|
Name |
Accession |
Description |
Interval |
E-value |
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
25-197 |
3.23e-27 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 110.65 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 25 DKGLHSISELSLDSSIHAINLHCNNISKISSIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNLITRVEGLEALV 104
Cdd:cd21340 11 DKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 105 N------------------------------LTKLNLSYNHINDLSGLMPLHglkyKLRYIDLHSNYIDSIHHLLQCTVG 154
Cdd:cd21340 91 NleelhienqrlppgekltfdprslaalsnsLRVLNISGNNIDSLEPLAPLR----NLEQLDASNNQISDLEELLDLLSS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254675308 155 LHFLTNLILEkdgeGNPICLIPGYRAIILQTLPQLRILDCKNI 197
Cdd:cd21340 167 WPSLRELDLT----GNPVCKKPKYRDKIILASKSLEVLDGKEI 205
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
30-196 |
1.96e-12 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 70.35 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 30 SISELSLDSSIHAINLHCNNISKISSIDHIWNLRHLDLSSNQISQI-EGLNTLTKLCTLNLSCNLITRV-EGLEALVNLT 107
Cdd:COG4886 83 SLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 108 KLNLSYNHINDLSglMPLHGLKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLIPGyraiILQTLP 187
Cdd:COG4886 163 SLDLSNNQLTDLP--EELGNLT-NLKELDLSNNQITDLPEPLG---NLTNLEELDL----SGNQLTDLPE----PLANLT 228
|
....*....
gi 254675308 188 QLRILDCKN 196
Cdd:COG4886 229 NLETLDLSN 237
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
43-222 |
2.85e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 66.88 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 43 INLHCNNISKIS-SIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNLITRVEGLEALVNLTKLNLSYNHINDLS- 120
Cdd:COG4886 210 LDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 121 GLMPLHGLKYKLRYIDLHSNYIDSIHHLLQCTVGLHFLTNLILEKDGEGNPICLIPGYRAIILQTLPQLRILDCKNIFGE 200
Cdd:COG4886 290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTL 369
|
170 180
....*....|....*....|..
gi 254675308 201 PVSLEEINSSHLQCLEGLLDNL 222
Cdd:COG4886 370 GLLGLLEATLLTLALLLLTLLL 391
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
646-1026 |
6.49e-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: 63.54 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 646 RRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDD 725
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 726 KQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcRENESLRKSHESDCDA 805
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 806 LRikcKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEkcsqEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKEL 885
Cdd:TIGR02168 836 TE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELE----SELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 886 ELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKErklkaerdkSLELqkDAMEKLQNMDDAFRRQVDEIVEAH 965
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---------SLTL--EEAEALENKIEDDEEEARRRLKRL 977
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675308 966 QAEIMQLANekqkyidcANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 1026
Cdd:TIGR02168 978 ENKIKELGP--------VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
656-1011 |
9.17e-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: 63.16 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 656 EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELL 735
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 736 KHEKTQLISELAAKESLIyglrterkvwgqelacqsstlsqsrGKLEAQIESLCReneslRKSHESdcdaLRIKCKIIED 815
Cdd:TIGR02169 757 KSELKELEARIEELEEDL-------------------------HKLEEALNDLEA-----RLSHSR----IPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 816 QNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQE---QLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 892
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 893 AystlnkkwhdkgelLSHLEMQVKEVKEKF---EDKERKLKAERDKSLELQKDAMEKLQN-------MDDAFRRQVDE-- 960
Cdd:TIGR02169 883 R--------------LGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSELKAKLEAleeelseIEDPKGEDEEIpe 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 254675308 961 ---IVEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEK 1011
Cdd:TIGR02169 949 eelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
423-1010 |
1.22e-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: 62.77 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 423 QLDQEREMRWKAEQTEkkLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIELM 502
Cdd:TIGR02168 333 DELAEELAELEEKLEE--LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 503 KARDQQEDHIRHLRTLERALEKMEkqkaqqqaaqirlIQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEH 582
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 583 RQeieTRQFFTDAEFQDALTKRLCKEERKHEQEVKEY---QEKIDILNQQYLDL---ENEFRIALTVEARRF------KD 650
Cdd:TIGR02168 478 DA---AERELAQLQARLDSLERLQENLEGFSEGVKALlknQSGLSGILGVLSELisvDEGYEAAIEAALGGRlqavvvEN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 651 VQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSeVCKLKQEAAANLQNQINTL--EILIEDDKQK 728
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKALSYLlgGVLVVDDLDN 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 729 SIQIELLKHEKTQLIS---ELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDA 805
Cdd:TIGR02168 634 ALELAKKLRPGYRIVTldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 806 LRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQE----------QLNEKSSQLDSIVEKLERHNERKEK 875
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleeRLEEAEEELAEAEAEIEELEAQIEQ 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 876 LKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKdAMEKLQNMDDAFR 955
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-EIEELEELIEELE 872
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 254675308 956 RQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGLLDETCKNKKMMEE 1010
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEE-LSEELRELESKRSELRRELEELREKLAQ 926
|
|
| LRR_9 |
pfam14580 |
Leucine-rich repeat; |
65-197 |
1.34e-08 |
|
Leucine-rich repeat;
Pssm-ID: 405295 [Multi-domain] Cd Length: 175 Bit Score: 55.54 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 65 LDLSSNQISQIEGLNTLTKLCTLNLSCNLITRV-EGL-EALVNLTKLNLSYNHINDLSGLMPLHGLKyKLRYIDLHSNyi 142
Cdd:pfam14580 47 IDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLK-KLTFLSLLRN-- 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 254675308 143 dsihhllqctvglhfltnlilekdgegnPICLIPGYRAIILQTLPQLRILDCKNI 197
Cdd:pfam14580 124 ----------------------------PVTNKPHYRLYVIYKVPQLRLLDFRKV 150
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
544-840 |
2.27e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 544 ELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRqEIETRQFFTDAEFQdalTKRLCKEERkhEQEVKEYQEKI 623
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLE---ELRLEVSEL--EEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 624 DILNQQYLDLENEFRIAltveARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKL 703
Cdd:TIGR02168 291 YALANEISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 704 KQEaaanLQNQINTLEILIEDDKQKSIQielLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGK-LE 782
Cdd:TIGR02168 367 LEE----LESRLEELEEQLETLRSKVAQ---LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQ 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675308 783 AQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQ 840
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
417-1026 |
2.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 417 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKD----VHSQALITTDRLKDAIFKERHCKAQLEIIV---HR 489
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevseLEEEIEELQKELYALANEISRLEQQKQILRerlAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 490 LQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRL---IQEVELKASAADREINLLRTSLHQEKQ 566
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeLEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 567 QVQQLhellalkeQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRialtvear 646
Cdd:TIGR02168 394 QIASL--------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-------- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 647 rfkDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDK 726
Cdd:TIGR02168 458 ---RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 727 QKSIQIELLKHEKTQ--LISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcRENESLRKSHESDCD 804
Cdd:TIGR02168 534 GYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 805 ALRI-------KCKIIEDQNETIRKLKDSLQE-----KDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNER 872
Cdd:TIGR02168 613 KLRKalsyllgGVLVVDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 873 KEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEK-----------------FEDKERKLKAERDK 935
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleeriaqlskelteLEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 936 SLELQKDAMEKLQNMD---DAFRRQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGL---LDETCKNKKMME 1009
Cdd:TIGR02168 773 AEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLNEEAAN-LRERLESLERRIAATerrLEDLEEQIEELS 851
|
650
....*....|....*..
gi 254675308 1010 EKIKQLACAISEIQKEM 1026
Cdd:TIGR02168 852 EDIESLAAEIEELEELI 868
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
435-1025 |
3.55e-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: 57.72 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 435 EQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEiivhRLQNEVKKLTIELMKARDQQEDHIRH 514
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN----KLNSDLSKINSEIKNDKEQKNKLEVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 515 LRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFFTD 594
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 595 AEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFrialtvearrfKDVQDGFEDVATELAKSKHALIWAQR 674
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI-----------SNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 675 KENESSSLIKDLTCMVKEQKTKLSEVCKLKQeaaanlQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELaakESLIY 754
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKE------QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL---NEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 755 GLRTERKvwgqELACQSSTLSQSRGKLEAQIESLCRENESLR---KSHESDCDALRIKCKIIEDQN----ETIRKLKDSL 827
Cdd:TIGR04523 346 QLKKELT----NSESENSEKQRELEEKQNEIEKLKKENQSYKqeiKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 828 QEKDGQIKLLQEQIALiEKCSQEQLNEKSSQLDSIVEKLERhneRKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGEL 907
Cdd:TIGR04523 422 ELLEKEIERLKETIIK-NNSEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 908 LSHLEMQVKEVKEKFED----------KERKLKAERDKSLELQKDAMEKLQNMDDAFRR-QVDEIVEAHQAEIMQLANEk 976
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDltkkisslkeKIEKLESEKKEKESKISDLEDELNKDDFELKKeNLEKEIDEKNKEIEELKQT- 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 254675308 977 QKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
467-1025 |
1.61e-07 |
|
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: 55.84 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 467 DRLKDAifKERHCKAQLEIivHRLQNEVKKLTIEL---MKARDQQEDHIRHLRTLERALE-KMEKQKAQQQAAQIRLIQE 542
Cdd:TIGR02169 315 RELEDA--EERLAKLEAEI--DKLLAEIEELEREIeeeRKRRDKLTEEYAELKEELEDLRaELEEVDKEFAETRDELKDY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 543 VElKASAADREINLLRTSLHQEKQQVQQLHELLAlkeqEHRQEIEtRQFFTDAEFQDALtKRLCKEERKHEQEVKEYQEK 622
Cdd:TIGR02169 391 RE-KLEKLKREINELKRELDRLQEELQRLSEELA----DLNAAIA-GIEAKINELEEEK-EDKALEIKKQEWKLEQLAAD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 623 IDILNQQYLDLENEFRialtvearrfkDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCK 702
Cdd:TIGR02169 464 LSKYEQELYDLKEEYD-----------RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 703 LKQEAAANLQ----NQINTleILIEDDKQKSIQIELLKHEK--------------------------------------- 739
Cdd:TIGR02169 533 VGERYATAIEvaagNRLNN--VVVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdp 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 740 ------------TQLISELAAKESLIYGLR---------------TERKVWGQELACQSSTLSQSRGKLEAQIESLCREN 792
Cdd:TIGR02169 611 kyepafkyvfgdTLVVEDIEAARRLMGKYRmvtlegelfeksgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 793 ESLRK---SHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIAL-IEKCSQEQLNEKSSqLDSIVEKLER 868
Cdd:TIGR02169 691 SSLQSelrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLEQEIENVKSE-LKELEARIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 869 HNERKEKLKQQLKAKELEL-----EEIRKAYSTLNKKWHDKGELLSHLE--MQVKEVKEKFEDKERKLKAERDKSLELQK 941
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEqkLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 942 DAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEK---QKYIDCANLKVQQVEDEMRGL---LDETCKNKKMMEEKIKQL 1015
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEAL 929
|
650
....*....|
gi 254675308 1016 ACAISEIQKE 1025
Cdd:TIGR02169 930 EEELSEIEDP 939
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
848-1026 |
1.70e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 848 SQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKER 927
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 928 KLKAERDKsLELQKDAMEKL------------QNMDDAFRRQ--VDEIVEAHQAEIMQLANEKQKyIDCANLKVQQVEDE 993
Cdd:COG4942 98 ELEAQKEE-LAELLRALYRLgrqpplalllspEDFLDAVRRLqyLKYLAPARREQAEELRADLAE-LAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|...
gi 254675308 994 MRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 1026
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
421-994 |
1.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 421 VEQLDQERE-----MRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEiivhRLQNEVK 495
Cdd:COG1196 202 LEPLERQAEkaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 496 KLTIELmkaRDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELL 575
Cdd:COG1196 278 ELELEL---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 576 ALKEQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGF 655
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 656 EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAAnLQNQINTLEILIEDDKQKSIQIELL 735
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 736 KHEKTQ------LISELAAKESLIYGLRTERKVWGQELACQSStlsqsrGKLEAQIESLCRENESLRKSHESDcdalrik 809
Cdd:COG1196 514 LLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDD------EVAAAAIEYLKAAKAGRATFLPLD------- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 810 ckiIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDsiVEKLERHNERKEKLKQQLKAKELELEE 889
Cdd:COG1196 581 ---KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV--AARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 890 IRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEI 969
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580
....*....|....*....|....*
gi 254675308 970 MQLANEKQKYIDCANLKVQQVEDEM 994
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPP 760
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-984 |
2.16e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 372 RKMRQPYLRDLYVRSSLVNCNNLRDLDEQKTGVIKVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDY---IDEL 448
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 449 HKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQ---NEVKKLTIELMKA----RDQQEDHIRHLRTLERA 521
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkaDAAKKKAEEKKKAdeakKKAEEDKKKADELKKAA 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 522 LEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSlhQEKQQVQQLHEllalKEQEHRQEIETRQFFTDAEFQDAL 601
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKK----KAEEAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 602 TKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGFEDV--ATELAKSKHALIWAQRKENES 679
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAEE 1568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 680 SSLIKDLtcmvKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTE 759
Cdd:PTZ00121 1569 AKKAEED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 760 RKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQN--ETIRKLKDSLQEKDGQIKLL 837
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKA 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 838 QEqialIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMqvke 917
Cdd:PTZ00121 1725 EE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV---- 1796
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675308 918 vkekfedkERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQL--ANEKQKYIDCAN 984
Cdd:PTZ00121 1797 --------DKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLeeADAFEKHKFNKN 1857
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
480-1025 |
2.16e-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: 55.12 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 480 KAQLEIIVHRLQNEVKKLTIELMKARDQQEDHIRHLRT----LERALEKMEKQKAQQQAAQIRLIQEVELKASAADREIN 555
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 556 LLRTS-------LHQEKQQVQQLHELLaLKEQEHRQEIetRQFFTDaeFQDALTKRLCKEERKHEQEVKEYQEKIDILNQ 628
Cdd:pfam15921 153 ELEAAkclkedmLEDSNTQIEQLRKMM-LSHEGVLQEI--RSILVD--FEEASGKKIYEHDSMSTMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 629 QyLDLENEFrialtVEARRFKdVQDGFEDVATElAKSKHALIWAQRKENessslIKDLTCMVKEQKTKLSEVCKLKQEAA 708
Cdd:pfam15921 228 E-LDTEISY-----LKGRIFP-VEDQLEALKSE-SQNKIELLLQQHQDR-----IEQLISEHEVEITGLTEKASSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 709 ANLQNQintLEILIEDDKQKSI----QIELLKHEKTQLISEL-AAK---ESLIYGLRTERKVWGQELA---CQSSTLSQS 777
Cdd:pfam15921 295 NSIQSQ---LEIIQEQARNQNSmymrQLSDLESTVSQLRSELrEAKrmyEDKIEELEKQLVLANSELTearTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 778 RGKLEAQIESLC-----RENE-SLRKSHES-----------DCDALRikcKIIEDQNETIRKLKDSLQ----EKDGQikl 836
Cdd:pfam15921 372 SGNLDDQLQKLLadlhkREKElSLEKEQNKrlwdrdtgnsiTIDHLR---RELDDRNMEVQRLEALLKamksECQGQ--- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 837 LQEQIALIEKcsqeqLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVK 916
Cdd:pfam15921 446 MERQMAAIQG-----KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 917 EVKEKFEdkerkLKAERDKSLELQKDAMEKLQNMDDAFRRQV---DEIVEAHQAEI---MQLANEKQKYIDCANLKVQQV 990
Cdd:pfam15921 521 KLRSRVD-----LKLQELQHLKNEGDHLRNVQTECEALKLQMaekDKVIEILRQQIenmTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590
....*....|....*....|....*....|....*...
gi 254675308 991 EDEM---RGLLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:pfam15921 596 EKEIndrRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
690-942 |
3.06e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 690 VKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQLISELAAKESLIYGLRTERkvwgqelac 769
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKA---EIEELTDELLNLVMDIEDPSAALNKLNTAA--------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 770 qsstlsqsrGKLEAQIESLCRENESLRKSHEsdCDAlrikCK-IIEDQNETIRKLKDSLQEKDGQIKLLQEQIaliekcs 848
Cdd:PHA02562 265 ---------AKIKSKIEQFQKVIKMYEKGGV--CPT----CTqQISEGPDRITKIKDKLKELQHSLEKLDTAI------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 849 qEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERK 928
Cdd:PHA02562 323 -DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....
gi 254675308 929 lKAERDKSLELQKD 942
Cdd:PHA02562 402 -KYHRGIVTDLLKD 414
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
507-892 |
3.64e-07 |
|
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: 54.13 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 507 QQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVQQLhellalkeqEHRQEI 586
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL---------EEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 587 ETRQFFTDAEFQDALTKrlckEERKHEQEVKEYQEKIDILNQQYLDLENEF-RIALTVE--ARRFKDVQDGFEDVATELa 663
Cdd:pfam07888 106 LSASSEELSEEKDALLA----QRAAHEARIRELEEDIKTLTQRVLERETELeRMKERAKkaGAQRKEEEAERKQLQAKL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 664 kskhaliwaQRKENESSSLIKDLtcmvKEQKTKLSEvcklKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLI 743
Cdd:pfam07888 181 ---------QQTEEELRSLSKEF----QELRNSLAQ----RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 744 SELAAKESLIYGLRTERKVWGQ--------------ELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDAlrik 809
Cdd:pfam07888 244 ERLNASERKVEGLGEELSSMAAqrdrtqaelhqarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR---- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 810 ckiIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERhnERKEKLKQQLKAKELeLEE 889
Cdd:pfam07888 320 ---IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV--AQKEKEQLQAEKQEL-LEY 393
|
...
gi 254675308 890 IRK 892
Cdd:pfam07888 394 IRQ 396
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
813-991 |
7.72e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 813 IEDQNETIRKLKDSLQEKDGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEE-IR 891
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 892 KAYST----------LNKKwhDKGELLSHLEM-------------QVKEVKEKFEDKERKLKAERD------KSLELQKD 942
Cdd:COG3883 94 ALYRSggsvsyldvlLGSE--SFSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAelealkAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675308 943 AMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANLKVQQVE 991
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
813-1025 |
1.53e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 813 IEDQNETIRKLKDSLQEKDGQIKLLQEQ----IALIEKCSQE----------QLNEKSSQLDSIVEKLERHNERKEKLKQ 878
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQaekaERYKELKAELrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 879 QLKAKELELEEIRKAYSTLNKK-------WHDKGELLSHLEMQVKEVKEKFEDKERKLK------AERDKSLELQKDAME 945
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEieelqkeLYALANEISRLEQQKQILRERLANLERQLEeleaqlEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 946 KLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCanlkvQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEEL-----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
445-975 |
1.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 445 IDELHKQADE-KKDVHSQALITTDRLKDAIFKERHCKAQLEIIvHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALE 523
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 524 KMEKQKAQQQAAqiRLIQEVELKASAADREINLLRTSLHQEKQQVQQLHELlalkEQEHRQEIETRQFFTDAEFQDALTK 603
Cdd:COG4717 127 LLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAEL----QEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 604 --RLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSS 681
Cdd:COG4717 201 leELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 682 LIKDLTCMVKEQKTKlSEVCKLKQEAAANLQNQINTLEiliedDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERK 761
Cdd:COG4717 281 LVLGLLALLFLLLAR-EKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 762 VWGQElacqsstlsqsrgKLEAQIESLCRENESL-RKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQ 840
Cdd:COG4717 355 EAEEL-------------EEELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 841 IALIEKcsqEQLNEKSSQLDsivEKLERHNERKEKLKQQLKAKELELEEIRkaystlnkkwhdKGELLSHLEMQVKEVKE 920
Cdd:COG4717 422 LEALDE---EELEEELEELE---EELEELEEELEELREELAELEAELEQLE------------EDGELAELLQELEELKA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 254675308 921 KFEDkerklKAERDKSLELQKDAMEKLQnmddafrrqvDEIVEAHQAEIMQLANE 975
Cdd:COG4717 484 ELRE-----LAEEWAALKLALELLEEAR----------EEYREERLPPVLERASE 523
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
82-142 |
2.71e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 45.59 E-value: 2.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675308 82 TKLCTLNLSCNLITRVEG--LEALVNLTKLNLSYNHINDLSGLMpLHGLKyKLRYIDLHSNYI 142
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPGA-FSGLP-SLRYLDLSGNRL 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
420-979 |
2.93e-06 |
|
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: 51.51 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 420 LVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQ--NEVKKL 497
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQklQSLCKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 498 TIELMKARDQQEDHIRHLRTLER---ALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQ---VQQL 571
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQlqtKEQI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 572 HELLALKEQEH---------------RQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKE----YQEKIDILNQQYLD 632
Cdd:TIGR00618 482 HLQETRKKAVVlarllelqeepcplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 633 LENEFRIaltvearrfkdvQDGFEDVATELAKSKHALIWAQRKENEssslIKDLTCMVKEQKTKLSEvckLKQEAAANLQ 712
Cdd:TIGR00618 562 KEQMQEI------------QQSFSILTQCDNRSKEDIPNLQNITVR----LQDLTEKLSEAEDMLAC---EQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 713 NQINTLEILIEdDKQKSIQIELLKHEKTQLISELAAKESLIYGLRT---ERKVWGQ---ELACQSSTLSQSRGKLE--AQ 784
Cdd:TIGR00618 623 PEQDLQDVRLH-LQQCSQELALKLTALHALQLTLTQERVREHALSIrvlPKELLASrqlALQKMQSEKEQLTYWKEmlAQ 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 785 IESLCRENES----LRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKdgQIKLLQEQIALIEKCSQEQLNE--KSSQ 858
Cdd:TIGR00618 702 CQTLLRELEThieeYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ--ARTVLKARTEAHFNNNEEVTAAlqTGAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 859 LDSIVEKLERHNERKEKLKQQLKAKELELEEIRKaystlnkkwHDKGELLSHLEMQVKE---VKEKFEDKERKLKAERDK 935
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP---------SDEDILNLQCETLVQEeeqFLSRLEEKSATLGEITHQ 850
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 254675308 936 SLELQKDAMEKLQNMDDAFR--RQVDEIVEAHQAEIMQLANEKQKY 979
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKiiQLSDKLNGINQIKIQFDGDALIKF 896
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
831-1025 |
3.10e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 831 DGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKaystlnkkwhdkgellsh 910
Cdd:COG3883 15 DPQIQAKQKELSEL----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 911 lemQVKEVKEKFEDKERKLKaERDKSLELQKDAMEKL------QNMDDAFRRQ--VDEIVEAhQAEIMQLANEKQKYIDC 982
Cdd:COG3883 73 ---EIAEAEAEIEERREELG-ERARALYRSGGSVSYLdvllgsESFSDFLDRLsaLSKIADA-DADLLEELKADKAELEA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 254675308 983 ANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
689-1026 |
3.65e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.73 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 689 MVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDD---KQKSIQ----IELLKHEKTQLISELAAKESLIYGLRTERK 761
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTlleKAKEIInieeALKGFQDPESELEDLAQTSDKLEKLVEQNT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 762 VWGQELACQSSTLSQsrgKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIR-----KLKDSLQEKDGQIKL 836
Cdd:COG5185 264 DLRLEKLGENAESSK---RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAaeaeqELEESKRETETGIQN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 837 LQEQIALIEKCSQEQLNEKSSQLDSIVEKlerhnERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKG-ELLSHLEMQV 915
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGE-----VELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAqEILATLEDTL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 916 KEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMR 995
Cdd:COG5185 416 KAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVS 495
|
330 340 350
....*....|....*....|....*....|.
gi 254675308 996 GLLDETCKNKKMMEEKIKQLACAISEIQKEM 1026
Cdd:COG5185 496 TLKATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
780-979 |
4.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 780 KLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIaliekcsqEQLNEKSSQL 859
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL--------EELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 860 DSIVEKLERHNERKEkLKQQLKAKELELEEIRKAYstlnKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLEL 939
Cdd:COG4717 122 EKLLQLLPLYQELEA-LEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254675308 940 QKDAMEKLQnmddAFRRQVDEIVEAHQAEIMQLANEKQKY 979
Cdd:COG4717 197 LAEELEELQ----QRLAELEEELEEAQEELEELEEELEQL 232
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
386-940 |
4.10e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 386 SSLVNCNNLRDLDEQKTGVIkvdknfsDNSTYRSLVEQLDQEREMRWKAEQTeKKLMD-------YIDELHKQADEKKdv 458
Cdd:pfam15921 356 SELTEARTERDQFSQESGNL-------DDQLQKLLADLHKREKELSLEKEQN-KRLWDrdtgnsiTIDHLRRELDDRN-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 459 hsqalITTDRLkDAIFK--ERHCKAQLEIIVHRLQ------NEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKA 530
Cdd:pfam15921 426 -----MEVQRL-EALLKamKSECQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 531 QQQAAqirlIQEVELKASAADREINLLRTSLHQEKQQVQQLHellalKEQEHRQEIETRQfftdaefqDALTKRLCKEER 610
Cdd:pfam15921 500 DLTAS----LQEKERAIEATNAEITKLRSRVDLKLQELQHLK-----NEGDHLRNVQTEC--------EALKLQMAEKDK 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 611 KheqevkeyqekIDILNQQyldLENEFRIAltvearrfkdVQDGFEDVATELAKSKhaliwAQRKENESSSLIKDLTCMV 690
Cdd:pfam15921 563 V-----------IEILRQQ---IENMTQLV----------GQHGRTAGAMQVEKAQ-----LEKEINDRRLELQEFKILK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 691 KEQKTKLSEvcklkqeaaanLQNQINTLEI----LIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQE 766
Cdd:pfam15921 614 DKKDAKIRE-----------LEARVSDLELekvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 767 LACQSSTLSQSRGKLEAQIESLCRENESLR---KSHE-SDCDALRIKCkiiedqnetirKLKDSLQEKDGQIKLLQEQIA 842
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlKSMEgSDGHAMKVAM-----------GMQKQITAKRGQIDALQSKIQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 843 LIEKCSQEQLNEKSSQldsiveklerhNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKF 922
Cdd:pfam15921 752 FLEEAMTNANKEKHFL-----------KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
570
....*....|....*...
gi 254675308 923 EDKERKLKAERDKSLELQ 940
Cdd:pfam15921 821 AECQDIIQRQEQESVRLK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
804-1025 |
9.80e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 804 DALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEqIALIEKCSQEQLNEKS-SQLDSIVEKLERHnerKEKLKQQLKA 882
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE-YEGYELLKEKEALERQkEAIERQLASLEEE---LEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 883 KELELEEIRKAYSTLNKKWHDKGELLShleMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEI- 961
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIe 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675308 962 -----VEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGlLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:TIGR02169 340 elereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE-FAETRDELKDYREKLEKLKREINELKRE 407
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
25-200 |
1.15e-05 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 49.02 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 25 DKGLHSISE-LSLDSSIHAINLHCNNISK------ISSIDHIWNLRHLDLSSNQISQ------IEGLNTLTKLCTLNLSC 91
Cdd:COG5238 194 DEGIEELAEaLTQNTTVTTLWLKRNPIGDegaeilAEALKGNKSLTTLDLSNNQIGDegvialAEALKNNTTVETLYLSG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 92 NLITrVEGLEALV-------NLTKLNLSYNHINDLSGLMPLHGLK--YKLRYIDLHSNYIDSihhllQCTVGL--HFLTN 160
Cdd:COG5238 274 NQIG-AEGAIALAkalqgntTLTSLDLSVNRIGDEGAIALAEGLQgnKTLHTLNLAYNGIGA-----QGAIALakALQEN 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675308 161 LILEK-DGEGNPICLIpGYRAII--LQTLPQLRILD-CKNIFGE 200
Cdd:COG5238 348 TTLHSlDLSDNQIGDE-GAIALAkyLEGNTTLRELNlGKNNIGK 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
774-978 |
1.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 774 LSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLN 853
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 854 EKSSQLDSIvEKLERHNERKEKLKQQlkaKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAER 933
Cdd:COG4942 105 ELAELLRAL-YRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254675308 934 DKsLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQK 978
Cdd:COG4942 181 AE-LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
780-974 |
2.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 780 KLEAQIESLcrenESLRKSHEsDCDALRIKCKIIEDQNETIRKLKDS--LQEKDGQIKLLQEQIALIEkcsqEQLNEKSS 857
Cdd:COG4913 246 DAREQIELL----EPIRELAE-RYAAARERLAELEYLRAALRLWFAQrrLELLEAELEELRAELARLE----AELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 858 QLDSIVEKLERHNERKEKLK-QQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKS 936
Cdd:COG4913 317 RLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190
....*....|....*....|....*....|....*...
gi 254675308 937 LELQKDAMEKLQNMDDAFRRQVDEIvEAHQAEIMQLAN 974
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRREL-RELEAEIASLER 433
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
417-981 |
2.71e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 417 YRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQ-----------------ADEKKDVHSQALITTDRLKDAI------ 473
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKeqeateellsleqklsvAQAAHSQFEQAYQLVRKIAGEVsrseaw 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 474 --FKE--------RHCKAQLEIIVHRLQnevkkltiELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEV 543
Cdd:PRK04863 496 dvAREllrrlreqRHLAEQLQQLRMRLS--------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 544 ElKASAADREINLLRTSLHQEKQQVQQLHELLALKEQEHR--QEIETR---QF---FTDAEFQDALTKRLCKEERKHEQE 615
Cdd:PRK04863 568 E-SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLaaQDALARlreQSgeeFEDSQDVTEYMQQLLERERELTVE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 616 VKEYQEKIDILNQQYLDL---ENEFRIALTVEARRFKDV--QDGFEDVATE--------LAKSKHALiwaqrkenesssL 682
Cdd:PRK04863 647 RDELAARKQALDEEIERLsqpGGSEDPRLNALAERFGGVllSEIYDDVSLEdapyfsalYGPARHAI------------V 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 683 IKDLtCMVKEQktklsevcklkqeaaanLQNQINTLE--ILIEDDKQK----SIQIELLKHEKTQLISEL---------- 746
Cdd:PRK04863 715 VPDL-SDAAEQ-----------------LAGLEDCPEdlYLIEGDPDSfddsVFSVEELEKAVVVKIADRqwrysrfpev 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 747 -----AAKESLIYGLRTERkvwgQELACQSSTLSQSRGKLEAQIESLCRE-NESLRKSHESDCDALrikckiIEDQNETI 820
Cdd:PRK04863 777 plfgrAAREKRIEQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFiGSHLAVAFEADPEAE------LRQLNRRR 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 821 RKLKDSLQEKDG-------QIKLLQEQIALIEKCS-----------QEQLNEKSSQLDSIVEK---LERHNERKEKLKQQ 879
Cdd:PRK04863 847 VELERALADHESqeqqqrsQLEQAKEGLSALNRLLprlnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPI 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 880 ---LKAKELELEEIRKAYSTLNKKWHDkgellshLEMQVKEVKE--------KFEDKERKLKAERDKSLELQKDaMEKLQ 948
Cdd:PRK04863 927 vsvLQSDPEQFEQLKQDYQQAQQTQRD-------AKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQR-LEQAE 998
|
650 660 670
....*....|....*....|....*....|...
gi 254675308 949 NMddafRRQVDEIVEAHQAeimQLANEKQKYID 981
Cdd:PRK04863 999 QE----RTRAREQLRQAQA---QLAQYNQVLAS 1024
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
809-1015 |
2.81e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 809 KCKIIEDQNETIRKLKDSLQEkdgQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELE 888
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQ---QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 889 EIRKAYSTLNK----------------KWHDKGELLSHLEMQVKEVKEKFEDKERKLKaERDKSLELQKDAMEKLQNMDD 952
Cdd:PHA02562 252 DPSAALNKLNTaaakikskieqfqkviKMYEKGGVCPTCTQQISEGPDRITKIKDKLK-ELQHSLEKLDTAIDELEEIMD 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675308 953 AFRRQVDEIVEAHQaeimQLANEKQKYIDCANlKVQQVEDEMRGLLDETCKNKKMMEEKIKQL 1015
Cdd:PHA02562 331 EFNEQSKKLLELKN----KISTNKQSLITLVD-KAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
542-1025 |
3.52e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 542 EVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEqEHRQEIETrqffTDAEFQDaLTKRLCKEERKHEqevkEYQE 621
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-ERREELET----LEAEIED-LRETIAETERERE----ELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 622 KIDILNQQYLDLENEFRIAL-----------TVEARRfKDVQDGFEDVATELAKSKHAliwAQRKENESSSLikdltcmv 690
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLaeaglddadaeAVEARR-EELEDRDEELRDRLEECRVA---AQAHNEEAESL-------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 691 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQLISELAAKESLIYGLRTERkvwgQELACQ 770
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGDAPVDLGNAEDFL----EELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 771 SSTLSQSRGKLEAQIESL---CRENESLRKshESDC--------DALRIKckIIEDQNETIRKLKDSLQEKDGQIKLLQE 839
Cdd:PRK02224 421 RDELREREAELEATLRTArerVEEAEALLE--AGKCpecgqpveGSPHVE--TIEEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 840 QIAliekcSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVK 919
Cdd:PRK02224 497 RLE-----RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 920 EKFEDKERKLkAERDKSLELQKDAMEKLQNMDDAfRRQVDEIVEaHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLD 999
Cdd:PRK02224 572 EEVAELNSKL-AELKERIESLERIRTLLAAIADA-EDEIERLRE-KREALAELNDERRERLAEKRERKRELEAEFDEARI 648
|
490 500 510
....*....|....*....|....*....|....
gi 254675308 1000 ETCKNKKM--------MEEKIKQLACAISEIQKE 1025
Cdd:PRK02224 649 EEAREDKEraeeyleqVEEKLDELREERDDLQAE 682
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
61-101 |
3.63e-05 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 41.85 E-value: 3.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 254675308 61 NLRHLDLSSNQISQIEGLNTLTKLCTLNLS-CNLITRVEGLE 101
Cdd:pfam12799 2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSgNNKITDLSDLA 43
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
467-766 |
3.71e-05 |
|
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: 47.76 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 467 DRLKdaifKERHCKAQLEIIVHRLQN-EVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQA---AQIRLIQE 542
Cdd:TIGR02169 201 ERLR----REREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 543 VELKASA-ADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQfFTDAEFQ------DALTKRLCKEERKHEQ- 614
Cdd:TIGR02169 277 LNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEIDkllaeiEELEREIEEERKRRDKl 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 615 --EVKEYQEKIDILNQQYLDLENEFRIALtveaRRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKE 692
Cdd:TIGR02169 356 teEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675308 693 QKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQE 766
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
507-930 |
4.94e-05 |
|
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: 47.37 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 507 QQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLR---TSLHQEKQQVQQLHELLALKEQEHR 583
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 584 QEIETRqfftdaefqdaltkrlcKEERKH-EQEVKEYQEKIDILNQQYLDLENEFRialtveARRFKDVQDGFEDVATEL 662
Cdd:TIGR02169 751 QEIENV-----------------KSELKElEARIEELEEDLHKLEEALNDLEARLS------HSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 663 AKSKHALIWAQRKENESSSLIKDLtcmvkeqktklsevcklkQEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQL 742
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYL------------------EKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 743 ISELAAKESLIYGLRTERKvwgqelacqssTLSQSRGKLEAQIESLCREneslrkshesdcdalrikckiIEDQNETIRK 822
Cdd:TIGR02169 867 EEELEELEAALRDLESRLG-----------DLKKERDELEAQLRELERK---------------------IEELEAQIEK 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 823 LKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLD--SIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 900
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
410 420 430
....*....|....*....|....*....|
gi 254675308 901 whdkgelLSHLEMQVKEVKEKFEDKERKLK 930
Cdd:TIGR02169 995 -------RAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-1011 |
5.08e-05 |
|
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: 47.36 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 728 KSIQIELLKHEKTQLISELAAKESLIYGLRTERKvwgqelacqsstlsqsrgKLEAQIESLCRENESLRKSHESDCDALR 807
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELE------------------ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 808 IKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEkcsqEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELEL 887
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELE----AQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 888 EEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFED--------KERK--LKAERDKSLELQKDAMEKLQNMD-DAFRR 956
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneierlEARLerLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675308 957 QVDEI------VEAHQAEIMQLANEKQKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEK 1011
Cdd:TIGR02168 441 ELEELeeeleeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
48-196 |
6.14e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 46.85 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 48 NNISKISSIDHIWNLRHLDLSSNQISQIEGLNTLTKLCTLNLSCNlitrvEGLEALVNLTKLNLSYNHINDLSGlmPLHG 127
Cdd:COG4886 62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLPE--ELAN 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675308 128 LKyKLRYIDLHSNYIDSIHHLLQctvGLHFLTNLILekdgEGNPICLIPGyraiILQTLPQLRILDCKN 196
Cdd:COG4886 135 LT-NLKELDLSNNQLTDLPEPLG---NLTNLKSLDL----SNNQLTDLPE----ELGNLTNLKELDLSN 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
445-891 |
6.21e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 445 IDELHKQADEKKDVHSQALITTDRLKDAIfkERHCKAQLEIivHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEK 524
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVL--EEHEERREEL--ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 525 MEKQKAQqqaaqirLIQEVELKaSAADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIET-RQFFTDAEfQDALTK 603
Cdd:PRK02224 291 LEEERDD-------LLAEAGLD-DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESlREDADDLE-ERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 604 R-----LCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIALTvearRFKDVQDGFEDVATELAK-------------- 664
Cdd:PRK02224 362 ReeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV----DLGNAEDFLEELREERDElrereaeleatlrt 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 665 --------------------------SKHALIWAQRKEN--ESSSLIKDLTCMVKEQKTKLSEVCKLKQEAA--ANLQNQ 714
Cdd:PRK02224 438 arerveeaealleagkcpecgqpvegSPHVETIEEDRERveELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 715 INTLEILIEDDK----QKSIQIELLKHEKTQLISELAAKESLIYGLRTErkvwGQELACQSSTLSQSRGKLEAQIESLCR 790
Cdd:PRK02224 518 REDLEELIAERRetieEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 791 ENESL--RKSHESDCDALRIKCKIIEDQNETIRklkDSLQEKDGQIKLLQEQI--ALIEKcSQEQLNEKSSQLDSIVEKL 866
Cdd:PRK02224 594 IRTLLaaIADAEDEIERLREKREALAELNDERR---ERLAEKRERKRELEAEFdeARIEE-AREDKERAEEYLEQVEEKL 669
|
490 500
....*....|....*....|....*
gi 254675308 867 ERHNERKEKLKQQLKAKELELEEIR 891
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEELE 694
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
25-142 |
1.12e-04 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 45.94 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 25 DKGLHSISE-LSLDSSIHAINLHCNNISKISSIDHIWNLRH------LDLSSNQISQ------IEGLNTLTKLCTLNLSC 91
Cdd:COG5238 278 AEGAIALAKaLQGNTTLTSLDLSVNRIGDEGAIALAEGLQGnktlhtLNLAYNGIGAqgaialAKALQENTTLHSLDLSD 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 92 NLITrVEGLEALV-------NLTKLNLSYNHINDLsGLMPL--HGLKYKLRYIDLHSNYI 142
Cdd:COG5238 358 NQIG-DEGAIALAkylegntTLRELNLGKNNIGKQ-GAEALidALQTNRLHTLILDGNLI 415
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
425-963 |
1.32e-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: 45.87 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 425 DQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQA----LITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIE 500
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAenarLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 501 LMKARDQQEDHIRhlrTLERALEKMEKQKAQQQAAQIRLIQEVElKASAADREINLLRTSLHQEKQQVQQLHELLalkeq 580
Cdd:pfam05483 249 ITEKENKMKDLTF---LLEESRDKANQLEEKTKLQDENLKELIE-KKDHLTKELEDIKMSLQRSMSTQKALEEDL----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 581 ehrqEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQqyldlenefriALTVEARRFKDVQDGFEDVAT 660
Cdd:pfam05483 320 ----QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE-----------LLRTEQQRLEKNEDQLKIITM 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 661 ELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSE---VCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKH 737
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEkkqFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 738 EKTQLISELaakESLIYGLRTErKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQN 817
Cdd:pfam05483 465 SEEHYLKEV---EDLKTELEKE-KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 818 ETIRKLKDSLQEKDGQIKLLQEQIalieKCSQEQLNEKSSQLDSIVEKLERHNERKEK----LKQQLKAKELELEEIRKA 893
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEV----KCKLDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHQE 616
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675308 894 YSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERD---KSLELQKDAMEKLQNMDDAFRRQVDEIVE 963
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnyqKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
603-975 |
1.34e-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: 46.19 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 603 KRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFrialtVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSL 682
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKL-----FDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 683 IKDLTcmvkEQKTKLSEVCKLKQEAAANLQNQINTLE--ILIEDDKQKSIQIELLKHEKTQLI---------SELAAKES 751
Cdd:TIGR00606 669 ITQLT----DENQSCCPVCQRVFQTEAELQEFISDLQskLRLAPDKLKSTESELKKKEKRRDEmlglapgrqSIIDLKEK 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 752 LIYGLRTERKVWGQELACQSSTLSQSRGKLE----------------AQIESLCRENESLRKSHESDCDALRIKckiieD 815
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimpeeesakvcltdvTIMERFQMELKDVERKIAQQAAKLQGS-----D 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 816 QNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQlNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYS 895
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 896 TLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANE 975
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE 978
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
433-938 |
1.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 433 KAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAifkerhcKAQLEIIVHrlqnEVKKLTIELMKARDQQEDHI 512
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-------EKELEEVLR----EINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 513 RHLRTLERALEKMEKQKAQQQAAQIRLiQEVELKASAADREINLLRTSLHQEKQQVQQLHELLALKEQ------------ 580
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsefyeeyl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 581 EHRQEIETRqfFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRI-----ALTVEARRFKDVQDGF 655
Cdd:PRK03918 307 DELREIEKR--LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 656 --EDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSE---------VCK--LKQEAAANLQNQInTLEIL- 721
Cdd:PRK03918 385 tpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpVCGreLTEEHRKELLEEY-TAELKr 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 722 IEDDKQKSI-QIELLKHEKTQLISELAAKESLIyglrTERKVWGQELACQSSTLSQSRGKLEAQIESLCRENESLRKshe 800
Cdd:PRK03918 464 IEKELKEIEeKERKLRKELRELEKVLKKESELI----KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK--- 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 801 sdcdaLRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQL 880
Cdd:PRK03918 537 -----LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675308 881 KAKELELEEIRKAYSTLNKKWHDKGELLSHLEM---QVKEVKEKFEDKERKLKAERDKSLE 938
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKKYSEEEYEELREEYLELS 672
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-980 |
1.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 413 DNSTYRSLVEQLDQEREMR--WKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQleiivhRL 490
Cdd:COG4913 260 LAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ------IR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 491 QN---EVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQ 567
Cdd:COG4913 334 GNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 568 VQQLHELLALKEQEhRQEIETRQFFTDAEFQDALtKRLCKEERKHEQEVKEYQEKIDILNQQ---------YLdleNEFR 638
Cdd:COG4913 414 LRDLRRELRELEAE-IASLERRKSNIPARLLALR-DALAEALGLDEAELPFVGELIEVRPEEerwrgaierVL---GGFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 639 IALTVEARRFKDVQDGFEDVATELA----KSKHALIWAQRKENESSSLIKDLTcmVKEQktklsevcklkqEAAANLQNQ 714
Cdd:COG4913 489 LTLLVPPEHYAAALRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPDSLAGKLD--FKPH------------PFRAWLEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 715 IN---------TLEILieDDKQKSIQIE-LLKHEKT--QLISELAAKESLIYGLRTERKVwgqelacqsSTLSQSRGKLE 782
Cdd:COG4913 555 LGrrfdyvcvdSPEEL--RRHPRAITRAgQVKGNGTrhEKDDRRRIRSRYVLGFDNRAKL---------AALEAELAELE 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 783 AQIESLCRENESLRKSHESdcdalrikckiIEDQNETIRKLKDsLQEKDGQIKLLQEQIAliekcsqeQLNEKSSQLDSI 862
Cdd:COG4913 624 EELAEAEERLEALEAELDA-----------LQERREALQRLAE-YSWDEIDVASAEREIA--------ELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 863 VEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVkEKFEDKERKLKAERDKSLELQKD 942
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDA 762
|
570 580 590
....*....|....*....|....*....|....*...
gi 254675308 943 AMEKLQnmdDAFRRQVDEIVEAHQAEIMQLANEKQKYI 980
Cdd:COG4913 763 VERELR---ENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
691-893 |
1.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 691 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELACQ 770
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 771 SSTLSQSRGKLEAQ-IESLCRENESLRKSHESDCDALRikcKIIEDQNEtIRKLKDSLQEKDGQIKLLQEQIALIEKCSQ 849
Cdd:COG3883 99 GGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLE---ELKADKAE-LEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675308 850 EQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKA 893
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
82-122 |
1.68e-04 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 39.92 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 254675308 82 TKLCTLNLSCNLITRVEGLEALVNLTKLNLSYN-HINDLSGL 122
Cdd:pfam12799 1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDL 42
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
800-953 |
1.70e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 800 ESDCDALRIKCKIIEDQ--NETIRKLKDSLQEKDGQIKLLQEQIALIEkcsQEQLNEKSSQLDSIVEKLERHNERkekLK 877
Cdd:COG2433 360 PPDVDRDEVKARVIRGLsiEEALEELIEKELPEEEPEAEREKEHEERE---LTEEEEEIRRLEEQVERLEAEVEE---LE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 878 QQLKAKELELE----EIRKAYSTLNKKwHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKdaMEKLQNMDDA 953
Cdd:COG2433 434 AELEEKDERIErlerELSEARSEERRE-IRKDREISRLDREIERLERELEEERERIEELKRKLERLKE--LWKLEHSGEL 510
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1021 |
2.68e-04 |
|
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: 43.76 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 865 KLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERD----KSLELQ 940
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 941 KDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDcanlKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAIS 1020
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 254675308 1021 E 1021
Cdd:COG1579 174 P 174
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
32-142 |
3.11e-04 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 43.88 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 32 SELSLDSSIHAINLHCNNISK--ISSIDHIW----NLRHLDLSSNQISQI------EGLNTLTKLCTLNLSCNLITRVeG 99
Cdd:cd00116 159 KALRANRDLKELNLANNGIGDagIRALAEGLkancNLEVLDLNNNGLTDEgasalaETLASLKSLEVLNLGDNNLTDA-G 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 254675308 100 LEALVN--------LTKLNLSYNHINDLSGLMPLHGLKYK--LRYIDLHSNYI 142
Cdd:cd00116 238 AAALASallspnisLLTLSLSCNDITDDGAKDLAEVLAEKesLLELDLRGNKF 290
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-1013 |
3.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 422 EQLDQEREMRwKAEQTEKklmdyIDELHKQADEKKDVHSQALITTDRLKDAIFK-ERHCKAQLEIIVHRLQNEVKKLTIE 500
Cdd:PTZ00121 1209 EEERKAEEAR-KAEDAKK-----AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADE 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 501 LMKARDqqedhIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSLHQEKQQVqqlhELLALKEQ 580
Cdd:PTZ00121 1283 LKKAEE-----KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 581 EHRQEIETrqfftdAEFQDALTKRLCKEERKHEQEVKEYQEKIDilnqqyldlenefrialtvEARRFKDVQDGFEDVAT 660
Cdd:PTZ00121 1354 AAADEAEA------AEEKAEAAEKKKEEAKKKADAAKKKAEEKK-------------------KADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 661 ELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKT 740
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 741 QLISELAAKESLIYGLRTERKVWGQELacqsSTLSQSRGKLEAQIESLCRENESLRKSHE-SDCDALRIKCKIieDQNET 819
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEA----KKAEEAKKADEAKKAEEAKKADEAKKAEEkKKADELKKAEEL--KKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 820 IRKLKDSLQEKDGQIKLLQEqiALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKlKQQLKAKEL-ELEEIRKAYSTLN 898
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK--AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELkKAEEEKKKVEQLK 1639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 899 KKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKlQNMDDAFRRQVDEIVEAHQ-----AEIMQLA 973
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEElkkkeAEEKKKA 1718
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 254675308 974 NEKQKYIDCANLKVQQVEDEMRGLLDETCKNKKMMEEKIK 1013
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
406-1025 |
4.26e-04 |
|
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: 44.58 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 406 KVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIF----KERHCKA 481
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 482 QLEIIVHRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELKASAADREINLLRTSL 561
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 562 HQEKQQVQQLHELLAL-KEQEHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFRIA 640
Cdd:pfam02463 303 LKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 641 LTVEARRFKDVQDGFEDVATELAKSKHALIWAQRKENESSSLIKDLTCMVKEQKTKLSEVCKLKQEAAANLQNQINTLEI 720
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 721 LIEDDKQKSIQIELLKHEKTQLISELAAKESL-----------IYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLC 789
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKleersqkeskaRSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 790 RENESLRKSHESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERH 869
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 870 NERKEKLKQQLKAKELELEEIRKaySTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQN 949
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKE--SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675308 950 MDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDCANlkvQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQKE 1025
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN---EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
38-116 |
4.49e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.43 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 38 SSIHAINLHCNNISKI--SSIDHIWNLRHLDLSSNQISQIEGlntltklctlnlscnlitrvEGLEALVNLTKLNLSYNH 115
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLddGAFKGLSNLKVLDLSNNLLTTLSP--------------------GAFSGLPSLRYLDLSGNR 60
|
.
gi 254675308 116 I 116
Cdd:pfam13855 61 L 61
|
|
| TIGR03545 |
TIGR03545 |
TIGR03545 family protein; This model represents a relatively rare but broadly distributed ... |
849-1013 |
6.05e-04 |
|
TIGR03545 family protein; This model represents a relatively rare but broadly distributed uncharacterized protein family, distributed in 1-2 percent of bacterial genomes, all of which have outer membranes. In many of these genomes, it is part of a two-gene pair.
Pssm-ID: 274640 Cd Length: 555 Bit Score: 43.55 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 849 QEQLNEKSSQLDSIVEKLERHNerkeklkqqLKAKELeLEEIRKAYSTLNKKWHDK------GELLSHLEMQVKEVKEK- 921
Cdd:TIGR03545 138 SSELKKVDSQLPDPRALLKGED---------LKTVET-AEEIEKSLKAMQQKWKKRkkdlpnKQDLEEYKKRLEAIKKKd 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 922 -------FEDKER--KLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQ-KYIDCANLKVQQVE 991
Cdd:TIGR03545 208 iknplelQKIKEEfdKLKKEGKADKQKIKSAKNDLQNDKKQLKADLAELKKAPQNDLKRLENKYAiKSGDLKNFAVDLFG 287
|
170 180
....*....|....*....|..
gi 254675308 992 DEMRGLLDETCKNKKMMEEKIK 1013
Cdd:TIGR03545 288 PEIRKYLQKFLKYYDQAEPLLN 309
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
549-980 |
7.44e-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: 43.66 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 549 AADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFF-TDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILN 627
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYkSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 628 QQYLDLENEFRI---ALTVEARRFKDVQD-------GFEDVATELAKSKHALiwaQRKENESSSL---IKDLTCM--VKE 692
Cdd:pfam10174 317 NQNSDCKQHIEVlkeSLTAKEQRAAILQTevdalrlRLEEKESFLNKKTKQL---QDLTEEKSTLageIRDLKDMldVKE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 693 QKT--------KLSEVCKLKQEAAANLQNQINTLE-----------ILIEDDKQKSIQIELLKHEKT------------- 740
Cdd:pfam10174 394 RKInvlqkkieNLQEQLRDKDKQLAGLKERVKSLQtdssntdtaltTLEEALSEKERIIERLKEQREredrerleelesl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 741 -QLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKLEAQIESLcrenESLRKSHESDCDALRIKCKIIEDQNET 819
Cdd:pfam10174 474 kKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL----EIAVEQKKEECSKLENQLKKAHNAEEA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 820 IRKLKDSLQekdgQIKLLQEQIAL-IEKCSQEQL-------------NEKSSQlDSIVEKLERHNER--KEKLKQQLKAK 883
Cdd:pfam10174 550 VRTNPEIND----RIRLLEQEVARyKEESGKAQAeverllgilreveNEKNDK-DKKIAELESLTLRqmKEQNKKVANIK 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 884 ELELEEIRKAYSTLNKKWHDKGELL-SHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEK---LQNMDDAFRRQVD 959
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKdghLTNLRAERRKQLE 704
|
490 500
....*....|....*....|.
gi 254675308 960 EIVEAHQAEIMQLANEKQKYI 980
Cdd:pfam10174 705 EILEMKQEALLAAISEKDANI 725
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
781-961 |
9.24e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 781 LEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNETIRklkDSLQEKDGQIKLLQEQIALIEKCSQEQ--------- 851
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRES---DRNQELQKRIRLLEKREAEAEEALREQaelnrlkkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 852 --------LNEKSSQL-------DSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVK 916
Cdd:pfam05557 84 ylealnkkLNEKESQLadareviSCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254675308 917 EVKE---KFEDKERKLKAERDKSLELQ--KDAMEKLQNMDDAFRRQVDEI 961
Cdd:pfam05557 164 SLAEaeqRIKELEFEIQSQEQDSEIVKnsKSELARIPELEKELERLREHN 213
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
735-1025 |
9.29e-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: 43.27 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 735 LKHEKTQLISELAAKESLIYGLRTERkvwgQELACQSS-------TLSQSRGKLEAQIESLCRENESLRKSHESDCDALR 807
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKL----ETLTNQNSdckqhieVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 808 IKCKIIEDQNE-------TIRKLKDSLQEKDGQIKLLQEQIALIekcsQEQLNEKSSQLDSIVEK--------------- 865
Cdd:pfam10174 363 KKTKQLQDLTEekstlagEIRDLKDMLDVKERKINVLQKKIENL----QEQLRDKDKQLAGLKERvkslqtdssntdtal 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 866 --LERHNERKEKLKQQLK-AKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDkeRKLKAERDKSLELQKD 942
Cdd:pfam10174 439 ttLEEALSEKERIIERLKeQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLID--LKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 943 AmeKLQNMDDAFRRQVDEIV-------EAHQAE------------IMQLANEKQKYIDCANlKVQQVEDEMRGLLDETCK 1003
Cdd:pfam10174 517 S--KLKSLEIAVEQKKEECSklenqlkKAHNAEeavrtnpeindrIRLLEQEVARYKEESG-KAQAEVERLLGILREVEN 593
|
330 340
....*....|....*....|..
gi 254675308 1004 NKKMMEEKIKQLACAISEIQKE 1025
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKE 615
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
705-967 |
1.08e-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: 42.44 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 705 QEAAANLQNQINTLEILIEDDKQksiQIELLKHEKTQLISELAAKESLIygLRTERKVwgqelacqsSTLSQSRGKLEAQ 784
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRI--AALARRI---------RALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 785 IESLCRENESLRKShesdcdalrikckiIEDQNETIRKLKDSLQ--EKDGQIKLL--QEQIALIEKcSQEQLNEKSSQLD 860
Cdd:COG4942 85 LAELEKEIAELRAE--------------LEAQKEELAELLRALYrlGRQPPLALLlsPEDFLDAVR-RLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 861 SIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKwhdkgellshLEMQVKEVKEKFEDKERKLKAERDKSLELQ 940
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAA----------LEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|....*..
gi 254675308 941 KDAmEKLQNMDDAFRRQVDEIVEAHQA 967
Cdd:COG4942 220 QEA-EELEALIARLEAEAAAAAERTPA 245
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
105-172 |
1.20e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 37.89 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675308 105 NLTKLNLSYNHINDLSGLMpLHGLKyKLRYIDLHSNYIDSIHhlLQCTVGLHFLTNLILekdgEGNPI 172
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGA-FKGLS-NLKVLDLSNNLLTTLS--PGAFSGLPSLRYLDL----SGNRL 61
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
811-960 |
1.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 811 KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKcsqeQLNEKSSQLDSIVEKLERHNERKEKLK--QQLKAKELELE 888
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675308 889 EIRKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKL---KAERDKSLELQKDAMEKLQNMDDAFRRQVDE 960
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
813-1026 |
1.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 813 IEDQNETIRKLKDSLQEKDGQIKLLQEQI-ALIEKCSQ--EQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEE 889
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRdELNAQVKElrEEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 890 IRKAYSTLNKKWHDKGEL---LSHLEMQV----------KEVKEKFEDKERKLKaERDKSLELQKDAMEKLQNMDDaFRR 956
Cdd:COG1340 97 LRKELAELNKAGGSIDKLrkeIERLEWRQqtevlspeeeKELVEKIKELEKELE-KAKKALEKNEKLKELRAELKE-LRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675308 957 QVDEIVEahqaEIMQLANEKQKYIDCANLKVQQVE------DEMRGLLDETCKNKKMMEEKIKQLACAISEIQKEM 1026
Cdd:COG1340 175 EAEEIHK----KIKELAEEAQELHEEMIELYKEADelrkeaDELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
737-929 |
1.42e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.04 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 737 HEKTQLISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRGKlEAQIESLCReneslrkSHESDCDALRIKCKIIEDQ 816
Cdd:pfam15619 11 HKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGT-ESELPQLIA-------RHNEEVRVLRERLRRLQEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 817 NetiRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQ-LNEK---SSQLDSIVEKLERHNERKEKLKQQLkakELELEEIRK 892
Cdd:pfam15619 83 E---RDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEReelQKKLEQLEAKLEDKDEKIQDLERKL---ELENKSFRR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 254675308 893 AYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKL 929
Cdd:pfam15619 157 QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
811-993 |
1.68e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 811 KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQeQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEI 890
Cdd:pfam13851 19 DITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENK-RLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 891 RKAYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDK--ERKLKAErDKSLELQKdameKLQNMDDafrrqVDEIVEAHQAE 968
Cdd:pfam13851 98 EKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAiqDVQQKTG-LKNLLLEK----KLQALGE-----TLEKKEAQLNE 167
|
170 180
....*....|....*....|....*
gi 254675308 969 IMQLANEKQKYIDCANLKVQQVEDE 993
Cdd:pfam13851 168 VLAAANLDPDALQAVTEKLEDVLES 192
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
778-892 |
1.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 778 RGKLEAQIESLCRENESLRKshESDCDALRIKCKIIEDQNETIRKLKDSLQ----EKDGQIKLLQEQiaLIEKcsQEQLN 853
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEkelrERRNELQKLEKR--LLQK--EENLD 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675308 854 EKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 892
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
422-638 |
2.15e-03 |
|
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: 42.35 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 422 EQLDQEREMRWKAEQTEKKLMDYIDELHKQADEKKDVHSQALITTDRLKDAIFKERHCKAQLEIIVHRLQNEVKKLTIEL 501
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 502 MKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRL----------IQEVELKASAADREINLLRTSLHQEKQQVQQL 571
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLrseleelseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675308 572 HELLAlkeqeHRQEIETRQFFTDAEFQDALTKRLCKEERKHEQEVKEYQEKIDILNQQYLDLENEFR 638
Cdd:TIGR02168 935 EVRID-----NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-592 |
2.26e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 392 NNLRDLDEQKTgviKVDKNFSDNSTYRSLVEQLDQEREMRWKAEQTEKKLMDYIDELHKQAdekkdvhsqalittdRLKD 471
Cdd:COG4717 68 LNLKELKELEE---ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL---------------QLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 472 AIFKERHCKAQLEIIVHRLQNEVKKLT--IELMKARDQQEDHIRHLRT-LERALEKMEKQKAQQQAAQIRLIQEVELKAS 548
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQEeLEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675308 549 AADREINLLRTSLHQEKQQVQQLHELLALKEQEHRQEIETRQFF 592
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
61-125 |
3.24e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 41.37 E-value: 3.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675308 61 NLRHLDLSSNQISQI--EGLNTLTKLCTLNLSCNLITRV--EGLEALVNLTKLNLSYnhiNDLSGLMPL 125
Cdd:PLN00113 476 RLENLDLSRNQFSGAvpRKLGSLSELMQLKLSENKLSGEipDELSSCKKLVSLDLSH---NQLSGQIPA 541
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
47-142 |
3.38e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 41.37 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 47 CNNISKISSID---------------HIWNLRHLDLSSNQIS-QIEG--LNTLTKLCTLNLSCNLITRVEGLEALVNLTK 108
Cdd:PLN00113 65 CNNSSRVVSIDlsgknisgkissaifRLPYIQTINLSNNQLSgPIPDdiFTTSSSLRYLNLSNNNFTGSIPRGSIPNLET 144
|
90 100 110
....*....|....*....|....*....|....*
gi 254675308 109 LNLSYNHindLSGLMPLH-GLKYKLRYIDLHSNYI 142
Cdd:PLN00113 145 LDLSNNM---LSGEIPNDiGSFSSLKVLDLGGNVL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
540-802 |
3.78e-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: 40.90 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 540 IQEVELKASAADREINLLRTSLHQEKQQVQQLHELLalkeQEHRQEIETRQfftdaefqdaltkrlcKEERKHEQEVKEY 619
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALA----------------RRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 620 QEKIDILNQQYLDLENEFRIALTVEARRFKDVQD-GFEDVATELAKSKHALIWAQRkenesSSLIKDLTCMVKEQKTKLS 698
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 699 EVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKEsliyglrterkvwgQELACQSSTLSQSR 778
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL--------------AELAAELAELQQEA 222
|
250 260
....*....|....*....|....
gi 254675308 779 GKLEAQIESLCRENESLRKSHESD 802
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
691-900 |
4.02e-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: 40.90 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 691 KEQKTKLSEVCKLKQEAAANLQNQINTLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELAcq 770
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 771 sstlsQSRGKLEAQIESLCRENE----SLRKSHESDCDALRIKC---KIIEDQNETIRKLKDSLQEKDGQIKLLQEQIAL 843
Cdd:COG4942 101 -----AQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 844 IEKCSQEQLNEKSSQLDSIVEK---LERHNERKEKLKQQLKAKELELEEIRKAYSTLNKK 900
Cdd:COG4942 176 LEALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
572-1010 |
4.17e-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: 41.11 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 572 HELLALKEQEHRQEIETRQFFTDAEFQdaLTKRLCKEERKHEQEVKEYQEKidiLNQQYLDLENEFRIALTVEARRFKDV 651
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQ--LLTLCTPCMPDTYHERKQVLEK---ELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 652 QdgfedvatELAKSKHALIWAQRKENESSSLIKDLTCMVKE------------QKTKLSEVCKLKQEAAANLQNQINTLE 719
Cdd:TIGR00618 253 E--------EQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 720 ILIEDdKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELaCQSSTLSQSRGKLEAQIESLcrenESLRKSH 799
Cdd:TIGR00618 325 KLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS-CQQHTLTQHIHTLQQQKTTL----TQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 800 ESDCDALRIKCKIIEDQNETIRKLKDSLQEKDGQIKLLQEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQ 879
Cdd:TIGR00618 399 CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 880 lkakeleleeirkaySTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKD----------------A 943
Cdd:TIGR00618 479 ---------------EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrrmqrgeqtyaqletS 543
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675308 944 MEKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKY--IDCANLKVQQVEDEMRGLLDETCKNKKMMEE 1010
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
813-977 |
5.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 813 IEDQNETIRKLKDSLQEKDGQIKLLQEQIALiekcSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRK 892
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQ----ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 893 AYSTLNKKWHDKGELLSHLEMQVKEVKEKFEDKERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQL 972
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
....*
gi 254675308 973 ANEKQ 977
Cdd:COG4372 196 AEKEE 200
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
43-79 |
5.83e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 35.68 E-value: 5.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 254675308 43 INLHCNNISKISSIDHIWNLRHLDLSSN-QISQIEGLN 79
Cdd:pfam12799 6 LDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
849-1000 |
6.09e-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: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 849 QEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAkeleLEEIRKAYSTL-NKKWHD-------------KGEL------- 907
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLaEYSWDEidvasaereiaelEAELerldass 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 908 --LSHLEMQVKEVKEKFED----------KERKLKAERDKSLELQKDAMEKLQNMDDAFRRQVDEIVEAHQAEIMQLANE 975
Cdd:COG4913 685 ddLAALEEQLEELEAELEEleeeldelkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|.
gi 254675308 976 K------QKYIDCANLKVQQVEDEMRGLLDE 1000
Cdd:COG4913 765 RelrenlEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
672-1025 |
6.43e-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: 40.39 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 672 AQRKENESSSLIKDLTCMVKEQKTK------LSEVCKLKQEAAANLQNQINTLEILIED----DKQKSIQIELLKHEKTQ 741
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNELKNKekelknLDKNLNKDEEKINNSNNKIKILEQQIKDlndkLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 742 LISELAAKESLIYGLRTERKVWGQELACQSSTLSQSRG---KLEAQIESLCRENESLRKSHESDCDALRIKCKIIEDQNE 818
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTeikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 819 TIRKLKD----------SLQEKDGQIKLLQEQIALIEKCS----------QEQLNEKSSQLDSIVEKLERHNERKEKLKQ 878
Cdd:TIGR04523 188 NIDKIKNkllklelllsNLKKKIQKNKSLESQISELKKQNnqlkdniekkQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 879 QLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQ-----VKEVKEKFEDKERKLKAERDK---------SLELQKDAM 944
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQisqnnkiisQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 945 EKLQNMDDAFRRQVDEIVEAHQAEIMQLANEKQKYIDcANLKVQQVEDEMRGLLDETCKNKKMMEEKIKQLACAISEIQK 1024
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
.
gi 254675308 1025 E 1025
Cdd:TIGR04523 427 E 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-729 |
7.50e-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: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 480 KAQLEiivhRLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEkqkaqqqaaqiRLIQEVELKASAADREINLLRT 559
Cdd:COG4942 26 EAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA-----------RRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 560 SLHQEKQQVQQLHELLA--LKEQEHRQEIETRQFFTDAEFQDALTKRLckeeRKHEQEVKEYQEKIDILNQQYLDLEnef 637
Cdd:COG4942 91 EIAELRAELEAQKEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 638 riALTVEARRFKDVQdgfEDVATELAKSKHALiwaQRKENESSSLIKDLTCMVKEQKTKLSEvcklKQEAAANLQNQINT 717
Cdd:COG4942 164 --ALRAELEAERAEL---EALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIAR 231
|
250
....*....|..
gi 254675308 718 LEILIEDDKQKS 729
Cdd:COG4942 232 LEAEAAAAAERT 243
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
851-964 |
8.85e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 851 QLNEKSSQLDSIVEKLERHNERKEKLKQ------QLKAKEL--ELEEIRKAYSTLNKKWHDKGELLSH------------ 910
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKeqdeasFERLAELrdELAELEEELEALKARWEAEKELIEEiqelkeeleqry 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675308 911 -----LEMQVKEVKEKFEDKERKLKAERDKSL--------------ELQKDAMEKLQNMDDAFRRQV---DEIVEA 964
Cdd:COG0542 485 gkipeLEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNLEEELHERVigqDEAVEA 560
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
489-1003 |
9.40e-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: 39.95 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 489 RLQNEVKKLTIELMKARDQQEDHIRHLRTLERALEKMEKQKAQQQAAQIRLIQEVELK---------ASAADREINLLRT 559
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkkqqlLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 560 SL----HQEKQQVQQLHELLALKEQEHRQEIETRQFFTDAEFQDALTKRlcKEERKHEQEVKEYQEKID---ILNQQYLD 632
Cdd:TIGR00618 275 QEavleETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR--AKLLMKRAAHVKQQSSIEeqrRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 633 LENEFRIALTVEARRfkdvqdgFEDVATELAKSKHALIWAQRKE------NESSSLIKDLTCMVKEQKTKLSE------- 699
Cdd:TIGR00618 353 QEIHIRDAHEVATSI-------REISCQQHTLTQHIHTLQQQKTtltqklQSLCKELDILQREQATIDTRTSAfrdlqgq 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 700 ------VCKLKQEAAANLQNQIN---TLEILIEDDKQKSIQIELLKHEKTQLISELAAKESLIYGLRTERKVWGQELAC- 769
Cdd:TIGR00618 426 lahakkQQELQQRYAELCAAAITctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCp 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 770 ---------QSSTLSQSRGKLEAQIESLCRENESLRKSHES---DCDALRIKCKIIEDQNETIRklkDSLQEKDGQIKLL 837
Cdd:TIGR00618 506 lcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDvyhQLTSERKQRASLKEQMQEIQ---QSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 838 QEQIALIEKCSQEQLNEKSSQLDSIVEKLERHNERKEKLKQQLKAKELELEEIRKAYSTLNKKWHDKGELLSHLEMQVKE 917
Cdd:TIGR00618 583 KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675308 918 V--------KEKFEDKERKLKAERDKSLELQKDaMEKLQNMDDAFRRQVDEIVEA--HQAEIMQLANEKQKYIDCANLKV 987
Cdd:TIGR00618 663 HalsirvlpKELLASRQLALQKMQSEKEQLTYW-KEMLAQCQTLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDAL 741
|
570
....*....|....*.
gi 254675308 988 QQVEDEMRGLLDETCK 1003
Cdd:TIGR00618 742 NQSLKELMHQARTVLK 757
|
|
| |
