|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
155-249 |
1.20e-38 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 138.56 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 155 QWPITPTDQAKYDSIFQSLNP-VNGKLSGAHVRPVLMNSGLDAHALARIWELSDQDKDGNLDRIEMSVALHLVYRSLQSD 233
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 392890153 234 PVPAQLPPNLIHPSKA 249
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
335-427 |
2.67e-35 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 128.93 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 335 EWPINTGD---YADQFAQTDTNKDGLVDGMDMRAPMMTTGLSAQILAHVWALADIKKCGQLNLEQFALTMHLLDMAKRGE 411
Cdd:smart00027 1 PWAISPEDkakYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 392890153 412 SIPSELPLHLIPPSFR 427
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
166-231 |
5.06e-22 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 89.97 E-value: 5.06e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 166 YDSIFQSLNPVN-GKLSGAHVRPVLMNSGLDAHALARIWELSDQDKDGNLDRIEMSVALHLVYRSLQ 231
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
343-409 |
1.33e-21 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 88.82 E-value: 1.33e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 343 YADQFAQTDTNKDGLVDGMDMRAPMMTTGLSAQILAHVWALADIKKCGQLNLEQFALTMHLLDMAKR 409
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
165-249 |
3.55e-21 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 88.97 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 165 KYDSIFQSLNPVNGKLSGAHVRPVLMNSGLDAHALARIWELSDQDKDGNLDRIEMSVALHLVYRSL--QSDPVPAQLPPN 242
Cdd:pfam12763 11 KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVngNIADVPDELPDW 90
|
....*..
gi 392890153 243 LIHPSKA 249
Cdd:pfam12763 91 LVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
15-81 |
5.49e-18 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 78.42 E-value: 5.49e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 15 FNHAFAEMNPHGAPRIGAAEAATFLKKSNLAMPVLGQIWELSDSQKVGSLDKRGAFVAFKLVAAAQQ 81
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
12-88 |
5.88e-12 |
|
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.
Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 62.29 E-value: 5.88e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 12 NDVFNHAFAEMNPHGAPRIGAAEAATFLKKSNLAMPVLGQIWELSDSQKVGSLDKRGAFVAFKLVAAAQQGKPVANS 88
Cdd:smart00027 9 KAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
454-674 |
3.39e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEdckandekemeelkKEIEMLDNQFKTVRGEIVKETSQREQKVAEL 613
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAE--------------EELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890153 614 TTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSL 674
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
454-672 |
3.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDckandekemeelkkEIEMLDNQFKTVRGEIVKETSQREQKVAEL 613
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE--------------ELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 614 TTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQ 672
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
450-672 |
6.35e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 450 ATSMEIKEaLEGENEEMKQLAESIQSML----VERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEA 525
Cdd:TIGR02168 674 ERRREIEE-LEEKIEELEEKIAELEKALaelrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 526 TRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQ 605
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392890153 606 REQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEK------SEEEMVQILRSQQRLLSTVIDQ 672
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneraSLEEALALLRSELEELSEELRE 905
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
498-676 |
8.71e-11 |
|
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: 62.63 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 498 NSSIKNLqVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKE 577
Cdd:COG1579 3 PEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 578 meelkkeiemLDN-----QFKTVRGEIvkETSQREQKVAELTTLERKEARDQIQ------MEKLDAAIENTTKLTEQVSD 646
Cdd:COG1579 82 ----------LGNvrnnkEYEALQKEI--ESLKRRISDLEDEILELMERIEELEeelaelEAELAELEAELEEKKAELDE 149
|
170 180 190
....*....|....*....|....*....|
gi 392890153 647 AVEKSEEEMVQILRSQQRLLSTvIDQSLLS 676
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK-IPPELLA 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-664 |
8.35e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQLAESIQSMLverKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQ 535
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAEL---QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 536 IEQLEsackAQKETKEdtekrmQQIDEDAKNAEDCKANdekeMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVAELTT 615
Cdd:TIGR02168 318 LEELE----AQLEELE------SKLDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 392890153 616 LERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQR 664
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
454-684 |
1.95e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAE-DCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVAE 612
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392890153 613 LTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSLLSDDTVYGET 684
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-665 |
2.54e-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: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQI-EQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKAndekemeelkkEIEMLDNQFKTVRGEIVKETSQREQKVAE 612
Cdd:COG4942 104 EELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------LAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392890153 613 LTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
454-677 |
3.87e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEM-------KQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEAT 526
Cdd:COG4372 63 QLEEELEQARSELeqleeelEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 527 RRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDA---------KNAEDCKANDEKEMEELKKEIEMLDNQFKTVRG 597
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 598 EIVKETSQREQKVAELTTLERKEArdqIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSLLSD 677
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEE---DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
497-665 |
4.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 497 KNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEK 576
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 577 EMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENT----TKLTEQVSDAVEKSE 652
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraelTLLNEEAANLRERLE 827
|
170
....*....|...
gi 392890153 653 EEMVQILRSQQRL 665
Cdd:TIGR02168 828 SLERRIAATERRL 840
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
449-665 |
6.77e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRR 528
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 529 LADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQ 608
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 609 KVAELTTLErkeardqiqmEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:TIGR02168 899 LSEELRELE----------SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
335-425 |
6.85e-08 |
|
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
Pssm-ID: 289529 Cd Length: 104 Bit Score: 51.22 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 335 EWPINTgdYADQFaQTDTNKDGLVDGmDMRAPMM-TTGLSAQILAHVWALADIKKCGQLNLEQFALTMHLL-DMA-KRGE 411
Cdd:pfam12763 6 EWEIKK--YWEIF-SGLKPENNKLTG-DQVSPVLkNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIfDLVnGNIA 81
|
90
....*....|....
gi 392890153 412 SIPSELPLHLIPPS 425
Cdd:pfam12763 82 DVPDELPDWLVPGS 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-665 |
7.70e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 457 EALEGENEEMKQLAESIQSMLVERKT----AEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADY 532
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 533 DTQIEQLESACKAQKETKEDTEKRMQQIDEDA-------KNAEDCKANDEKEMEELkkeiemlDNQFKTVRGEIVKETSQ 605
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlrerlESLERRIAATERRLEDL-------EEQIEELSEDIESLAAE 860
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 606 REQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-665 |
1.00e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADmtIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKAQKETKEDTEkrmQQIDEDAKNAEDCKAndekEMEELKKEIEMLDNQFKTVRGEIV----------KET 603
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNG----KKEELEEELEELEAALRDLESRLGdlkkerdeleAQL 898
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 604 SQREQKVAEL-TTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMV------QILRSQQRL 665
Cdd:TIGR02169 899 RELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqaELQRVEEEI 967
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
447-682 |
1.21e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 447 LPEATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEAT 526
Cdd:TIGR02169 284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 527 RRLADYDTQIEQLEsacKAQKETKEDTEKRMQQIDEDAKNAEDCKAN-DEKEMEELKKEIEMLD--NQFKTVRGEIVKET 603
Cdd:TIGR02169 364 EELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRElDRLQEELQRLSEELADlnAAIAGIEAKINELE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 604 SQREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVID----QSLLSDDT 679
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgravEEVLKASI 520
|
....*
gi 392890153 680 --VYG 682
Cdd:TIGR02169 521 qgVHG 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
472-672 |
1.71e-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: 55.06 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 472 SIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKE 551
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 552 DTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLD 631
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392890153 632 AAIENTTKLTEQVSDAVEKSEEEMVQI---LRSQQRLLSTVIDQ 672
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESE 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-672 |
2.08e-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: 54.69 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKnssiknLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR------VKEKIGELEAEIASLERSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKAQKETKEDTEKRM--QQIDEDAKNAEdcKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVA 611
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIeeERKRRDKLTEE--YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890153 612 ELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQI---LRSQQRLLSTVIDQ 672
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAAD 463
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
479-635 |
2.22e-07 |
|
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: 52.62 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 479 ERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIE-------------QLESAcKA 545
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkeyealqkEIESL-KR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 546 QKETKEDTEKR-MQQIDEDAKNAEDCKAndekemeelkkeiemldnQFKTVRGEIVKETSQREQKVAELTTlERKEARDQ 624
Cdd:COG1579 104 RISDLEDEILElMERIEELEEELAELEA------------------ELAELEAELEEKKAELDEELAELEA-ELEELEAE 164
|
170
....*....|.
gi 392890153 625 IqmEKLDAAIE 635
Cdd:COG1579 165 R--EELAAKIP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-665 |
3.54e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 457 EALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRrladYDTQI 536
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE----YIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 537 EQLESACKAQ---KETKEDTEKRMQQIDEDAKNAEDCKAndekemeelkkEIEMLDNQFKtvrgEIVKETSQREQKVAEL 613
Cdd:PRK03918 300 EFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEE-----------RLEELKKKLK----ELEKRLEELEERHELY 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392890153 614 TTLERKEAR-DQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:PRK03918 365 EEAKAKKEElERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-678 |
3.81e-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: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 439 AQSVSTPQLPEATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQL 518
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 519 ERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQqidedaknaedckandekemeelkkeiemlDNQFKTVRGE 598
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------------------------------EAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 599 IVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIeNTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVID-QSLLSD 677
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnQSGLSG 520
|
.
gi 392890153 678 D 678
Cdd:TIGR02168 521 I 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
478-674 |
8.18e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 478 VERKTAEEAVLQLEADMTIKNSSiKNLQVELATLESTVKQLERQKGEatrrLADYDTQIEQLESACKAQKETKEDTEKRM 557
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALS-EQLRKALFELDKLQEELEQLREE----LEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 558 QQIDEDAKNAEdckandekemeelkKEIEMLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENT 637
Cdd:COG4372 83 EELNEQLQAAQ--------------AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 392890153 638 TKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSL 674
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
454-660 |
1.77e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGEN-EEMKQLAEsiqsmlvERKTAEEAVLQLEADMTIKNSSIKNLQV---ELATLESTVKQLERQKGEATRRL 529
Cdd:PRK03918 507 ELEEKLKKYNlEELEKKAE-------EYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKEL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 530 A--------DYDTQIEQLESACK-------AQKEtKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEML-----D 589
Cdd:PRK03918 580 EelgfesveELEERLKELEPFYNeylelkdAEKE-LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkysE 658
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392890153 590 NQFKTVRGEIVKETSQREQKVAELTTLERKeaRDQIQ--MEKLDAAIENTTKLTEQVSDaVEKSEEEmVQILR 660
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKR--REEIKktLEKLKEELEEREKAKKELEK-LEKALER-VEELR 727
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
447-668 |
1.98e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 447 LPEATSME--IKEALEGENE-EMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATL-------ESTVK 516
Cdd:pfam10174 441 LEEALSEKerIIERLKEQRErEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkDSKLK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 517 QLE---RQKGEATRRL-----------------ADYDTQIEQLESACKAQKE--TKEDTE-KRMQQIDEDAKNAEDCK-- 571
Cdd:pfam10174 521 SLEiavEQKKEECSKLenqlkkahnaeeavrtnPEINDRIRLLEQEVARYKEesGKAQAEvERLLGILREVENEKNDKdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 572 --ANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQKvAELTTLERKEARDQIQMEKLDAAIENttklTEQVSDAVE 649
Cdd:pfam10174 601 kiAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLEELMGALEK----TRQELDATK 675
|
250
....*....|....*....
gi 392890153 650 KSEEEMVQILRSQQRLLST 668
Cdd:pfam10174 676 ARLSSTQQSLAEKDGHLTN 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
469-665 |
2.45e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 469 LAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKE 548
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 549 TKEDTEKRMQQIDEDAKNaedckandekemeelkkeiemLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQME 628
Cdd:COG4372 109 EAEELQEELEELQKERQD---------------------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 392890153 629 KLDAAIENTTKltEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:COG4372 168 ALEQELQALSE--AEAEQALDELLKEANRNAEKEEEL 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
452-653 |
4.10e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 452 SMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLAD 531
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 532 YDTQIEQL----ESACKAQKETKEDTEKRmqQIDEDAKNAEDCKANDEKEMEELKKEIemldnqfktvRGEIVKETSQRE 607
Cdd:PTZ00121 1442 EAKKADEAkkkaEEAKKAEEAKKKAEEAK--KADEAKKKAEEAKKADEAKKKAEEAKK----------KADEAKKAAEAK 1509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392890153 608 QKVAELTTLERKEARDQIQMEKLDAAIENTTKLTE-QVSDAVEKSEE 653
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkKKADELKKAEE 1556
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
451-573 |
7.72e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 451 TSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADmtiknssIKNLQVELATLESTVKQLERQKGEATRRLA 530
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE-------KKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 392890153 531 DYDTQIEQLESAckaqketKEDTEKRMQQIDEDAKNAEDCKAN 573
Cdd:TIGR04523 628 KLSSIIKNIKSK-------KNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
479-666 |
1.09e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 479 ERKTAEEA-VLQLEA---DMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTE 554
Cdd:COG1196 208 QAEKAERYrELKEELkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 555 KRMQQIDEDAKNAEdckandekemeelkKEIEMLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAI 634
Cdd:COG1196 288 AEEYELLAELARLE--------------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190
....*....|....*....|....*....|..
gi 392890153 635 ENTTKLTEQVSDAVEKSEEEMVQILRSQQRLL 666
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
459-665 |
2.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 459 LEGENEEMKQ-LAESIQSMLVERktaeeavLQLEADMTIKnSSIKNLQVELATLestvKQLERQKGEATRRLADYDTQIE 537
Cdd:COG4717 28 IYGPNEAGKStLLAFIRAMLLER-------LEKEADELFK-PQGRKPELNLKEL----KELEEELKEAEEKEEEYAELQE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 538 QLESAckaqKETKEDTEKRMQQIDEDAKNAEDCKANdekemeelkkeiEMLDNQFKTVRGEIVKETSQRE---QKVAELT 614
Cdd:COG4717 96 ELEEL----EEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALEAELAELPERLEeleERLEELR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392890153 615 TLERK--EARDQIQM--EKLDAAIENTTKLTE-QVSDAVEKSEEEMVQILRSQQRL 665
Cdd:COG4717 160 ELEEEleELEAELAElqEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEEL 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
446-633 |
3.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 446 QLPEATSMEIKEaLEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNL--QVELATLESTVKQLERQKG 523
Cdd:COG4717 64 RKPELNLKELKE-LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 524 EATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDaknAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKET 603
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190
....*....|....*....|....*....|
gi 392890153 604 SQREQKVAELTTLERKEARDQIQmEKLDAA 633
Cdd:COG4717 220 EELEELEEELEQLENELEAAALE-ERLKEA 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
454-655 |
3.69e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEgENEEMKQLAESIQSMLVERKTAEEAvLQLEADMTIKNSSIKN---------LQVELATLESTVKQLERQKGE 524
Cdd:TIGR02169 171 KKEKALE-ELEEVEENIERLDLIIDEKRQQLER-LRREREKAERYQALLKekreyegyeLLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 525 ATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAedckandekemeelkkeiemLDNQFKTVRGEIVKETS 604
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR--------------------VKEKIGELEAEIASLER 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392890153 605 QREQKVAELTTLERKEARDQI-------QMEKLDAAIENTTKLTEQVSDAVEKSEEEM 655
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAeidkllaEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
456-625 |
3.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADmtIKNSSiknlQVELATLESTVKQLERQKGEATRRLADYDTQ 535
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNG----GDRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 536 IEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDckandekemeelkkeieMLDNQFKTVRGEIVKETSQREQKVAELTT 615
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELE-----------------ALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170
....*....|....*....
gi 392890153 616 LERK---------EARDQI 625
Cdd:COG4913 431 LERRksniparllALRDAL 449
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
457-671 |
4.30e-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: 46.94 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 457 EALEGENEEMKQLAESIQSMLvERKTAEeaVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQI 536
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKEL-KSKEKE--LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 537 EQLESACKAQ--KETKEDTEKRMQQIDEDAKNAEdcKANDEkemeeLKKEIEMLDNQFKTVRGEIVKETSQREQKVAELT 614
Cdd:TIGR04523 548 NKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLK--KKQEE-----KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 615 TLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVID 671
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
454-734 |
6.22e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMK-QLAESIQSMLVERKT--------AEEAVLQLEADMTIKNSSIKNLQVELATLESTV-KQLERQKG 523
Cdd:COG5185 282 ENANNLIKQFENTKeKIAEYTKSIDIKKATesleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLtENLEAIKE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 524 EATRRLADYD--TQIEQLESACKAQKETKEDTEKRMQQIDEDAKNA----EDCKANDEKEMEElkkeiemldnqfktVRG 597
Cdd:COG5185 362 EIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEIlatlEDTLKAADRQIEE--------------LQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 598 EIVKETSQREQKVAELTTL-ERKEARDQIQMEKLDAAIENTTKLTEQ-VSDAVEKSEEEMVQIlrsqQRLLSTVIDQSLL 675
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELiSELNKVMREADEESQSRLEEAYDEINRsVRSKKEDLNEELTQI----ESRVSTLKATLEK 503
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 676 SDDTVYGETAGTSSQNHVQQPPDPFASARANPAADPFAQVDQFGSSGHFDAAFPTDPFA 734
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQA 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-672 |
6.59e-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: 46.55 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESACKA-QKETKEDtEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKtvrgEIVKETSQREQKVAE 612
Cdd:TIGR04523 475 RSINKIKQNLEQkQKELKSK-EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK----EKESKISDLEDELNK 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890153 613 L-TTLERKEARDQIQ-----MEKLDAAIENTTKLTEQVSDAVEKSEEEmVQILRSQQRLLSTVIDQ 672
Cdd:TIGR04523 550 DdFELKKENLEKEIDeknkeIEELKQTQKSLKKKQEEKQELIDQKEKE-KKDLIKEIEEKEKKISS 614
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
449-656 |
8.71e-05 |
|
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: 45.89 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGENEEMKQLAESIQsMLVERKTAEEAVLQLEADMT-IKNSSIKNLQVELATLESTVKQLERQKGEATR 527
Cdd:pfam05557 33 EKKASALKRQLDRESDRNQELQKRIR-LLEKREAEAEEALREQAELNrLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 528 RLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEiemlDNQFKTVRGEIVKETSQRE 607
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA----EQRIKELEFEIQSQEQDSE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890153 608 ------QKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSD------AVEKSEEEMV 656
Cdd:pfam05557 188 ivknskSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDlkrkleREEKYREEAA 248
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
456-560 |
9.46e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 43.46 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQLAESIQSMLV-------ERKTAEEAVLQLEADMTIKNSSIKNLQVELAtlestvkQLERQKGEATRR 528
Cdd:pfam11559 23 FDTAEGVEENIARIINVIYELLQqrdrdleFRESLNETIRTLEAEIERLQSKIERLKTQLE-------DLERELALLQAK 95
|
90 100 110
....*....|....*....|....*....|..
gi 392890153 529 LADYDTQIEQLESACKAQKETKEDTEKRMQQI 560
Cdd:pfam11559 96 ERQLEKKLKTLEQKLKNEKEELQRLKNALQQI 127
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
449-664 |
1.13e-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: 45.88 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGE---------NEEMKQLAESIQSMLVERKTAEEAVLQLEADM-TIKNSSIKNLQVELATLEST-VKQ 517
Cdd:pfam17380 368 EEIAMEISRMRELErlqmerqqkNERVRQELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQREVRRLEEErARE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 518 LERQKGEATRRladyDTQIEQLESACKAQKETKEDTEKRmqqiDEDAKNAEDCKAND-EKEMEElkKEIEMLDNQFKtvR 596
Cdd:pfam17380 448 MERVRLEEQER----QQQVERLRQQEEERKRKKLELEKE----KRDRKRAEEQRRKIlEKELEE--RKQAMIEEERK--R 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392890153 597 GEIVKETSQREQKVAEltTLERKEA----RDQIQMEKLDAAIENTTKLTEQVS--DAVEKSEEEMVQILRSQQR 664
Cdd:pfam17380 516 KLLEKEMEERQKAIYE--EERRREAeeerRKQQEMEERRRIQEQMRKATEERSrlEAMEREREMMRQIVESEKA 587
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
465-796 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 465 EMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLadyDTQIEQLESACK 544
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 545 AQKETKEDTekrmQQIDE--DAKNAEDCKANDEKEMEELKKEIEMLDnQFKTVRGEIVKETSQREQKVAELTTLERKEAR 622
Cdd:COG3883 94 ALYRSGGSV----SYLDVllGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 623 DQIQMEKLDAAIENT-TKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSLLSDDTVYGETAGTSSQNHVQQPPDPFA 701
Cdd:COG3883 169 AKAELEAQQAEQEALlAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 702 SARANPAADPFAQVDQFGSSGHFDAAFPTDPFAQGGFPSDSGFAQSAPAKPAPPRPAPPKSARETPVNDPFAPSQGQSTQ 781
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASA 328
|
330
....*....|....*
gi 392890153 782 PAGFADFADFGSAFN 796
Cdd:COG3883 329 GGGGGSGGGGGSSGG 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
449-657 |
1.24e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAV----LQLEADMTIKNSSIKNLQVELATLESTVKQLE--RQK 522
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 523 GEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKE 602
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 603 TSQReQKVAELTTLERKEARDQIQMEKldAAIENTTKLTEQV----SDAVEKSEEEMVQ 657
Cdd:PTZ00121 1566 AEEA-KKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEkkmkAEEAKKAEEAKIK 1621
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
456-695 |
1.33e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMK-------QLAESIQSMLVERKTAEEAVLQLEADmtiKNSSIKNLQV----ELATLESTVKQLERQKGE 524
Cdd:pfam02463 207 KKALEYYQLKEKleleeeyLLYLDYLKLNEERIDLLQELLRDEQE---EIESSKQEIEkeeeKLAQVLKENKEEEKEKKL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 525 ATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELkkeiemlDNQFKTVRGEIVKETS 604
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-------EKELKELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 605 QREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVS--DAVEKSEEEMVQILRSQQRLLSTVIDQSLLSDDTVYG 682
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELelKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
250
....*....|...
gi 392890153 683 EtAGTSSQNHVQQ 695
Cdd:pfam02463 437 E-SIELKQGKLTE 448
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
426-671 |
1.76e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 426 FRPPTEPSALHHPAQSVSTPQLPEA---TSMEIKEALEGENEEMKQLAE---SIQSMLVERKTAEEAVLQLEADMTIKNS 499
Cdd:pfam15905 29 FRKQKAAESQPNLNNSKDASTPATArkvKSLELKKKSQKNLKESKDQKElekEIRALVQERGEQDKRLQALEEELEKVEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 500 SIKNLQVELATLESTVKQLERQKGEATR-------RLADYDTQ-------IE------QLESACKAQKETKEDTEKRMQq 559
Cdd:pfam15905 109 KLNAAVREKTSLSASVASLEKQLLELTRvnellkaKFSEDGTQkkmsslsMElmklrnKLEAKMKEVMAKQEGMEGKLQ- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 560 idEDAKNAEDCKANdekemeelkkeIEMLDNQFKTVRGEIVKETSQREQKVAELTTLErkEARDQIQMEKLDAAI----- 634
Cdd:pfam15905 188 --VTQKNLEHSKGK-----------VAQLEEKLVSTEKEKIEEKSETEKLLEYITELS--CVSEQVEKYKLDIAQleell 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 392890153 635 ---------------ENTTKLTEQVSDAVEK------SEEEMVQILRSQQRLLSTVID 671
Cdd:pfam15905 253 kekndeieslkqsleEKEQELSKQIKDLNEKckllesEKEELLREYEEKEQTLNAELE 310
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
454-662 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSML------VERKTAEEAVLQLEADMT-IKNSS--IKNLQVELATLESTVKQLERQKGE 524
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAeyswdeIDVASAEREIAELEAELErLDASSddLAALEEQLEELEAELEELEEELDE 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 525 ATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDE---DAKNAEdckandekemeelkkeiEMLDNQFKTVR----G 597
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAA-----------------ALGDAVERELRenleE 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392890153 598 EIVKETSQREQKVAELTTLeRKEARDQIQMEK--LDAAIENTT----KLTEQVSDAVEKSEEEMVQILRSQ 662
Cdd:COG4913 774 RIDALRARLNRAEEELERA-MRAFNREWPAETadLDADLESLPeylaLLDRLEEDGLPEYEERFKELLNEN 843
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
452-664 |
2.06e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 452 SMEIKEALEGENEeMKQLaesiqSMLVERktAEEAVLQLEADMTIKNSSIKNLQVELATLestVKQLERQKGEATRRLAD 531
Cdd:pfam05483 243 SLLLIQITEKENK-MKDL-----TFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRSMST 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 532 YDTQIEQLESACKAQKETKEDTEKRMQQIDEdAKNAE-----DCKANDEKEMEELKKEIEMLDN---QFKTVRGEIVKET 603
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELNK-AKAAHsfvvtEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKS 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 604 SQREqkvaELTTLERKEardQIQMEKLDAAIENTTKL------TEQVSDAVEKSEEEMVQILRSQQR 664
Cdd:pfam05483 391 SELE----EMTKFKNNK---EVELEELKKILAEDEKLldekkqFEKIAEELKGKEQELIFLLQAREK 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-653 |
2.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVER-KTAEEAvlQLEADMTIKNSSIKNLQVELATLESTvkqlERQKGEATRRLady 532
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEA--KIKAEELKKAEEEKKKVEQLKKKEAE----EKKKAEELKKA--- 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 533 dtqiEQLESACKAQKETKEDTEKR----MQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRgEIVKETSQREQ 608
Cdd:PTZ00121 1656 ----EEENKIKAAEEAKKAEEDKKkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKI 1730
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392890153 609 KVAElttLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEE 653
Cdd:PTZ00121 1731 KAEE---AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
453-680 |
3.28e-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: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 453 MEIkEALEGENEE--MKQLAESIQSMlverktaEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLA 530
Cdd:TIGR04523 295 SEI-SDLNNQKEQdwNKELKSELKNQ-------EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 531 DYDTQIEQLESACKAQKET-------KEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEML--------------- 588
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEiknlesqINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLketiiknnseikdlt 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 589 --DNQFKTVRGEIVKETSQREQKVAEL--------TTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEE--EMV 656
Cdd:TIGR04523 447 nqDSVKELIIKNLDNTRESLETQLKVLsrsinkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkEKI 526
|
250 260
....*....|....*....|....*..
gi 392890153 657 QILRSQQRLLSTVIDQ---SLLSDDTV 680
Cdd:TIGR04523 527 EKLESEKKEKESKISDledELNKDDFE 553
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
463-549 |
4.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 463 NEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLEstvKQLERQKGEATRRLADYDTQIEQLESA 542
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 392890153 543 CKAQKET 549
Cdd:COG1579 165 REELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
455-680 |
4.77e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 455 IKEALEGENEEmKQLAESIQSMLVERKTAEEAVLQLEADMTI---KNSSIKNLQVELATLESTVKQLERQKGEATRRLAD 531
Cdd:TIGR04523 165 KKQKEELENEL-NLLEKEKLNIQKNIDKIKNKLLKLELLLSNlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 532 YDTQI----EQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANdekeMEELKKEIEMLDNQ-----FKTVRGEIVK- 601
Cdd:TIGR04523 244 KTTEIsntqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ----LNQLKSEISDLNNQkeqdwNKELKSELKNq 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 602 ---------ETSQREQKVAELT-------------TLERKEARDQI--------------------------QMEKLDAA 633
Cdd:TIGR04523 320 ekkleeiqnQISQNNKIISQLNeqisqlkkeltnsESENSEKQRELeekqneieklkkenqsykqeiknlesQINDLESK 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 392890153 634 IENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQ-----SLLSDDTV 680
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseikDLTNQDSV 451
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
446-655 |
6.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 446 QLPEATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAvlQLEADMTI-----KNSSIKNLQVELATLESTVKQLER 520
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARET--RDEADEVLeeheeRREELETLEAEIEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 521 QKGEATRRLADYDTQIEQLESACKAQKETKE----DTEKRMQQIDEDAKNAEDCKandekemeelkkeiemldNQFKTVR 596
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELR------------------DRLEECR 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 597 GEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEM 655
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
449-569 |
6.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGENEEMKQLAESIQ----SMLVERKTAEEavLQLEADMtiKNSSIKNLQVElatlestVKQLERQKGE 524
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAEEAQelheEMIELYKEADE--LRKEADE--LHKEIVEAQEK-------ADELHEEIIE 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 392890153 525 ATRRLADYDTQIEQLESACKAQKETKEDTEkrmqqIDEDAKNAED 569
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKREKEKEE-----LEEKAEEIFE 274
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
454-674 |
6.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQV---ELATLESTVKQLERQ------KGE 524
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRqqtevlSPE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 525 ATRRLADydtQIEQLES---ACKAQKETKEDTEKRMQQIDEDAKNAEDckANDEKEMeelkkeiemLDNQFKTVRGEIVK 601
Cdd:COG1340 134 EEKELVE---KIKELEKeleKAKKALEKNEKLKELRAELKELRKEAEE--IHKKIKE---------LAEEAQELHEEMIE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 602 ETSQREQKVAELTTL--ERKEARDQIQM--EKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSL 674
Cdd:COG1340 200 LYKEADELRKEADELhkEIVEAQEKADElhEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
457-569 |
7.33e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.94 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 457 EALEGENEEMKQLAESI--QSMLVERKTA------EEAVLQLEAdmtiKNSSIKNLQVELATLESTVKQLERQKGEATRR 528
Cdd:pfam00261 95 EILEAQLKEAKEIAEEAdrKYEEVARKLVvvegdlERAEERAEL----AESKIVELEEELKVVGNNLKSLEASEEKASER 170
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392890153 529 LADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAED 569
Cdd:pfam00261 171 EDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLED 211
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-653 |
8.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEG-ENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADY 532
Cdd:PTZ00121 1228 AVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 533 DTQIEQLESACKAQKETKEDTEKrmqqIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKeTSQREQKVAE 612
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADA 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392890153 613 LttleRKEARDQIQMEKLDAAIENTTKLTEQVSDAVE---KSEE 653
Cdd:PTZ00121 1383 A----KKKAEEKKKADEAKKKAEEDKKKADELKKAAAakkKADE 1422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
462-637 |
9.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 462 ENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKgEATRRLADYDTQIEQLES 541
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 542 ACKAQ--KETKEDTEKRMQQIDEDAKNAEDcKANDEKEMEELkkeiemLDNQFKTVR--GEIVKETSQREQKVAELTTLE 617
Cdd:COG4717 417 ELEELleALDEEELEEELEELEEELEELEE-ELEELREELAE------LEAELEQLEedGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|
gi 392890153 618 RKEARDQIQMEKLDAAIENT 637
Cdd:COG4717 490 EEWAALKLALELLEEAREEY 509
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
453-538 |
9.54e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 453 MEIKEALEGENEEMKQLAESIQSML-VERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLAD 531
Cdd:smart00787 178 RDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAE 257
|
....*..
gi 392890153 532 YDTQIEQ 538
Cdd:smart00787 258 AEKKLEQ 264
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-573 |
9.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQLAESIQSMLVERKT----AEEAVLQLEADMTIKNSSIKNLQVELATLEstvKQLERQKGEATRRLAD 531
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKE---KELEQKQQELEKKEEE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 532 YDT----QIEQLESAC-------------KAQKETKEDTEKRMQQIDEDAKNAEDCKAN 573
Cdd:PRK12704 133 LEElieeQLQELERISgltaeeakeilleKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
496-671 |
1.10e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.93 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 496 IKNSSIKNLQ---------VELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKN 566
Cdd:PRK06669 6 FKRSNVINKEklktheiqkYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 567 AEDcKANdekemeelkkeiemldNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSD 646
Cdd:PRK06669 86 KTD-EAS----------------SIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKGREEGLEEVRELIEQLNK 148
|
170 180
....*....|....*....|....*.
gi 392890153 647 AVEKSEEEMVQILRS-QQRLLSTVID 671
Cdd:PRK06669 149 IIEKLIKKREEILESsEEEIVELALD 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-653 |
1.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLE-----ADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRR 528
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 529 LADYDTQIEQLES-ACKAQKETKEDTEKRMQQIDEDAKNAEDCK--------ANDEKEMEELKKEIEMLDNQFKTVR-GE 598
Cdd:PTZ00121 1368 AAEKKKEEAKKKAdAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaaakkkADEAKKKAEEKKKADEAKKKAEEAKkAD 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392890153 599 IVKETSQREQKVAELttleRKEARDQIQMEKLDAAIENTTKLTE---QVSDAVEKSEE 653
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEA----KKKAEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADE 1501
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
456-707 |
1.40e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQ-LAESIQSMlverKTAEEAVLQLEADM-TIKNSSIKNLqvELATLESTVKQLERQKGEATRRLADYD 533
Cdd:PRK11281 75 IDRQKEETEQLKQqLAQAPAKL----RQAQAELEALKDDNdEETRETLSTL--SLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 TQIEQLESAC-KAQKETKEDtEKRMQQIDEDAKNAEDCKandekemeelkkeiemldnqfKTVRgeivkeTSQREQKVAE 612
Cdd:PRK11281 149 SQLVSLQTQPeRAQAALYAN-SQRLQQIRNLLKGGKVGG---------------------KALR------PSQRVLLQAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 613 LTTLErkeardqIQMEKLDAAIENTTKLTE----QVSDAVEKseeemVQILRSQQRLLSTVIDQSLLsddtvygetagTS 688
Cdd:PRK11281 201 QALLN-------AQNDLQRKSLEGNTQLQDllqkQRDYLTAR-----IQRLEHQLQLLQEAINSKRL-----------TL 257
|
250 260
....*....|....*....|.
gi 392890153 689 SQNHVQQP--PDPFASARANP 707
Cdd:PRK11281 258 SEKTVQEAqsQDEAARIQANP 278
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
456-679 |
1.40e-03 |
|
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: 42.34 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 456 KEALEGENEEMKQLAESIQSMLVERK---TAEEAVLQLEADMTI--KNSSIKNLQVElatlestVKQLERQKGEATRRLA 530
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSSDrilELDQELRKAERELSKaeKNSLTETLKKE-------VKSLQNEKADLDRKLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 531 DYDTQIEQLESACKAQKETKEDTEKRMQQiDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIvKETSQREQKV 610
Cdd:TIGR00606 519 KLDQEMEQLNHHTTTRTQMEMLTKDKMDK-DEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI-NQTRDRLAKL 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 611 -AELTTLERKEARDQIQMEKLDaaiENTTKLTEQVSDAVeKSEEEMVQILRSQQRLLSTVIDQSLLSDDT 679
Cdd:TIGR00606 597 nKELASLEQNKNHINNELESKE---EQLSSYEDKLFDVC-GSQDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
454-657 |
1.57e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKqlaESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLE-------------- 519
Cdd:pfam01576 75 EILHELESRLEEEE---ERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEedillledqnskls 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 520 RQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEdckandekemeelkkeiemldnqfkTVRGEI 599
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE-------------------------KGRQEL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392890153 600 VKETSQREqkvAELTTLERKEARDQIQMEKLDAAIentTKLTEQVSDAVEKSEEEMVQ 657
Cdd:pfam01576 207 EKAKRKLE---GESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQ 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-654 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMlVERKTAEEAvlqLEADMTIKNSSIKNLQvELATLESTVKQLERQKGEATR----RL 529
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKA-EEAKKADEA---KKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKnmalRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 530 ADYDTQIEQ--LESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTvrGEIVKETSQRE 607
Cdd:PTZ00121 1583 AEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENK 1660
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392890153 608 QKVAElttLERKEARDQIQMEKLDAAIENTTKLTEQvsdaVEKSEEE 654
Cdd:PTZ00121 1661 IKAAE---EAKKAEEDKKKAEEAKKAEEDEKKAAEA----LKKEAEE 1700
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
479-675 |
1.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 479 ERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQ 558
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 559 QIDEDAKNaedckandekemeelkkeieMLDNQFKTVRGEIVK---ETSQREQKVAELTTLERKEARDQIQMEKLDAAIE 635
Cdd:COG4942 101 AQKEELAE--------------------LLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 392890153 636 NTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSLL 675
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-655 |
2.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 479 ERKtaEEAVLQLEAdmTIKNssIKNLQVELATLESTVKQLERQKGEATR------------------RLADYDTQIEQLE 540
Cdd:TIGR02168 172 ERR--KETERKLER--TREN--LDRLEDILNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 541 SACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEE---------------------LKKEIEMLDNQFKTVRGEI 599
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyalaneisrleqqkqiLRERLANLERQLEELEAQL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392890153 600 VKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEM 655
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
454-743 |
2.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATL-------ESTVKQLER------ 520
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 521 -----QKGEATRRLADYDTQ-IEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANdekemeelkkeiemLDNQFKT 594
Cdd:COG3883 114 fsdflDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE--------------LEAQQAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 595 VRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAientTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSl 674
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA----AAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392890153 675 LSDDTVYGETAGTSSQNHVQQPPDPFASARANPAADPFAQVDQFGSSGHFDAAFPTDPFAQGGFPSDSG 743
Cdd:COG3883 255 AGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVV 323
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
449-653 |
2.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 449 EATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKnlqvelaTLESTVKQLERQKGEATRR 528
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE-------AVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 529 LADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQ 608
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392890153 609 KVAELTTL--ERKEARDQIQmeKLDAAIENttklteqVSDAVEKSEE 653
Cdd:PRK02224 410 AEDFLEELreERDELREREA--ELEATLRT-------ARERVEEAEA 447
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
433-672 |
2.74e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 433 SALHHPAQSVSTPQLPEATSMEIKE----ALEGENEemKQLAESiqSMLveRKTAEEAVLQLEAD---MTIKNSSIKNLq 505
Cdd:pfam10174 91 QLLQQDFTTSPVDGEDKFSTPELTEenfrRLQSEHE--RQAKEL--FLL--RKTLEEMELRIETQkqtLGARDESIKKL- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 506 veLATLEST--VKQLERQKGEATRRLADYDTQIEQLESACkaqketkEDTEKRMQQIDEDAKNAEDCKANDEKEmeelkk 583
Cdd:pfam10174 164 --LEMLQSKglPKKSGEEDWERTRRIAEAEMQLGHLEVLL-------DQKEKENIHLREELHRRNQLQPDPAKT------ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 584 eiemldnqfKTVRGEIvketsqrEQKVAELTTLER--KEARDQIQMEKLDAAIenttklteqvsdAVEKSEEEMVQI--L 659
Cdd:pfam10174 229 ---------KALQTVI-------EMKDTKISSLERniRDLEDEVQMLKTNGLL------------HTEDREEEIKQMevY 280
|
250
....*....|...
gi 392890153 660 RSQQRLLSTVIDQ 672
Cdd:pfam10174 281 KSHSKFMKNKIDQ 293
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
457-717 |
2.90e-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: 41.31 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 457 EALEGENEEMkQLAESIQSMLVERKTAEEAVLQLEADM----TIKNSSIKNlqvelatlestVKQLERQKGEATRRLADY 532
Cdd:pfam01576 630 EAREKETRAL-SLARALEEALEAKEELERTNKQLRAEMedlvSSKDDVGKN-----------VHELERSKRALEQQVEEM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 533 DTQIEQLESACKAQKETKEDTEKRMQQIdeDAKNAEDCKANDEKEMEELKKeiemLDNQFKTVRGEIVKETSQREQKVAE 612
Cdd:pfam01576 698 KTQLEELEDELQATEDAKLRLEVNMQAL--KAQFERDLQARDEQGEEKRRQ----LVKQVRELEAELEDERKQRAQAVAA 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 613 LTTLER--KEARDQIQM--EKLDAAIENTTKLTEQVSD------AVEKSEEEMVQILRSQQRLLSTVIDQSL-LSDDTVY 681
Cdd:pfam01576 772 KKKLELdlKELEAQIDAanKGREEAVKQLKKLQAQMKDlqreleEARASRDEILAQSKESEKKLKNLEAELLqLQEDLAA 851
|
250 260 270
....*....|....*....|....*....|....*.
gi 392890153 682 GETAgtssQNHVQQPPDPFASARANPAADPFAQVDQ 717
Cdd:pfam01576 852 SERA----RRQAQQERDELADEIASGASGKSALQDE 883
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
454-665 |
3.30e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLeadmtikNSSIKNLQVELATLESTVKQLERQKGEATRRLADYD 533
Cdd:COG1340 40 ELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-------KEERDELNEKLNELREELDELRKELAELNKAGGSID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 534 T---QIEQLEsacKAQkETKE---DTEKR-MQQIDEDAKNAEDCKANDEkemeelkkeiemLDNQFKTVRGEIVKETSQR 606
Cdd:COG1340 113 KlrkEIERLE---WRQ-QTEVlspEEEKElVEKIKELEKELEKAKKALE------------KNEKLKELRAELKELRKEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392890153 607 E---QKVAELTTlERKEARDQI-----QMEKLDAAIEnttKLTEQVSDAVEKSEEEMVQILRSQQRL 665
Cdd:COG1340 177 EeihKKIKELAE-EAQELHEEMielykEADELRKEAD---ELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
454-569 |
4.18e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIK----------NSSIKNLQVELATLESTVKQLERQKG 523
Cdd:pfam05667 346 DLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKkktldllpdaEENIAKLQALVDASAQRLVELAGQWE 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392890153 524 EATRRLADydtQIEQLESACKAQK-ETKEDTEK------RMQQIDEDAKNAED 569
Cdd:pfam05667 426 KHRVPLIE---EYRALKEAKSNKEdESQRKLEEikelreKIKEVAEEAKQKEE 475
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
454-664 |
4.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENE-EMKQLAESIQSMLVERKTAEEAVLQLE----ADMTIKNSSIKNLQVELA--TLESTVKQLERQKGEAT 526
Cdd:PTZ00121 1429 EKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEeakkADEAKKKAEEAKKADEAKkkAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 527 RRLADYDTQIEQ---LESACKAQKETKEDTEKRMQQID--EDAKNAEDCKANDEKEMEELKKEIEMlDNQFKTVRGEIVK 601
Cdd:PTZ00121 1509 KKKADEAKKAEEakkADEAKKAEEAKKADEAKKAEEKKkaDELKKAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 602 ETSQ-REQKVAELTTLE--------RKEARDQIQMEKLDAAIENTTKLT-------EQVSDAVE-KSEEEMVQILRSQQR 664
Cdd:PTZ00121 1588 KAEEaRIEEVMKLYEEEkkmkaeeaKKAEEAKIKAEELKKAEEEKKKVEqlkkkeaEEKKKAEElKKAEEENKIKAAEEA 1667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
431-689 |
5.82e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 431 EPSALHHPAQSVSTPQLPEATSMEIK-EALEGENEEMKQLAESIQSMLVERKTAEEaVLQLEADMTIKNSSIKNLQVELA 509
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEDK 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 510 TLESTVKQLE---RQKGEATRRLADYDTQIEQL----ESACKAQKETKEDTEKRMQQIDEDAKNAEDckanDEKEMEELK 582
Cdd:PTZ00121 1675 KKAEEAKKAEedeKKAAEALKKEAEEAKKAEELkkkeAEEKKKAEELKKAEEENKIKAEEAKKEAEE----DKKKAEEAK 1750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 583 KEIEMLDNQFKTVRGEIVKETSQREQKVAELTT-LERKEARDQIQMEK--------LDAAIENTTKLTEQVSDA--VEKS 651
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKkikdifdnFANIIEGGKEGNLVINDSkeMEDS 1830
|
250 260 270
....*....|....*....|....*....|....*...
gi 392890153 652 EEEMVQILRSQQRLLSTVIDQSLLSDDTVYGETAGTSS 689
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
454-659 |
6.87e-03 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 39.15 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 454 EIKEALEGENEEMKQLAESIQSMlvERKTAEEAVLQLEADMTIKN---SSIKNLQvelatlestvkqlERQKGEATRRLA 530
Cdd:pfam06705 24 EIEVKRVDEDTRVKMIKEAIAHL--EKLIQTESKKRQESFEDIQEefkKEIDNMQ-------------ETIKEEIDDMAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 531 DYDTQIEQL-ESACKAQKETKEDTEKRMQQIDEDAKNA----EDCKANDEKEMEELKKEIEMLDNQ----FKTVRGEIVK 601
Cdd:pfam06705 89 NFRKALAELnDTINNVETNLQNEIAIHNDAIEALRKEAlkslNDLETGIATENAERKKMYDQLNKKvaegFARISAAIDT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392890153 602 ETSQREQKVAELTT------LERKEARDQIQMEKLD--AAIENTTKLTEQvsdAVEKSEEEMVQIL 659
Cdd:pfam06705 169 EKNARDSAVSAATTeltntkLVEKCVNEQFENAVLSeiAAIKEELDREKA---ERKAADDKIVQAV 231
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
423-542 |
8.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 423 PPSFRPPTEPSALHHPAQsvstpqlpeATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIK 502
Cdd:PRK11448 131 PGPFVPPEDPENLLHALQ---------QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 392890153 503 NLQVELATLESTVKQLERQKG-----------EATRRLADydtqiEQLESA 542
Cdd:PRK11448 202 QLQEKAAETSQERKQKRKEITdqaakrlelseEETRILID-----QQLRKA 247
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
437-665 |
9.30e-03 |
|
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: 39.64 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 437 HPAQSVSTPQLPEATSMEIKEALEGENEEMKQLAESIQSMLV-------ERKTAEEAVLQLEADMtiKNSSIKNLQVELA 509
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSkimkldnEIKALKSRKKQMEKDN--SELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 510 TlESTVKQLERQKG----EATRRLADYDTQIEQL--ESACKAQKETKEDTEKRMQQIDEDaKNAEDCKANDEKEMEELKK 583
Cdd:TIGR00606 299 T-DEQLNDLYHNHQrtvrEKERELVDCQRELEKLnkERRLLNQEKTELLVEQGRLQLQAD-RHQEHIRARDSLIQSLATR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392890153 584 EI-------EMLDNQFKTVRgEIVKETSQREQKVAE--LTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEE 654
Cdd:TIGR00606 377 LEldgfergPFSERQIKNFH-TLVIERQEDEAKTAAqlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE 455
|
250
....*....|.
gi 392890153 655 MVQILRSQQRL 665
Cdd:TIGR00606 456 LKFVIKELQQL 466
|
|
| |
