|
Name |
Accession |
Description |
Interval |
E-value |
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
822-859 |
8.61e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 8.61e-14
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 822 LEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFAQQL 859
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
512-550 |
3.69e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 3.69e-12
10 20 30
....*....|....*....|....*....|....*....
gi 4559271 512 FLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFRSRL 550
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
819-856 |
9.79e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 9.79e-10
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 819 LRCLEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFA 856
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
586-624 |
1.65e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.87 E-value: 1.65e-09
10 20 30
....*....|....*....|....*....|....*....
gi 4559271 586 ILEAQIASGGVIDPVRGVRVPPEMAVQQGLLNNAVLQFL 624
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-207 |
3.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSADE 96
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 97 FRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgppvEANHYQKCRRLEE 176
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----LAEELLEALRAAA 396
|
170 180 190
....*....|....*....|....*....|.
gi 4559271 177 ELLAQRREVENLKQKMDQQIKEHEHQLLRLQ 207
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| PLEC |
smart00250 |
Plectin repeat; |
857-894 |
1.61e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 1.61e-06
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 857 QQLRQCELVITGISHPVSNKMMSVVEAVNANIISKEMG 894
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
512-547 |
1.99e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.99e-06
10 20 30
....*....|....*....|....*....|....*.
gi 4559271 512 FLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFR 547
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-211 |
2.00e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRK-------MILLQEESDK 89
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsedIESLAAEIEE 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 90 FKRSADEFRKKMEKLMESKVVTETDLSGIKHDfvslqRENFRAQENAklWETNIRELERQLQCYREKMQQgppvEANHYQ 169
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSE-----LEELSEELRE--LESKRSELRRELEELREKLAQ----LELRLE 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 4559271 170 KCRRLEEELLAQRRE--------VENLKQKMDQQIKEHEHQLLRLQCEIQ 211
Cdd:TIGR02168 933 GLEVRIDNLQERLSEeysltleeAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
898-935 |
2.31e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 2.31e-06
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 898 LEFQYLTGGLIEPKVFSRLTIEEALHVGIIDVLIATRL 935
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-210 |
5.01e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 2 LVSEFKQKCDQQSMIIQKTEKEvrslsAELSASKEEKR-REEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKM 80
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAE-----TELCAEAEEMRaRLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 81 ILLQEEsdkfkrsADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQG 160
Cdd:pfam01576 106 QDLEEQ-------LDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4559271 161 PPVEANHYQKCRRLEEELLAQ---RREVENLKQKMDQQIKEHEHQLLRLQCEI 210
Cdd:pfam01576 179 SKLKNKHEAMISDLEERLKKEekgRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-219 |
8.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 3 VSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQD-----ELHLKTIEEQMTH 77
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 78 RKMIL-LQEESDKFKRSADEFRKKMEKLmESKvvtETDLSGIKHDFVSLQRENFRAQENAKLWETnIRELERQLQCYREK 156
Cdd:PRK03918 306 LDELReIEKRLSRLEEEINGIEERIKEL-EEK---EERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKR 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4559271 157 MQQGPPVEA-NHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQ-----CEIQKKSTTQDH 219
Cdd:PRK03918 381 LTGLTPEKLeKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEH 449
|
|
| PLEC |
smart00250 |
Plectin repeat; |
896-928 |
1.29e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|...
gi 4559271 896 RCLEFQYLTGGLIEPKVFSRLTIEEALHVGIID 928
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PLEC |
smart00250 |
Plectin repeat; |
584-616 |
1.82e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|...
gi 4559271 584 KHILEAQIASGGVIDPVRGVRVPPEMAVQQGLL 616
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLEC |
smart00250 |
Plectin repeat; |
788-818 |
5.13e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 35.54 E-value: 5.13e-03
10 20 30
....*....|....*....|....*....|.
gi 4559271 788 SPIAGYWLTASGERISLLKASRRNLVDRVTA 818
Cdd:smart00250 8 SAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
473-509 |
9.08e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 34.77 E-value: 9.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 4559271 473 KFLTKATSIAGLYLESSKEKMSFTSAAQKIIIDKMIA 509
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
822-859 |
8.61e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 8.61e-14
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 822 LEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFAQQL 859
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
512-550 |
3.69e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 3.69e-12
10 20 30
....*....|....*....|....*....|....*....
gi 4559271 512 FLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFRSRL 550
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
819-856 |
9.79e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 9.79e-10
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 819 LRCLEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFA 856
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
586-624 |
1.65e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.87 E-value: 1.65e-09
10 20 30
....*....|....*....|....*....|....*....
gi 4559271 586 ILEAQIASGGVIDPVRGVRVPPEMAVQQGLLNNAVLQFL 624
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-207 |
3.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSADE 96
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 97 FRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgppvEANHYQKCRRLEE 176
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----LAEELLEALRAAA 396
|
170 180 190
....*....|....*....|....*....|.
gi 4559271 177 ELLAQRREVENLKQKMDQQIKEHEHQLLRLQ 207
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| PLEC |
smart00250 |
Plectin repeat; |
857-894 |
1.61e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 1.61e-06
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 857 QQLRQCELVITGISHPVSNKMMSVVEAVNANIISKEMG 894
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
512-547 |
1.99e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.99e-06
10 20 30
....*....|....*....|....*....|....*.
gi 4559271 512 FLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFR 547
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-211 |
2.00e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRK-------MILLQEESDK 89
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsedIESLAAEIEE 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 90 FKRSADEFRKKMEKLMESKVVTETDLSGIKHDfvslqRENFRAQENAklWETNIRELERQLQCYREKMQQgppvEANHYQ 169
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSE-----LEELSEELRE--LESKRSELRRELEELREKLAQ----LELRLE 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 4559271 170 KCRRLEEELLAQRRE--------VENLKQKMDQQIKEHEHQLLRLQCEIQ 211
Cdd:TIGR02168 933 GLEVRIDNLQERLSEeysltleeAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
898-935 |
2.31e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 2.31e-06
10 20 30
....*....|....*....|....*....|....*...
gi 4559271 898 LEFQYLTGGLIEPKVFSRLTIEEALHVGIIDVLIATRL 935
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
13-216 |
2.59e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 13 QSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKR 92
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 93 SADEFRKKMEKLMeskvvtetdlsgikhdfVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgppvEANHYQKCR 172
Cdd:COG4942 98 ELEAQKEELAELL-----------------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA----RREQAEELR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4559271 173 RLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQCEIQKKSTT 216
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-217 |
3.71e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 5 EFKQKCDQQSMIIQKTEKEVRSLSAELSASkeekrrEEQKAQLqRAQVQELNDRLKRVQDELHLKTIE-EQMTHRKMILl 83
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQEL------EEKLEEL-RLEVSELEEEIEELQKELYALANEiSRLEQQKQIL- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 84 qeesdkfkrsadefRKKMEKLMESKVVTETDLsgikhdfVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQGPPV 163
Cdd:TIGR02168 308 --------------RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 4559271 164 EANHYQKCRRLEEELLAQRREVENLKQKMDQ---QIKEHEHQLLRLQCEIQKKSTTQ 217
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEI 423
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
17-151 |
4.30e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSADE 96
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 4559271 97 FRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQ 151
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-214 |
5.70e-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: 50.45 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMIL-LQEESDKFKRSAD 95
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 96 EFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgppveanhyqkcrrLE 175
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE--------------VD 377
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4559271 176 EELLAQRREVENLKQKMDQ---QIKEHEHQLLRLQCEIQKKS 214
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLS 419
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-207 |
2.44e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 4 SEFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQ--RAQVQELNDRLKRVQDELHLKTIEEQMTHRKMI 81
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAelEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 82 LLQEESDKFKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgp 161
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-- 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4559271 162 pvEANHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQ 207
Cdd:COG1196 377 --AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-211 |
5.00e-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: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 16 IIQKTEKEVRSLsaELSASKEEKRREeQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSAD 95
Cdd:TIGR02168 194 ILNELERQLKSL--ERQAEKAERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 96 EFRKKMEKLMESKVVTETDL-------SGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQGPPVEANHY 168
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4559271 169 QKCRRLEEELLAQRREVENLKQKMDQQ----------IKEHEHQLLRLQCEIQ 211
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELeeqletlrskVAQLELQIASLNNEIE 403
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-210 |
5.01e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 2 LVSEFKQKCDQQSMIIQKTEKEvrslsAELSASKEEKR-REEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKM 80
Cdd:pfam01576 31 LEKKHQQLCEEKNALQEQLQAE-----TELCAEAEEMRaRLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 81 ILLQEEsdkfkrsADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQG 160
Cdd:pfam01576 106 QDLEEQ-------LDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4559271 161 PPVEANHYQKCRRLEEELLAQ---RREVENLKQKMDQQIKEHEHQLLRLQCEI 210
Cdd:pfam01576 179 SKLKNKHEAMISDLEERLKKEekgRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5-216 |
5.10e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 5 EFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDE---LHLKTIEE-------Q 74
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkaLKKKGSAEnkqlnayE 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 75 MTHRKMIL-LQEESDKFKRSADEFRKKME--KLMESKVVTETDLSGIKHD-FVSLQRE-NFRAQ----ENAKLWETN--- 142
Cdd:pfam05483 636 IKVNKLELeLASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADeAVKLQKEiDKRCQhkiaEMVALMEKHkhq 715
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4559271 143 ----IRELERQLQCYREKMQQGPPVEANhyqkcrrLEEELLAQRREVENLKQKMDQQIKEHEhqllRLQCEIQKKSTT 216
Cdd:pfam05483 716 ydkiIEERDSELGLYKNKEQEQSSAKAA-------LEIELSNIKAELLSLKKQLEIEKEEKE----KLKMEAKENTAI 782
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-211 |
6.66e-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: 46.98 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 1 NLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKE---EKRRE----EQKAQLQRAQVQELNDRLKRVQDELH-----L 68
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDlsslEQEIENVKSELKELEARIEELEEDLHkleeaL 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 69 KTIEEQMTHRKMILLQEESDKFKrsadEFRKKMEKLMESkvvTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELER 148
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKLE----EEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4559271 149 Q---LQCYREKMQQgppVEANHYQKCRRLEEELLAQRREVENLKQKMDQ----------QIKEHEHQLLRLQCEIQ 211
Cdd:TIGR02169 855 EienLNGKKEELEE---ELEELEAALRDLESRLGDLKKERDELEAQLRElerkieeleaQIEKKRKRLSELKAKLE 927
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
17-198 |
6.99e-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: 46.30 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEE---------- 86
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 87 -----SDKFKRSADEFRKKMEKLMESKVVTETD---LSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQ 158
Cdd:COG4942 116 lgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARreqAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4559271 159 QGPPVEANHYQKCRRLEEELLAQRREVENLKQKMDQQIKE 198
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-219 |
8.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 3 VSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQD-----ELHLKTIEEQMTH 77
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 78 RKMIL-LQEESDKFKRSADEFRKKMEKLmESKvvtETDLSGIKHDFVSLQRENFRAQENAKLWETnIRELERQLQCYREK 156
Cdd:PRK03918 306 LDELReIEKRLSRLEEEINGIEERIKEL-EEK---EERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKR 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4559271 157 MQQGPPVEA-NHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQ-----CEIQKKSTTQDH 219
Cdd:PRK03918 381 LTGLTPEKLeKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEH 449
|
|
| PLEC |
smart00250 |
Plectin repeat; |
896-928 |
1.29e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 1.29e-04
10 20 30
....*....|....*....|....*....|...
gi 4559271 896 RCLEFQYLTGGLIEPKVFSRLTIEEALHVGIID 928
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1-197 |
1.34e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 1 NLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDEL-HLKTIEEQMTHRK 79
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsSLKEKIEKLESEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 80 MILLQEESD-KFKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQ 158
Cdd:TIGR04523 534 KEKESKISDlEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
170 180 190
....*....|....*....|....*....|....*....
gi 4559271 159 QgppvEANHYQKCRRLEEELLAQRREVENLKQKMDQQIK 197
Cdd:TIGR04523 614 S----LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PLEC |
smart00250 |
Plectin repeat; |
584-616 |
1.82e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|...
gi 4559271 584 KHILEAQIASGGVIDPVRGVRVPPEMAVQQGLL 616
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-217 |
2.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 5 EFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQ 84
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 85 EESDKFKRSADEFRKKMEKLMESKVVTETDLSGIKhdfvslqRENFRAQENAKLWETNIRELERQlqcyREKMQQGPPVE 164
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK-------AEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKE 1642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4559271 165 ANHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHqlLRLQCEIQKKSTTQ 217
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEA 1693
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-207 |
7.65e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRR-EEQKAQLQR------AQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDK 89
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEElEEELAELEEeleeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 90 FKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQGPPVEANHYQ 169
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
170 180 190
....*....|....*....|....*....|....*...
gi 4559271 170 KCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQ 207
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-222 |
1.35e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 16 IIQKTEKEVRSLSAELSA-----SKEEKRREEQKA---QLQRAQ--VQELNDRLKRVQDE-------------------- 65
Cdd:TIGR02169 147 FISMSPVERRKIIDEIAGvaefdRKKEKALEELEEveeNIERLDliIDEKRQQLERLRRErekaeryqallkekreyegy 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 66 LHLKTIEEQMTHRKMIL-----LQEESDKFKRSADEFRKKMEKLMES--------KVVTETDLSGIKHDFVSLQREnfra 132
Cdd:TIGR02169 227 ELLKEKEALERQKEAIErqlasLEEELEKLTEEISELEKRLEEIEQLleelnkkiKDLGEEEQLRVKEKIGELEAE---- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 133 QENAklwETNIRELERQLQCYREKMQQGpPVEANHYQ-KCRRLEEELLAQRREVENLKqkmdQQIKEHEHQLLRLQCEIQ 211
Cdd:TIGR02169 303 IASL---ERSIAEKERELEDAEERLAKL-EAEIDKLLaEIEELEREIEEERKRRDKLT----EEYAELKEELEDLRAELE 374
|
250
....*....|.
gi 4559271 212 KKSTTQDHTFA 222
Cdd:TIGR02169 375 EVDKEFAETRD 385
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
12-204 |
2.01e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 12 QQSMIIQKTEKEVRSLSAELSASKEEKRREEQKA---------------------------QLQRAQVQELNDRLKRV-Q 63
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAekarqaemdrqaaiyaeqermamererELERIRQEERKRELERIrQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 64 DELHLKTIEEQMTHRKMILLQEESDKFKRSADEFRKkmEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNI 143
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARK--VKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4559271 144 RELERQLQCYREKMQQgppveanhYQKCRRLEEEllAQRREVENLKQKMDQQIKEHEHQLL 204
Cdd:pfam17380 446 REMERVRLEEQERQQQ--------VERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKI 496
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
39-209 |
2.04e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 39 RREEQKAQLQRAQVQELNDRLKRVQDELHLKtiEEQMTHRKMILLQEESDKFKRSADEFRKKMEKLMESKVVTEtdlsgi 118
Cdd:pfam15558 33 AWEELRRRDQKRQETLERERRLLLQQSQEQW--QAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 119 KHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREK---MQQGPPVEANHYQKCRRLEEEL------LAQRREVENLK 189
Cdd:pfam15558 105 NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQnslQLQERLEEACHKRQLKEREEQKkvqennLSELLNHQARK 184
|
170 180
....*....|....*....|
gi 4559271 190 QKMDQQIKEHEHqLLRLQCE 209
Cdd:pfam15558 185 VLVDCQAKAEEL-LRRLSLE 203
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
11-197 |
2.05e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 11 DQQSMIIQKTEKE------VRSLSAELSASKEEKRREEQKAqlQRAQVQELNDRLKRVQDELHL--KTIEEQMTHRKmil 82
Cdd:pfam15709 319 DPSKALLEKREQEkasrdrLRAERAEMRRLEVERKRREQEE--QRRLQQEQLERAEKMREELELeqQRRFEEIRLRK--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 83 lQEESDKFKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQREnfRAQENAKLWETNIR---ELERQLQCYREKMQQ 159
Cdd:pfam15709 394 -QRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK--KQQEEAERAEAEKQrqkELEMQLAEEQKRLME 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 4559271 160 GPPVEANHYQKCRRLEEEllAQRREVENLKQKMDQQIK 197
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEE--KARLEAEERRQKEEEAAR 506
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
35-217 |
2.16e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 35 KEEKRREEQKaqlQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSA---DEFRKKMEKLMESKvvt 111
Cdd:pfam10174 456 KEQREREDRE---RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkDSKLKSLEIAVEQK--- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 112 etdlsgiKHDFVSLQRENFRAQENAKLWETN------IRELERQLQCYREkmqqgppvEANhyqKCRRLEEELLAQRREV 185
Cdd:pfam10174 530 -------KEECSKLENQLKKAHNAEEAVRTNpeindrIRLLEQEVARYKE--------ESG---KAQAEVERLLGILREV 591
|
170 180 190
....*....|....*....|....*....|..
gi 4559271 186 ENLKQKMDQQIKEHEHQLLRlQCEIQKKSTTQ 217
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLR-QMKEQNKKVAN 622
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-178 |
2.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 1 NLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKEEKrreEQKAQLQRAQvQELndRLKRVQDELHLKTIEEQMTHRKM 80
Cdd:pfam01576 271 AQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL---EDTLDTTAAQ-QEL--RSKREQEVTELKKALEEETRSHE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 81 ILLQEESDKFKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQG 160
Cdd:pfam01576 345 AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES 424
|
170
....*....|....*...
gi 4559271 161 PPVEANHYQKCRRLEEEL 178
Cdd:pfam01576 425 ERQRAELAEKLSKLQSEL 442
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3-153 |
2.35e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 3 VSEFKQKCDQQSMIIQKTEKEVRSLSAELSasKEEKRREEQKAQLQRAQVQELNDRLKR-VQDELHLKTIEEQMTHRKMI 81
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELE--KEKRDRKRAEEQRRKILEKELEERKQAmIEEERKRKLLEKEMEERQKA 528
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4559271 82 LLQEESdkfKRSADEFRKKMEKLMESKVVTEtdlsgiKHDFVSLQRENFRAQENAKLWETNIRELERQLQCY 153
Cdd:pfam17380 529 IYEEER---RREAEEERRKQQEMEERRRIQE------QMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
16-216 |
2.77e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 16 IIQKTEKEVRSLSAELSASKEekrreeqkaqlqraQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSAD 95
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKK--------------QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 96 EFRKKMEKLMESKVVTETDLSGIKHDFVSLQREnfRAQENAKLWETNIRELERQLQCYREKMqqgppveANHYQKCRRLE 175
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQI-------SQNNKIISQLN 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4559271 176 EELLAQRREVENL---KQKMDQQIKEHEHQLLRLQCEIQKKSTT 216
Cdd:TIGR04523 342 EQISQLKKELTNSeseNSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-250 |
3.92e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSA-------ELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHL--KTIEEqmthrkmilLQEES 87
Cdd:TIGR02169 800 LSKLEEEVSRIEArlreieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlnGKKEE---------LEEEL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 88 DKFKRSADEFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQGPPVEANH 167
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 168 ------YQKCRRLEEELLA----------QRREVE----NLKQKMDQQIKEHEHQLLRL-QCEIQKKSttqdhTFASAFD 226
Cdd:TIGR02169 951 lsledvQAELQRVEEEIRAlepvnmlaiqEYEEVLkrldELKEKRAKLEEERKAILERIeEYEKKKRE-----VFMEAFE 1025
|
250 260
....*....|....*....|....*
gi 4559271 227 TAGRECHHP-AEISPGnSGHLNLKT 250
Cdd:TIGR02169 1026 AINENFNEIfAELSGG-TGELILEN 1049
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-207 |
4.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 41 EEQKAQLQRAQvqELNDRLKRVQDELHLKTIEEqmthrkmilLQEESDKFKRSADEFRKKMEKLMESKVVTETDLSGIKH 120
Cdd:COG1196 206 ERQAEKAERYR--ELKEELKELEAELLLLKLRE---------LEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 121 DFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQGppveanhyqkcRRLEEELLAQRREVENLKQKMDQQIKEHE 200
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-----------EERLEELEEELAELEEELEELEEELEELE 343
|
....*..
gi 4559271 201 HQLLRLQ 207
Cdd:COG1196 344 EELEEAE 350
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-189 |
4.97e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASKEEKRreeqkaqLQRAQVQELNDRLKRVQDELhlktieeqmthrkmILLQEESDKFKRSADE 96
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELE-------DLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 97 FRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQgppVEANHY---QKCRR 173
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK---YEQELYdlkEEYDR 480
|
170
....*....|....*.
gi 4559271 174 LEEELLAQRREVENLK 189
Cdd:TIGR02169 481 VEKELSKLQRELAEAE 496
|
|
| PLEC |
smart00250 |
Plectin repeat; |
788-818 |
5.13e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 35.54 E-value: 5.13e-03
10 20 30
....*....|....*....|....*....|.
gi 4559271 788 SPIAGYWLTASGERISLLKASRRNLVDRVTA 818
Cdd:smart00250 8 SAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
13-215 |
5.13e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 13 QSMIIQKTEKEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKR 92
Cdd:pfam05483 193 EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 93 SADEFR---KKMEKLMESKVVTETDLSGIKhdfVSLQRE---NFRAQENAKLWETNIRELERQLQCyreKMQQGPPVEAN 166
Cdd:pfam05483 273 LEEKTKlqdENLKELIEKKDHLTKELEDIK---MSLQRSmstQKALEEDLQIATKTICQLTEEKEA---QMEELNKAKAA 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4559271 167 HyqkcRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQCEIQKKST 215
Cdd:pfam05483 347 H----SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
17-212 |
7.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 17 IQKTEKEVRSLSAELSASkeekrrEEQKAQLQrAQVQELNDRLKRVQDElhLKTIEEQMThrkmiLLQEESDKFKRSADE 96
Cdd:COG3883 18 IQAKQKELSELQAELEAA------QAELDALQ-AELEELNEEYNELQAE--LEALQAEID-----KLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 97 FRKKMEKLMESKVVTETDLSGIK--------HDFVS--LQRENFRAQENAKLweTNIRELERQLQCYREKMQQgppvean 166
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDvllgsesfSDFLDrlSALSKIADADADLL--EELKADKAELEAKKAELEA------- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4559271 167 hyqkcrrLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQCEIQK 212
Cdd:COG3883 155 -------KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
28-223 |
7.77e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 28 SAELSASKEEKRREEQKAQLQ------RAQVQELNDRL---------KRVQDELHLKTIEEQmthrKMILLQEESDKFK- 91
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNqllrtlDDQWKEKRDELngelsaadaAVAKDRSELEALEDQ----HGAFLDADIETAAa 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 92 --RSADEFRKKMEKLMESKVVTETDLSGIKHDFVSlqRENFRAQENAklweTNIRELERQLQCYREKMQQGPPVEANHYQ 169
Cdd:pfam12128 345 dqEQLPSWQSELENLEERLKALTGKHQDVTAKYNR--RRSKIKEQNN----RDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4559271 170 K-CRRLEEELLAQRRE-----------VENLKQKMDQQIKEHE--HQLLRLQCEIQKKSTTQDHTFAS 223
Cdd:pfam12128 419 AlESELREQLEAGKLEfneeeyrlksrLGELKLRLNQATATPEllLQLENFDERIERAREEQEAANAE 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
473-509 |
9.08e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 34.77 E-value: 9.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 4559271 473 KFLTKATSIAGLYLESSKEKMSFTSAAQKIIIDKMIA 509
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-202 |
9.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 22 KEVRSLSAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQ--MTHRKMILLQEESDKFKRSADEFRK 99
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4559271 100 KMEKLMEskvvTETDLSGIKHDFVSLQREnfRAQENAKLWETNIRELERQLQCYREKMQQgppveanhyqkCRRLEEELL 179
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEE--LEELLEQLSLATEEELQDLAEELEELQQR-----------LAELEEELE 216
|
170 180
....*....|....*....|...
gi 4559271 180 AQRREVENLKQKMDQQIKEHEHQ 202
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAA 239
|
|
| |
