|
Name |
Accession |
Description |
Interval |
E-value |
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
23-125 |
1.60e-46 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 155.86 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 23 VIFNSVEKFYIPGGDITCYYTLTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVtlPVDLNSESAKQQEVQFKAYYLPKDD 102
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78
|
90 100
....*....|....*....|....
gi 154426076 103 -EYYQFCYVDQDGVVRGASIPFQF 125
Cdd:pfam17751 79 eGFYQFCYVSNLGSVVGISTPFQF 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-346 |
5.23e-12 |
|
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: 68.17 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQhnKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELE----TLKSINKKLEQTMKEQKDCWEIELLQLKE 214
Cdd:TIGR02169 217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 215 QNQKMSSEnekmgvrVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLflsLTEQREHQKKLEQTVEEMKQKET 294
Cdd:TIGR02169 295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL---EREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 154426076 295 TAAKKQQELTDqnmdLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLL 346
Cdd:TIGR02169 365 ELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
133-345 |
3.83e-09 |
|
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: 58.24 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 133 ILVVTTQSEVEEIEQHNKELCKENRELkdscvslQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCwEIELLQL 212
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 213 KEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKL-----------VQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKK 281
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154426076 282 LEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-347 |
4.65e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQK 218
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 219 MSSENEkmgvRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAK 298
Cdd:COG1196 374 LAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 154426076 299 KQQELTDQNMDLSKRLSEnmiihdvLQREKEKMEKENDYLKRENNRLLS 347
Cdd:COG1196 450 EEAELEEEEEALLELLAE-------LLEEAALLEAALAELLEELAEAAA 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
166-341 |
6.63e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 166 LQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCwEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREME 245
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 246 KlvQGVQ-----------------DKTEQLEHLKEENGQLFLSLTEQRE----HQKKLEQTVEEMKQKETTAAKKQQELT 304
Cdd:COG3883 97 R--SGGSvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAeleaKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 154426076 305 DQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRE 341
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-334 |
1.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweiELLQLKEQNQ 217
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 218 KMSSEN--------------EKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEengQLFLSLTEQREHQKKLE 283
Cdd:COG4942 115 RLGRQPplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA---ELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 154426076 284 QtveEMKQKETTAAKKQQELTDQnmdlSKRLSENMIIHDVLQREKEKMEKE 334
Cdd:COG4942 192 A---LKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-340 |
1.39e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 140 SEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEqtMKEQKDCWEIELLQLKEQNQKM 219
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQTQKSL 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 220 SSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKK 299
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 154426076 300 QQELTDQNMDLSKRLSEnmIIHDVLQREKEKMEKENDYLKR 340
Cdd:TIGR04523 661 WPEIIKKIKESKTKIDD--IIELMKDWLKELSLHYKKYITR 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-347 |
6.88e-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: 55.06 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 144 EIEQHNKELckenRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweiELLQLKEQNQKMSSEN 223
Cdd:TIGR02168 233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK----ELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 224 EKMGVRVDQLQ-------AQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTA 296
Cdd:TIGR02168 305 QILRERLANLErqleeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 154426076 297 AKKQQELTDQNMDLSKRLSEnmiihdvLQREKEKMEKENDYLKRENNRLLS 347
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLK 428
|
|
| Zn-C2H2_CALCOCO2 |
cd21968 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
424-450 |
1.01e-07 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.
Pssm-ID: 412014 Cd Length: 27 Bit Score: 47.83 E-value: 1.01e-07
10 20
....*....|....*....|....*..
gi 154426076 424 LNCPICDKTFPAKEKQIFEDHVFCHTL 450
Cdd:cd21968 1 FECPICSKIFEATSKQEFEDHVFCHSL 27
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-345 |
1.27e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILvvttQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTM---KEQKDC 204
Cdd:TIGR02169 687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 205 WEIELLQLKEQNQKMSSENEKM-----GVRVDQLQAQLSNQG----------REMEKLVQGVQDKTEQLEHLKEENGQLF 269
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEeevsriearlREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 270 LSLTEQREHQKK----LEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR02169 843 IDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
128-347 |
1.40e-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: 53.87 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNS-------DMQATLQKKQEELETL----KSINKKLEQ 196
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSvkeliikNLDNTRESLETQLKVLsrsiNKIKQNLEQ 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 197 TMKEQKDcWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEE--NGQLFLSLTE 274
Cdd:TIGR04523 487 KQKELKS-KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDE 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154426076 275 QREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLLS 347
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-345 |
1.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKE---QKDCWEIELLQLKEQ 215
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerRIAATERRLEDLEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 216 NQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETT 295
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 154426076 296 AAKKQQELTDQNMDLSKRLSEN-MIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-345 |
2.61e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKsinKKLEQTMKEQKDcweiellqLKEQNQ 217
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELES--------LEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 218 KMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTA- 296
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAe 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 154426076 297 -AKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR02168 442 lEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-311 |
2.76e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 143 EEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETlksinkKLEQTMKEQKDCwEIELLQLKEQNQKMSSE 222
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA------EIASLERSIAEK-ERELEDAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 223 NEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQRE----HQKKLEQTVEEMKQKETTAAK 298
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkdYREKLEKLKREINELKRELDR 410
|
170
....*....|...
gi 154426076 299 KQQELTDQNMDLS 311
Cdd:TIGR02169 411 LQEELQRLSEELA 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-346 |
2.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweiELLQLKEQNQK 218
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE----RLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 219 MSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAK 298
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 154426076 299 KQQ-------ELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLL 346
Cdd:COG1196 408 AEEallerleRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-334 |
3.75e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQtmkeqkdcwEIELLQLKEQNQK 218
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------DIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 219 msSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAK 298
Cdd:COG1196 316 --ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190
....*....|....*....|....*....|....*.
gi 154426076 299 KQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKE 334
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-345 |
5.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcwEIELLQLKEQNQKMS 220
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE--YIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 221 SENEKmgvrvdqLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEEngqlFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQ 300
Cdd:PRK03918 310 REIEK-------RLSRLEEEINGIEERIKELEEKEERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 154426076 301 QELTDQNMDLSKRLSENmiihdvLQREKEKMEKENDYLKRENNRL 345
Cdd:PRK03918 379 KRLTGLTPEKLEKELEE------LEKAKEEIEEEISKITARIGEL 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-345 |
5.77e-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: 51.94 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQK-------KQEELETLKSINKKLE---QTMKEQKDCWEIE 208
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKKLQQEKELLEkeiERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 209 LLQLKEQNQKMSSENEKMGVRVDQLQAQLS-------NQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKK 281
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154426076 282 LEQTVE----EMKQKETTAAKKQQELTDQNMDLSKRLSENMIihDVLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR04523 522 LKEKIEklesEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
240-352 |
7.27e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 240 QGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTdqnmdlsKRLSENmi 319
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS-------RLDREI-- 474
|
90 100 110
....*....|....*....|....*....|...
gi 154426076 320 ihDVLQREKEKMEKENDYLKRENNRLLSYMGLD 352
Cdd:COG2433 475 --ERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
157-345 |
8.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 157 RELKDSCVSLQKQNSDMQATLQKKQEELETLksinkkleqtmkeqkdcwEIELLQLKEQNQKMSSEnekmgvrVDQLQAQ 236
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAEL------------------EAELEELRLELEELELE-------LEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 237 LSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSE 316
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180
....*....|....*....|....*....
gi 154426076 317 nmIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:COG1196 370 --AEAELAEAEEELEELAEELLEALRAAA 396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
123-345 |
8.92e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 123 FQFRPENEEDILVV--TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKE 200
Cdd:COG4372 16 FGLRPKTGILIAALseQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 201 QKDCWEiELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEEngqlflsLTEQREHQK 280
Cdd:COG4372 96 LAQAQE-ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154426076 281 KLEQTVEEMKQKETTAA-KKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:COG4372 168 ALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-345 |
9.61e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTM---KEQKDCWEIELLQLK 213
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 214 EQNQKMSSENEKMG--------------VRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQ 279
Cdd:TIGR02168 323 AQLEELESKLDELAeelaeleekleelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154426076 280 KKLEQTVEEmkqkettAAKKQQELTDQNMDLSKRLSENMIihDVLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR02168 403 ERLEARLER-------LEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
173-341 |
1.53e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 173 MQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQ 252
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 253 DKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENmiihdvlQREKEKME 332
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELE 156
|
....*....
gi 154426076 333 KENDYLKRE 341
Cdd:COG4372 157 EQLESLQEE 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-345 |
1.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDscvSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcWEIELLQLKEQN 216
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-LEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 217 QKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTA 296
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 154426076 297 AKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
141-303 |
2.11e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweiELLQLKEQNQKMS 220
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEE----DIKTLTQRVLERE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 221 SENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQ 300
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE 229
|
...
gi 154426076 301 QEL 303
Cdd:pfam07888 230 AEN 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-339 |
2.22e-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: 50.06 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEI 207
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 208 ELLQLKEQNQKMSSENEKMG---VRVDQLQAQLSNQGREMEKLVQgvqdkteQLEHLKEE----NGQLFLSLTEQREHQK 280
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDieslAAEIEELEELIEELES 873
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154426076 281 KLEQTVEEMKQKE----------TTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLK 339
Cdd:TIGR02168 874 ELEALLNERASLEealallrselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
138-316 |
2.95e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweiellQLKEQNQ 217
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-------ELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 218 KMSSENEKMGV---------------RVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKL 282
Cdd:COG3883 94 ALYRSGGSVSYldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....
gi 154426076 283 EQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSE 316
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
140-360 |
4.31e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 140 SEVEE-IEQHNKELCKENRELKDSCVSLQKQ----NSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcWEIELLQLKE 214
Cdd:pfam15921 320 SDLEStVSQLRSELREAKRMYEDKIEELEKQlvlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHK-REKELSLEKE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 215 QNQKMSSENEKMGVRVDQLQAQLSNQGRE------------------MEKLVQGVQDKTEQLEHLKeengqlflSLTEQR 276
Cdd:pfam15921 399 QNKRLWDRDTGNSITIDHLRRELDDRNMEvqrleallkamksecqgqMERQMAAIQGKNESLEKVS--------SLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 277 EHQKK-LEQTVEEMKQKETTAAKKQQELTDQNMDLSKR----LSENMIIHDVLQREKEKMEkENDYLKRENNRlLSYMGL 351
Cdd:pfam15921 471 ESTKEmLRKVVEELTAKKMTLESSERTVSDLTASLQEKeraiEATNAEITKLRSRVDLKLQ-ELQHLKNEGDH-LRNVQT 548
|
....*....
gi 154426076 352 DCDSLSYQV 360
Cdd:pfam15921 549 ECEALKLQM 557
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
127-315 |
5.45e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 127 PENEEDILVVTTQSeVEEIEQHNKELcKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQT--------- 197
Cdd:PRK10929 105 DALEQEILQVSSQL-LEKSRQAQQEQ-DRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAqltalqaes 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 198 --MKEQKDcwEIELLQLKEQNQ----KMSSE-NEKMGVRVDQLQAQLSNQ-----GREMEKLVQgvqdKTEQLEhlkEEN 265
Cdd:PRK10929 183 aaLKALVD--ELELAQLSANNRqelaRLRSElAKKRSQQLDAYLQALRNQlnsqrQREAERALE----STELLA---EQS 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 154426076 266 GQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLS 315
Cdd:PRK10929 254 GDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALN 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-345 |
1.07e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 146 EQHNKELCKEnRELKDscvsLQKQNSDMQATLQKKQEELETLKSINKKLEQ---TMKEQKDCWEIELLQLKEQNQKMSSE 222
Cdd:TIGR02168 667 KTNSSILERR-REIEE----LEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 223 NEKMGVRVDQLQAQLsnqgremeklvqgvQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTV----EEMKQKETTAAK 298
Cdd:TIGR02168 742 VEQLEERIAQLSKEL--------------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkEELKALREALDE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 154426076 299 KQQELTDQNMDLSKrlsenmiihdvLQREKEKMEKENDYLKRENNRL 345
Cdd:TIGR02168 808 LRAELTLLNEEAAN-----------LRERLESLERRIAATERRLEDL 843
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
144-336 |
1.92e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 144 EIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCweIELLQLKeqnqKMSSEN 223
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV--VEELTAK----KMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 224 EKMgvRVDQLQAQLSNQGR-------EMEKLVQGVQDKTEQLEHLKEENgqlflslteqrEHQKKLEQTVEEMKQKETTA 296
Cdd:pfam15921 494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEG-----------DHLRNVQTECEALKLQMAEK 560
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 154426076 297 AKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKE-ND 336
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEiND 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
139-307 |
2.36e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELEtlksinKKLEQTMKEQKDCWEIELL-------- 210
Cdd:COG3883 43 QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG------ERARALYRSGGSVSYLDVLlgsesfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 211 ---------QLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKK 281
Cdd:COG3883 117 fldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180
....*....|....*....|....*.
gi 154426076 282 LEQTVEEMKQKETTAAKKQQELTDQN 307
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
141-347 |
3.53e-05 |
|
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: 46.50 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKdscvSLQKQNSDMQATLQKKQEELETLKSI--------------NKKLEQTMKEQKDCWE 206
Cdd:pfam02463 181 ETENLAELIIDLEELKLQEL----KLKEQAKKALEYYQLKEKLELEEEYLlyldylklneeridLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 207 IELLQLKEQNQKMSSENEKMGVRVDQLQ--------AQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLT----- 273
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKkekee 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 274 -EQREHQKK--------LEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNR 344
Cdd:pfam02463 337 iEELEKELKeleikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
...
gi 154426076 345 LLS 347
Cdd:pfam02463 417 LED 419
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
137-349 |
3.92e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWE--IELLQLKE 214
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEqdSPLETFLE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 215 QNQ--------KMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEEN-GQLFLSLTEQREHQKKLEQT 285
Cdd:TIGR00606 920 KDQqekeelisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETElNTVNAQLEECEKHQEKINED 999
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154426076 286 VEEMKQKETTAAKKQQELTDQ-----NMDLSKRLSENMIIHD-------VLQREKE--KMEKENDYLKRENNRLLSYM 349
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQDNltlrkRENELKEVEEELKQHLkemgqmqVLQMKQEhqKLEENIDLIKRNHVLALGRQ 1077
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-301 |
4.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDscvslQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEqkdcweieLLQLKEQN 216
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE--------LRELEEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 217 QKMSSENEKMGVRVDQLQAQLSNQGREmeklvqGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTA 296
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
....*
gi 154426076 297 AKKQQ 301
Cdd:COG4717 240 ALEER 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-341 |
4.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQ-------KKQEELETLKSINKKLEQTMKEQKDCWEIELLQLK 213
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyeeekkMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 214 EQNQKMSSEN-----EKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEEngqlflslteqREHQKKleqtVEE 288
Cdd:PTZ00121 1642 EAEEKKKAEElkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKK----AEE 1706
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 154426076 289 MKQKETTAAKKQQELtdqnmdlSKRLSENMIIHDVLQREKEKMEKENDYLKRE 341
Cdd:PTZ00121 1707 LKKKEAEEKKKAEEL-------KKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
129-314 |
5.24e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 129 NEEDILVV----TTQSEVEEIEQHNKELckenrelkdscVSLQKQNSDMQATLQKKQEELETLKSIN------------- 191
Cdd:PRK11281 55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNdeetretlstlsl 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 192 ----KKLEQTMKEQKDcWEIELLQLK----------EQNQKMSSENEKmgvRVDQLQAQLSNQGREMEKLVQGVQDK--- 254
Cdd:PRK11281 124 rqleSRLAQTLDQLQN-AQNDLAEYNsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALRPSQRVLlqa 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 255 --------TEQLEHLKEENGQLFLSLTEQR----------EHQ----------KKL---EQTVEEMKQKETTAAKK---- 299
Cdd:PRK11281 200 eqallnaqNDLQRKSLEGNTQLQDLLQKQRdyltariqrlEHQlqllqeainsKRLtlsEKTVQEAQSQDEAARIQanpl 279
|
250
....*....|....*.
gi 154426076 300 -QQELtDQNMDLSKRL 314
Cdd:PRK11281 280 vAQEL-EINLQLSQRL 294
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-347 |
5.37e-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: 45.78 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 150 KELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKmgvr 229
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK---- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 230 VDQLQAQLSNQGREMEKLVQgvQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMD 309
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
170 180 190
....*....|....*....|....*....|....*...
gi 154426076 310 LSKRLSENmiihdvlQREKEKMEKENDYLKRENNRLLS 347
Cdd:TIGR04523 361 KQRELEEK-------QNEIEKLKKENQSYKQEIKNLES 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-302 |
5.73e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELET----LKSINKKLEQTmKEQKDCWEIELLQLK 213
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLEKL-KREINELKRELDRLQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 214 EQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKE----ENGQLFLSLTEQREHQKKLEQTVEEM 289
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskYEQELYDLKEEYDRVEKELSKLQREL 492
|
170
....*....|...
gi 154426076 290 KQKETTAAKKQQE 302
Cdd:TIGR02169 493 AEAEAQARASEER 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
174-334 |
8.38e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 174 QATLQKKQEELE-TLKSINKKLEQTMKEQkdcweieLLQLKEQNQKMSSENEKmgvrvdqlqaQLSNQGREMEKLVQGVQ 252
Cdd:PRK12704 30 EAKIKEAEEEAKrILEEAKKEAEAIKKEA-------LLEAKEEIHKLRNEFEK----------ELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 253 DKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVlqreKEKME 332
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKV----EEEAR 168
|
..
gi 154426076 333 KE 334
Cdd:PRK12704 169 HE 170
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-346 |
9.37e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 157 RELKDSCVSLQKQNSDMQATLQKKQEELET--------LKSINKKLEQTmKEQKDCWEIELLQLKEQNQKMSSENEKMGV 228
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELelallvlrLEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 229 RVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNM 308
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190
....*....|....*....|....*....|....*...
gi 154426076 309 DLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLL 346
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-345 |
9.51e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 175 ATLQKKQEELetLKSINKKLEQTMKEQKDCWE--IELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKL--VQG 250
Cdd:COG4717 49 ERLEKEADEL--FKPQGRKPELNLKELKELEEelKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 251 VQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLS----KRLSENMIIHDVLQR 326
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQ 206
|
170
....*....|....*....
gi 154426076 327 EKEKMEKENDYLKRENNRL 345
Cdd:COG4717 207 RLAELEEELEEAQEELEEL 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-290 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 140 SEVEEIEQHNKELCKENRELKDSCVSlqkqnsdmqaTLQKKQEELE-------TLKSINKKLEQTMKEQKDCwEIELLQL 212
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVE----------ELEERLKELEpfyneylELKDAEKELEREEKELKKL-EEELDKA 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 213 KEQNQKMSSENEKMGVRVDQLQ--------AQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQ 284
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEkkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
....*.
gi 154426076 285 TVEEMK 290
Cdd:PRK03918 712 ELEKLE 717
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
117-344 |
1.12e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 117 RGASIPFQFRPENEEDILVVTTQSEVEEIEQHNKElcKENRELKDSCVSLQ----KQNSDMQATLQKKQE----ELETLK 188
Cdd:pfam17380 325 RQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNErvrqELEAAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 189 SInKKLEQTMKEQKDCWEIELLQLKEQNQKmssenekmgVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEEngql 268
Cdd:pfam17380 403 KV-KILEEERQRKIQQQKVEMEQIRAEQEE---------ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---- 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154426076 269 flsltEQREHQKKLEQTVEEMKQKEttAAKKQQELTDQNMDLSKRlsenMIIHDVLQR---EKEKMEKENDYLKRENNR 344
Cdd:pfam17380 469 -----EEERKRKKLELEKEKRDRKR--AEEQRRKILEKELEERKQ----AMIEEERKRkllEKEMEERQKAIYEEERRR 536
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
426-448 |
1.23e-04 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 39.09 E-value: 1.23e-04
10 20
....*....|....*....|....
gi 154426076 426 CPICDKTFPAKEKQ-IFEDHVFCH 448
Cdd:cd21965 1 CPICNKQFPPQVDQeAFEDHVESH 24
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
151-343 |
1.30e-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: 44.24 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 151 ELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKS----INKKLEQTMKEQKDCwEIELLQLKEQNQKMSSE---- 222
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkIKKQLSEKQKELEQN-NKKIKELEKQLNQLKSEisdl 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 223 -NEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQ 301
Cdd:TIGR04523 301 nNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 154426076 302 ELTDQNMDLSKRLS--ENMIIH------------DVLQREKEKMEKENDYLKRENN 343
Cdd:TIGR04523 381 SYKQEIKNLESQINdlESKIQNqeklnqqkdeqiKKLQQEKELLEKEIERLKETII 436
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
172-307 |
1.35e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 172 DMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQK------MSSENEKMGVRvdqLQAQLS--NQGRE 243
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHtglqliLSGEESQRGER---ILAYFGylNQARQ 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154426076 244 --MEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQK----ETTAAKKQQELTD--QN 307
Cdd:PRK11637 170 etIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTltglESSLQKDQQQLSElrAN 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
143-329 |
1.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 143 EEIEQHNKELCKENRELKDscvsLQKQNSDMQATLQKKQEeLETLKSINKKLEQTMKEQKDCwEIELLQLKEQNQKMSSE 222
Cdd:COG3206 182 EQLPELRKELEEAEAALEE----FRQKNGLVDLSEEAKLL-LQQLSELESQLAEARAELAEA-EARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 223 NEKMG--VRVDQLQAQLSNQGREMEKL----------VQGVQDKTEQLEH-LKEENGQLFLSLTEQRE----HQKKLEQT 285
Cdd:COG3206 256 LPELLqsPVIQQLRAQLAELEAELAELsarytpnhpdVIALRAQIAALRAqLQQEAQRILASLEAELEalqaREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 154426076 286 VEEMKQKETTAAKKQQELTD--QNMDLSKRLSENMiihdvLQREKE 329
Cdd:COG3206 336 LAQLEARLAELPELEAELRRleREVEVARELYESL-----LQRLEE 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-316 |
1.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 150 KELCKENRELKDScvslQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcwEIELLQLKEQNQKMSSENEKMGVR 229
Cdd:COG4717 74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 230 VDQLQAQ---LSNQGREMEKLVQGVQDKTEQLEHLKEENGQlflsltEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQ 306
Cdd:COG4717 148 LEELEERleeLRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170
....*....|
gi 154426076 307 NMDLSKRLSE 316
Cdd:COG4717 222 LEELEEELEQ 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
139-316 |
1.77e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQtmkeqkdcweiELLQLKEQNQK 218
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEE-----------DILLLEDQNSK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 219 MSSENEKMGVRVDQLQAQLSNQgremeklvqgvQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQK-ETTAA 297
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEE-----------EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlEGEST 218
|
170
....*....|....*....
gi 154426076 298 kkqqELTDQNMDLSKRLSE 316
Cdd:pfam01576 219 ----DLQEQIAELQAQIAE 233
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
185-293 |
1.82e-04 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 42.30 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 185 ETLKSINKKLEQTMKEQKDcweiELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEqlehLKEE 264
Cdd:TIGR04211 62 PSARERLPELQQELAELQE----ELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIE----LDEE 133
|
90 100
....*....|....*....|....*....
gi 154426076 265 NGQLFLSLTEQREHQKKLEQTVEEMKQKE 293
Cdd:TIGR04211 134 NRELREELAELKQENEALEAENERLQENE 162
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-345 |
2.14e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 143 EEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSinkKLEQTMKEqkdcweiellqlKEQNQKMSSE 222
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQ------------KNNALKKIRE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 223 NEkmgVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMK---QKETTAAKK 299
Cdd:pfam01576 269 LE---AQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkalEEETRSHEA 345
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 154426076 300 Q-QELTDQNMDLSKRLSENMiihDVLQREKEKMEKENDYLKRENNRL 345
Cdd:pfam01576 346 QlQEMRQKHTQALEELTEQL---EQAKRNKANLEKAKQALESENAEL 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-334 |
2.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 150 KELCKENRELKDSCVSLQKQnsdmQATLQKKQEELETLKSINKKLEQTMKEQKDCWEI--ELLQLKEQNQKMSSENEKmg 227
Cdd:COG4913 613 AALEAELAELEEELAEAEER----LEALEAELDALQERREALQRLAEYSWDEIDVASAerEIAELEAELERLDASSDD-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 228 vrVDQLQAQLsnqgremEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETT------AAKKQQ 301
Cdd:COG4913 687 --LAALEEQL-------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelrallEERFAA 757
|
170 180 190
....*....|....*....|....*....|....
gi 154426076 302 ELTDQNM-DLSKRLSENMiihDVLQREKEKMEKE 334
Cdd:COG4913 758 ALGDAVErELRENLEERI---DALRARLNRAEEE 788
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
130-342 |
3.23e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.40 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 130 EEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQtmkeqkdcweiEL 209
Cdd:pfam15818 212 EENINLTIKEQKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEA-----------EL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 210 LQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQreHQKKLEQTVEEM 289
Cdd:pfam15818 281 KALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKET--HIKLQEHYNKLC 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 290 KQKETTAAKKQQ---ELTDQNMDLSKRLSENMIIH----DVLQREKEKMEKENDYLKREN 342
Cdd:pfam15818 359 NQKKFEEDKKFQnvpEVNNENSEMSTEKSENLIIQkynsEQEIREENTKSFCSDTEYRET 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-340 |
3.43e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIE-LLQLKEQNQKM 219
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKaVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 220 SSE-NEKMGVRVDQLQ--AQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSL------TEQREHQKKLEQTVEEMK 290
Cdd:TIGR00618 313 HTElQSKMRSRAKLLMkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIReiscqqHTLTQHIHTLQQQKTTLT 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 154426076 291 QKETTAAKKQQELTDQNMDLSKRLSEN--MIIHDVLQREKEKMEKENDYLKR 340
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFrdLQGQLAHAKKQQELQQRYAELCA 444
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
128-339 |
4.17e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILVVTTQSEVEEIEQHNKELcKENRElkdscvSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEI 207
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKEKEI-PELRN------KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 208 ELLQL-------KEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQG-------VQDKTEQLEHLKEENGQL---FL 270
Cdd:TIGR00606 795 ERFQMelkdverKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 271 SLTEQREHQKKL-EQTVE----------EMKQKETT----AAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKEN 335
Cdd:TIGR00606 875 QIGTNLQRRQQFeEQLVElstevqslirEIKDAKEQdsplETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
....
gi 154426076 336 DYLK 339
Cdd:TIGR00606 955 GYMK 958
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-336 |
4.91e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 130 EEDILVVTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQnsdmQATLQKKQEELETLKSIN--KKLEQTMKEQKDCWEI 207
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 208 ELLQLKEQNQKMSSENEKMgvrvdqlQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKleqTVE 287
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKK-------EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---KAE 1747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 154426076 288 EMKQKETTAAKKQQELTDQNMDLSK-RLSENMIIHDVLQREKEKMEKEND 336
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
137-356 |
5.68e-04 |
|
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: 42.37 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNsdmqATLQKKQEELETLKSIN----KKLEQTMKEqkdcweieLLQL 212
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQEN----KKLQERLDQLESGDDSGtpggKKYLLLQKQ--------LEQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 213 KEQNQKMSSENEKMGVRVDQLQAQLSnqgrEMEKLVQGVQDKTEQLEHLKEENGqlflSLTEQREHQKKLEQTVEEMKQK 292
Cdd:pfam05622 72 QEENFRLETARDDYRIKCEELEKEVL----ELQHRNEELTSLAEEAQALKDEMD----ILRESSDKVKKLEATVETYKKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 293 ---------------------------------ETTAAKKQQELTDQNM-DLSKRLSENMIIHDVLQREKEKMEKENDYL 338
Cdd:pfam05622 144 ledlgdlrrqvklleernaeymqrtlqleeelkKANALRGQLETYKRQVqELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250
....*....|....*...
gi 154426076 339 KRENNRLLSymglDCDSL 356
Cdd:pfam05622 224 QKEKERLII----ERDTL 237
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
178-306 |
6.56e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 178 QKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQ 257
Cdd:pfam15709 362 RLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 154426076 258 LEHLK-EENGQLFLSLTEQ-REHQKKL-----EQTVEEMKQKETTAAKKQQELTDQ 306
Cdd:pfam15709 442 EEAERaEAEKQRQKELEMQlAEEQKRLmemaeEERLEYQRQKQEAEEKARLEAEER 497
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
142-299 |
7.10e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 142 VEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKEQNQKMSS 221
Cdd:pfam17078 68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 222 ENEKmgvRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVE---EMKQKETTAAK 298
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNlypESRNKILEYAE 224
|
.
gi 154426076 299 K 299
Cdd:pfam17078 225 K 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
128-312 |
7.99e-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: 42.03 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILVVTTQSEVEE-IEQHNKELCKenreLKDSCVSLQKQNSDMQATLQKKQEE-----------LETLKSINKKLE 195
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 196 QTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFlslteQ 275
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW-----D 405
|
170 180 190
....*....|....*....|....*....|....*..
gi 154426076 276 REHQKKLeqTVEEMKqkettaakkqQELTDQNMDLSK 312
Cdd:pfam15921 406 RDTGNSI--TIDHLR----------RELDDRNMEVQR 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-305 |
8.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEE-IEQHN--KELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWE------- 206
Cdd:PRK02224 489 EEVEEVEErLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeae 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 207 ---IELLQLKEQNQKMSSENEKMGvRVDQLQAQLSNQGREMEKLvqgvqdkTEQLEHLKEENGQLFLSLTEQREHQKKLE 283
Cdd:PRK02224 569 earEEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERL-------REKREALAELNDERRERLAEKRERKRELE 640
|
170 180
....*....|....*....|....*..
gi 154426076 284 QT-----VEEMKQKETTAAKKQQELTD 305
Cdd:PRK02224 641 AEfdearIEEAREDKERAEEYLEQVEE 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
165-338 |
8.85e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 165 SLQKQNSDMQA---TLQKKQEELETLKsinKKLEQTMKE-QKDCWEIEL--LQLKEQNQKMSSENEKMGVRVDQLQAQLS 238
Cdd:pfam01576 381 ALESENAELQAelrTLQQAKQDSEHKR---KKLEGQLQElQARLSESERqrAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 239 NQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENM 318
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
170 180
....*....|....*....|
gi 154426076 319 IIHDVLQREKEKMEKENDYL 338
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEAL 557
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
124-347 |
1.01e-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: 41.88 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 124 QFRPENEEDILVvTTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKE--- 200
Cdd:pfam02463 257 KQEIEKEEEKLA-QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKeke 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 201 -------QKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSnQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLT 273
Cdd:pfam02463 336 eieelekELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-LESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154426076 274 EQREHQKKLEQTVEEMKQKETTA---AKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLLS 347
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEEsieLKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-341 |
1.12e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQ-----NSDMQATLQKKQEELETLK---SINKKLEQTMKEQKDCWEIELL 210
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQnqiSQNNKIISQLNEQISQLKKELT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 211 QLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMK 290
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 154426076 291 QKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRE 341
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
141-303 |
1.73e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDcweielLQLKEQNQKMS 220
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------RIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 221 SENEKMgvrVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEE----NGQLFLSLTEQREHQKKLEQTVEEMKQKETTA 296
Cdd:COG1579 85 VRNNKE---YEALQKEIESLKRRISDLEDEILELMERIEELEEElaelEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
....*..
gi 154426076 297 AKKQQEL 303
Cdd:COG1579 162 EAEREEL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
128-345 |
2.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 128 ENEEDILVVTTqSEVEEIEQHNKELCKENRELKDSCVSLQKqnsdmqatLQKKQEELETLKSINKKLEQTMKEQKdcwEI 207
Cdd:PRK03918 448 EHRKELLEEYT-AELKRIEKELKEIEEKERKLRKELRELEK--------VLKKESELIKLKELAEQLKELEEKLK---KY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 208 ELLQLKEQNQkmssENEKMGVRVDQLQAQLSNQGREMEKLvQGVQDKTEQLEH----LKEENGQLflsLTEQREHQKKLE 283
Cdd:PRK03918 516 NLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKkldeLEEELAEL---LKELEELGFESV 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154426076 284 QTVEEMKQKETTAAKKQQELTDQNMDLSKRLSEnmiihdvLQREKEKMEKENDYLKRENNRL 345
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEEELDKAFEELAETEKRL 642
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
135-341 |
2.01e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 40.97 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 135 VVTTQSEVEEIEQHNKELcKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQT--------MKEQKDCwe 206
Cdd:NF012221 1534 VVATSESSQQADAVSKHA-KQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTdqnaletnGQAQRDA-- 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 207 iellqLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEK--------LVQGVQdktEQLEHLKEENGQLFLSLTEQreH 278
Cdd:NF012221 1611 -----ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQwrnpfaggLLDRVQ---EQLDDAKKISGKQLADAKQR--H 1680
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154426076 279 QKKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSenmiihDVLQREKEKMEKENDYLKRE 341
Cdd:NF012221 1681 VDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKA------DAEKRKDDALAKQNEAQQAE 1737
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
143-288 |
2.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 143 EEIEQHNKELckenRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQ-----LKEQNQ 217
Cdd:COG1579 31 AELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQkeiesLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154426076 218 KMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREhqkKLEQTVEE 288
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE---ELAAKIPP 174
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
139-264 |
2.15e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.95 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLqkkqEELETLKSINKKLEQTMKEQKDcweiellqLKEQNQK 218
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKIDALQVVEKDLRSCI----KLLEEIEAELAKLEEAKKKLKE--------LRDALEE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 154426076 219 MSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEE 264
Cdd:pfam18595 69 KEIELRELERREERLQRQLENAQEKLERLREQAEEKREAAQARLEE 114
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
131-422 |
2.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 131 EDILVVTTQSE----VEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELET--------LKSINKKLEQTM 198
Cdd:pfam15921 633 EKVKLVNAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnklkmqLKSAQSELEQTR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 199 KEQKDCWEIELLQLKEQNQKMSSENEKMGvRVDQLQAQLsnqgremEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREH 278
Cdd:pfam15921 713 NTLKSMEGSDGHAMKVAMGMQKQITAKRG-QIDALQSKI-------QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 279 QKKLEQTVEEMKQKETtaaKKQQELTDQNMDLSKRLSENMIIHDVLQREkekmEKENDYLKRENNrllsymgLDCDSLSY 358
Cdd:pfam15921 785 KNKMAGELEVLRSQER---RLKEKVANMEVALDKASLQFAECQDIIQRQ----EQESVRLKLQHT-------LDVKELQG 850
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154426076 359 QVPTSNqggTRQDPGLV----FGNPYSGIQES-SAPSLLS--IKKCPTCKSDFAADvfdhnlaLEQHLQTL 422
Cdd:pfam15921 851 PGYTSN---SSMKPRLLqpasFTRTHSNVPSSqSTASFLShhSRKTNALKEDPTRD-------LKQLLQEL 911
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-341 |
2.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKE---LCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCwEIELLQLKEQNQ 217
Cdd:PRK03918 284 ELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 218 KMSSENEKMGvRVDQLQAQLSnqGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETTAA 297
Cdd:PRK03918 363 LYEEAKAKKE-ELERLKKRLT--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 154426076 298 KKQQELTDQN-MDLSKRLSENmiIHDVLQREKEKMEKENDYLKRE 341
Cdd:PRK03918 440 VCGRELTEEHrKELLEEYTAE--LKRIEKELKEIEEKERKLRKEL 482
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
137-311 |
2.29e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQ------------NSDMQATLQKKQEELETLKSINKKLEQTMKEQ-KD 203
Cdd:pfam06008 72 QVNAESERTLGHAKELAEAIKNLIDNIKEINEKvatlgendfalpSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAeLK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 204 CWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQlflsltEQREHQKKLE 283
Cdd:pfam06008 152 AAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA------NLREFQRKKE 225
|
170 180
....*....|....*....|....*...
gi 154426076 284 QTVEEMKQKETTAAKKQQELTDQNMDLS 311
Cdd:pfam06008 226 EVSEQKNQLEETLKTARDSLDAANLLLQ 253
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
137-237 |
3.31e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 37.66 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEqtmkeqkdcweiELLQLKEqn 216
Cdd:pfam10473 49 NSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLE------------NLLEEKE-- 114
|
90 100
....*....|....*....|.
gi 154426076 217 QKMSSENEKMGVRVDQLQAQL 237
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQL 135
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
137-352 |
3.54e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELK---DSCVSLQKQnsdmQATLQKKQEELETLKSINKKLEQTMKEQKDC--------- 204
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQqhgNALAQLEPI----VSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaltevvq 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 205 ------WE--IELL--------QLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQL 268
Cdd:PRK04863 967 rrahfsYEdaAEMLaknsdlneKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 269 FLSLTEQ-----REHQKKLEQTVEEMKQKeTTAAKKQQELTDQNMD-LSKRLSE---------------NMIIHDVLqre 327
Cdd:PRK04863 1047 GVPADSGaeeraRARRDELHARLSANRSR-RNQLEKQLTFCEAEMDnLTKKLRKlerdyhemreqvvnaKAGWCAVL--- 1122
|
250 260
....*....|....*....|....*
gi 154426076 328 keKMEKENDYLKRENNRLLSYMGLD 352
Cdd:PRK04863 1123 --RLVKDNGVERRLHRRELAYLSAD 1145
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
138-359 |
3.66e-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: 39.70 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEIELLQLKE--- 214
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfea 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 215 ----QNQKMSSENEKMGVRVDQLQ---AQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEqrehQKKLEQTVE 287
Cdd:pfam05483 357 ttcsLEELLRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154426076 288 EMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRLLSYmgldCDSLSYQ 359
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH----CDKLLLE 500
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
140-345 |
3.87e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.72 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 140 SEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQatlQKKQEELETLKSINKKLEQTmKEQKD---------CWEIELL 210
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELE---QELAQYLKKIEDLNKKLKRH-KALVRrlqrrvlllTKERDGY 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 211 Q--LKEQNQKMSSENEKMgvrvdqlqaQLSNQGREMEKLVQGVQDKTEQLEHLKEengQLFLSLTEQREHQKKLEQTVEE 288
Cdd:pfam05557 359 RaiLESYDKELTMSNYSP---------QLLERIEEAEDMTQKMQAHNEEMEAQLS---VAEEELGGYKQQAQTLERELQA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 154426076 289 MKQKETTAakkqqeltdqnmDLSKRLSEnmiiHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:pfam05557 427 LRQQESLA------------DPSYSKEE----VDSLRRKLETLELERQRLREQKNEL 467
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
172-339 |
3.98e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.51 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 172 DMQATLQKKQEELETLKSINKKLEQtmkeqkdcweiELLQLKEQNQKmssenekmgvRVDQLQAQLSNQGREM-EKLVQG 250
Cdd:pfam04012 33 DMQSELVKARQALAQTIARQKQLER-----------RLEQQTEQAKK----------LEEKAQAALTKGNEELaREALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 251 VQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETT------AAKKQQELTDQNMDLSkrLSENMiihDVL 324
Cdd:pfam04012 92 KKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLlkarlkAAKAQEAVQTSLGSLS--TSSAT---DSF 166
|
170
....*....|....*...
gi 154426076 325 QREKEK---MEKENDYLK 339
Cdd:pfam04012 167 ERIEEKieeREARADAAA 184
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
138-351 |
4.61e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 39.69 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 138 TQSEVEEIEQHNKELCKENRE--LKDSCVSLQKQNSDMQATlqKKQEELETLKSINKKLEQTMKEQKDCWEIELL----- 210
Cdd:COG5644 171 SESEIESSDSDHDDENSDSKLdnLRNYIVSLKKDEADAESV--LSSDDNDSIEEIKYDPHETNKESGSSETIDITdllds 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 211 ----QLKEQNQKMSSENEKMGVRVDQ-LQAQLSNQG------REMEKLVQGVQD--KTEQL--------EHLKEENGqLF 269
Cdd:COG5644 249 ipmeQLKVSLKPLVSESSKLDAPLAKsIQDRLERQAayeqtkNDLEKWKPIVADnrKSDQLifpmnetaRPVPSNNG-LA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 270 LSLTEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNM---DLSKRLSENMIIHDVLQREKEKME-----KENDYLKRE 341
Cdd:COG5644 328 SSFEPRTESERKMHQALLDAGLENESALKKQEELALNKLsveEVAERTRQLRFMRELMFREERKAKrvakiKSKTYRKIR 407
|
250
....*....|
gi 154426076 342 NNRLLSYMGL 351
Cdd:COG5644 408 KNRKEKEMAL 417
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
193-349 |
5.24e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.18 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 193 KLEQTMKEQKDCWEIELLQLKEQNQKMSSENEKMGVRVDQLQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSL 272
Cdd:pfam17078 3 KVIESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154426076 273 TEQREHQKKLEQTVEEMKQKETTAAKKQQELTDQNMDLskrLSENMIIHDVLQREKEKMEKENDYLKREN-NRLLSYM 349
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLQIQYDAL---VDSQNEYKDHYQQEINTLQESLEDLKLENeKQLENYQ 157
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
137-310 |
5.87e-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: 39.39 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 137 TTQSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLE-QTMKEQKDCWEIE--LLQLK 213
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgKNIKLSKDVSSLEsqLQDTQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 214 EQNQKMSSENEKMGVRVDQ-------LQAQLSNQGREMEKLVQGVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTV 286
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQledernsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
170 180 190
....*....|....*....|....*....|....*
gi 154426076 287 EEMKQK-----------ETTAAKKQQELTDQNMDL 310
Cdd:pfam01576 555 EALTQQleekaaaydklEKTKNRLQQELDDLLVDL 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-345 |
5.98e-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: 38.93 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 124 QFRPENEEDILVVTT------QSEVEEIEQ--HNKE---------------LCKENRELKDSCVSLQKQNSDMQATLQKK 180
Cdd:pfam05483 369 QQRLEKNEDQLKIITmelqkkSSELEEMTKfkNNKEveleelkkilaedekLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 181 QEELETLK---SINKKLEQTMKEQKDCWEIELLQLKEQNQKMSS-------ENEKMGVRVDQLQAQLSNQGREMEKLVQG 250
Cdd:pfam05483 449 EKEIHDLEiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 251 VQDKTEQLEHLKEENGQLFLSLTEQREhqkKLEQTVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEK 330
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
250
....*....|....*
gi 154426076 331 MEKENDYLKRENNRL 345
Cdd:pfam05483 606 KNKNIEELHQENKAL 620
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
129-345 |
6.65e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.35 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 129 NEEDILVVTTQSEVEEIEQHNKELCKENRELKDscvsLQKQNSDMQATLQKKQEELETLKSINKKLEQ---TMKEQKDcw 205
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKE----LKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRK-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 206 EIELLQLKEQNQKMSSENEKMGV-RVDQLQAQLSNQGREMEKLVQgVQDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQ 284
Cdd:COG1340 117 EIERLEWRQQTEVLSPEEEKELVeKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKELAEEAQELHE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154426076 285 TVEEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRENNRL 345
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-341 |
6.82e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 141 EVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEEL----------ETLKSINKKLEQTMKEQKDCWEIELL 210
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkaeeakkadEAKKAEEKKKADELKKAEELKKAEEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 211 QLKEQNQKmSSENEKMGVRVDQL--QAQLSNQGREMEKLVQGVQDKTEQLEHLKEE--NGQLFLSLTEQREHQKKLEQTV 286
Cdd:PTZ00121 1564 KKAEEAKK-AEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKE 1642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 154426076 287 EEMKQKETTAAKKQQELTDQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKRE 341
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
302-347 |
6.87e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 38.66 E-value: 6.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 154426076 302 ELTDQNMDLSKRLSEnmiihdvLQREKEKMEKENDYLKRENNRLLS 347
Cdd:PRK03992 12 ELEEQIRQLELKLRD-------LEAENEKLERELERLKSELEKLKS 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
171-340 |
8.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 171 SDMQATLQKKQEELETLKSIN------KKLEQTMKEQKDC------W--EIELLQLKEQNQKMSSENEKMGVRVDQLQAQ 236
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRelaeryAAARERLAELEYLraalrlWfaQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 237 LSNQGREMEKLVQGV-QDKTEQLEHLKEENGQLFLSLTEQREHQKKLEQTVEEMKQKETT-----------AAKKQQELT 304
Cdd:COG4913 318 LDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeefaalraeAAALLEALE 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 154426076 305 DQNMDLSKRLSENMIIHDVLQREKEKMEKENDYLKR 340
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
139-244 |
9.06e-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: 38.52 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMQATLQKKQEELETLKSINKKLEQTMKEQKDCWEiELLQLKEQ-NQ 217
Cdd:pfam05622 310 QQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQS-ELQKKKEQiEE 388
|
90 100
....*....|....*....|....*..
gi 154426076 218 KMSSENEKMGVRVDQLQAQLSNQGREM 244
Cdd:pfam05622 389 LEPKQDSNLAQKIDELQEALRKKDEDM 415
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
139-259 |
9.21e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 36.51 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154426076 139 QSEVEEIEQHNKELCKENRELKDSCVSLQKQNSDMqatlqkkQEELEtlksinkKLEQTMKEQKdcweiellQLKEQNQK 218
Cdd:pfam12718 13 QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQL-------EEEVE-------KLEEQLKEAK--------EKAEESEK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 154426076 219 MSSENEKMGVRVDQLQAQLSNQGRE----MEKLVQgVQDKTEQLE 259
Cdd:pfam12718 71 LKTNNENLTRKIQLLEEELEESDKRlketTEKLRE-TDVKAEHLE 114
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