDREHKLANLHQKTKVQEEKIKTLQKER------------EDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLE 861
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340
....*....|....*....|....*....
gi 147647143 862 GRLEEKESLVKLQQ---------EELNKH 881
Cdd:PRK03918 487 KVLKKESELIKLKElaeqlkeleEKLKKY 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
610-870 |
4.06e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 610 VKDQICDVRISDIMDV---YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAET---EARTLASMLREVE 683
Cdd:PRK02224 192 LKAQIEEKEEKDLHERlngLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 684 RKNEELSVLLKAQQVESERAQSDIEHLFQhnrKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVK 763
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLA---EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 764 KLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIR 843
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
250 260
....*....|....*....|....*..
gi 147647143 844 KELSIKASSlevqkaqLEGRLEEKESL 870
Cdd:PRK02224 429 AELEATLRT-------ARERVEEAEAL 448
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
757-884 |
4.09e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 757 KQIETVKKLNESLKEQNEKsiaqliEKEEQRKEVQNQLVDREHKLAN-LHQKTKVQEEKIKTLQKEREDKEETIDilrKE 835
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKK------EAEAIKKEALLEAKEEIHKLRNeFEKELRERRNELQKLEKRLLQKEENLD---RK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 147647143 836 LSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHM 884
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
596-868 |
4.41e-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: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 596 NIEELIEKLQSGMVVKDQICDVRISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEA--- 672
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 673 -RTLASMLREVERKNEELSVLLKAQQVESERAQSD---IEHLFQH--NRKLE---------SVAEEHEILTKSYMELLQ- 736
Cdd:pfam15921 376 dDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNsitIDHLRREldDRNMEvqrleallkAMKSECQGQMERQMAAIQg 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 737 RNESTEKKNK---DLQITCDSLNKQIE--TVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDR-----EHKLANLhQ 806
Cdd:pfam15921 456 KNESLEKVSSltaQLESTKEMLRKVVEelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvDLKLQEL-Q 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 807 KTKVQEEKIKTLQKERE-------DKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG-----RLEEKE 868
Cdd:pfam15921 535 HLKNEGDHLRNVQTECEalklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeindrRLELQE 608
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-880 |
4.86e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 667 QAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNK 746
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 747 DLQITCDSLNKQiETVKKLNESLKEQNEKSIAQLIEK--EEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKERED 824
Cdd:PTZ00121 1287 EEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAKKkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 825 KEETidilrkELSRTEQIRKELSIKASSLEVQKAQlegRLEEKESLVKLQQEELNK 880
Cdd:PTZ00121 1366 AEAA------EKKKEEAKKKADAAKKKAEEKKKAD---EAKKKAEEDKKKADELKK 1412
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-874 |
9.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 627 EMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLL-KAQQVESE--RA 703
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKeKLIKLKGEikSL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 704 QSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNEST--------EKKNKDLQ------ITCDSLNKQIETVKKLNESL 769
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEpfyneyLELKDAEKELEREEKELKKL 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 770 KEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLAnlhqktkvqEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELsik 849
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEI--- 692
|
250 260
....*....|....*....|....*
gi 147647143 850 ASSLEVQKAQLEGRLEEKESLVKLQ 874
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 ... |
671-880 |
1.01e-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: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 671 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNE--------STE 742
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIdllqellrDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 743 KKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKER 822
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 147647143 823 EDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
650-859 |
1.24e-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: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 650 ALAQADRLIAQHRCQRTQAETEART----LASMLREVERKNEELSVL---LKAQQVESERAQSDIEhlfqhnRKLESVAE 722
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAaqaeLDALQAELEELNEEYNELqaeLEALQAEIDKLQAEIA------EAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 723 EHEILTK------------SYMELLQRNESTEkknkDL--------QITcDSLNKQIETVKklneSLKEQNEKSIAQLIE 782
Cdd:COG3883 84 RREELGEraralyrsggsvSYLDVLLGSESFS----DFldrlsalsKIA-DADADLLEELK----ADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147647143 783 KEEQRKEVQNQLvdrEHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQ 859
Cdd:COG3883 155 KLAELEALKAEL---EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
689-880 |
1.31e-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: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 689 LSVLLKAQQVESERAQSDIEhlfQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIetvKKLNES 768
Cdd:COG4942 11 LALAAAAQADAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 769 LKEqNEKSIAQL-IEKEEQRKEVQNQLV---------------------DREHKLANLHQKTKVQEEKIKTLQKEREDKE 826
Cdd:COG4942 85 LAE-LEKEIAELrAELEAQKEELAELLRalyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 147647143 827 ETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
693-878 |
1.45e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 693 LKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQI----ETVKKLNES 768
Cdd:COG3883 18 IQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerrEELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 769 LKEQ-----------NEKSIAQLIekeeQRKEVQNQLVDREHKLANLHQKTKvqeEKIKTLQKEREDKEETIDILRKELs 837
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFL----DRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAEL- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 147647143 838 rtEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 878
Cdd:COG3883 167 --EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
635-827 |
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 147647143 635 SKESRLQDLLETKALALAQADRLIAQHRCQRtqaeteartlasmLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN 714
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMR-------------RLEVERKRREQEEQRRLQQEQLERAEKMREELELEQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 RKlesVAEEHEILTKSYMELLQRNESTEKKNK-DLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQR-KEVQN 792
Cdd:pfam15709 383 QR---RFEEIRLRKQRLEEERQRQEEEERKQRlQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRqKELEM 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 147647143 793 QLVDREHKLANLHQKTKV------QEEKIKTLQ--KEREDKEE 827
Cdd:pfam15709 460 QLAEEQKRLMEMAEEERLeyqrqkQEAEEKARLeaEERRQKEE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
669-877 |
1.67e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 669 ETEARTLASMLREVERKNEELSVLLKA-QQVESERAQ--SDIEHL-FQHNRKLESVAEEHEILTKSYMELL---QRNEST 741
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKlDELEEELAEllKELEELgFESVEELEERLKELEPFYNEYLELKdaeKELERE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 742 EKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQK- 820
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKt 695
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147647143 821 ---------EREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRL---------EEKESLVKLQQEE 877
Cdd:PRK03918 696 leklkeeleEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIaseifeeltEGKYSGVRVKAEE 770
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
636-880 |
2.23e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 636 KESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASmlrEVERKNEELsvllkaQQVESERAQSDIEhLFQHNR 715
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL------EQLEEELEQARSE-LEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 716 KLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLV 795
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 796 DREHKLANLHQKTKVQ-----EEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESL 870
Cdd:COG4372 161 SLQEELAALEQELQALseaeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250
....*....|
gi 147647143 871 VKLQQEELNK 880
Cdd:COG4372 241 ALELEEDKEE 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
670-880 |
3.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 670 TEARTLASMLreVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQ 749
Cdd:COG4717 38 TLLAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 750 ITCDSLNKQIetvkklneslkeQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQktkvQEEKIKTLQKEREDKEETI 829
Cdd:COG4717 116 EELEKLEKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 147647143 830 DILRKELS-RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:COG4717 180 EELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
596-879 |
3.41e-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: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 596 NIEELIEKlqsgmvvKDQICDvRISDIMDVYEMKLSTLASKESRLQ-------DLLETKALALAQADRLIAQHRCQRTQA 668
Cdd:pfam05483 283 NLKELIEK-------KDHLTK-ELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEF 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 669 ETEARTLASMLR------------------EVERKN---EELSVLLKAQQVESERAQS---DIEHLFQHNRKLESVAEEH 724
Cdd:pfam05483 355 EATTCSLEELLRteqqrleknedqlkiitmELQKKSselEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 725 EILTKSYMELLQRNEStEKKNKDLQITCDSLNKQ--IETVKKLNESLKEQNEKSI-------AQLIEKEEQRKEVQNQLV 795
Cdd:pfam05483 435 KGKEQELIFLLQAREK-EIHDLEIQLTAIKTSEEhyLKEVEDLKTELEKEKLKNIeltahcdKLLLENKELTQEASDMTL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 796 DREHKLANLHQKTKVQE---EKIKTLQKEREDKEETIDILRKELsrtEQIRKELSIKASSLEVQKAQLEGRLEEKESLVK 872
Cdd:pfam05483 514 ELKKHQEDIINCKKQEErmlKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
....*..
gi 147647143 873 LQQEELN 879
Cdd:pfam05483 591 ILENKCN 597
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
686-869 |
6.10e-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: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 686 NEELSVLLKAQQVESEraqsdiehLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKkl 765
Cdd:COG1579 3 PEDLRALLDLQELDSE--------LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 766 neslkeqneksiaQLIEKEEQR-KEVQN--QLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELsrtEQI 842
Cdd:COG1579 73 -------------ARIKKYEEQlGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AEL 136
|
170 180
....*....|....*....|....*..
gi 147647143 843 RKELSIKASSLEVQKAQLEGRLEEKES 869
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEELEA 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
643-881 |
6.67e-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: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 643 LLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL--------LKAQQVESERAQSDIEHLFQHN 714
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLadetladrLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 RKLESVA----------EEHEILTKSYMELLQRNestekknKDLQITCDSLNKQIETV---------------KKLNESL 769
Cdd:COG3096 917 KALAQLEplvavlqsdpEQFEQLQADYLQAKEQQ-------RRLKQQIFALSEVVQRRphfsyedavgllgenSDLNEKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 770 KEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDI------------LRKELS 837
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeaeerarirrdeLHEELS 1069
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 147647143 838 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
664-822 |
9.87e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 664 QRTQAETEARTLASMLREVERKNEELsvlLKAQQVESERAQsdiehlfqhNRKLESVAEEHEILTKSYMELLQRNESTEK 743
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAA---LLEAKELLLRER---------NQQRQEARREREELQREEERLVQKEEQLDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 744 KNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKT---KVQEEKIKTLQK 820
Cdd:PRK12705 96 RAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAqrvKKIEEEADLEAE 175
|
..
gi 147647143 821 ER 822
Cdd:PRK12705 176 RK 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
631-829 |
1.19e-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: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 631 STLASKESRLQDLLETKALALAQADRLIAQHrcQRTQAETEA---------RTLASMLREVERKNEELSVLLKAQQvESE 701
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEY--NELQAELEAlqaeidklqAEIAEAEAEIEERREELGERARALY-RSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 702 RAQSDIEHLFQhnrklesvaeeheilTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLI 781
Cdd:COG3883 100 GSVSYLDVLLG---------------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 147647143 782 EKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETI 829
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
647-863 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 647 KALAL---AQA-------DRLIAQHRCQRTQAETEAR-------TLASMLREVERKNEELSVL--LKAQQVESERAQSDI 707
Cdd:COG4913 192 KALRLlhkTQSfkpigdlDDFVREYMLEEPDTFEAADalvehfdDLERAHEALEDAREQIELLepIRELAERYAAARERL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 708 EHL---------FQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETV--KKLnESLKEQneks 776
Cdd:COG4913 272 AELeylraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRL-EQLERE---- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 777 IAQLiekEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKE----REDKEETIDILRKELSRTEQIRKELSIKASS 852
Cdd:COG4913 347 IERL---ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
250
....*....|.
gi 147647143 853 LEVQKAQLEGR 863
Cdd:COG4913 424 LEAEIASLERR 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
755-877 |
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 147647143 755 LNKQIETVKKLNESLKE-QNEKSIAQLIEKEE---QRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETID 830
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEaEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 147647143 831 ILRKELSRTEQirkELSIKASSLEVQKAQLEGRLEEkesLVKLQQEE 877
Cdd:PRK12704 114 KKEKELEQKQQ---ELEKKEEELEELIEEQLQELER---ISGLTAEE 154
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
638-846 |
2.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 638 SRLQDLLETkalALAQADRL--IAQHRCQRTQAETEA---RTLASMLR--EVERKNEELSVLLKAQQVESERAQSDIEhl 710
Cdd:COG4913 238 ERAHEALED---AREQIELLepIRELAERYAAARERLaelEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELE-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 711 fQHNRKLESVAEEHEILTKSYMEL-LQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKE 789
Cdd:COG4913 313 -RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 147647143 790 VQNQLVDREHKLANLHQKTKVQEEKiktLQKEREDKEETIDILRKELS----RTEQIRKEL 846
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSnipaRLLALRDAL 449
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
597-876 |
2.72e-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: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSgmvVKDQIcdVRISDIMDVYEMKLSTLASKESRLQDLL------ETKALALAQADRLIAQhRCQRTQAET 670
Cdd:TIGR00606 746 IPELRNKLQK---VNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQ-QAAKLQGSD 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 671 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQI 750
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 751 TCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT-LQKEREDKEETI 829
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETEL 979
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 147647143 830 DILRKELS----RTEQIRKELSIKASSLEVQKAQlEGRLEEKESLVKLQQE 876
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 ... |
601-876 |
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 147647143 601 IEKLQSGMVVKDQICDV---RISDIMDVYEMKLSTLASKESRLQDL----------LETKALALAQADRLIAQHRCQRtq 667
Cdd:pfam10174 382 IRDLKDMLDVKERKINVlqkKIENLQEQLRDKDKQLAGLKERVKSLqtdssntdtaLTTLEEALSEKERIIERLKEQR-- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 668 aETEARTLASMLREVERKNEELSVLLKAQQVE-SERAQSDIE------HLFQHNRKLESVAEEHEILTKSYMELLQRNES 740
Cdd:pfam10174 460 -EREDRERLEELESLKKENKDLKEKVSALQPElTEKESSLIDlkehasSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 741 TEKKNKDLQI---TCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ------ 811
Cdd:pfam10174 539 QLKKAHNAEEavrTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQmkeqnk 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 812 -EEKIKTLQKE--REDKEETIDILRKELSRT--------EQIRKELSIKASSLEVQKAQL---EGRLEEKES-LVKLQQE 876
Cdd:pfam10174 619 kVANIKHGQQEmkKKGAQLLEEARRREDNLAdnsqqlqlEELMGALEKTRQELDATKARLsstQQSLAEKDGhLTNLRAE 698
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
587-867 |
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 147647143 587 HLKDGVPGL-NIEELIEKLQSGMVVKDQICDVRISDIMDvyemkLSTLASKESRLQDLLETKAlalAQADRLIAQHRCQR 665
Cdd:pfam15921 535 HLKNEGDHLrNVQTECEALKLQMAEKDKVIEILRQQIEN-----MTQLVGQHGRTAGAMQVEK---AQLEKEINDRRLEL 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 666 TQAETEARTLASMLREVERKNEELS---VLLKAQQVESERAQSDIEH--------LFQHNRKLESVAEEHEILTKSYmel 734
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLElekVKLVNAGSERLRAVKDIKQerdqllneVKTSRNELNSLSEDYEVLKRNF--- 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 735 lqRNESTEkknkdLQITCDSLNKQIETVkklnESLKEQNEKSIAQLIEKEEQRKEV----QNQLVDREHKLANLHQKTKV 810
Cdd:pfam15921 684 --RNKSEE-----METTTNKLKMQLKSA----QSELEQTRNTLKSMEGSDGHAMKVamgmQKQITAKRGQIDALQSKIQF 752
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 147647143 811 QEEKIKTLQKEREDKEETIDILRKELSrteQIRKELSIKASSLEVQKAQlEGRLEEK 867
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELS---TVATEKNKMAGELEVLRSQ-ERRLKEK 805
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
770-880 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 770 KEQNEKsiaQLIEKEEQRKEVQNQLVDREHKLANlhqktkvQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIK 849
Cdd:pfam20492 1 REEAER---EKQELEERLKQYEEETKKAQEELEE-------SEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100 110
....*....|....*....|....*....|.
gi 147647143 850 ASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVER 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
626-878 |
3.71e-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: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 626 YEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELsvllkaqQVESERAQS 705
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQL-------QNEKKKMQQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEHLfqhnrklesvaEEHeiltksymelLQRNESTEKKNKDLQITCDSlnkqieTVKKLNES---LKEQNEKSIAQLIE 782
Cdd:pfam01576 104 HIQDL-----------EEQ----------LDEEEAARQKLQLEKVTTEA------KIKKLEEDillLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 783 KEEQRKEVQNQLVDREHKLANLhQKTKVQEEKIKTLQKEREDKEETidiLRKELsrtEQIRKELSIKASSLEVQKAQLEG 862
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSL-SKLKNKHEAMISDLEERLKKEEK---GRQEL---EKAKRKLEGESTDLQEQIAELQA 229
|
250
....*....|....*.
gi 147647143 863 RLEEKESLVKLQQEEL 878
Cdd:pfam01576 230 QIAELRAQLAKKEEEL 245
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
663-880 |
4.13e-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: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 663 CQRTQAE-TEARTLASMLREVERKN-----EELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEE----HEILTKSYM 732
Cdd:pfam07888 39 CLQERAElLQAQEAANRQREKEKERykrdrEQWERQRRELESRVAELKEELRQSREKHEELEEKYKElsasSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 733 ELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKV-- 810
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElr 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147647143 811 --QEEKIKTLQKEREDKEETIDIL----RKELsRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQ---QEELNK 880
Cdd:pfam07888 199 nsLAQRDTQVLQLQDTITTLTQKLttahRKEA-ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRdrtQAELHQ 276
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
655-871 |
4.25e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 655 DRLIAQHRCQRTQAETEARTLASMLREVERKNEELSvlLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSyMEL 734
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELE--EKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKE-LRQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 735 LQRNESTEKKNKDLqitcdslnkqIETVKKLNESLKEQNEKsiaqLIEKEEQRKEVQnqlVDREHKLANLHQKTKVQEek 814
Cdd:PRK00409 596 LQKGGYASVKAHEL----------IEARKRLNKANEKKEKK----KKKQKEKQEELK---VGDEVKYLSLGQKGEVLS-- 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147647143 815 iktlQKEREDKEETIDILR-----KELSRTEQIRKEL--SIKASSLEVQKAQLE----G-RLEEKESLV 871
Cdd:PRK00409 657 ----IPDDKEAIVQAGIMKmkvplSDLEKIQKPKKKKkkKPKTVKPKPRTVSLEldlrGmRYEEALERL 721
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
701-844 |
4.64e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 701 ERAQSDIEHLfQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLkEQNEKSIAQL 780
Cdd:PRK12704 45 EEAKKEAEAI-KKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL-EKKEKELEQK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 781 IEKEEQRKEvqnqlvdrehKLANLHQKTKVQEEKIKTLQKErEDKEETIDILRKELSR--TEQIRK 844
Cdd:PRK12704 123 QQELEKKEE----------ELEELIEEQLQELERISGLTAE-EAKEILLEKVEEEARHeaAVLIKE 177
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
715-893 |
5.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 RKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQitcDSLNKQIETVKKLNESLKEQNEKsIAQLIEKEEQRKEVQNQL 794
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 795 VDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRK------ELSIKASSLEVQKAQLEGRLEEKE 868
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEkaeeyiKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180
....*....|....*....|....*
gi 147647143 869 SLVKLQQEELNKHSHMIAMIHSLSG 893
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKK 345
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
597-880 |
5.98e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSGMVVKDQicDVRISDIMDVYEMKLSTLA------------------SKESRLQDLLETKALALAQADRLI 658
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEK--DIIDEDIDGNHEGKAEAKAhvgqdeglkpsykdfdfdAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 659 AQHRCQRTQAETEARTLASMLREVE--RKNEELSVLLKAQQVESERAqsdiehlFQHNRKLESvAEEHEILTKSymellQ 736
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEeaRKAEDARKAEEARKAEDAKR-------VEIARKAED-ARKAEEARKA-----E 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 737 RNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLAnlHQKTKVQEEKIK 816
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA--EEAKKAEEERNN 1251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 817 TLQKEREDKEETIDILRKELSRTEQIRKELSIKASSlEVQKAQLEGRLEEKESL--VKLQQEELNK 880
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-EKKKADEAKKAEEKKKAdeAKKKAEEAKK 1316
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
700-888 |
1.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 700 SERAQSDIEHLFQHNRKLESVAEEHEILTKsymELLQRNESTEKKNKDLQitcdSLNKQIETVKKLNESLKEQNEKSIAQ 779
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQARE---ELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 780 LIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQ 859
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180
....*....|....*....|....*....
gi 147647143 860 LEGRLEEKESLVKLQQEELNKHSHMIAMI 888
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIES 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
687-895 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 687 EELSVLLKAQQVESERAQSDIE-HLFQHNRKLESVAEEH--EILTKSYMELLQRNESTEKKNKDLQITC------DSLNK 757
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYkkEINDKEKQVSLLLIQITEKENKMKDLTFlleesrDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 758 QIETVKKLNESLKEQNEKsiaqlieKEEQRKEVQNQLVDREHKLANlhQKTKVQEEKI--KTLQKEREDKEETIDILRKE 835
Cdd:pfam05483 273 LEEKTKLQDENLKELIEK-------KDHLTKELEDIKMSLQRSMST--QKALEEDLQIatKTICQLTEEKEAQMEELNKA 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 836 LSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHSLSGGK 895
Cdd:pfam05483 344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
644-881 |
1.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 644 LETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVL--------LKAQQVESERAQSDIEHLFQHNR 715
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLadetladrVEEIREQLDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 716 ---KLESVA-------EEHEILTKSYMELLQRNESTEKKNKDL------------QITCDSLNKQIEtvkkLNESLKEQN 773
Cdd:PRK04863 919 alaQLEPIVsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALtevvqrrahfsyEDAAEMLAKNSD----LNEKLRQRL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 774 EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKE----------------REDKEEtidiLRKELS 837
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQElqdlgvpadsgaeeraRARRDE----LHARLS 1070
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 147647143 838 RTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
633-891 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 633 LASKESRLQDLLETKAlalAQADRLIAQHRCQRTQAETEARTLASMLREVER---KNEELS-----VLLKAQQVESERAQ 704
Cdd:pfam05483 434 LKGKEQELIFLLQARE---KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklKNIELTahcdkLLLENKELTQEASD 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 705 SDIEhLFQHNRKLESVAEEHEILTKSyMELLQRNESTEKKnkDLQITCDSLNKQIETVK-KLNESlkEQNEKSIA-QLIE 782
Cdd:pfam05483 511 MTLE-LKKHQEDIINCKKQEERMLKQ-IENLEEKEMNLRD--ELESVREEFIQKGDEVKcKLDKS--EENARSIEyEVLK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 783 KEEQRKEVQN-------QLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQ--------IRKELS 847
Cdd:pfam05483 585 KEKQMKILENkcnnlkkQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeeiidnYQKEIE 664
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 147647143 848 IKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAMIHSL 891
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL 708
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
782-867 |
2.21e-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: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 782 EKEEQRKEVQNQLVDREHKlanlhQKTKVQEEKIKTLQKEREDKEETID--ILRKELS------RTEQIRKELSIKASSL 853
Cdd:pfam05300 59 DEEELRKKIKEELYKRLEQ-----EQAKVQEELARLAEREREAAQESLTraILRERAStederlKAQQLAKQLEEKEAEL 133
|
90
....*....|....*...
gi 147647143 854 EVQ----KAQLeGRLEEK 867
Cdd:pfam05300 134 KKQdafyKEQL-ARLEEK 150
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
767-881 |
2.34e-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: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 767 ESLKEQNEKSIAqliEKEEQRKEVQNQLVDREHKlanlhQKTKVQEEKIKtLQKEREDKEETIDILRK---ELSRTEQIR 843
Cdd:pfam07767 208 EKKRLKEEEKLE---RVLEKIAESAATAEAREEK-----RKTKAQRNKEK-RRKEEEREAKEEKALKKklaQLERLKEIA 278
|
90 100 110
....*....|....*....|....*....|....*....
gi 147647143 844 KELSIKASSLEVQKAQLE-GRLEEKESLVKLQQEELNKH 881
Cdd:pfam07767 279 KEIAEKEKEREEKAEARKrEKRKKKKEEKKLRPRKLGKH 317
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
597-850 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSgmvvkdqiCDVRISDimdvYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAE-----TE 671
Cdd:TIGR02169 739 LEELEEDLSS--------LEQEIEN----VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskleEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 672 ARTLASMLREVERKNEELSvlLKAQQVESERA----------------QSDIEHLFQHNRKLESVAEEHEI----LTKSY 731
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLT--LEKEYLEKEIQelqeqridlkeqiksiEKEIENLNGKKEELEEELEELEAalrdLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 732 MELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQL----------------------IEKEEQRKE 789
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiedpkgedeeipeeelsledVQAELQRVE 964
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 147647143 790 VQ-------NQLVDREHKLANLHQKTkvQEEKIKTLQKEREDKEETIDilrkelsRTEQIRKELSIKA 850
Cdd:TIGR02169 965 EEiralepvNMLAIQEYEEVLKRLDE--LKEKRAKLEEERKAILERIE-------EYEKKKREVFMEA 1023
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
588-880 |
2.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 588 LKDGVPGLNIEELIEKLQSGMVVKDQIcdvrisdimdvyEMKLSTLASKESRLQDLLETKALALAQADRliAQHRC---- 663
Cdd:PRK03918 377 LKKRLTGLTPEKLEKELEELEKAKEEI------------EEEISKITARIGELKKEIKELKKAIEELKK--AKGKCpvcg 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 664 QRTQAETEARTLASMLREVERKNEELSVL------LKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQR 737
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELKEIeekerkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 738 NESTEKKNKDLQITcdsLNKQIETVKKLNESLKEQNEKsiaqLIEKEEQRKEVQNQLVDREHKLANLHQKT-KVQEEKIK 816
Cdd:PRK03918 523 KAEEYEKLKEKLIK---LKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESvEELEERLK 595
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 817 TLQKEREDKEETIDIlRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESlvklQQEELNK 880
Cdd:PRK03918 596 ELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK----ELEELEK 654
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
662-887 |
3.64e-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: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 662 RCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNEST 741
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 742 EKKnkdlqitcdslnKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEvQNQLVDREhKLANLHQKTKVQEEKIKTLQKE 821
Cdd:pfam13868 113 EDQ------------AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE-EEREEDER-ILEYLKEKAEREEEREAEREEI 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 822 REDKEETIDILRKELSRTEQIRKEL----------SIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIAM 887
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQDEKAERdelraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
636-883 |
3.68e-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: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 636 KESRLQDLLETKalaLAQADRLiaqhRCQRTQAETEARTLASMLREVERKNEELSVL-------------LKAQQVESER 702
Cdd:pfam05557 95 KESQLADAREVI---SCLKNEL----SELRRQIQRAELELQSTNSELEELQERLDLLkakaseaeqlrqnLEKQQSSLAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 703 AQSDIEHLFQHNRKLESVAEEheilTKSYMELLQRNESTEKKNKDLQitcdSLNKQIETVKKLNESLKEQNEKSIAQLIE 782
Cdd:pfam05557 168 AEQRIKELEFEIQSQEQDSEI----VKNSKSELARIPELEKELERLR----EHNKHLNENIENKLLLKEEVEDLKRKLER 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 783 KEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRkelSIKASSLEVQKAQLEG 862
Cdd:pfam05557 240 EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENS---SLTSSARQLEKARREL 316
|
250 260
....*....|....*....|.
gi 147647143 863 RLEEKESLVKLQQEELNKHSH 883
Cdd:pfam05557 317 EQELAQYLKKIEDLNKKLKRH 337
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-846 |
3.81e-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: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 646 TKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHE 725
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 726 ILTKSYMELL----QRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKL 801
Cdd:COG1196 655 GGSAGGSLTGgsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 147647143 802 ANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKEL 846
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
779-864 |
4.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 779 QLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQirkelsikasSLEVQKA 858
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA----------EIEERRE 86
|
....*.
gi 147647143 859 QLEGRL 864
Cdd:COG3883 87 ELGERA 92
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
662-882 |
4.59e-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: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 662 RCQRTQAETEARTLASMLREVERKNEELSVLLKAQQVESeRAQSDIEHLFQHNRKLESVAEEHEILTKSYME-----LLQ 736
Cdd:pfam10174 45 RALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDEL-RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEenfrrLQS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 737 RNESTEKKNKDLQITCDSLNKQIET-----------VKKLNESL--KEQNEKSI-------AQLIEKEEQRKEVQNQLVD 796
Cdd:pfam10174 124 EHERQAKELFLLRKTLEEMELRIETqkqtlgardesIKKLLEMLqsKGLPKKSGeedwertRRIAEAEMQLGHLEVLLDQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 797 RE----HKLANLHQKTKVQEE--KIKTLQKEREDKEETIDILrkelsrteqirkELSIKASSLEVQKAQLEGRL--EEKE 868
Cdd:pfam10174 204 KEkeniHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSL------------ERNIRDLEDEVQMLKTNGLLhtEDRE 271
|
250
....*....|....
gi 147647143 869 SLVKlQQEELNKHS 882
Cdd:pfam10174 272 EEIK-QMEVYKSHS 284
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
675-876 |
4.62e-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: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 675 LASMLREVERKN----EELSVLLKAQQVESER-AQSDIEHLFQHNRKlesvAEEHEILTksymELLQRNESTEKKNKDLQ 749
Cdd:pfam01576 24 AESELKELEKKHqqlcEEKNALQEQLQAETELcAEAEEMRARLAARK----QELEEILH----ELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 750 ITcdslnkqietVKKLNESLKEQNEksiaQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETI 829
Cdd:pfam01576 96 NE----------KKKMQQHIQDLEE----QLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 147647143 830 DILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKEslvKLQQE 876
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE---KGRQE 205
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
671-878 |
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 147647143 671 EARTLASMLREVERKNEELSVLLKAQQVESERAQSDIE----HLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNK 746
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 747 DLQITCDSLNKQIETVKKLNESLKE---QNEKSIAQLIEKEEQRKEVQNQLVD-----REHKL------ANLHQKTKVQE 812
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSmaaQRDRTQAELHQARLQAAQLTLQLADaslalREGRArwaqerETLQQSAEADK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147647143 813 EKIKTLQKEREDKEETidiLRKELSRTEQIRKELSIKASSLEVQ-----------KAQLEGRLEEKESLVKLQQEEL 878
Cdd:pfam07888 318 DRIEKLSAELQRLEER---LQEERMEREKLEVELGREKDCNRVQlsesrrelqelKASLRVAQKEKEQLQAEKQELL 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
597-842 |
5.67e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSGMVVKDQICDV--RISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEART 674
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLeeRREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 675 LASMLREVERKNEELSVL--LKAQQVESERAQSDIEHLfqhNRKLESVAEeheiltksyMELLQRNESTEKKNKDLQITC 752
Cdd:PRK02224 574 VAELNSKLAELKERIESLerIRTLLAAIADAEDEIERL---REKREALAE---------LNDERRERLAEKRERKRELEA 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 753 DSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLhqktkvqeekiKTLQKEREDKEETIDIL 832
Cdd:PRK02224 642 EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL-----------EELRERREALENRVEAL 710
|
250
....*....|
gi 147647143 833 RKELSRTEQI 842
Cdd:PRK02224 711 EALYDEAEEL 720
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
668-895 |
5.69e-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: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 668 AETEARTLASMLREVERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKD 747
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKV 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 748 LQitcdslnKQIETVKKLNESLKEqNEKSIAQLIEK----------EEQRKEVQ---------------NQLVDREHKLA 802
Cdd:TIGR00606 787 CL-------TDVTIMERFQMELKD-VERKIAQQAAKlqgsdldrtvQQVNQEKQekqheldtvvskielNRKLIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 803 NLHQKTKVQEEKIKTLQ-----KEREDKEETIDILRKEL----SRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKL 873
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQigtnlQRRQQFEEQLVELSTEVqsliREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
250 260 270
....*....|....*....|....*....|
gi 147647143 874 QQEEL--------NKHSHMIAMIHSLSGGK 895
Cdd:TIGR00606 939 AQDKVndikekvkNIHGYMKDIENKIQDGK 968
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
639-876 |
6.15e-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: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 639 RLQDLLET-KALALAQADRLIAQHRCQRTQAETEARTLASM--LREVERKNEELSVLLKAQQVESERAQSDIEHLFQHN- 714
Cdd:pfam15921 430 RLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKe 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 715 RKLESVAEEHEILtKSYMEL----LQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKsiaqliekeeqrkev 790
Cdd:pfam15921 510 RAIEATNAEITKL-RSRVDLklqeLQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN--------------- 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 791 QNQLVDREHKLANLHQKTKVQeekiktLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESL 870
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQ------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA 647
|
....*..
gi 147647143 871 VK-LQQE 876
Cdd:pfam15921 648 VKdIKQE 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
753-881 |
6.45e-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: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 753 DSLNKQIETVKK---LNESLKE-QNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEET 828
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 147647143 829 IDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKEslvkLQQEELNKH 881
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE----EELAELEEE 331
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
736-877 |
6.69e-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: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 736 QRNESTEKKNKDLQITCDSLNKQIETVK-KLNE-------------SLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKL 801
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQqEINEktteisntqtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 802 ANLHQKTKV-----QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG-------RLEEKES 869
Cdd:TIGR04523 291 NQLKSEISDlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESensekqrELEEKQN 370
|
....*...
gi 147647143 870 LVKLQQEE 877
Cdd:TIGR04523 371 EIEKLKKE 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
680-846 |
7.17e-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: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 680 REVERKNEELSvLLKAQQVESERAQSD----IEHLFQHNRKLESVAEEHEILTKSYMELLQRNEsTEKKNKDLQITCDSL 755
Cdd:TIGR04523 489 KELKSKEKELK-KLNEEKKELEEKVKDltkkISSLKEKIEKLESEKKEKESKISDLEDELNKDD-FELKKENLEKEIDEK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 756 NKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKE 835
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
170
....*....|.
gi 147647143 836 LsrtEQIRKEL 846
Cdd:TIGR04523 647 V---KQIKETI 654
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
627-881 |
7.22e-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: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 627 EMKLSTLASKESRLQDLlETKALALAQADRLIAQHRCQ-RTQAETEARTLASMLREVERKNEELSVLLKAQQVESERAQS 705
Cdd:TIGR00618 392 TQKLQSLCKELDILQRE-QATIDTRTSAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEHLFQHNRKLESVAEEHEILTKsYMELLQRNE-----STEKKNKDLQ------ITCDSLNKQIETVKKLNESLkeqnE 774
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPcplcgSCIHPNPARQdidnpgPLTRRMQRGEQTYAQLETSE----E 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 775 KSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDilrKELSRTEQIRKELSIKASSLE 854
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---KLSEAEDMLACEQHALLRKLQ 622
|
250 260
....*....|....*....|....*..
gi 147647143 855 VQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
747-880 |
9.64e-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: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 747 DLQITCD--SLNKQIETVKKLNESLKEQNEKSIAQ-LIEKEEQRKEVQNQLVDR--EHKLANLHQKTKVQEE--KIKTLQ 819
Cdd:pfam15709 288 ESQVSIDgrSSPTQTFVVTGNMESEEERSEEDPSKaLLEKREQEKASRDRLRAEraEMRRLEVERKRREQEEqrRLQQEQ 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147647143 820 KEREDK-EETIDI----------LRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKL-------QQEELNK 880
Cdd:pfam15709 368 LERAEKmREELELeqqrrfeeirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLqelqrkkQQEEAER 446
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
640-880 |
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 147647143 640 LQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVE--------RKNEELSVLLKAQQV--ESERAQSDIEh 709
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEeelerteeRLAEALEKLEEAEKAadESERGRKVLE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 710 lfqhNRKLESvAEEHEILTKSYMELLQRNESTEKKnkdlqitCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKE 789
Cdd:pfam00261 85 ----NRALKD-EEKMEILEAQLKEAKEIAEEADRK-------YEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 790 VQNQLvdrehklanlhQKTKVQEEKikTLQKErEDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKES 869
Cdd:pfam00261 153 VGNNL-----------KSLEASEEK--ASERE-DKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|.
gi 147647143 870 LVKLQQEELNK 880
Cdd:pfam00261 219 KYKAISEELDQ 229
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
658-877 |
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 147647143 658 IAQHRCQRTQAETEARTLASMLREVERKNEELSvllkAQQVESERAQSDIEHLF--QHNRKLeSVAEEHEILTKS--YME 733
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRKELAELN----KAGGSIDKLRKEIERLEwrQQTEVL-SPEEEKELVEKIkeLEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 734 LLQRNESTEKKNKDLQitcdslnkqiETVKKLNEsLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEE 813
Cdd:COG1340 148 ELEKAKKALEKNEKLK----------ELRAELKE-LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 814 KIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEE 877
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGE 280
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
758-882 |
1.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 758 QIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELS 837
Cdd:PRK12705 43 QKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 147647143 838 -RTEQIRKELSIKAS-SLEVQKAQLEGRL-----EEKESLVKLQQEELNKHS 882
Cdd:PRK12705 123 eLEKQLDNELYRVAGlTPEQARKLLLKLLdaeleEEKAQRVKKIEEEADLEA 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
682-880 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 682 VERKNEELSVLLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKsyMELLQRNESTekKNKDLQITCDSLNKQIET 761
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNK--IKILEQQIKD--LNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 762 VKKLNESLK---EQNEKSIAQLIEKEEQRKEV--------------QNQLVDREHKLANLHQKTKVQEEKIKTLQKERED 824
Cdd:TIGR04523 105 LSKINSEIKndkEQKNKLEVELNKLEKQKKENkknidkflteikkkEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 825 KEETIDILRKELSRTEQI----------RKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLlsnlkkkiqkNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
739-827 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 739 ESTEKKNKDLQITCDSLNkQIE-----TVKKLNESLKEQN--EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQ 811
Cdd:pfam18595 12 AELERKARELQAKIDALQ-VVEkdlrsCIKLLEEIEAELAklEEAKKKLKELRDALEEKEIELRELERREERLQRQLENA 90
|
90
....*....|....*.
gi 147647143 812 EEKIKTLQKEREDKEE 827
Cdd:pfam18595 91 QEKLERLREQAEEKRE 106
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
685-846 |
1.35e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 42.30 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 685 KNEELSVLLKAQQVESERAQsdIEHL-FQHNRKLESVaEEHEILTKSYMELLQRNESTEKKNKdlqITCDSlnkqietvk 763
Cdd:pfam03999 132 LPLLIDPLPSLEELESFRKH--LENLrNEKERRLEEV-NELKKQIKLLMEELDLVPGTDFEED---LLCES--------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 764 KLNESLKEQNEKSIAQLIEK-EEQRKEVQNQLVDREHKLANLHQKTKV-QEEKIKTLQKEREDKEETIDILRKELSRTEQ 841
Cdd:pfam03999 197 EDNFCLSRENIDKLRKLIKQlEEQKAEREEKIDDLREKILELWNRLQVpQEEQESFVRENNSLSQDTIDALREELQRLEE 276
|
....*
gi 147647143 842 IRKEL 846
Cdd:pfam03999 277 LKKKN 281
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
744-860 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 744 KNKDLQITCDSLNKQIETVKKLNESLK----EQNEKSIAQLIEKEEQRKEVQNQLVDRE----HKLANLHQKTKVQEEKI 815
Cdd:pfam13870 14 ELITLKHTLAKIQEKLEQKEELGEGLTmidfLQLQIENQALNEKIEERNKELKRLKLKVtntvHALTHLKEKLHFLSAEL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 147647143 816 KTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 860
Cdd:pfam13870 94 SRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGLL 138
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
629-880 |
1.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 629 KLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLAsmlREVERKNEELSVL---LKAQQVESERAQS 705
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAqeeLESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 706 DIEHLFQHNRKLEsvaEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEE 785
Cdd:COG4372 116 ELEELQKERQDLE---QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 786 QRKEVQNQLVDREHKLAN---LHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEG 862
Cdd:COG4372 193 NRNAEKEEELAEAEKLIEslpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*...
gi 147647143 863 RLEEKESLVKLQQEELNK 880
Cdd:COG4372 273 TEEEELEIAALELEALEE 290
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
774-877 |
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 147647143 774 EKSIAQLIEKEEQRKEVQNQLVDREHKLANL-HQKTKVQEEKIKTLQKEREDKEETIDILRKELS------RTEQIRKEL 846
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELeEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|.
gi 147647143 847 SIKASSLEVQKAQLEGRLEEKESLVKLQQEE 877
Cdd:PRK00409 603 SVKAHELIEARKRLNKANEKKEKKKKKQKEK 633
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
639-903 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 639 RLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLA---SMLREVERKNEELSVLLK--AQQVESERAQSDIEHLFQH 713
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqklSVADAARRQFEKAYELVCkiAGEVERSQAWQTARELLRR 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 714 NRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQneksiaqliekEEQRKEVQNQ 793
Cdd:COG3096 504 YRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL-----------EAQLEELEEQ 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 794 LVDREHKLANLHQktkvQEEKIKTLQKEREDKEEtidILRKELSRTEQIRKELSIK-ASSLEVQKA-----QLEGRLEEK 867
Cdd:COG3096 573 AAEAVEQRSELRQ----QLEQLRARIKELAARAP---AWLAAQDALERLREQSGEAlADSQEVTAAmqqllEREREATVE 645
|
250 260 270
....*....|....*....|....*....|....*...
gi 147647143 868 ESLVKLQQEELNKHshmiamIHSLS--GGKINPETVNL 903
Cdd:COG3096 646 RDELAARKQALESQ------IERLSqpGGAEDPRLLAL 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
777-900 |
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 147647143 777 IAQLIEKEEQRKEvqnQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEEtIDILRKELSRTEQirKELSIKASSLEVQ 856
Cdd:TIGR02169 165 VAEFDRKKEKALE---ELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEG--YELLKEKEALERQ 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 147647143 857 KAQLEGRLEEKE-SLVKLQQE--ELNKHSHMIAMIHSLSGGKINPET 900
Cdd:TIGR02169 239 KEAIERQLASLEeELEKLTEEisELEKRLEEIEQLLEELNKKIKDLG 285
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
671-888 |
1.79e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 671 EARTLASMLREVERKNEELSV----LLKAQQVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMEllQRNESTEKKNK 746
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLD--SKRTSWLNALA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 747 DLQ-ITCDSLNKQIETV-KKLNESLKEQNEKsiaqLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKiktlQKERED 824
Cdd:PRK01156 576 VISlIDIETNRSRSNEIkKQLNDLESRLQEI----EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN----KILIEK 647
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 825 KEETIDILRKELSRTEQI---RKELSIKASSLEVQKAQLEGRLE-------EKESLVKLQQEELNKHSHMIAMI 888
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIipdLKEITSRINDIEDNLKKSRKALDdakanraRLESTIEILRTRINELSDRINDI 721
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
769-877 |
1.86e-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: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 769 LKEQNEKSIAQlIEKEEQRKEVQNqlvDREHKLANLHQKTKVQEEKI----KTLQKEREDKEETID---ILRKELSRTEQ 841
Cdd:COG2268 197 IIRDARIAEAE-AERETEIAIAQA---NREAEEAELEQEREIETARIaeaeAELAKKKAEERREAEtarAEAEAAYEIAE 272
|
90 100 110
....*....|....*....|....*....|....*.
gi 147647143 842 IRKELSIKAsSLEVQKAQLEGRLEEKESLVKLQQEE 877
Cdd:COG2268 273 ANAEREVQR-QLEIAEREREIELQEKEAEREEAELE 307
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
629-846 |
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 147647143 629 KLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEARTLASMLREVERKNEELsvllkaqqvESERAQSDIE 708
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---------EELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 709 HLFQHNRKL--ESVAEEHEILTKSYmELLQRNESTEKKNKDLQITCDSLNKQIETVKKLN--ESLKEQNEKSIAQLIEKE 784
Cdd:COG4717 367 ELEQEIAALlaEAGVEDEEELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 785 EQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRT--EQIRKEL 846
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEllEEAREEY 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
673-876 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 673 RTLASMLREVERKNEELSVLLKAQ-----QVESERAQSDIEHLFQHNRKLESVAEEHEILTKSYMELLQRNESTEKKNKd 747
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRsqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 748 LQITCDSLNKQIETVKKLNESLKEQNEK------------SIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTkvqeeki 815
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERinrarkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR------- 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 147647143 816 KTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEvqkaQLEGRLEEKESLVKLQQE 876
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE----ISCQQHTLTQHIHTLQQQ 387
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
682-885 |
2.72e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 41.26 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 682 VERKNEELSVLLKAQQVESEraqsdiEHLFQHNRKLESVAEEHEiltKSYMELLQRNESTEKKNKDLQ-------ITCDS 754
Cdd:COG5059 348 SSREIEEIKFDLSEDRSEIE------ILVFREQSQLSQSSLSGI---FAYMQSLKKETETLKSRIDLImksiisgTFERK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 755 LNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKER--EDKEETIDIL 832
Cdd:COG5059 419 KLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKasKLRSSASTKL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 147647143 833 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMI 885
Cdd:COG5059 499 NLRSSRSHSKFRDHLNGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSL 551
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
807-881 |
2.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147647143 807 KTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKH 881
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
648-876 |
2.89e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 648 ALALAQADRLIAQHRcQRTQAETE-ARTLASMLREVERKNEELsvLLKAQQVESERAQSDIEHLfqhnrkLESVAEEHEI 726
Cdd:NF041483 181 AAARAEAERLAEEAR-QRLGSEAEsARAEAEAILRRARKDAER--LLNAASTQAQEATDHAEQL------RSSTAAESDQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 727 LTKSYMELL----QRNESTEKKNKDLQITCDSL--------NKQIETVKKLNESLKEQNEKSIAQLI-----EKEEQRKE 789
Cdd:NF041483 252 ARRQAAELSraaeQRMQEAEEALREARAEAEKVvaeakeaaAKQLASAESANEQRTRTAKEEIARLVgeatkEAEALKAE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 790 VQNQLVDR----EHKLANLHQK--TKVQEEKIKTLQKEREDKEETIDILRKELSRT--------EQIRKELSIKASSLEV 855
Cdd:NF041483 332 AEQALADAraeaEKLVAEAAEKarTVAAEDTAAQLAKAARTAEEVLTKASEDAKATtraaaeeaERIRREAEAEADRLRG 411
|
250 260 270
....*....|....*....|....*....|
gi 147647143 856 QKA----QLEGRL-----EEKESLVKLQQE 876
Cdd:NF041483 412 EAAdqaeQLKGAAkddtkEYRAKTVELQEE 441
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
597-877 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 597 IEELIEKLQSGMVVKDQICDV-----RISDI-MDVYEMKlSTLASKESRLQDLLETkalalaqadrLIAQHRCQRTQAET 670
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDwertrRIAEAeMQLGHLE-VLLDQKEKENIHLREE----------LHRRNQLQPDPAKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 671 EA-RTLASM----LREVERKNEELSvllkaQQVESERAQSDIeHLFQHNRKLES--VAEEHEILTKSYMELLQRNES-TE 742
Cdd:pfam10174 229 KAlQTVIEMkdtkISSLERNIRDLE-----DEVQMLKTNGLL-HTEDREEEIKQmeVYKSHSKFMKNKIDQLKQELSkKE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 743 KKNKDLQITCDSLNKQIETVKK----LNESL--KEQnEKSIAQ---------LIEKEEQRKEVQNQLVDRE-------HK 800
Cdd:pfam10174 303 SELLALQTKLETLTNQNSDCKQhievLKESLtaKEQ-RAAILQtevdalrlrLEEKESFLNKKTKQLQDLTeekstlaGE 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 147647143 801 LANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEE 877
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 ... |
753-869 |
3.29e-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: 38.39 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 753 DSLNKQIETVKKLNESLKEQNEKSIAQLiekEEQRKEVQNQLVDREHKLANlhqktkvQEEKIKTLQKEREDKEETIDIL 832
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDL---EKQAEIAREAQQNYERELVL-------HAEDIKALQALREELNELKAEI 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 147647143 833 RKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKES 869
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
774-879 |
3.35e-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: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 774 EKSIAQLIEKEEQRKEVQNQLVDREHKLANLHQ------KTKVQEEKIKTLQKEREDKEET---IDILRKELSRTEQIRK 844
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASsddLAALEEQLEELEAELE 702
|
90 100 110
....*....|....*....|....*....|....*
gi 147647143 845 ELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELN 879
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
724-878 |
3.43e-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: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 724 HEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEK------EEQRK--EVQNQLV 795
Cdd:pfam08614 2 FLELIDAYNRLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQlreelaELYRSrgELAQRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 796 DREHKLANLHQKTKVQEEKIKTLQKERedkeetidilrkelsrteqirkelsikaSSLEVQKAQLEGRLEEKESLVKLQQ 875
Cdd:pfam08614 82 DLNEELQELEKKLREDERRLAALEAER----------------------------AQLEEKLKDREEELREKRKLNQDLQ 133
|
...
gi 147647143 876 EEL 878
Cdd:pfam08614 134 DEL 136
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
722-902 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 722 EEHEILTK--SYMELLQRNESTEKKN-KDLQITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQNQLVDRE 798
Cdd:pfam10174 356 EKESFLNKktKQLQDLTEEKSTLAGEiRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 799 HKLANLHQKTKVQEEKIKTL--QKEREDKE----------------ETIDILRKELSRTEQIRKELSIKASSLEVQKAQL 860
Cdd:pfam10174 436 TALTTLEEALSEKERIIERLkeQREREDRErleeleslkkenkdlkEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 147647143 861 EGRLEEKESLVKLQQEELNKHSHMIAMIHSL-SGGKINPETVN 902
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAeEAVRTNPEIND 558
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
601-868 |
4.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 601 IEKLQSG-MVVKDQICDVR--ISDIMDVYE---MKLSTLASKESRLQDLLETKALALAQADRLIAQHRC---QRTQAETE 671
Cdd:PRK01156 161 INSLERNyDKLKDVIDMLRaeISNIDYLEEklkSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 672 ARTLASMLREVERKNEELSvllkaqqveseRAQSDIEHLFQHNRKLESVAEEHEILTKSYMeLLQRNE---------STE 742
Cdd:PRK01156 241 LNELSSLEDMKNRYESEIK-----------TAESDLSMELEKNNYYKELEERHMKIINDPV-YKNRNYindyfkyknDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 743 KKNKDLQITCDSLNKQIETVKKLNESLKEQNeksiaQLIEKEEQRKEVQNQLVDrehkLANLHQKTKVQEEKIKTLQKER 822
Cdd:PRK01156 309 NKKQILSNIDAEINKYHAIIKKLSVLQKDYN-----DYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIESLKKKI 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 147647143 823 EDKEETIDILRKELSRT---------------EQIRKEL---SIKASSLEVQKAQLEGRLEEKE 868
Cdd:PRK01156 380 EEYSKNIERMSAFISEIlkiqeidpdaikkelNEINVKLqdiSSKVSSLNQRIRALRENLDELS 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
748-878 |
4.86e-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: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 748 LQITCDSLNKQIETVKKLNESLKEQNE--KSIAQLIEKEEQRKEVQNQLVDREHKLANLhQKTKVQeekIKTLQKEREDK 825
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERL-DASSDD---LAALEEQLEEL 697
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 147647143 826 EETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEEL 878
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
617-880 |
5.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 617 VRISDIMDVYEMKLSTLASKESRLQDLLETKALALAQADRLiaqhrcqrtqaETEARTLASMLREVERKNEEL------- 689
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELeerhely 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 690 ----SVLLKAQQVESERAQSDIEHLfqhNRKLESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQIETVKKL 765
Cdd:PRK03918 365 eeakAKKEELERLKKRLTGLTPEKL---EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 766 NESLKEQNEKSI------------AQLIEKEEQRKEVQNQLVDREHKLANlhQKTKVQEEKIKTLQKEREDKEETIDIlr 833
Cdd:PRK03918 442 GRELTEEHRKELleeytaelkrieKELKEIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKELEEKLKKYNL-- 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 147647143 834 KELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKlQQEELNK 880
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK-KLAELEK 563
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
674-831 |
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 147647143 674 TLASMLREVERKNEELSVLLKAQQveseRAQSDIEHLFQHNRkleSVAEEHEiltKSYMELLQRNESTEKKNKDLQITCD 753
Cdd:smart00435 232 TLQEQLKELTAKDGNVAEKILAYN----RANREVAILCNHQR---TVSKTHE---KSMEKLQEKIKALKYQLKRLKKMIL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 754 SLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQRKEVQnqlvdrehklanlhqKTKVQ----EEKIKTLQKEREDKEETI 829
Cdd:smart00435 302 LFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEE---------------KKKKQierlEERIEKLEVQATDKEENK 366
|
..
gi 147647143 830 DI 831
Cdd:smart00435 367 TV 368
|
|
| COG5134 |
COG5134 |
Uncharacterized conserved protein [Function unknown]; |
739-860 |
6.19e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227463 Cd Length: 272 Bit Score: 39.68 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 739 ESTEKKNKDLQITCDSLNKQiETVKKLNESL-KEQNEKSIAQlIEKEEQRKEVQNQLVDREHKLANLHQKTKVQEEKIKT 817
Cdd:COG5134 103 ESGGRRKIEPQDINEDPAKA-ENVEKVPESDaIEALEKQLTQ-QKSEKHNSSAINFIDELNKRLWSDPFVSSQRLRKQFR 180
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 147647143 818 LQKEREDKEETidilrKELSRTEQIRKELSIKASSLEVQKAQL 860
Cdd:COG5134 181 ERKKIEKKQEA-----KDLSLKNRAALDIDILPSSSDKDKALL 218
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
717-833 |
7.21e-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: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 717 LESVAEEHEILTKSYMELLQRNESTEKKNKDLQITCDSLNKQ---IETVKKLNESLKEQNEKS----IAQLIEKEEQRKE 789
Cdd:pfam02841 178 LQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEqelLREKQKEEEQMMEAQERSyqehVKQLIEKMEAERE 257
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 147647143 790 VQNQLVDREhklanLHQKTKVQEEKIKT-LQKEREDKEETIDILR 833
Cdd:pfam02841 258 QLLAEQERM-----LEHKLQEQEELLKEgFKTEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
800-886 |
7.26e-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: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 800 KLANLHQKTKVQEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELN 879
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
....*..
gi 147647143 880 KHSHMIA 886
Cdd:COG4942 101 AQKEELA 107
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
749-880 |
7.47e-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: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 749 QITCDSLNKQIETVKKLNESLKEQNEKSIAQLIEKEEQ---RKEVQNQLVDREHKLANLHQKTKVQEEKIKTLQKEREDK 825
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKerlKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 147647143 826 EETIDILRKELSRTEQIRkelSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNK 880
Cdd:pfam11600 81 EKAEKLRLKEEKRKEKQE---ALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
811-886 |
8.86e-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: 8.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147647143 811 QEEKIKTLQKEREDKEETIDILRKELSRTEQIRKELSIKASSLEVQKAQLEGRLEEKESLVKLQQEELNKHSHMIA 886
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
613-797 |
9.60e-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: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 613 QICDVRISDImdvyEMKLSTLASKESRLQDLLETKALALAQADRLIAQHRCQRTQAETEartlasmLREVERKNEELSVL 692
Cdd:COG1579 13 QELDSELDRL----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-------IEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147647143 693 LKaqQVESERAQSDIEHLFQHNRKLESVAEEHEIltksymELLQRNESTEKKNKDLQITCDSLNKQIETVKKLNESLKEQ 772
Cdd:COG1579 82 LG--NVRNNKEYEALQKEIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....*.
gi 147647143 773 NEKSIAQLIEK-EEQRKEVQNQLVDR 797
Cdd:COG1579 154 LEAELEELEAErEELAAKIPPELLAL 179
|
|
| |
