|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-202 |
1.23e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQV 121
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 122 EVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTKLEATTKAKELL 199
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLELQIASL 398
|
...
gi 79325918 200 EAH 202
Cdd:TIGR02168 399 NNE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-201 |
5.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAkQLGKAQARADELEKQVE 122
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEA 201
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
16-201 |
5.10e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 16 FTTSVFADadePEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEV--- 92
Cdd:COG3883 8 APTPAFAD---PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 93 --------SSLQKKGSSDSAKQ-----------LGKAQARADELEKQVEVLKNFLEQKNK---EKDSTEARTNEAEKKLR 150
Cdd:COG3883 85 reelgeraRALYRSGGSVSYLDvllgsesfsdfLDRLSALSKIADADADLLEELKADKAEleaKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79325918 151 ELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEA 201
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-196 |
6.83e-09 |
|
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: 56.09 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKK-GSSDSAKQLGKAQARADELEKQV 121
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYEALQKEIESLKRRI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79325918 122 EVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKlERAIKIAEEEMLRTKLEATTKAK 196
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA-ELEELEAEREELAAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-201 |
1.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLqteVSSLQKKG---------SSDSAKQLGKA--- 110
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL---LRALYRLGrqpplalllSPEDFLDAVRRlqy 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 111 -QARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKiAEEEMLRTKL 189
Cdd:COG4942 141 lKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQ 219
|
170
....*....|..
gi 79325918 190 EATTKAKELLEA 201
Cdd:COG4942 220 QEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-201 |
1.75e-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: 56.60 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSdSAKQLGKAQARADELEKQVE 122
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEA 201
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-201 |
1.89e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 48 AKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAkQLGKAQARADELEKQVEV---- 123
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIARleer 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 124 ---LKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLE 200
Cdd:COG1196 311 rreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
.
gi 79325918 201 A 201
Cdd:COG1196 391 A 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-200 |
6.77e-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: 54.64 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQGKDEVVAEK----EKLLKERE---DKIASLQTEVSSL------QKKGSSDSAKQLGKA 110
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKqneiEKLKKENQsykQEIKNLESQINDLeskiqnQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 111 QARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNssldklqKTNEEQKNKIGKLERAIKIAEEEMLRTKLE 190
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-------NTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
170
....*....|
gi 79325918 191 ATTKAKELLE 200
Cdd:TIGR04523 491 LKSKEKELKK 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-201 |
1.28e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQgkdevVAEKEKLLKEREDKiasLQTEVSSLQKKgssdsakqlgKAQARADELEKQV 121
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAE-----KAERYRELKEELKE---LEAELLLLKLR----------ELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 122 EVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEA 201
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-206 |
2.44e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKkgssdsakQLGKAQARADELEKQV 121
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--------EEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 122 EVLKnfleqknKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEmlrtKLEATTKAKELLEA 201
Cdd:COG1196 305 ARLE-------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAE 373
|
....*
gi 79325918 202 HGSWL 206
Cdd:COG1196 374 LAEAE 378
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-203 |
2.73e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLqkkgssdsAKQLGKAQARADELEKQVE 122
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL--------AAEIEELEELIEELESELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEAH 202
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
.
gi 79325918 203 G 203
Cdd:TIGR02168 957 E 957
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
83-177 |
4.19e-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: 51.69 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 83 DKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKT 162
Cdd:COG4942 20 DAAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90
....*....|....*
gi 79325918 163 NEEQKNKIGKLERAI 177
Cdd:COG4942 99 LEAQKEELAELLRAL 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-201 |
5.47e-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: 51.30 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 16 FTTSVFADADEPEVSEAAgsdgsskihLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSL 95
Cdd:COG4942 11 LALAAAAQADAAAEAEAE---------LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 96 QkkgssdsaKQLGKAQARADELEKQVEVLKNFLE------QKNKEKDSTE-------------------ARTNEAEKKLR 150
Cdd:COG4942 82 E--------AELAELEKEIAELRAELEAQKEELAellralYRLGRQPPLAlllspedfldavrrlqylkYLAPARREQAE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79325918 151 ELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEmlRTKLEATTKAKELLEA 201
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEE--RAALEALKAERQKLLA 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
43-206 |
1.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDE---KTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAK-QLGKAQARADELE 118
Cdd:COG4717 73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEaELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 119 KQVEVLKNFLEQ-----------KNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--L 185
Cdd:COG4717 153 ERLEELRELEEEleeleaelaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqL 232
|
170 180
....*....|....*....|.
gi 79325918 186 RTKLEATTKAKELLEAHGSWL 206
Cdd:COG4717 233 ENELEAAALEERLKEARLLLL 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
43-191 |
2.07e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVE 122
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-LAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEA 191
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-202 |
2.58e-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: 49.67 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 38 SSKIHLDQLNAKIRALESQIDEKTREvqgkdevvAEKEKLLKEREDKIASLQTEVSSLQKKgssdsakqlgKAQARADEL 117
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQ--------AEKAERYKELKAELRELELALLVLRLE----------ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 118 EKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTKLEATTKA 195
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEELEAQ 324
|
....*..
gi 79325918 196 KELLEAH 202
Cdd:TIGR02168 325 LEELESK 331
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
61-203 |
2.62e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 61 TREVQGKDEVvaekeklLKEREDKIASLqTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLKNFLEQKnkekdstEA 140
Cdd:PRK09039 45 SREISGKDSA-------LDRLNSQIAEL-ADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAEL-------AG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79325918 141 RTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIkiaeeEMLRTKLEATTKAKELLEAHG 203
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI-----AALRRQLAALEAALDASEKRD 167
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-200 |
2.75e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQGKDEVvaekEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKqvev 123
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKELEE---- 235
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79325918 124 LKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEE-EMLRTKLEATTKAKELLE 200
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIE 313
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-183 |
2.79e-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: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALE-----SQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADEL 117
Cdd:TIGR02169 774 LHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 118 EKQVEVLKNFLEQKNKEKDSTEARTNE--------------AEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEE 183
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDlesrlgdlkkerdeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-201 |
4.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVqgkdEVVAEKEKLLKERedkIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVE 122
Cdd:COG1196 304 IARLEERRRELEERLEELEEEL----AELEEELEELEEE---LEELEEELEEAEEE-LEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEA 201
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-184 |
5.29e-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: 48.91 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVqgkDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVE 122
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQL---ERLRREREKAERYQALLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSS-LDKLQKTNEEQKNKIGKLERAIKIAEEEM 184
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-202 |
5.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREdkIASLQTEVSSLQKKGSSDSAKQL---GKAQARADELE 118
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELraaLEQAEEYQELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 119 KQVEVLKNFLEQKNKE---------KDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLER----AIKIAEEEML 185
Cdd:COG4717 402 EELEELEEQLEELLGEleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgelAELLQELEEL 481
|
170 180
....*....|....*....|....
gi 79325918 186 RTKLEATTK-------AKELLEAH 202
Cdd:COG4717 482 KAELRELAEewaalklALELLEEA 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-183 |
5.85e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 38 SSKIHLDQLNAKIRALESQIDEKTREVQGKDEV--VAEKEKLLKEREDK-----IASLQTEVSSLQKKgSSDSAKQLGKA 110
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikKLQQEKELLEKEIErlketIIKNNSEIKDLTNQ-DSVKELIIKNL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 111 QARADELEKQVEVL-------KNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEE 183
Cdd:TIGR04523 460 DNTRESLETQLKVLsrsinkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
22-182 |
7.91e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 22 ADADEPEVSEAAGSDGSSKIHLDQLNAKI------RALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSL 95
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 96 ------QKKGSSDSAKQLGKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNeAEKKLRELNSSLDKLQKTNEEQKNK 169
Cdd:PRK02224 550 eaeaeeKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRER 628
|
170
....*....|....
gi 79325918 170 IG-KLERAIKIAEE 182
Cdd:PRK02224 629 LAeKRERKRELEAE 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-184 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 45 QLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGS-----------SDSAKQLGKAQAR 113
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 114 ADELEK---QVEVLKNFLEQKNKE-----------KDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKI 179
Cdd:TIGR02169 814 LREIEQklnRLTLEKEYLEKEIQElqeqridlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
....*
gi 79325918 180 AEEEM 184
Cdd:TIGR02169 894 LEAQL 898
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-198 |
1.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 48 AKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTevssLQKKGSSDsaKQLGKAQARADELEKQVEVLknf 127
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR----LAEYSWDE--IDVASAEREIAELEAELERL--- 680
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79325918 128 leqknkEKDSTEARtnEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTKLEATTKAKEL 198
Cdd:COG4913 681 ------DASSDDLA--ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARL 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-200 |
1.49e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLlKEREDKIASLQTEVSSLqKKGSSDSAKQLGKAQARADELEKQV 121
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEY-LDELREIEKRLSRLEEEINGIEERI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 122 evlknfleqknKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEE------QKNKIGKLERAIKIAEEEMLRTKLEATTKA 195
Cdd:PRK03918 331 -----------KELEEKEERLEELKKKLKELEKRLEELEERHELyeeakaKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
....*
gi 79325918 196 KELLE 200
Cdd:PRK03918 400 KEEIE 404
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
63-201 |
1.59e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 63 EVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQkkgssdsaKQLGKAQARADELEKQVEVLKNFLEQKN---------- 132
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALE--------ARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeql 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 133 -------------KEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEmLRTKLEATTKAKELL 199
Cdd:COG1579 83 gnvrnnkeyealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE-LDEELAELEAELEEL 161
|
..
gi 79325918 200 EA 201
Cdd:COG1579 162 EA 163
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-203 |
1.73e-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: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 19 SVFADADEPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEK---LLKEREDK----IASLQTE 91
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKeieQLEQEEEKlkerLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 92 VSSLQKKGSSDSAKQ------LGKAQARADELEKQVEVLK-----NFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQ 160
Cdd:TIGR02169 746 LSSLEQEIENVKSELkelearIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 161 KTNE-----------------EQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLEAHG 203
Cdd:TIGR02169 826 LEKEylekeiqelqeqridlkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-191 |
2.67e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKI--ASLQTEVSSLQKKgssdsAKQLGKAQARADELEKQ 120
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAE-----LERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79325918 121 VEVLKnfleqknKEKDSTEARTNEAEKKLRELNSSLDKLQktnEEQKNKIGKLERAIKIAEEEmLRTKLEA 191
Cdd:COG4913 694 LEELE-------AELEELEEELDELKGEIGRLEKELEQAE---EELDELQDRLEAAEDLARLE-LRALLEE 753
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-198 |
3.24e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDE---KTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGS-----SDSAKQLGKAQAR 113
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeakkkADAAKKKAEEAKK 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 114 ADELEK-QVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKnkigKLERAIKIAEEemLRTKLEAT 192
Cdd:PTZ00121 1344 AAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----KAEEDKKKADE--LKKAAAAK 1417
|
....*.
gi 79325918 193 TKAKEL 198
Cdd:PTZ00121 1418 KKADEA 1423
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-201 |
7.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 22 ADADEPEVSEAAGSdgSSKIHLDQLNAKIRALESQIDEKTR--EVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKG 99
Cdd:PTZ00121 1354 AAADEAEAAEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 100 SSDSAKQLGKAQARADELEKQVEVLKnflEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKI 179
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
170 180
....*....|....*....|..
gi 79325918 180 AEEEMLRTKLEATTKAKELLEA 201
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKA 1530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
42-152 |
7.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQV 121
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
90 100 110
....*....|....*....|....*....|....
gi 79325918 122 ---EVLKNFLEQKNKEKDSTEARTNEAEKKLREL 152
Cdd:COG4913 759 lgdAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
37-182 |
7.98e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 37 GSSKIHLDQLNAKIRALESQIDEKTREVQgkdEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADE 116
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAE---ALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADE 588
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79325918 117 LEKQVEVLKNFLEQKNKEKDSTEARtneaekklRELNSSLDKLqktnEEQKNKIGKLERAIKIAEE 182
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEAR--------KRLNKANEKK----EKKKKKQKEKQEELKVGDE 642
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
82-249 |
7.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 82 EDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVEVLKNFLEQKNKEKD--STEARTNEAEKKLRELNS----- 154
Cdd:COG4913 609 RAKLAALEAELAELEEE-LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDAssddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 155 -----SLDKLQKTNEEQKNKIGKLERAIKIAEEEmLRTKLEATTKAKELLEAHGSWLPPWLavhwfkfQTYTETHWEAHG 229
Cdd:COG4913 688 aaleeQLEELEAELEELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLEL-------RALLEERFAAAL 759
|
170 180
....*....|....*....|
gi 79325918 230 KPAVETVILKVTEAKAQAEK 249
Cdd:COG4913 760 GDAVERELRENLEERIDALR 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-200 |
9.66e-05 |
|
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: 44.63 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREV-QGKDEVVAEKEKLLKER-EDKIASLQTEVSSLQKKGSSDSAKQlGKAQARADELEKQV 121
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKIsDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKKKQ-EEKQELIDQKEKEK 598
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 122 EVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQktneEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKELLE 200
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK----SKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
43-183 |
1.21e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREV---------QGK---------DEVVAEKEKLL-------KEREDKIASLQTEVSSLqk 97
Cdd:PRK11637 105 IDELNASIAKLEQQQAAQERLLaaqldaafrQGEhtglqlilsGEESQRGERILayfgylnQARQETIAELKQTREEL-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 98 kgssdsakqlgkAQARADELEKQVEvLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQ------KTNEEQ-KNKI 170
Cdd:PRK11637 183 ------------AAQKAELEEKQSQ-QKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQqqlselRANESRlRDSI 249
|
170
....*....|....
gi 79325918 171 GKLERAIKI-AEEE 183
Cdd:PRK11637 250 ARAEREAKArAERE 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-184 |
1.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQG--------KDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgssdsAKQLG-KAQAR 113
Cdd:COG4913 304 LARLEAELERLEARLDALREELDEleaqirgnGGDRLEQLEREIERLERELEERERRRARLEAL-----LAALGlPLPAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 114 ADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGK-----------LERAIKIAEE 182
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparllalrdaLAEALGLDEA 458
|
..
gi 79325918 183 EM 184
Cdd:COG4913 459 EL 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
40-186 |
1.32e-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: 42.99 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 40 KIHLDQLNAKIRALESQIdektrevqgkdevvAEKEKLLKEREDKIASLQT--EVSSLQkkgssdsaKQLGKAQARADEL 117
Cdd:COG1579 51 KTELEDLEKEIKRLELEI--------------EEVEARIKKYEEQLGNVRNnkEYEALQ--------KEIESLKRRISDL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 118 EKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDK-LQKTNEEQKNKIGKLERAIKIAEEEMLR 186
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELEELEAEREELAAKIPPELLA 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
41-201 |
1.38e-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: 42.99 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 41 IHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKkgssdsakQLGKAQARADELEKQ 120
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL--------EIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 121 VEVLKNFLEQKN--KEKDSTEARTNEAEKKLRELNSSLDKLQKtneeqknkigklerAIKIAEEEMLRTKLEATTKAKEL 198
Cdd:COG1579 82 LGNVRNNKEYEAlqKEIESLKRRISDLEDEILELMERIEELEE--------------ELAELEAELAELEAELEEKKAEL 147
|
...
gi 79325918 199 LEA 201
Cdd:COG1579 148 DEE 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-200 |
1.61e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 56 QIDEKTREVQGKDEVVAEKEKLLKEREDKIASL----QTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLKNFLEQK 131
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 132 NKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIaeeemLRTKLEATTKAKELLE 200
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-----LESKIQNQEKLNQQKD 411
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
43-197 |
1.82e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDsaKQLgkaQARADELEKQVE 122
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN--KSL---ESQISELKKQNN 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTKLEATTKAKE 197
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqLKSEISDLNNQKE 305
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-198 |
1.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 24 ADEPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDE---KTREVQGKDEVVAEKEKLlKEREDKIASLQTEVSSLQK--- 97
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAakkKAEEAKKAAEAAKAEAEA-AADEAEAAEEKAEAAEKKKeea 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 98 KGSSDSAKQLGKAQARADELEKQVEVLKNFLEQKNK----EKDSTEARTN-EAEKKLRELNSSLDKLQKTNEEQKN--KI 170
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKaaaaKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKaeEA 1456
|
170 180 190
....*....|....*....|....*....|..
gi 79325918 171 GKLERAIKIAEE----EMLRTKLEATTKAKEL 198
Cdd:PTZ00121 1457 KKAEEAKKKAEEakkaDEAKKKAEEAKKADEA 1488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-237 |
2.26e-04 |
|
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: 43.51 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 26 EPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQK---KGSSD 102
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrreRLQQE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 103 SAKQLGKAQ-ARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERaikiae 181
Cdd:TIGR02168 423 IEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER------ 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 79325918 182 eemLRTKLEATTKAKELLEAHGSWLPPWLAVHWFKFQtyTETHWEAhgkpAVETVI 237
Cdd:TIGR02168 497 ---LQENLEGFSEGVKALLKNQSGLSGILGVLSELIS--VDEGYEA----AIEAAL 543
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-200 |
2.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEV---VAEKEKLLKEREDKIASLQTEVSSLQK--KGSSDSAKQLGKAQARADEL 117
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELEEriEELKKEIEELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 118 EKQVE---VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLqktnEEQKNKIGKLERAIKIAEEEM--LRTKLEAT 192
Cdd:PRK03918 289 KEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLeeLEERHELY 364
|
....*...
gi 79325918 193 TKAKELLE 200
Cdd:PRK03918 365 EEAKAKKE 372
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-188 |
2.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 49 KIRALESQIDEKTREVQGKDEVVAEKEKLlKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLKNFL 128
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAK-KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 129 EQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKtNEEQKNKIGKLERAIKIAEEEMLRTK 188
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK-DEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-201 |
2.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 48 AKIRALESQIDEKTREVQGkdeVVAEKEKLLKERE--DKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLK 125
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK---VLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 126 NFLEQKN---KEKDSTEARTNEAEKKLRELNSSLDKLQ-KTNEEQKNKIGKLERA-------------IKIAEEEMLRTK 188
Cdd:PRK03918 546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFyneylelkdaekeLEREEKELKKLE 625
|
170
....*....|...
gi 79325918 189 LEATTKAKELLEA 201
Cdd:PRK03918 626 EELDKAFEELAET 638
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-201 |
2.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIdEKTREVQGKDEVVAEKeklLKEREDKIASLQTEVSSLQKKGSSDSAKQLG-------------K 109
Cdd:PRK03918 534 LIKLKGEIKSLKKEL-EKLEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKelepfyneylelkD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 110 AQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDklQKTNEEQKNKIGKLERAIKIAEEEM--LRT 187
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELeeLEK 687
|
170
....*....|....
gi 79325918 188 KLEATTKAKELLEA 201
Cdd:PRK03918 688 RREEIKKTLEKLKE 701
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
20-179 |
2.94e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 20 VFADADEPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQgkdevvaEKEKLLKEREDKIASLQTEVSSLQKKg 99
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 100 ssdsakqlgkaqaRADELEKQVEVlknfleqknkekdstEARTNEAEkklrELNSSLDKLQKTNEEQKNKIGKLERAIKI 179
Cdd:COG2433 457 -------------ERREIRKDREI---------------SRLDREIE----RLERELEEERERIEELKRKLERLKELWKL 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
43-203 |
3.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEvvaekeklLKEREDKIASLQTEVSslqkkgssDSAKQLGKAQARADELEKQVE 122
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKE--------LEREEKELKKLEEELD--------KAFEELAETEKRLEELRKELE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 123 VLK------------NFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQ---KTNEEQKNKIGKLERAIKIAEEemLRT 187
Cdd:PRK03918 651 ELEkkyseeeyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKeelEEREKAKKELEKLEKALERVEE--LRE 728
|
170
....*....|....*.
gi 79325918 188 KLEattKAKELLEAHG 203
Cdd:PRK03918 729 KVK---KYKALLKERA 741
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
101-201 |
3.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 101 SDSAKQLGKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIA 180
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100
....*....|....*....|...
gi 79325918 181 EEEM--LRTKLEATTKAKELLEA 201
Cdd:COG4372 107 QEEAeeLQEELEELQKERQDLEQ 129
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-184 |
3.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 46 LNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSS-------------DSAKQLGKAQA 112
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaalrDLESRLGDLKK 889
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79325918 113 RADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKN------KIGKLERAIKIAEEEM 184
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEI 967
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
51-198 |
4.22e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 51 RALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQK---KGSSDSAKQLGKAQARADELEKQVEVLKN- 126
Cdd:COG5022 850 KFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSlklVNLELESEIIELKKSLSSDLIENLEFKTEl 929
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 127 --FLEQKNKEKDSTEARTNEAEK-----KLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEATTKAKEL 198
Cdd:COG5022 930 iaRLKKLLNNIDLEEGPSIEYVKlpelnKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY 1008
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
44-198 |
4.54e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQgkdEVVAEKEKL---LKEREDKIASLQTEVSSLQK------KGS---------SDSAK 105
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELL---NLVMDIEDPsaaLNKLNTAAAKIKSKIEQFQKvikmyeKGGvcptctqqiSEGPD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 106 QLGKAQARADELEKQVEVLKNFLEQKNKEKDSTeartNEAEKKLRELNSSLdklqktnEEQKNKIGKLERAIKIAEEEML 185
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEF----NEQSKKLLELKNKI-------STNKQSLITLVDKAKKVKAAIE 368
|
170
....*....|...
gi 79325918 186 RTKLEATTKAKEL 198
Cdd:PHA02562 369 ELQAEFVDNAEEL 381
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
39-202 |
4.72e-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: 42.31 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 39 SKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKkgssdsakQLGKAQARADELE 118
Cdd:TIGR04523 94 NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK--------ELEKLNNKYNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 119 KQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQK---NKIGKLERAIKIAEEEMLRTKLEATTKA 195
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKsleSQISELKKQNNQLKDNIEKKQQEINEKT 245
|
....*..
gi 79325918 196 KELLEAH 202
Cdd:TIGR04523 246 TEISNTQ 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
40-198 |
4.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 40 KIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgssDSAKQLGKAQ----ARAD 115
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKAEeenkIKAA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 116 ELEKQVEVLKNFLEQKNKEKDStEARTNEAEKKLRELNSSLDKLQKTNEEQKNK---IGKLERAIKIAEEEMLRTKLEAT 192
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDK 1743
|
....*.
gi 79325918 193 TKAKEL 198
Cdd:PTZ00121 1744 KKAEEA 1749
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
115-195 |
5.89e-04 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 42.02 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 115 DELEKQV-EVLKNFLEQKNKE-----KDSTEARTNEAEKKLRELNSSLDKLQKtnEEQKNKIGKLERAIKIAEEEMLRTK 188
Cdd:CHL00094 505 DEVERMVkEAEKNAAEDKEKRekidlKNQAESLCYQAEKQLKELKDKISEEKK--EKIENLIKKLRQALQNDNYESIKSL 582
|
....*..
gi 79325918 189 LEATTKA 195
Cdd:CHL00094 583 LEELQKA 589
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
39-200 |
6.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 39 SKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKkgssdsakQLGKAQARADELE 118
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE--------QLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 119 KQvevlknfLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTKLEATTKAK 196
Cdd:COG4372 101 EE-------LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLesLQEELAALEQEL 173
|
....
gi 79325918 197 ELLE 200
Cdd:COG4372 174 QALS 177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
45-130 |
6.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 45 QLNAKIRALESQIDEKTREVqgkdevVAEKEKLLKEREDKIASLQTEVSSLQKKgssdsAKQLGKAQARADELEKQVEVL 124
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRI------LASLEAELEALQAREASLQAQLAQLEAR-----LAELPELEAELRRLEREVEVA 363
|
....*.
gi 79325918 125 KNFLEQ 130
Cdd:COG3206 364 RELYES 369
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
43-167 |
6.86e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQID-EKTREVQGKDEVVAEKEKL-----LKER-EDKIASLQTEVSSLQKK-----GSSDSAKQLGK- 109
Cdd:PRK09039 55 LDRLNSQIAELADLLSlERQGNQDLQDSVANLRASLsaaeaERSRlQALLAELAGAGAAAEGRagelaQELDSEKQVSAr 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79325918 110 AQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKL----RELNSSLdkLQKTNEEQK 167
Cdd:PRK09039 135 ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIadlgRRLNVAL--AQRVQELNR 194
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-200 |
7.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 42 HLDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLK---------------------EREDKIASLQTEVSSLQKKgS 100
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEE-V 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 101 SDSAKQLGKAQArADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIA 180
Cdd:PRK02224 492 EEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
170 180
....*....|....*....|..
gi 79325918 181 EEEM--LRTKLEATTKAKELLE 200
Cdd:PRK02224 571 REEVaeLNSKLAELKERIESLE 592
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
43-137 |
7.98e-04 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 38.32 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgssdsakqLGKAQARADELekqve 122
Cdd:cd22887 6 LQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEK--------LRKLQEENDEL----- 72
|
90
....*....|....*
gi 79325918 123 vLKNFLEQKNKEKDS 137
Cdd:cd22887 73 -VERWMAKKQQEADK 86
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-201 |
8.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 22 ADADEPEVSEAAGSDGSSKIHLDQL----NAKIRALESQidEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQK 97
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDK--KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 98 KgSSDSAKQLGKAQARADELEKQVEVLKNFLEQKNKekdSTEARTN-EAEKKLRELNSSLDKLQKTnEEQKNKIGKLERA 176
Cdd:PTZ00121 1444 K-KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK---AEEAKKAdEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKA 1518
|
170 180
....*....|....*....|....*
gi 79325918 177 IKIAEEEMLRtKLEATTKAKELLEA 201
Cdd:PTZ00121 1519 EEAKKADEAK-KAEEAKKADEAKKA 1542
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
44-192 |
9.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQK------KGSSDSAKQLGKAQARADEL 117
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqeleKAKRKLEGESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 118 EKQVEVLKNFLEQKNKEKDSTEART-------NEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM--LRTK 188
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELeaLKTE 307
|
....
gi 79325918 189 LEAT 192
Cdd:pfam01576 308 LEDT 311
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
43-183 |
1.18e-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: 41.16 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLqkkgssdsakqlgKAQARADELEKQVE 122
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-------------DFELKKENLEKEID 564
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEE 183
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-197 |
1.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQGKDEVVAEK----EKLLKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEK 119
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79325918 120 QVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKnkigKLERAIKIAEEEmlRTKLEATTKAKE 197
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEE--KKKAEELKKAEE 1726
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
43-156 |
1.43e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREvqgKDEVVAEKeklLKEREDKIASLQTEVSSLQKKgssdsakqlgkaQARADELEKQVE 122
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKE---QDEASFER---LAELRDELAELEEELEALKAR------------WEAEKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSL 156
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
76-185 |
1.52e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 76 KLLKER-----EDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVEVL-KNFLEQKNKEKDS--TEARTNEAEK 147
Cdd:pfam05622 292 KMLRLGqegsyRERLTELQQLLEDANRR-KNELETQNRLANQRILELQQQVEELqKALQEQGSKAEDSslLKQKLEEHLE 370
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 79325918 148 KLRELNSSLDKLQKTNEEQKN--------KIGKLERAIKIAEEEML 185
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPkqdsnlaqKIDELQEALRKKDEDMK 416
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
44-202 |
1.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 44 DQLNAKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgSSDSAKQLGKAQARADELEKQVEV 123
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER-FGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 124 LKNFL-----EQKNKEKDSTEART-----------------------NEAEKKLRELNSSLDKLQKTNEEQKNKIGKLER 175
Cdd:PRK02224 424 LREREaeleaTLRTARERVEEAEAlleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
170 180
....*....|....*....|....*...
gi 79325918 176 AIKIAEE-EMLRTKLEAttkAKELLEAH 202
Cdd:PRK02224 504 LVEAEDRiERLEERRED---LEELIAER 528
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
47-162 |
2.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 47 NAKIRALESQIDEKTREVqgkdevvAEKEKLLKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLKN 126
Cdd:COG3206 262 SPVIQQLRAQLAELEAEL-------AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
90 100 110
....*....|....*....|....*....|....*.
gi 79325918 127 FLEQKNKEkdstEARTNEAEKKLRELNSSLDKLQKT 162
Cdd:COG3206 335 QLAQLEAR----LAELPELEAELRRLEREVEVAREL 366
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
23-189 |
2.30e-03 |
|
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: 40.49 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 23 DADEPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQGkdevvaekeklLKEREDKIASLQTEVSSLQKkgssd 102
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH-----------LKNEGDHLRNVQTECEALKL----- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 103 sakQLGKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLEraIKIAEE 182
Cdd:pfam15921 556 ---QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE--ARVSDL 630
|
....*..
gi 79325918 183 EMLRTKL 189
Cdd:pfam15921 631 ELEKVKL 637
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
78-181 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 78 LKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQVEVLKnflEQKNKEKDSTEaRTNEAEKKLRELNSSLD 157
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALK---ARWEAEKELIE-EIQELKEELEQRYGKIP 488
|
90 100 110
....*....|....*....|....*....|.
gi 79325918 158 KLQKTNEEQKNKIGKLERAIK-------IAE 181
Cdd:COG0542 489 ELEKELAELEEELAELAPLLReevteedIAE 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-176 |
3.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 49 KIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKkgssdSAKQLGKAQARADELEKQVEVLKNF- 127
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGLt 385
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 79325918 128 LEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERA 176
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
46-195 |
4.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 46 LNAKIRAlESQIDEKTREVQG-KDEVVAE-KEKLLKEREDkiasLQTEVSSlqkkgssdsakqlgkaqaRADELEKQVEV 123
Cdd:PRK12704 34 KEAEEEA-KRILEEAKKEAEAiKKEALLEaKEEIHKLRNE----FEKELRE------------------RRNELQKLEKR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 124 LKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGK----LERAIKIAEEE---MLRTKLEATTKA 195
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqeLERISGLTAEEakeILLEKVEEEARH 169
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
43-183 |
4.53e-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: 37.96 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALEsqidEKTREVQGKdEVVAEKEklLKEREDKIASLQTEVSSLQKkgsSDSAKQLgkaqARADELEKQVE 122
Cdd:pfam15619 62 IARHNEEVRVLR----ERLRRLQEK-ERDLERK--LKEKEAELLRLRDQLKRLEK---LSEDKNL----AEREELQKKLE 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKL-RELNSSLDKLQKTNEEQKN---KIGKLERAIKIAEEE 183
Cdd:pfam15619 128 QLEAKLEDKDEKIQDLERKLELENKSFrRQLAAEKKKHKEAQEEVKIlqeEIERLQQKLKEKERE 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-202 |
5.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 25 DEPEVSEAAGSdgsSKIHLDQLNAkiraLESQIDEKTREVQGKDEVVAEKEKLLKEREDkIASLQTEVSSLQkkgssdsa 104
Cdd:COG4913 219 EEPDTFEAADA---LVEHFDDLER----AHEALEDAREQIELLEPIRELAERYAAARER-LAELEYLRAALR-------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 105 kqLGKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLREL--------NSSLDKLQKTNEEQKNKIGKLERA 176
Cdd:COG4913 283 --LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERR 360
|
170 180
....*....|....*....|....*.
gi 79325918 177 IKIAEEEMLRTKLEATTKAKELLEAH 202
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALR 386
|
|
| PRK12435 |
PRK12435 |
ferrochelatase; Provisional |
249-328 |
5.64e-03 |
|
ferrochelatase; Provisional
Pssm-ID: 183526 [Multi-domain] Cd Length: 311 Bit Score: 38.41 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 249 KWAEPHVEN-VKTKYIPAIKETVTIHVEPHFRTLSIKA--KEAYHSSKSAVSPHIVTvqefVDPYYQEaKKFSKPYVDQV 325
Cdd:PRK12435 86 KHIEPFIEDaVEQMHNDGIEEAISIVLAPHYSTFSVKSynKRAKEEAEKLGGPTITS----IESWYDE-PKFIQYWADQI 160
|
...
gi 79325918 326 ATT 328
Cdd:PRK12435 161 KET 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-197 |
5.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 51 RALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKgssdSAKQLGKAQA--RADELEKQVEVLKnfl 128
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADELKKAEEkkKADEAKKAEEKKK--- 1303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79325918 129 EQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKigkleRAIKIAEEEMLRTKLEATTKAKE 197
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA-----AEAAKAEAEAAADEAEAAEEKAE 1367
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
37-184 |
6.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 37 GSSKIHLDQLNAKIRALESQIDEKTREVqgkdevVAEKEKLLKEREDKIASLQTEVSSLQKkgssdSAKQLGKAQARADE 116
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKA------LFELDKLQEELEQLREELEQAREELEQ-----LEEELEQARSELEQ 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79325918 117 LEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEM 184
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
43-182 |
8.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNaKIRALESQIDEKTREVQGKDEVVAEKEKLLKEREDKIASLQTEVSSLQKKGSSDsakQLGKAQARADELEKQVE 122
Cdd:PRK02224 588 IESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA---RIEEAREDKERAEEYLE 663
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 123 VLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLqktnEEQKNKIGKLERAIKIAEE 182
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVENELEELEELRERR----EALENRVEALEALYDEAEE 719
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-186 |
8.80e-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: 38.62 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 22 ADADEPEVSEAAGSDGSSKIHLDQLNAKIRALESQIDEKTREVQGKDEVVAEK-EKLLKEREDKIASLQTEVSSLQKkgs 100
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRlRKSTLQVEQLTTELAAERSTSQK--- 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 101 SDSAKQL--------------------GKAQARADELEKQVEVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQ 160
Cdd:pfam01576 936 SESARQQlerqnkelkaklqemegtvkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDER 1015
|
170 180 190
....*....|....*....|....*....|...
gi 79325918 161 KTNEEQKNKIGK-------LERAIKIAEEEMLR 186
Cdd:pfam01576 1016 RHADQYKDQAEKgnsrmkqLKRQLEEAEEEASR 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-203 |
8.84e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 112 ARADELEKQVEVLKNFLEQKNKEKdstEARTNEAEKKLRELNSSLDKLQKTNEEQKNKIGKLERAIKIAEEEMLRTKLEA 191
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELK---ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90
....*....|..
gi 79325918 192 TTKAKELLEAHG 203
Cdd:COG1196 277 EELELELEEAQA 288
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
43-201 |
9.48e-03 |
|
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: 38.40 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 43 LDQLNAKIRALESQIDEKTREVQ-GKDEVVAEKEklLKEREDKIASLQTEVSSLQKKGSSDSAKQLGKAQARADELEKQV 121
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKeEIENIVGEVE--LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79325918 122 EVLKNFLEQKNKEKDSTEARTNEAEKKLRELNSSLDKLQKTNEEQKNKigKLERAIKIAEEEmLRTKLEATTKAKELLEA 201
Cdd:COG5185 416 KAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS--RLEEAYDEINRS-VRSKKEDLNEELTQIES 492
|
|
| |
