|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-201 |
8.47e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 29 IDGGDEPKLRSDGG-DIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsv 107
Cdd:TIGR02168 661 ITGGSAKTNSSILErRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD------ 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 108 elLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:TIGR02168 735 --LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170
....*....|....
gi 18400540 188 LRTKHEATTKAKEL 201
Cdd:TIGR02168 813 TLLNEEAANLRERL 826
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
45-201 |
1.34e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLeteVSSLRKKGSSDSV-----------ELLSKA 113
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---ARALYRSGGSVSYldvllgsesfsDFLDRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 114 QARATELEKQVEVLKKFLEQKNK---EKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRT 190
Cdd:COG3883 122 SALSKIADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
170
....*....|.
gi 18400540 191 KHEATTKAKEL 201
Cdd:COG3883 202 EAELAAAEAAA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-203 |
2.39e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVsslRKKGSSDSVELlskaQARATELEKQV 124
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRV----KEKIGELEAEI 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELME 203
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-189 |
4.04e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARATELEKQV 124
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLR 189
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-203 |
4.67e-10 |
|
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: 60.93 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLeteVSSLRKKGSSDSVELLSKAQArATELEK 122
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPED-FLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 123 QVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELM 202
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
.
gi 18400540 203 E 203
Cdd:COG4942 217 E 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
43-187 |
7.34e-10 |
|
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: 59.17 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKK--------GSSDSVELLSKAQ 114
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqlGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400540 115 ARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-203 |
5.05e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsVELLSKAQARateLEKQV 124
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-----EYELLAELAR---LEQDI 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELME 203
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-203 |
8.01e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQV 124
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE--------LEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELME 203
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-203 |
8.30e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQID---DKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRK--KGSSDSVELLSKAQARATE 119
Cdd:PRK03918 208 EINEISSELPELREELEkleKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEEriEELKKEIEELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 120 LEKQVE---VLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLhktnEEQKNKIRKLERALKISEEEM--LRTKHEA 194
Cdd:PRK03918 288 LKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRLeeLEERHEL 363
|
....*....
gi 18400540 195 TTKAKELME 203
Cdd:PRK03918 364 YEEAKAKKE 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-203 |
1.67e-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: 56.99 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQI--------DDKTKELKGREELVTEKEKL------LQERQDKVASLETEVSSLRKKGSSdSVELL 110
Cdd:TIGR02168 289 ELYALANEISRLEQQKqilrerlaNLERQLEELEAQLEELESKLdelaeeLAELEEKLEELKEELESLEAELEE-LEAEL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 111 SKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRT 190
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
170
....*....|...
gi 18400540 191 KHEATTKAKELME 203
Cdd:TIGR02168 448 ELEELQEELERLE 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
44-203 |
6.43e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 44 IELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQ 123
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE--------IEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 124 VEVLK--KFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKEL 201
Cdd:COG1579 82 LGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
..
gi 18400540 202 ME 203
Cdd:COG1579 162 EA 163
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-181 |
6.51e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELlSKAQARATELEKQV 124
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-EELEEELEELEAAL 877
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALK 181
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-203 |
7.43e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLlQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARATELEKQV 124
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERI 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 125 EVLkkflEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNkIRKLERALKISEEEMLRTKHEATTKAKELME 203
Cdd:PRK03918 331 KEL----EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE-LERLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
45-191 |
7.56e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARATELEKQV 124
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-LAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTK 191
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-201 |
1.61e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLR------KKGSSDSVELLSKAQARAT 118
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKqeiknlESQINDLESKIQNQEKLNQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 119 ELEKQVEVLKKFLEQKNKEKELIEAQT-------SETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTK 191
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIiknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
170
....*....|
gi 18400540 192 HEATTKAKEL 201
Cdd:TIGR04523 489 KELKSKEKEL 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-180 |
2.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQ--ERQDKVASLETEVSSLRKKgssdsVELLSKAQARATELEK 122
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEysWDEIDVASAEREIAELEAE-----LERLDASSDDLAALEE 692
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 123 QVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERAL 180
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
45-189 |
2.86e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQV 124
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE--------AEELQEELEELQKER 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLR 189
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
45-195 |
4.13e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTE--KEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSkAQARATELEK 122
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQIAALRA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 123 QVEV-LKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEqknkIRKLERALKISEE--EMLRTKHEAT 195
Cdd:COG3206 306 QLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE----LRRLEREVEVARElyESLLQRLEEA 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-204 |
6.50e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQ--DKVASLETEVSSLRKKGSSDSVELLSKAQARATELEK 122
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 123 QVEVLKKFLEQKN---KEKELIEAQTSETEKKLNELNSRVEKL-HKTNEEQKNKIRKLERA-------------LKISEE 185
Cdd:PRK03918 540 EIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFyneylelkdaekeLEREEK 619
|
170
....*....|....*....
gi 18400540 186 EMLRTKHEATTKAKELMEV 204
Cdd:PRK03918 620 ELKKLEEELDKAFEELAET 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-209 |
1.60e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDD---KTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVE-LLSKAQARATEL 120
Cdd:COG4717 72 ELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEaELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 121 EKQVEVLKKFLEQ-KNKEKELIEAQTS----------ETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM-- 187
Cdd:COG4717 152 EERLEELRELEEElEELEAELAELQEEleelleqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeq 231
|
170 180
....*....|....*....|..
gi 18400540 188 LRTKHEATTKAKELMEVHGAWL 209
Cdd:COG4717 232 LENELEAAALEERLKEARLLLL 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
49-203 |
1.80e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 49 LNAKIRAlESQIDDKTKELKG-REELVTE-KEKLLQERQDkvasLETEVSSLRKKgssdsvelLSKAQARateLEKQVEV 126
Cdd:PRK12704 34 KEAEEEA-KRILEEAKKEAEAiKKEALLEaKEEIHKLRNE----FEKELRERRNE--------LQKLEKR---LLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 127 LKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQknkIRKLERALKISEEE---ML------RTKHEATTK 197
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERISGLTAEEakeILlekveeEARHEAAVL 174
|
....*.
gi 18400540 198 AKELME 203
Cdd:PRK12704 175 IKEIEE 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-201 |
3.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQerqdKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKqv 124
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEP-- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 eVLKKFLEQKNKEKELiEAQTSETEKKLNELNSRVEKLHKTN---EEQKNKIRKLERalKISEEEMLRTKHEATTKAKEL 201
Cdd:PRK03918 600 -FYNEYLELKDAEKEL-EREEKELKKLEEELDKAFEELAETEkrlEELRKELEELEK--KYSEEEYEELREEYLELSREL 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
47-204 |
3.88e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 47 DQLNAKIRALESQIDDKTKELKGREELvtekEKLLQERQDKVASLETEVSSLRKKGSSDSVELlSKAQARATELEKqvev 126
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEE---- 235
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 127 LKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERaLKISEEEMLRTKHEATTKAKELMEV 204
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-209 |
4.06e-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: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALEsqIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELlSKAQARATELEKQV 124
Cdd:COG1196 221 ELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 EVLKKfleQKNKEKELIEaQTSETEKKLN----ELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKE 200
Cdd:COG1196 298 ARLEQ---DIARLEERRR-ELEERLEELEeelaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
....*....
gi 18400540 201 LMEVHGAWL 209
Cdd:COG1196 374 LAEAEEELE 382
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
45-205 |
4.11e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKgreELVTEKEKLlqerQDKVASLETEVSSLRKKGS--------SDSVELLSKAQAR 116
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALN---KLNTAAAKI----KSKIEQFQKVIKMYEKGGVcptctqqiSEGPDRITKIKDK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 117 ATELEKQvevLKKFLEQKNKEKElIEAQTSETEKKLNELNSRVEKLHKT--NEEQKNK-----IRKLERALKISEEEMLR 189
Cdd:PHA02562 308 LKELQHS---LEKLDTAIDELEE-IMDEFNEQSKKLLELKNKISTNKQSliTLVDKAKkvkaaIEELQAEFVDNAEELAK 383
|
170 180
....*....|....*....|
gi 18400540 190 TKHEAT----TKAKELMEVH 205
Cdd:PHA02562 384 LQDELDkivkTKSELVKEKY 403
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
43-201 |
4.30e-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: 49.25 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGsSDSVELLSKAQARATELEK 122
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKL-KKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 123 QVEVLKkflEQKNK-EKELI--EAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAK 199
Cdd:TIGR04523 111 EIKNDK---EQKNKlEVELNklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
..
gi 18400540 200 EL 201
Cdd:TIGR04523 188 NI 189
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-201 |
4.56e-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: 49.30 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 38 RSDGGDIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARA 117
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR-IEELEEDLHKLEEAL 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 118 TELEK-----QVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLE--RALKISEEEMLRT 190
Cdd:TIGR02169 782 NDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqIKSIEKEIENLNG 861
|
170
....*....|..
gi 18400540 191 KHEAT-TKAKEL 201
Cdd:TIGR02169 862 KKEELeEELEEL 873
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
85-180 |
5.13e-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: 48.22 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 85 QDKVASLETEVSSLRKKGSSDSvELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHK 164
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|....*.
gi 18400540 165 TNEEQKNKIRKLERAL 180
Cdd:COG4942 98 ELEAQKEELAELLRAL 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-207 |
5.29e-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: 48.90 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKkgssdsveLLSKAQARATELEKQV 124
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------EIEELEELIEELESEL 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELMEV 204
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
...
gi 18400540 205 HGA 207
Cdd:TIGR02168 956 AEA 958
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-201 |
6.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 25 ADAGIDGGDEPKLRSDGGDIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRK---- 100
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadea 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 101 -------KGSSDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEA----QTSETEKKLNELNSRVEKLHKTNEEQ 169
Cdd:PTZ00121 1397 kkkaeedKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeakKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
170 180 190
....*....|....*....|....*....|....*....
gi 18400540 170 KN--KIRKLERALKISEE-----EMLRTKHEATTKAKEL 201
Cdd:PTZ00121 1477 KKaeEAKKADEAKKKAEEakkkaDEAKKAAEAKKKADEA 1515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-201 |
6.84e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSD--SVELLSKAQ----ARAT 118
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEeenkIKAA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 119 ELEKQVEVLKKFLEQKNKEKElIEAQTSETEKKLNELNSRVEKLHKTNEEQKNK---IRKLERALKISEEEMLRTKHEAT 195
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDK 1743
|
....*.
gi 18400540 196 TKAKEL 201
Cdd:PTZ00121 1744 KKAEEA 1749
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
45-193 |
7.70e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQV 124
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ--------LQAAQAELAQAQEEL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHE 193
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
30-182 |
8.78e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 30 DGGDEPKLRSDGGDIELDQLNAKIRALESQIddktKELkgrEELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvel 109
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQV----ERL---EAEVEELEAELEEKDERIERLERELSEARSE-------- 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18400540 110 lskaqaRATELEKQVEVLKKfleqknkekelieaqtsetEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKI 182
Cdd:COG2433 457 ------ERREIRKDREISRL-------------------DREIERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-185 |
8.83e-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: 48.09 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsVELLSKAQARATELEKQV 124
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-----IQKNKSLESQISELKKQN 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELnsrVEKLHKTNEEQKNKIRKLERALKISEE 185
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQL---KDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
45-172 |
1.02e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELkgrEELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQV 124
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEA---EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18400540 125 EVLKKFLEQKNKEKELIEAQtseteKKLNELNSRVEKlHKTNEEQKNK 172
Cdd:PRK00409 594 RQLQKGGYASVKAHELIEAR-----KRLNKANEKKEK-KKKKQKEKQE 635
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-204 |
1.07e-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: 48.14 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 42 GDIELDQLNAKIRALESQIDDKTKElkgREELVTEKEKLLQERQDKVASLET----------EVSSLRKKgssdsvelLS 111
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKR---RDKLTEEYAELKEELEDLRAELEEvdkefaetrdELKDYREK--------LE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 112 KAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTK 191
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170
....*....|...
gi 18400540 192 HEATTKAKELMEV 204
Cdd:TIGR02169 476 EEYDRVEKELSKL 488
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
55-177 |
1.14e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 55 ALESQIDDKTKELKGREEL--------VTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQVEV 126
Cdd:COG2433 381 ALEELIEKELPEEEPEAERekeheereLTEEEEEIRRLEEQVERLEAEVEELEAE--------LEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18400540 127 LKKFLEQK-NKEKEL--IEAQTSETEKKLNELNSRVEKLHKTNEEQKnKIRKLE 177
Cdd:COG2433 453 ARSEERREiRKDREIsrLDREIERLERELEEERERIEELKRKLERLK-ELWKLE 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-195 |
1.26e-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: 47.71 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREE----LVTEKEKLLQERQD---KVASLETEVSSLRKKGSSDSVELlSKAQARA 117
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEqikkLQQEKELLEKEIERlkeTIIKNNSEIKDLTNQDSVKELII-KNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 118 TELEKQVEVL--------------KKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKIS 183
Cdd:TIGR04523 464 ESLETQLKVLsrsinkikqnleqkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
170
....*....|..
gi 18400540 184 EEEMLRTKHEAT 195
Cdd:TIGR04523 544 EDELNKDDFELK 555
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
36-200 |
1.43e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 36 KLRSDGGDIELDQ--LNAKI------RALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRkkgsSDSV 107
Cdd:PRK02224 479 ELEAELEDLEEEVeeVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE----AEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 108 ELLSKAQARATELEKQVEVLKKFLEQKNKEKELIE---------AQTSETEKKLNELNSRVEKLHKTNEEQKNKI----- 173
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAELNDERRERLaekre 634
|
170 180
....*....|....*....|....*....
gi 18400540 174 RKLERALKISEE--EMLRTKHEATTKAKE 200
Cdd:PRK02224 635 RKRELEAEFDEAriEEAREDKERAEEYLE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-201 |
1.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQV 124
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELN----------SRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEA 194
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAqleeleeaeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
....*..
gi 18400540 195 TTKAKEL 201
Cdd:COG1196 449 EEEAELE 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-203 |
2.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 60 IDDKTKELKGR-EELVTEKEKL-----LQERQDKvasLETEVSSLRKKgssdsvellsKAQARATELEKQVEVLKKFLEQ 133
Cdd:COG1196 191 LEDILGELERQlEPLERQAEKAeryreLKEELKE---LEAELLLLKLR----------ELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 134 KNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELME 203
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-187 |
2.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQIDD-KTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRkkgssdsvellSKAQARATELE 121
Cdd:COG4913 315 EARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALG-----------LPLPASAEEFA 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 122 KQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKN----------KIRK-LERALKISEEEM 187
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksniparllALRDaLAEALGLDEAEL 460
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
74-205 |
3.41e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 74 VTEKEKLLQERQDKVasleTEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKK---FLEQKNKEKELIEAQTSE--T 148
Cdd:COG5022 877 VELAERQLQELKIDV----KSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEliaRLKKLLNNIDLEEGPSIEyvK 952
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 149 EKKLNELNSRVEKLHKTNEEQKNKIRKLE---RALKISEEEMLRTKHEATTKAKELMEVH 205
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTilvREGNKANSELKNFKKELAELSKQYGALQ 1012
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
44-156 |
3.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 44 IELDQLNAKIRALESQIDdktkELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQ 123
Cdd:COG4717 132 QELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
90 100 110
....*....|....*....|....*....|...
gi 18400540 124 VEVLKKFLEQKNKEKELIEAQTSETEKKLNELN 156
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-187 |
3.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEK--------------------------------EKLLQERQDKVASLE 92
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 93 TEVSSLRKKgssdsVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQtseTEKKLNELNSRVEKLHKTNEEQKNK 172
Cdd:COG4942 157 ADLAELAAL-----RAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|....*
gi 18400540 173 IRKLERALKISEEEM 187
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-198 |
3.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 46 LDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQdkVASLETEVSSLRKKGSSDSVELLSKAQARA---TELEK 122
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAeeyQELKE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 123 QVEVLKKFLEQKNKE---------KELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKIS----EEEMLR 189
Cdd:COG4717 403 ELEELEEQLEELLGEleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAellqELEELK 482
|
....*....
gi 18400540 190 TKHEATTKA 198
Cdd:COG4717 483 AELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
57-191 |
5.66e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 57 ESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKaqaRATELEKQVEVLKKFLEQKNK 136
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSRELAGLRAELEELEK 687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 137 EKElieaqtsETEKKLNELNSRVEKLhktnEEQKNKIRKLERALKISEEemLRTK 191
Cdd:PRK03918 688 RRE-------EIKKTLEKLKEELEER----EKAKKELEKLEKALERVEE--LREK 729
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
65-213 |
6.00e-05 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 44.61 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 65 KELKGREELVTEKEKLLQE--RQDKVASLETEVSSLRKKGSSDSVELLSKAQARATE-LEKQVEVLKKfleqknkEKELI 141
Cdd:pfam14932 28 EELQAFEELQKSGKPILEGaaLDEALKTISAESPGLLNQQDVEALEESLEEIREATEdLEAELQELQK-------TKQLK 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 142 EAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKiseEEMLRTKHEATT---KAKELMEVHGAWLPPWF 213
Cdd:pfam14932 101 INRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELA---ALNAKTNNVLQSlqsEVKELASFFSASEPPVF 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-200 |
6.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKG----REELVTEKEKLLQERQDKVASLETEVSSLRK-----------------KGS 103
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNaedfLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 104 ------SDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELiEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKL- 176
Cdd:PRK02224 465 phvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEELr 543
|
170 180
....*....|....*....|....
gi 18400540 177 ERALKISEEEmlRTKHEATTKAKE 200
Cdd:PRK02224 544 ERAAELEAEA--EEKREAAAEAEE 565
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
41-180 |
7.14e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 41 GGDIELDQLNAKIRALEsqiddktkelkgrEELVTEKEKLlQERQDKVASLETEVSSL-----RKKGSSDSVE-LLSKAQ 114
Cdd:PRK09039 50 GKDSALDRLNSQIAELA-------------DLLSLERQGN-QDLQDSVANLRASLSAAeaersRLQALLAELAgAGAAAE 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 115 ARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERAL 180
Cdd:PRK09039 116 GRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-186 |
8.79e-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: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELkgrEELvteKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQV 124
Cdd:COG4913 303 ELARLEAELERLEARLDALREEL---DEL---EAQIRGNGGDRLEQLEREIERLERE--------LEERERRRARLEALL 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400540 125 EVLKkfLEQKNKEKELIEAQtSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEE 186
Cdd:COG4913 369 AALG--LPLPASAEEFAALR-AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
36-181 |
9.94e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 36 KLRSDGGDIELDQLNAKIRALESQiddktkelkgREELVTEKEKLLQERqdkVASLETEVSSLRKKGSsdsvELLSKAQA 115
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQLEIE----------KEALKKEQDEASFER---LAELRDELAELEEELE----ALKARWEA 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 116 RATELEkQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEK------------------LHKTNEEQKNKIRKLE 177
Cdd:COG0542 466 EKELIE-EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevvsrwtgipVGKLLEGEREKLLNLE 544
|
....
gi 18400540 178 RALK 181
Cdd:COG0542 545 EELH 548
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
53-186 |
1.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 53 IRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELEKQVEVLKKFLE 132
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE--------LEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18400540 133 QKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEE 186
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-201 |
1.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 46 LDQLNAKIRALESQIDD---------KTKELKGREELVTEKEKLLQ--ERQDKVASLETEVSSLRKKgssdsvelLSKAQ 114
Cdd:COG1196 188 LERLEDILGELERQLEPlerqaekaeRYRELKEELKELEAELLLLKlrELEAELEELEAELEELEAE--------LEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 115 ARATELEKQVEVLKKFLEQKNKEKE-------LIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEeaqaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170
....*....|....
gi 18400540 188 LRTKHEATTKAKEL 201
Cdd:COG1196 340 EELEEELEEAEEEL 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
36-208 |
1.29e-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: 44.66 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 36 KLRSDGGDIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSslrkkgssdsvellskaqa 115
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS------------------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 116 ratELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEAT 195
Cdd:TIGR02168 278 ---ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170
....*....|...
gi 18400540 196 TKAKELMEVHGAW 208
Cdd:TIGR02168 355 SLEAELEELEAEL 367
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
56-195 |
1.40e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 56 LESQIDDKTKELKGREELVTEKEKLlqerQDKVASLETEVSSLRK----KGSSDSvELLSKAQARATELEKQVEVLKKFL 131
Cdd:smart00787 153 LEGLKEDYKLLMKELELLNSIKPKL----RDRKDALEEELRQLKQledeLEDCDP-TELDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400540 132 EQKNKEKELIEAQTSETEKKLNELNSRVEKLhktnEEQKNKIRKLERalkiSEEEMLRTKHEAT 195
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEA----EKKLEQCRGFTF----KEIEKLKEQLKLL 283
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-181 |
1.53e-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: 44.28 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 44 IELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARaTELEKQ 123
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR-SELRRE 916
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 124 VEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTN--------EEQKNKIRKLERALK 181
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLENKIK 982
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-201 |
1.55e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 51 AKIRALESQIDD---KTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARATELEKQVEVL 127
Cdd:PTZ00121 1270 AAIKAEEARKADelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 128 KKFLEQKNKE-------KELIEAQTSETEKKLNELNSRVEKLHKTNEEQKnkirKLERALKISEEemLRTKHEATTKAKE 200
Cdd:PTZ00121 1349 KAEAEAAADEaeaaeekAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----KAEEDKKKADE--LKKAAAAKKKADE 1422
|
.
gi 18400540 201 L 201
Cdd:PTZ00121 1423 A 1423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-186 |
1.65e-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: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDD---KTKELKGREE----LVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSV-ELLSKAQAR 116
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDltkKISSLKEKIEklesEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKnKEIEELKQT 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 117 ATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEE 186
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-204 |
1.85e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 52 KIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSS---------DSVELLSKAQARATELEK 122
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleeleERHELYEEAKAKKEELER 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 123 --------QVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHK-------------------TNEEQKNKIRK 175
Cdd:PRK03918 377 lkkrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakgkcpvcgrelTEEHRKELLEE 456
|
170 180
....*....|....*....|....*....
gi 18400540 176 LERALKISEEEMLRTKHEATTKAKELMEV 204
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-201 |
3.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKK---------GSSDSVELLSKAQA 115
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 116 RATELEKQVEV-LKKFLEQKNKEKELIEA-----------------QTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLE 177
Cdd:PRK02224 423 ELREREAELEAtLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE 502
|
170 180 190
....*....|....*....|....*....|....*
gi 18400540 178 RALKISEE-----------EMLRTKHEATTKAKEL 201
Cdd:PRK02224 503 DLVEAEDRierleerredlEELIAERRETIEEKRE 537
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
108-193 |
3.31e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 108 ELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....*.
gi 18400540 188 LRTKHE 193
Cdd:COG4942 100 EAQKEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-187 |
3.52e-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: 43.12 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 57 ESQIDDKTKELKGREELVTEKEKLLQ--ERQDKVA----SLETEVSSLRKKGSSDSVEllsKAQARATELEKQVEVLKKF 130
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKslERQAEKAerykELKAELRELELALLVLRLE---ELREELEELQEELKEAEEE 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 131 LEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
119-201 |
3.66e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.41 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 119 ELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLE---RALKISEEEMLRTKHEAT 195
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKseySDLKSRFEELLKKRLLEV 211
|
....*.
gi 18400540 196 TKAKEL 201
Cdd:COG4026 212 FSLEEL 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
63-201 |
3.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 63 KTKELKGREELVTEKEKLLQ---ERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKE 139
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 140 LiEAQTSETEKKLNELNSRVEKLHKTNEEQKN--KIRKLERALKISEE----EMLRTKHEATTKAKEL 201
Cdd:PTZ00121 1396 A-KKKAEEDKKKADELKKAAAAKKKADEAKKKaeEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEA 1462
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
43-137 |
4.00e-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: 39.09 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELek 122
Cdd:cd22887 3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEK--------LRKLQEENDEL-- 72
|
90
....*....|....*
gi 18400540 123 qvevLKKFLEQKNKE 137
Cdd:cd22887 73 ----VERWMAKKQQE 83
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-191 |
4.19e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 27 AGIDGGDEPKLRSDGGDIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDS 106
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 107 VEL---------LSKAQA-------RATELEKQVEVLKKFLE-------QKNKEKELIEAQTSETEKKLNELNSRVEKLH 163
Cdd:pfam15921 531 QELqhlknegdhLRNVQTecealklQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
170 180
....*....|....*....|....*...
gi 18400540 164 KTNEEQKNKIRKLERalKISEEEMLRTK 191
Cdd:pfam15921 611 ILKDKKDAKIRELEA--RVSDLELEKVK 636
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
120-204 |
4.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 120 LEKQVE-VLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKA 198
Cdd:COG2433 382 LEELIEkELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI 461
|
....*.
gi 18400540 199 KELMEV 204
Cdd:COG2433 462 RKDREI 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
87-204 |
4.61e-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: 41.45 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 87 KVASLETEVSSLRKKgssdsvelLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKL---- 162
Cdd:COG1579 11 DLQELDSELDRLEHR--------LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeql 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18400540 163 --HKTNEEQKN---KIRKLERALKISEEEMLRTKHEATTKAKELMEV 204
Cdd:COG1579 83 gnVRNNKEYEAlqkEIESLKRRISDLEDEILELMERIEELEEELAEL 129
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
50-204 |
7.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 50 NAKIRALESQIDDKTKELKGRE------ELVTEKEKLLQERQDKVASLETEVSSLRkkgssdsvELLSKAQAratELEKQ 123
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLEnqlkkaHNAEEAVRTNPEINDRIRLLEQEVARYK--------EESGKAQA---EVERL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 124 VEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKL-HKTNEEQKNKIRKLERALKiseEEMLRTKHEATTKAKELM 202
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIkHGQQEMKKKGAQLLEEARR---REDNLADNSQQLQLEELM 661
|
..
gi 18400540 203 EV 204
Cdd:pfam10174 662 GA 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
34-189 |
7.78e-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: 42.08 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 34 EPKLRSDGGDIELdqLNAKIRALESQIDDKTKELKGREELVTEKEKLLQ--ERQDKvasletevsSLRKKGSSDSVELLS 111
Cdd:pfam01576 895 EEELEEEQSNTEL--LNDRLRKSTLQVEQLTTELAAERSTSQKSESARQqlERQNK---------ELKAKLQEMEGTVKS 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 112 KAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQK-------NKIRKLERALKISE 184
Cdd:pfam01576 964 KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdqaekgnSRMKQLKRQLEEAE 1043
|
....*
gi 18400540 185 EEMLR 189
Cdd:pfam01576 1044 EEASR 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-203 |
7.85e-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: 41.97 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 99 RKKGSSDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLER 178
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100
....*....|....*....|....*...
gi 18400540 179 ALKISEEEM---LRTKHEATTKAKELME 203
Cdd:TIGR02168 755 ELTELEAEIeelEERLEEAEEELAEAEA 782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
31-179 |
7.89e-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: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 31 GGDEPKLRSDGGDIELDQLNAKIRALESQIDDKTKELkgreelvTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELL 110
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY-------TPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400540 111 SKAQARATELEKQVEVLK-KFLEQKNKEKEL--IEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERA 179
Cdd:COG3206 323 EALQAREASLQAQLAQLEaRLAELPELEAELrrLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
51-203 |
7.91e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 51 AKIRALESQIDDKTKELKGREELVTEKEKllqerqdKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKKF 130
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEK-------RAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 131 LEQKNKEKeLIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKH---EATTKAKELME 203
Cdd:pfam00261 74 DESERGRK-VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEEraeLAESKIVELEE 148
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-186 |
8.03e-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: 41.93 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRkkgssdsvELLSKAQARATELEKQV 124
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK--------ETIIKNNSEIKDLTNQD 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEE 186
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
81-186 |
8.32e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 81 LQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKkflEQKNKEKELIEaQTSETEKKLNELNSRVE 160
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALK---ARWEAEKELIE-EIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|....*...
gi 18400540 161 KLHKTNEEQKNKIRKLERALK--ISEEE 186
Cdd:COG0542 489 ELEKELAELEEELAELAPLLReeVTEED 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-187 |
8.62e-04 |
|
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: 41.29 E-value: 8.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 110 LSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-191 |
1.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREE--LVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEK 122
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 123 QVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTnEEQKNKIRKLERALKISEEEMLRTK 191
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-180 |
1.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 43 DIELDQLNAKIRALESQID--DKT--------KELKGREELVTEKEKLLQERQDKVASLETEVSSLRkkgssdsvELLSK 112
Cdd:COG4913 660 EIDVASAEREIAELEAELErlDASsddlaaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAE--------EELDE 731
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 113 AQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNelnsrvEKLHKTNEEQKNKIRKLERAL 180
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE------ERIDALRARLNRAEEELERAM 793
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
46-201 |
1.55e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 46 LDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLR------KKGSSDSVELLSKAQARATE 119
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkiKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 120 LEKQVEVLKKFLEQKNKEKE-----LIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEA 194
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
....*..
gi 18400540 195 TTKAKEL 201
Cdd:TIGR04523 366 EEKQNEI 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-201 |
1.62e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 113 AQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKtneeqknKIRKLERALKISEEEMLRTKH 192
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALEQELAALEAELAELEK 90
|
....*....
gi 18400540 193 EATTKAKEL 201
Cdd:COG4942 91 EIAELRAEL 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-180 |
1.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKekllqerQDKVASLETEVSSLRkkgssdsvELLSKAQARATELEKQV 124
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEEL-------REEAAELESELEEAR--------EAVEDRREEIEELEEEI 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERAL 180
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
33-205 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 33 DEPKLRSDGGDIELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVElLSK 112
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ-LNA 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 113 AQARATELEKQVEVLK-KFLEQKNKEKELIEAQTSETEKKLNElnsrVEKLHKTNEEqknkirklerALKISEEEMLRTK 191
Cdd:pfam05483 634 YEIKVNKLELELASAKqKFEEIIDNYQKEIEDKKISEEKLLEE----VEKAKAIADE----------AVKLQKEIDKRCQ 699
|
170
....*....|....
gi 18400540 192 HEaTTKAKELMEVH 205
Cdd:pfam05483 700 HK-IAEMVALMEKH 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-201 |
1.95e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 50 NAKIRALESQIDD----KTKELKGREELV--TEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQ-------AR 116
Cdd:PTZ00121 1461 EAKKKAEEAKKADeakkKAEEAKKADEAKkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEeakkadeAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 117 ATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATT 196
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
....*
gi 18400540 197 KAKEL 201
Cdd:PTZ00121 1621 KAEEL 1625
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
104-191 |
2.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 104 SDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKIS 183
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
....*...
gi 18400540 184 EEEMLRTK 191
Cdd:COG4372 107 QEEAEELQ 114
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
110-183 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18400540 110 LSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKIS 183
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
45-157 |
2.66e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.00 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQD-------KVASLETEVSSLRKKgssdsvelLSKAQARA 117
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvLHAEDIKALQALREE--------LNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18400540 118 TELEKQVEVLKKFLEQK----NKEKELIEAQTSETEKKLNELNS 157
Cdd:pfam07926 74 AELKAEAESAKAELEESeeswEEQKKELEKELSELEKRIEDLNE 117
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-201 |
2.74e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 44 IELDQLNAKIRALESQID---------------DKTKELKG----REELVTEKEKLLQERQDKVASLETEVSSLrKKGSS 104
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNqlkseisdlnnqkeqDWNKELKSelknQEKKLEEIQNQISQNNKIISQLNEQISQL-KKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 105 DSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIEAQTsetekklNELNSRVEKLHKTNEEQKNKIRKLERALKISE 184
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
170
....*....|....*..
gi 18400540 185 EEMLRTKHEATTKAKEL 201
Cdd:TIGR04523 426 KEIERLKETIIKNNSEI 442
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
46-181 |
3.20e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.84 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 46 LDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVAS--------LETEVSSLRKKGSSDSVELLS------ 111
Cdd:PLN03229 549 LSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASsgdeldddLKEKVEKMKKEIELELAGVLKsmglev 628
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 112 ---KAQARATELEKQVEVLKKFLEQKNKE--KELIEA-QTSETEKKLNELNSRVEKLHKTNE-EQKNKIRKLERALK 181
Cdd:PLN03229 629 igvTKKNKDTAEQTPPPNLQEKIESLNEEinKKIERViRSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIK 705
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
54-201 |
3.25e-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: 40.16 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 54 RALESQIDDKTKELkgrEELVTEkeklLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKKFLEQ 133
Cdd:pfam01576 688 RALEQQVEEMKTQL---EELEDE----LQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELED 760
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 134 KNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALK----------ISEEEMLRTKHEATTKAKEL 201
Cdd:pfam01576 761 ERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKdlqreleearASRDEILAQSKESEKKLKNL 838
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
71-188 |
3.29e-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: 39.67 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 71 EELVTEKEKLLQERQDKVASLETEvsslrkkgssdsvelLSKAQARATELEKQVEVLKKFLEQ---KNKEKELIEAQTSE 147
Cdd:pfam05622 303 RERLTELQQLLEDANRRKNELETQ---------------NRLANQRILELQQQVEELQKALQEqgsKAEDSSLLKQKLEE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18400540 148 TEKKLNELNSRVEKLHKTNEEQKN--------KIRKLERALKISEEEML 188
Cdd:pfam05622 368 HLEKLHEAQSELQKKKEQIEELEPkqdsnlaqKIDELQEALRKKDEDMK 416
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
45-200 |
3.62e-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: 39.67 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDdktkelkgreelvtekekLLQERQDKVASLETEVSSLRKKgssdsVELLSkaqaratELEKQV 124
Cdd:pfam05622 105 ELTSLAEEAQALKDEMD------------------ILRESSDKVKKLEATVETYKKK-----LEDLG-------DLRRQV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 evlkKFLEQKNKEKELIEAQTSETEKKLNELNSRVE-------KLHKTNEEQKNKIRKLERALKISEEemlrtKHEATTK 197
Cdd:pfam05622 155 ----KLLEERNAEYMQRTLQLEEELKKANALRGQLEtykrqvqELHGKLSEESKKADKLEFEYKKLEE-----KLEALQK 225
|
...
gi 18400540 198 AKE 200
Cdd:pfam05622 226 EKE 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
63-201 |
3.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 63 KTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgSSDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKELIE 142
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18400540 143 AQtsETEKKLNELNSRVEKLHKTnEEQKNKIRKLERALKISEEEMLRtKHEATTKAKEL 201
Cdd:PTZ00121 1485 AD--EAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEA 1539
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
45-139 |
3.87e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 37.99 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKgssdsvelLSKAQARATELekqv 124
Cdd:pfam08614 93 KLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEK--------LRKLEKENREL---- 160
|
90
....*....|....*
gi 18400540 125 evLKKFLEQKNKEKE 139
Cdd:pfam08614 161 --VERWMKRKGQEAE 173
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
45-201 |
4.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKA-QARATELEKQ 123
Cdd:COG4372 116 ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDELLKEANRN 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18400540 124 VEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKEL 201
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-177 |
4.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 45 ELDQLNaKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVEllsKAQARATELEKQV 124
Cdd:PRK02224 587 RIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE---EAREDKERAEEYL 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 18400540 125 EVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLhktnEEQKNKIRKLE 177
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEIGAVENELEELEELRERR----EALENRVEALE 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
60-193 |
5.58e-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: 39.33 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 60 IDDKTKELKGREELVTEKEKLLQERQDKV-ASLETEVSSLRKKGSSdsvelLSKAQARATELEKQVEVLKKFLEQKNKEK 138
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNES-----LEKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 139 ELIEAqtseTEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHE 193
Cdd:pfam15921 489 MTLES----SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-201 |
5.65e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 54 RALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKKFLEQ 133
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 134 KNKEKEliEAQTSETEKKLNELNS-RVEKLHKTNEEQKNKI----------RKLERALKISEEE------MLRTKHEATT 196
Cdd:PTZ00121 1639 KKKEAE--EKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAeeakkaeedeKKAAEALKKEAEEakkaeeLKKKEAEEKK 1716
|
....*
gi 18400540 197 KAKEL 201
Cdd:PTZ00121 1717 KAEEL 1721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
121-187 |
6.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 6.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 121 EKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEM 187
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
56-206 |
7.41e-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: 38.95 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 56 LESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKGSSdsvellskaQARATELEKQvevlkkfleqkN 135
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSE---------RLRAVKDIKQ-----------E 654
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18400540 136 KEKELIEAQTSETEkkLNELNSRVEKLHKT----NEEQKNKIRKLERALKISEEEMLRTKHeaTTKAKELMEVHG 206
Cdd:pfam15921 655 RDQLLNEVKTSRNE--LNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQSELEQTRN--TLKSMEGSDGHA 725
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
67-182 |
7.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.54 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 67 LKGREELVTEKEKLLQERQdkvasleTEVSSLRKKGSSDSVELLSKAQARA-TELEKQVEVLKKFLEQKNKEKELIEAQT 145
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQ-------KEAEEKLEAALLEAKELLLRERNQQrQEARREREELQREEERLVQKEEQLDARA 97
|
90 100 110
....*....|....*....|....*....|....*..
gi 18400540 146 SETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKI 182
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEKQLDNELYR 134
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
54-199 |
8.11e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 54 RALESQIDDKTKELKGREELVTEKEKLLQERQDkvasLETEVSSLRKKGSSDSVELLSKAQARATELEKQVEVLKKFLEQ 133
Cdd:pfam02463 208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERID----LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18400540 134 KNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAK 199
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
45-101 |
8.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 8.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 18400540 45 ELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSSLRKK 101
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
44-186 |
8.64e-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: 38.46 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 44 IELDQLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVAS-------LETEVSSLRKKGSSDSVELLSKAQA- 115
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkekiekLESEKKEKESKISDLEDELNKDDFEl 554
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18400540 116 RATELEKQVEVLKKFLEQKNKEKELIEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEE 186
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
48-202 |
9.07e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.41 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 48 QLNAKIRALESQIDDKTKELKGREELVTEKEKLLQERQDKVASLETEVSS---LRKKGSSDSVELLSKAQARATELEKQV 124
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSellKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 125 EVLKKFLEQKNKEKELIEAQT-------SETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTK 197
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKReaeeeeeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
....*
gi 18400540 198 AKELM 202
Cdd:pfam02463 411 LELAR 415
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
54-389 |
9.28e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 38.52 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 54 RALESQIDDKTKELKgreelvteKEKLLQERQDKVASLETEVSsLRKKGSSdsvellSKAQARATELEKQVEVLKKFLEQ 133
Cdd:COG5022 813 RSYLACIIKLQKTIK--------REKKLRETEEVEFSLKAEVL-IQKFGRS------LKAKKRFSLLKKETIYLQSAQRV 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 134 KNKEKELIEaqtsetekkLNELNSRVEKLHKTNEEQKNKIRKLERALKISEEEMLRTKHEATTKAKELMEvhgawlppwf 213
Cdd:COG5022 878 ELAERQLQE---------LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLN---------- 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 214 avhwsSFQTVAGTHWDAHGKPVMEKVTQKVTLAKNQAEKwaKPHMANVKTKYIPAIKeTVKTHVEPHVQTLST--KAKEA 291
Cdd:COG5022 939 -----NIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE--YEDLLKKSTILVREGN-KANSELKNFKKELAElsKQYGA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 292 YHASKSAVTPHIVKFQEH---VDPYYQEAKKFSKPyvdqvatatKPHVDKVRATMKPYT-----TKTVHYYKEFLESAST 363
Cdd:COG5022 1011 LQESTKQLKELPVEVAELqsaSKIISSESTELSIL---------KPLQKLKGLLLLENNqlqarYKALKLRRENSLLDDK 1081
|
330 340
....*....|....*....|....*.
gi 18400540 364 YHHQLQAnVESKLKSHELLEPFATKE 389
Cdd:COG5022 1082 QLYQLES-TENLLKTINVKDLEVTNR 1106
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
59-192 |
9.54e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 38.37 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 59 QIDDKTKELKGreELVTEKEKLLQERQDKVASLETEVSSLRKKGSsdsvellskaqaraTELEKQVEVLKKFLEQKNKEK 138
Cdd:PRK05771 32 HIEDLKEELSN--ERLRKLRSLLTKLSEALDKLRSYLPKLNPLRE--------------EKKKVSVKSLEELIKDVEEEL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 18400540 139 ELIEAQTSETEKKLNELNSRVEKLhktnEEQKNKIRKLErALKISEEEMLRTKH 192
Cdd:PRK05771 96 EKIEKEIKELEEEISELENEIKEL----EQEIERLEPWG-NFDLDLSLLLGFKY 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-201 |
9.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 25 ADAGIDGGDEPKLRSDGGDIELDQLNAKIRALESQIDDKTK--ELKGREELVTEKEKLLQERQDKVASLETEVSSLRKKG 102
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18400540 103 SSDSVELLSKAQARATELEKQVEVLKKFLEQKNKEKeliEAQTSETEKKLNELNSRVEKLHKTNEEQKNKIRKLERALKI 182
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
170
....*....|....*....
gi 18400540 183 SEEEMLRTKHEATTKAKEL 201
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEA 1527
|
|
| |
