|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
120-213 |
1.36e-39 |
|
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: 141.26 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 120 WAVRPEEKSKFDGIFESLAP-VNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 198
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1207195109 199 VPSVLPSSLIPPSKR 213
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
270-366 |
5.13e-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: 128.16 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 270 NWVVPVADRGRYDDIFLKTDSDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSkG 349
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 1207195109 350 LDPPQALTPDMIPPSER 366
Cdd:smart00027 80 YPIPASLPPSLIPPSKR 96
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
124-213 |
1.70e-26 |
|
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: 104.38 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 124 PEEKSKFDGIFESLAPVNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPS 201
Cdd:pfam12763 6 EWEIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPD 85
|
90
....*....|..
gi 1207195109 202 VLPSSLIPPSKR 213
Cdd:pfam12763 86 ELPDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
130-195 |
4.62e-25 |
|
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: 98.83 E-value: 4.62e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 130 FDGIFESLAPVN-GLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 195
Cdd:cd00052 1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
281-347 |
3.89e-24 |
|
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: 96.13 E-value: 3.89e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 281 YDDIFLKTDSDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVS 347
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
11-101 |
1.78e-23 |
|
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: 95.42 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 11 SSGNPVYENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQSGHDISIS 90
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1207195109 91 SLNLPVPPPKF 101
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
17-83 |
3.07e-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: 90.74 E-value: 3.07e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 17 YENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQS 83
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
418-604 |
1.52e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180
....*....|....*....|....*...
gi 1207195109 577 TQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
411-595 |
2.55e-20 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 93.81 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 411 TGIKELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:COG4372 35 KALFELDKLQEELEQLREELE-----------QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagRIQLETI 570
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEA 181
|
170 180
....*....|....*....|....*
gi 1207195109 571 IKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAE 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-611 |
1.51e-19 |
|
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: 94.35 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTH--WDTLREK-YTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEkaLAELRKElEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207195109 571 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-610 |
1.74e-18 |
|
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: 91.27 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190
....*....|....*....|....*....|....
gi 1207195109 577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
448-606 |
3.84e-18 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 87.26 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 448 IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHS 527
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 528 QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-604 |
7.00e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196 267 AELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 573
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190
....*....|....*....|....*....|.
gi 1207195109 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-604 |
1.02e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 573
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190
....*....|....*....|....*....|.
gi 1207195109 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
415-604 |
1.80e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:COG1196 275 ELEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSL 574
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190
....*....|....*....|....*....|
gi 1207195109 575 KATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
414-604 |
4.28e-16 |
|
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: 80.96 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEm 493
Cdd:COG4942 27 AELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 dqQKAKLEDMLN-----------DVRQKCQEESQMISSLQ-------------TQIHSQESDLQSQEEELGRAKADLNRL 549
Cdd:COG4942 102 --QKEELAELLRalyrlgrqpplALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 550 QQEEAQLEQSLQAGRIQLETIIKSLKAtqdEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
443-632 |
1.41e-15 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 79.56 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 523 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIqdSQHEISKNI 602
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL--SEAEAEQAL 185
|
170 180 190
....*....|....*....|....*....|
gi 1207195109 603 EQYSSTLNGTHGGSMTNLADMSEGFPEKEN 632
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-604 |
1.43e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 385 AALTEMRRAIMfKLWDSSSSVGSGEFTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE 464
Cdd:COG1196 267 AELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 465 MQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 545 DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-631 |
2.64e-15 |
|
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: 80.87 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:TIGR02168 239 EELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADL----NRLQQEEAQLEQsLQAGRIQLEt 569
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeeleSRLEELEEQLET-LRSKVAQLE- 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 570 iiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLngthggSMTNLADMSEGFPEKE 631
Cdd:TIGR02168 393 --LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL------EEAELKELQAELEELE 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-609 |
4.90e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.43 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAftHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQDAQDR 489
Cdd:COG4717 70 LKELKELEEELKEAEEKEE--EYAELQEELeELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDL-QSQEEELGRAKADLNRLQQEEAQLEQslqagriqle 568
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEE---------- 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195109 569 tiikSLKATQDEINQARSKLSQIQDSQ--HEISKNIEQYSSTL 609
Cdd:COG4717 214 ----ELEEAQEELEELEEELEQLENELeaAALEERLKEARLLL 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
444-588 |
1.37e-14 |
|
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: 74.19 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-----QKCQEEsqmI 518
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKE---I 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 519 SSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 588
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-604 |
4.21e-14 |
|
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: 77.02 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTH--WDTLR-EKYTLEQDIRETEEA-------IRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEekLEELRlEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195109 564 RIQLETIIKSLKATQDEINQARSKLS--QIQDSQHEISKNIEQ 604
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEE 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
413-606 |
8.14e-14 |
|
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: 75.87 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEE 492
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 569
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiQELQEQRIDLKE 847
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195109 570 IIKSLKATQDEIN-QARSKLSQIQDSQHEISKNIEQYS 606
Cdd:TIGR02169 848 QIKSIEKEIENLNgKKEELEEELEELEAALRDLESRLG 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
406-610 |
2.08e-13 |
|
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: 74.72 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 406 GSGEFTGIKE-LDDISQEIAQLQSTLAFTHW---DTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 481
Cdd:TIGR02169 285 GEEEQLRVKEkIGELEAEIASLERSIAEKEReleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 482 QKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLq 561
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195109 562 agriqletiikslKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02169 444 -------------EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-602 |
1.34e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQE-------LEAQKQDA 486
Cdd:TIGR02168 719 KELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeieeLEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207195109 567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNI 602
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-604 |
1.77e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAftHWDTLREKYTLEQDIRETEEAIRHKT--TEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:COG4913 242 EALEDAREQIELLEPIRE--LAERYAAARERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 EMDQQKAKLEdmlndvRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ----L 567
Cdd:COG4913 320 ALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalL 393
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207195109 568 ETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-604 |
3.02e-12 |
|
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: 70.43 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKakledmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKS 573
Cdd:TIGR04523 390 ESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV----KELIIKN 458
|
170 180 190
....*....|....*....|....*....|.
gi 1207195109 574 LKATQDEINQarsKLSQIQDSQHEISKNIEQ 604
Cdd:TIGR04523 459 LDNTRESLET---QLKVLSRSINKIKQNLEQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-604 |
1.76e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQ-DRLE 491
Cdd:COG4913 262 ERYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETII 571
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 572 KSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-604 |
2.89e-11 |
|
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: 67.40 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAIRHKTTE----VQEMQNDLDRETSSLQELEAQKQDAQD 488
Cdd:TIGR02169 244 RQLASLEEELEKLTEEI-----SELEKRLeEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 489 RLEEmDQQKAKLEdmlndvRQKCQEEsqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE 568
Cdd:TIGR02169 319 DAEE-RLAKLEAE------IDKLLAE---IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207195109 569 TIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
413-593 |
3.08e-11 |
|
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: 67.35 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQStlafthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR04523 376 KKENQSYKQEIKNLES-----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 572
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKIS 520
|
170 180
....*....|....*....|....*
gi 1207195109 573 SLKATQD----EINQARSKLSQIQD 593
Cdd:TIGR04523 521 SLKEKIEklesEKKEKESKISDLED 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
431-605 |
3.17e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 431 AFTHWDT--LREKYTLEQDireTEEAIRHKTTEVQEMQNDLdretsslQELEAQKQDAQDRLEEMDQQKAKLEDMLNDvr 508
Cdd:COG4913 589 RHEKDDRrrIRSRYVLGFD---NRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEY-- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 509 qkcQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 588
Cdd:COG4913 657 ---SWDEIDVASAEREI----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170
....*....|....*..
gi 1207195109 589 SQIQDSQHEISKNIEQY 605
Cdd:COG4913 730 DELQDRLEAAEDLARLE 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
444-603 |
4.26e-11 |
|
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: 66.58 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 524 QIH------SQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQLET-------IIKSLKATQDEINQARSKLSQ 590
Cdd:TIGR04523 209 KIQknksleSQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNQlkdeqnkIKKQLSEKQKELEQNNKKIKE 285
|
170
....*....|...
gi 1207195109 591 IQDSQHEISKNIE 603
Cdd:TIGR04523 286 LEKQLNQLKSEIS 298
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
413-592 |
4.65e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.58 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIRETEEAIR--HKTTEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG3206 218 LQQLSELESQLAEARAELA-----EAEARLaALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQTQI---HSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG3206 293 VIALRAQIAALRAQLQ------QEAQRILASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
170 180
....*....|....*....|....*.
gi 1207195109 567 LETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:COG3206 367 YESLLQRLEEARLAEALTVGNVRVID 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-562 |
6.48e-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: 63.41 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK--QDAQDRLE 491
Cdd:COG1579 31 AELAELEDELAALEARLE-----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQA 562
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
413-608 |
7.76e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLafthwDTLREKY--------TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQE------ 478
Cdd:COG3883 29 QAELEAAQAELDALQAEL-----EELNEEYnelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 479 -----LEAQK-QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE 552
Cdd:COG3883 104 yldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 553 EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSST 608
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-595 |
8.37e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196 323 EELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH---SQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAeleEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180
....*....|....*....|....*
gi 1207195109 571 IKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAE 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
415-614 |
9.78e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqelEAQKQDAQDRLEEMD 494
Cdd:PRK02224 252 ELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakadlnrLQQEEAQLEQSLQAGRIQLETIIKSL 574
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEE----------LREEAAELESELEEAREAVEDRREEI 386
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207195109 575 KATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHG 614
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
445-595 |
1.33e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE-SQMISS 520
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 521 LQTQ------------------------------------IHSQESD---LQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG3883 95 LYRSggsvsyldvllgsesfsdfldrlsalskiadadadlLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|....
gi 1207195109 562 AGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
414-599 |
2.75e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE-- 491
Cdd:COG3206 182 EQLPELRKELEEAEAAL---------EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 --------------EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEE-LGRAKADLNRLQQEEAQL 556
Cdd:COG3206 253 pdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 557 EQSLQagriQLETIIKSLKATQDEINQ-------ARSKLSQIQDSQHEIS 599
Cdd:COG3206 333 QAQLA----QLEARLAELPELEAELRRlerevevARELYESLLQRLEEAR 378
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
414-610 |
3.01e-10 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 62.63 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAirhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRL- 490
Cdd:pfam00038 61 RQLDTLTVERARLQLELdnLRLAAEDFRQKYEDELNLRTSAEN------DLVGLRKDLDEATLARVDLEAKIESLKEELa 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 -------EEMDQQKAKLED-----------------MLNDVR-------QKCQEESQM-----ISSLQTQIHSQESDLQS 534
Cdd:pfam00038 135 flkknheEEVRELQAQVSDtqvnvemdaarkldltsALAEIRaqyeeiaAKNREEAEEwyqskLEELQQAAARNGDALRS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 535 QEEELgrakADLNR-LQQEEAQLeQSLQAGRIQLETIIKSLKATQD-EINQARSKLS----QIQDSQHEISKNIEQYSST 608
Cdd:pfam00038 215 AKEEI----TELRRtIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQEL 289
|
..
gi 1207195109 609 LN 610
Cdd:pfam00038 290 LN 291
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-604 |
3.13e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 466 QNDLDRETSS-LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:COG4942 18 QADAAAEAEAeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 545 DLNRLQQEEAQL-------------------EQSLQAGRI---------QLETIIKSLKATQDEINQARSKLSQIQDSQH 596
Cdd:COG4942 98 ELEAQKEELAELlralyrlgrqpplalllspEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
|
....*...
gi 1207195109 597 EISKNIEQ 604
Cdd:COG4942 178 ALLAELEE 185
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
416-604 |
3.98e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEI-AQL-----QSTLAfthwdtlrEKYtleQDIRETEEAIrhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG1196 191 LEDILGELeRQLeplerQAEKA--------ERY---RELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAdlnRLQQEEAQLEQSLQagriQLET 569
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEE----ELAE 327
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195109 570 IIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
435-604 |
4.18e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 435 WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEeMDQQKAKLEDmLNDVRQKCQEE 514
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAE-LEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 515 SQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170
....*....|
gi 1207195109 595 QHEISKNIEQ 604
Cdd:COG4913 764 ERELRENLEE 773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-564 |
4.87e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 410 FTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRhkTTEVQEMQNDLDRetssLQELEAQKQDAQDR 489
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELA----RLEAELERLEARLDALREELD--ELEAQIRGNGGDR----LEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQ----EEELGRAKADLNRLQQEEAQLEQ---SLQA 562
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEElealEEALAEAEAALRDLRRELRELEAeiaSLER 433
|
..
gi 1207195109 563 GR 564
Cdd:COG4913 434 RK 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
414-595 |
5.22e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.15 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE----MQND-------------------LD 470
Cdd:COG3883 44 AELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGEraraLYRSggsvsyldvllgsesfsdfLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 471 RETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN 547
Cdd:COG3883 120 RLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195109 548 RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
476-604 |
7.07e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 60.32 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 476 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---------DL 546
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEY 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 547 NRLQQEEA-------QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1579 92 EALQKEIEslkrrisDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
414-597 |
8.20e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.77 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG3883 23 KELSELQAELEAAQAELD-----------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 --DQQKA-----KLEDMLNdvrqkcqeeSQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAG 563
Cdd:COG3883 92 arALYRSggsvsYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEaklAELEAL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1207195109 564 RIQLETIIKSLKATQDEINQARSKLSQIQDSQHE 597
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-605 |
9.21e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL-- 490
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEE-----KLKERLEeLEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsh 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 ----------EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQES---DLQSQEEELGRAKADLN---------- 547
Cdd:TIGR02169 791 sripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNgkkeeleeel 870
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 548 -RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ-------ARSKLSQIQDSQHEISKNIEQY 605
Cdd:TIGR02169 871 eELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqiekKRKRLSELKAKLEALEEELSEI 936
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
414-604 |
1.07e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQnDLDRETSSLQE-------LEAQKQDA 486
Cdd:PRK03918 231 KELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEkaeeyikLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQM------ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEqSL 560
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKeerleeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-GL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207195109 561 QAGRI--QLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK03918 385 TPEKLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
440-631 |
1.09e-09 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 60.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaQKQDAQDRLEEmdqQKAKLEDMLNDVRQKCQEESQMIS 519
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSRE---QLQELEEQLAT---ERSARREAEAELERLQEELRYLEE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 520 SLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQagriQL-ETIIKS---LKATQDEINQARSKL---- 588
Cdd:pfam09787 129 ELRRSKATLQSRIKDREAEIEKLRNQLTSKSQsssSQSELENRLH----QLtETLIQKqtmLEALSTEKNSLVLQLerme 204
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195109 589 SQIQDSQHEISKNIeqySSTLNGTHGGSMTNLADMSEGFPEKE 631
Cdd:pfam09787 205 QQIKELQGEGSNGT---SINMEGISDGEGTRLRNVPGLFSESD 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
481-610 |
1.19e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 560
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 561 QAGRIQLETIIKS-----------LKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4942 100 EAQKEELAELLRAlyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
422-600 |
1.51e-09 |
|
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: 61.68 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 422 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 501
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 502 DMLNDVRQKCQEES---QMISSLQTQIHSQESDlqsqEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETIIKSLKATQ 578
Cdd:pfam05557 153 QLRQNLEKQQSSLAeaeQRIKELEFEIQSQEQD----SEIVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLK 227
|
170 180
....*....|....*....|..
gi 1207195109 579 DEINQARSKLSQIQDSQHEISK 600
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAAT 249
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
413-609 |
1.86e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQDiRETEEAIRHKTTEVQEM---QNDLDRETSSLQELEAQKQDAQDR 489
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALH-------ALQLTLTQE-RVREHALSIRVLPKELLasrQLALQKMQSEKEQLTYWKEMLAQC 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI-----------HSQESDLQSQEEELGRAK----ADLNRLQqEEA 554
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdalnqslkelmHQARTVLKARTEAHFNNNeevtAALQTGA-ELS 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 555 QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSSTL 609
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRL 837
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-609 |
2.42e-09 |
|
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: 61.19 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQST------------LAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 481
Cdd:TIGR04523 426 KEIERLKETIIKNNSEikdltnqdsvkeLIIKNLDNTRES--LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 482 QKQDAQDRLEEMDQQKAKLEdmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA--KADLNRLQQEEAQLEQS 559
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLK-------EKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQT 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 560 lqagriqletiIKSLKATQDEINQarsKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:TIGR04523 577 -----------QKSLKKKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKI 612
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
415-592 |
2.43e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLA-----FTHWDTLREKYTLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG4913 625 ELAEAEERLEALEAELDalqerREALQRLAEYSWDEIDVASAEREIA----ELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqlet 569
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE-------- 772
|
170 180
....*....|....*....|...
gi 1207195109 570 iiKSLKATQDEINQARSKLSQIQ 592
Cdd:COG4913 773 --ERIDALRARLNRAEEELERAM 793
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
426-613 |
2.76e-09 |
|
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: 61.24 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 426 LQSTLAFTHWDTLRE---KY---TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 499
Cdd:TIGR02169 620 FGDTLVVEDIEAARRlmgKYrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 500 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqleTIIKSLKATQD 579
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-------ELEARIEELEE 772
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195109 580 EINQARSKLSQIQDS-QHEISKNIEQYSSTLNGTH 613
Cdd:TIGR02169 773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEV 807
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
468-610 |
2.77e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 468 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-RAKA-- 544
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeRARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 545 --------------------------DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEI 598
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA---EL 173
|
170
....*....|..
gi 1207195109 599 SKNIEQYSSTLN 610
Cdd:COG3883 174 EAQQAEQEALLA 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
476-611 |
3.39e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 476 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqesDLQSQEEELGRAKADLNRLQQEEAQ 555
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 556 LEQsLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:COG4913 687 LAA-LEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
414-589 |
4.08e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.91 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEM 493
Cdd:pfam07888 104 KELSASSEELSEEKDAL-------LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKS 573
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQER 245
|
170
....*....|....*.
gi 1207195109 574 LKATQDEINQARSKLS 589
Cdd:pfam07888 246 LNASERKVEGLGEELS 261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-603 |
4.25e-09 |
|
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: 60.42 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwdtlrEKytLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqELEAQKQDAQDRLEEM 493
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI---------EK--LESEKKEKESKISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEEL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqLETIIKS 573
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQE 646
|
170 180 190
....*....|....*....|....*....|....
gi 1207195109 574 LKATQDEINQARSKLSQI----QDSQHEISKNIE 603
Cdd:TIGR04523 647 VKQIKETIKEIRNKWPEIikkiKESKTKIDDIIE 680
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
488-604 |
4.35e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.53 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 DRLEEMDQqKAKLEdmLNDVRQKcqeESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE----EAQLEQS---L 560
Cdd:COG4372 2 DRLGEKVG-KARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207195109 561 QAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-604 |
5.50e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQT 523
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 524 QIHSQESDLQ-------------------SQEE--ELGR--------AKADLNRLQQEEAQLEQsLQAGRIQLETIIKSL 574
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplalllSPEDflDAVRrlqylkylAPARREQAEELRADLAE-LAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1207195109 575 KATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
445-643 |
6.01e-09 |
|
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: 60.06 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------------RLEEMD----QQKAKLEDM---- 503
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtimerfqmELKDVErkiaQQAAKLQGSdldr 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 504 -LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ-AGRI--QLETIIKSLKATQD 579
Cdd:TIGR00606 823 tVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrRQQFeeQLVELSTEVQSLIR 902
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 580 EINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKenggFGAMEDPFK 643
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI----HGYMKDIEN 962
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
441-610 |
9.29e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 441 KYTLEQDIRETEEAIRHKTTEVQEMQNDLD---------RETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKc 511
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 512 qeesqmISSLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQEEAQLEQSLQAG-------RIQLETIIKSLKATQDEI- 581
Cdd:COG3206 242 ------LAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRIl 315
|
170 180
....*....|....*....|....*....
gi 1207195109 582 NQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
416-613 |
9.37e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQ 495
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 496 QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEelgRAKADLNRLQQEEAQLEQsLQAGRIQLETIIKSLK 575
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQRKEEEAERKQ-LQAKLQQTEEELRSLS 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195109 576 AtqdEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 613
Cdd:pfam07888 192 K---EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
414-605 |
1.39e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR---ETSSLQE-----------L 479
Cdd:COG4372 52 EELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAELAQAQEELESlqeEAEELQEeleelqkerqdL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 480 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEElgRAKADLNRLQQEEAQLEQS 559
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEK 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207195109 560 LQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-625 |
1.46e-08 |
|
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: 58.65 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLA-----FTHWDTLREKYtlEQDIRETEEAIRHKTTEVQEMQN---DLDRETSSLQEleaQKQD 485
Cdd:pfam01576 152 KERKLLEERISEFTSNLAeeeekAKSLSKLKNKH--EAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQE---QIAE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 486 AQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 566 QLETIIKSlKATQDEINQAR-SKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:pfam01576 307 ELEDTLDT-TAAQQELRSKReQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLE 366
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
421-640 |
1.48e-08 |
|
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: 58.65 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 421 QEIAQLQSTLAfthwdtlREKYTLEQDIRETEEaiRHkTTEVQEMQNDLD---RETSSL----QELEAQKQDAQDRLE-- 491
Cdd:pfam01576 327 QEVTELKKALE-------EETRSHEAQLQEMRQ--KH-TQALEELTEQLEqakRNKANLekakQALESENAELQAELRtl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 -----EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR-- 564
Cdd:pfam01576 397 qqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQel 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 565 IQLETIIK-----SLKATQDEinqaRSKLSQIQDSQHEISKNIEQYSSTLNgthggsmTNLADMSEGFpEKENGGFGAME 639
Cdd:pfam01576 477 LQEETRQKlnlstRLRQLEDE----RNSLQEQLEEEEEAKRNVERQLSTLQ-------AQLSDMKKKL-EEDAGTLEALE 544
|
.
gi 1207195109 640 D 640
Cdd:pfam01576 545 E 545
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
414-612 |
1.56e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLqstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMqNDLDRETSS-----LQELEAQKQDaqD 488
Cdd:PRK02224 579 SKLAELKERIESL---------ERIRTLLAAIADAEDEIERLREKREALAEL-NDERRERLAekrerKRELEAEFDE--A 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 489 RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelgrakadLNRLQQEEAQLEQSLQAgriqLE 568
Cdd:PRK02224 647 RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-----------LEELRERREALENRVEA----LE 711
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195109 569 TIIKSLKATQDEINQARSKLSQiqdsqheisKNIEQYSSTLNGT 612
Cdd:PRK02224 712 ALYDEAEELESMYGDLRAELRQ---------RNVETLERMLNET 746
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
414-604 |
1.66e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 57.94 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdtlrekytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:pfam06160 237 KEIQQLEEQLEENLALLE-------------NLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQ---EESQMISSLQTQIHSQESDLQSQEEELGRAKAD----LNRLQQEEAQLEQsLQAgriQ 566
Cdd:pfam06160 304 EEQNKELKEELERVQQSYTlneNELERVRGLEKQLEELEKRYDEIVERLEEKEVAyselQEELEEILEQLEE-IEE---E 379
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195109 567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-592 |
2.00e-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: 58.14 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 446 QDI-RETEEAIRH------KTTEVQEMQNDLdrETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMI 518
Cdd:TIGR02168 192 EDIlNELERQLKSlerqaeKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 519 SSLQTQIHSQESDLQSQEEELGRAKADLNRL-------QQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
.
gi 1207195109 592 Q 592
Cdd:TIGR02168 350 K 350
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-591 |
2.63e-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: 57.76 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAF---------THWDTLREKYTLEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESlaaeieeleELIEELESELEALLNERASLEEALALLrSELEELSEELRELESKRSELRREL 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQDRLEEMDQQKAKLEdmlndvrqkcqeesQMISSLQTQIHSQESD-LQSQEEELGRAKADLNRLQQEEAQLEQSLQA 562
Cdd:TIGR02168 918 EELREKLAQLELRLEGLE--------------VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195109 563 -GRIQLETI--IKSLK------ATQDE-INQARSKLSQI 591
Cdd:TIGR02168 984 lGPVNLAAIeeYEELKerydflTAQKEdLTEAKETLEEA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
415-561 |
3.32e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAFTHWDTLREKYT-------LEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQD 485
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEqaeeyqeLKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEE 443
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 486 AQDRLEEMDQQKAKLEDMLNDVrqkcqEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG4717 444 LEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
430-605 |
3.50e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 430 LAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR-------ETSSLQELEAQKQDAQDRLEEMDQQKAKLE- 501
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQl 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 502 ----------------DMLNDVRQKCQEESQMISsLQTQIHSQESDLQSQEEELGR--AKADLNRLQQEEAQLEQSLQAG 563
Cdd:COG4717 366 eeleqeiaallaeagvEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEEL 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195109 564 RIQLETIIKSLKATQDEINQARS--KLSQIQDSQHEISKNIEQY 605
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
440-601 |
3.59e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 54.76 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQ 516
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 517 MISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQAGRIQLETI------------IKSLKATQDEI 581
Cdd:cd00176 76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEdlgkdlesveelLKKHKELEEEL 155
|
170 180
....*....|....*....|
gi 1207195109 582 NQARSKLSQIQDSQHEISKN 601
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEE 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
414-570 |
4.23e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEiAQLQstlAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDR 489
Cdd:PRK12704 49 KEAEAIKKE-ALLE---AKEEIHKLRNE--FEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLET 569
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQA 197
|
.
gi 1207195109 570 I 570
Cdd:PRK12704 198 I 198
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
444-604 |
4.72e-08 |
|
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: 56.67 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE----------EMDQQKAKLED----MLNDVRQ 509
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAeaeealreqaELNRLKKKYLEalnkKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 510 KCQEESQMISSL-------QTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDEIN 582
Cdd:pfam05557 98 QLADAREVISCLknelselRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQSSLAEAEQRIK 173
|
170 180
....*....|....*....|...
gi 1207195109 583 QARSKL-SQIQDSqhEISKNIEQ 604
Cdd:pfam05557 174 ELEFEIqSQEQDS--EIVKNSKS 194
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
421-593 |
4.90e-08 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 54.61 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 421 QEIAQLQSTLAFthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlQELEAQKQDAQDRLEEMDQQKAKL 500
Cdd:pfam12795 17 KLLQDLQQALSL-----LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAK-AEAAPKEILASLSLEELEQRLLQT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 501 EDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADL-NRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 579
Cdd:pfam12795 91 SAQLQELQNQLAQLNSQLIELQTRP----ERAQQQLSEARQRLQQIrNRLNGPAPPGEPLSEAQRWALQAELAALKAQID 166
|
170
....*....|....
gi 1207195109 580 EINQARSKLSQIQD 593
Cdd:pfam12795 167 MLEQELLSNNNRQD 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-553 |
5.54e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHW----------DTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDelkdyrekleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEE 553
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-609 |
5.93e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAFTHWDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDR---- 489
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksi 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 ----------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQ-------QE 552
Cdd:TIGR02169 853 ekeienlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEE 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 553 EAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQIQdsqheiSKNIEQYSSTL 609
Cdd:TIGR02169 933 LSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVN------MLAIQEYEEVL 985
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-551 |
6.66e-08 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.40 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE---SQM 517
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkDRE 466
|
90 100 110
....*....|....*....|....*....|....
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ 551
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
409-592 |
7.26e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 409 EFTGIKE-LDDISQEIAQLQstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRET-SSLQELEAQKQ-- 484
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLK--------KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKel 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 485 -----------DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQ--EEELGRAKADLNRLQQ 551
Cdd:PRK03918 598 epfyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----EELEKKysEEEYEELREEYLELSR 673
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195109 552 EEAQLEQSLQAGRIQLETIIKS---LKATQDEINQARSKLSQIQ 592
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-610 |
8.18e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLA--FTHWDTL-REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQD---AQ 487
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEklNNKYNDLkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakaDLNRLQQEEAQLEQS------LQ 561
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL----NQLKDEQNK------IKKQLSEKQKELEQNnkkikeLE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 562 AGRIQLETIIKSLK--ATQDEINQARSKLS----QIQDSQHEISKNIEQYSStLN 610
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNKELKSELKnqekKLEEIQNQISQNNKIISQ-LN 341
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
415-596 |
8.77e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIA----QLQSTLAFTHwdtLREK-YTLEQDI------RETEEAIrhkttEVQEMQNDLDRETSSLQELEAQK 483
Cdd:pfam15921 364 ERDQFSQESGnlddQLQKLLADLH---KREKeLSLEKEQnkrlwdRDTGNSI-----TIDHLRRELDDRNMEVQRLEALL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQDRLE-EMDQQKAKLedmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQA 562
Cdd:pfam15921 436 KAMKSECQgQMERQMAAI--------QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195109 563 GRiqletiiKSLKATQDEINQARSKLS-QIQDSQH 596
Cdd:pfam15921 508 KE-------RAIEATNAEITKLRSRVDlKLQELQH 535
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
413-592 |
9.27e-08 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 53.84 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:pfam12795 29 LDKIDASKQRAAAYQKALddAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 --------------EEMDQQKAKLEDMLN--DVRQKCQEESQM------ISSLQTQIHSQESDLQS--QEEELGRAKADL 546
Cdd:pfam12795 109 ielqtrperaqqqlSEARQRLQQIRNRLNgpAPPGEPLSEAQRwalqaeLAALKAQIDMLEQELLSnnNRQDLLKARRDL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 547 --NRLQQEEAQLE--QSLQAGRIQLETiIKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam12795 189 ltLRIQRLEQQLQalQELLNEKRLQEA-EQAVAQTEQLAEEAAGDHPLVQ 237
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
391-609 |
9.49e-08 |
|
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: 55.88 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 391 RRAIMFKLWDSSSSVGSGEFTGIKELDDISQEIAQL--QST--------LAF------THWDTLREKYTLE-QDIRETEE 453
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliQITekenkmkdLTFlleesrDKANQLEEKTKLQdENLKELIE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 454 AIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-----------QDRLEEMDQQKA--------------KLEDMLNDVR 508
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAahsfvvtefeattcSLEELLRTEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 509 QKCQEESQMISSLQTQIHSQESDLQS----------QEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQ 578
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449
|
250 260 270
....*....|....*....|....*....|.
gi 1207195109 579 DEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
414-590 |
9.90e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLA-FTHWDT-LREKYTLEQDIRET---EEAIRHKTTEVQEMQNDLDRETSSLQELEAQK----- 483
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAyLTQKREaQEEQLKKQQLLKQLrarIEELRAQEAVLEETQERINRARKAAPLAAHIKavtqi 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 -QDAQDRLEEMDQQKAKLEDMLNDVR--QKCQEESQMISSLQTQIHSQESDLQSQ-------EEELGRAKADLNRLQQEE 553
Cdd:TIGR00618 306 eQQAQRIHTELQSKMRSRAKLLMKRAahVKQQSSIEEQRRLLQTLHSQEIHIRDAhevatsiREISCQQHTLTQHIHTLQ 385
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195109 554 AQLEQSLQAGRI--QLETIIKSLKATQDEINQARSKLSQ 590
Cdd:TIGR00618 386 QQKTTLTQKLQSlcKELDILQREQATIDTRTSAFRDLQG 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
481-610 |
1.05e-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: 55.83 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQES--DLQSQEEELGRA--KADLNRLQQEEAQL 556
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykELKAELRELELAllVLRLEELREELEEL 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 557 EQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
416-604 |
1.43e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 55.23 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQST-------LAFTHWDTLREKYTL-EQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQ 487
Cdd:PRK04778 214 MEEIPELLKELQTElpdqlqeLKAGYRELVEEGYHLdHLDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 DRLEEMDQQ-----KAKledmlNDVRQKCQEESQMISslqtqiHSQEsdlqsQEEELgraKADLNRLQQ------EEAQL 556
Cdd:PRK04778 289 ERIDQLYDIlerevKAR-----KYVEKNSDTLPDFLE------HAKE-----QNKEL---KEEIDRVKQsytlneSELES 349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195109 557 EQSLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK04778 350 VRQLEK---QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
17-78 |
2.10e-07 |
|
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: 50.06 E-value: 2.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 17 YENFYRQVDPGNtGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLV 78
Cdd:pfam12763 12 YWEIFSGLKPEN-NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
504-601 |
2.15e-07 |
|
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: 51.16 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 504 LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ 583
Cdd:pfam11559 40 IYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119
|
90
....*....|....*....
gi 1207195109 584 ARSKLSQIQDSQ-HEISKN 601
Cdd:pfam11559 120 LKNALQQIKTQFaHEVKKR 138
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
414-606 |
2.57e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.09 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQST-------LAFTHWDTLREKYTLEQDirETEEairhkttEVQEMQNDLDRETSSLQELEAQkqDA 486
Cdd:pfam06160 193 ELMEDIPPLYEELKTElpdqleeLKEGYREMEEEGYALEHL--NVDK-------EIQQLEEQLEENLALLENLELD--EA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMDQQKAKLEDMLN---DVRQKCQEESQMISSLQTQIHSQESDLQsqeEELGRAKadLN-RLQQEEAQLEQSLQA 562
Cdd:pfam06160 262 EEALEEIEERIDQLYDLLEkevDAKKYVEKNLPEIEDYLEHAEEQNKELK---EELERVQ--QSyTLNENELERVRGLEK 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195109 563 griQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:pfam06160 337 ---QLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
432-604 |
2.65e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 52.06 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 432 FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-----------KQDAQDRLEEMDQQKAKL 500
Cdd:cd00176 12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlieeghpdAEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 501 EDMLNDVRQKCQE------ESQMISSLQTQIHSQESDLQSQeeELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKSL 574
Cdd:cd00176 92 RELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEA----HEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1207195109 575 KATQDEINQARSKLS--QIQDSQHEISKNIEQ 604
Cdd:cd00176 166 NELAEELLEEGHPDAdeEIEEKLEELNERWEE 197
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
417-637 |
2.81e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 53.14 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 417 DDISQEIAQLQSTLA-----FTHW--DTLREKYTLEQDIRE-TEEAIRHKTTEVQEMQNDLDR--ETSSLQELEAQKQDA 486
Cdd:cd22656 40 DKLSSDFDPLLDAYKsikdhCTDFkdDTYPSIVSLAGDIYNyAQNAGGTIDSYYAEILELIDDlaDATDDEELEEAKKTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMD------QQKA-KLEDMLNDVRQKCQEESQMISSLQTQIHSQ----------------ESDLQSQEEELG-RA 542
Cdd:cd22656 120 KALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiarkeikdlQKELEKLNEEYAaKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 543 KADLNRLQQEEAQLEQSLQAG-RIQ--LETIIKSLKATQDEINQARSKLSQIQDSQHEISknieqysstlngthgGSMTN 619
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAAlRLIadLTAADTDLDNLLALIGPAIPALEKLQGAWQAIA---------------TDLDS 264
|
250
....*....|....*...
gi 1207195109 620 LADMSEGFPEKENGGFGA 637
Cdd:cd22656 265 LKDLLEDDISKIPAAILA 282
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
475-612 |
2.88e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 52.30 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 475 SLQELEAQK-------------QDAQDRLEEMDQQKAKLEDmlndVRQKCQEESQMISSLQTQIHSQEsdlQSQEEELgr 541
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAAA----YQKALDDAPAELRELRQELAALQ---AKAEAAP-- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 542 aKADLNRLQQEeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGT 612
Cdd:pfam12795 72 -KEILASLSLE--ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGP 139
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
413-585 |
2.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAI---RHKTTEVQEMQNDLDRETSSLQELEAQK---- 483
Cdd:PRK04863 893 ADRVEEIREQLDEAEEAKRFvqQHGNALAQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFALTEVVQRRahfs 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 -QDAQD--------------RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-------- 540
Cdd:PRK04863 973 yEDAAEmlaknsdlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpads 1052
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 541 ----RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:PRK04863 1053 gaeeRARARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
424-609 |
3.23e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 424 AQLQSTLafTHWDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-------ELEAQKQDAQDRLEEMDQQ 496
Cdd:TIGR00618 549 HQLTSER--KQRASLKEQ---MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteklsEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 497 KAKLEDMLNDVRQKCQEESQmissLQTQIHSQESDLQSQEEELGRAkadlnRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQSEKEQLTY 694
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
414-603 |
3.31e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHWDTLrEKYTLEQdireTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:PRK11281 94 AKLRQAQAELEALKDDNDEETRETL-STLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDV-----------RQKCQEESQMissLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQeeAQLEQSL 560
Cdd:PRK11281 169 SQRLQQIRNLLKGGkvggkalrpsqRVLLQAEQAL---LNAQNDLQRKSLEgnTQLQDLLQKQRDYLTARI--QRLEHQL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 561 QAgriqLETII--KSLKATQDEINQARS--KLSQIQDS---QHEISKNIE 603
Cdd:PRK11281 244 QL----LQEAInsKRLTLSEKTVQEAQSqdEAARIQANplvAQELEINLQ 289
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
443-589 |
3.40e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 51.75 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIrhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMdQQKAKL------EDMLNDVRQKCQEESQ 516
Cdd:COG1842 27 MLDQAIRDMEEDL-------VEARQALAQVIANQKRLERQLEELEAEAEKW-EEKARLalekgrEDLAREALERKAELEA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195109 517 MISSLQTQIhsqesdlQSQEEELGRAKADLNRLqqeEAQLEQsLQAGRIQLETIIKSLKATQdEINQARSKLS 589
Cdd:COG1842 99 QAEALEAQL-------AQLEEQVEKLKEALRQL---ESKLEE-LKAKKDTLKARAKAAKAQE-KVNEALSGID 159
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
467-609 |
3.48e-07 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 52.84 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 467 NDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDM---LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAK 543
Cdd:pfam09787 37 EGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLrteLQELEAQQQEEAESSREQLQELEEQLATERSARRE---AE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 544 ADLNRLQQEEAQLEQSLQAGRIQLETIIKSLkatQDEINQARSKL---SQIQDSQHEISKNIEQYSSTL 609
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKATLQSRIKDR---EAEIEKLRNQLtskSQSSSSQSELENRLHQLTETL 179
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
420-598 |
3.54e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 420 SQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAirhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 499
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEK-------EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 500 LEDMLNDVRQKCQE-------ESQMISSLQTQIhsQESDLQSQE----------EELGRAKADLNRLQQEEAQLEQsLQA 562
Cdd:pfam13868 78 LEEQIEEREQKRQEeyeeklqEREQMDEIVERI--QEEDQAEAEeklekqrqlrEEIDEFNEEQAEWKELEKEEER-EED 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195109 563 GRI-----QLETIIKSLKATQDEINQA--------RSKLSQIQDSQHEI 598
Cdd:pfam13868 155 ERIleylkEKAEREEEREAEREEIEEEkereiarlRAQQEKAQDEKAER 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-604 |
4.37e-07 |
|
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: 54.03 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETE----EAIRHKTT---EVQEMQNDLDRETSSLQE-------- 478
Cdd:pfam01576 384 SENAELQAELRTLQQAKQ----DSEHKRKKLEGQLQELQarlsESERQRAElaeKLSKLQSELESVSSLLNEaegknikl 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 479 ------LEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEE-------SQMISSLQTQIhsqeSDLQSQ-EE 537
Cdd:pfam01576 460 skdvssLESQLQDTQELLQEETRQKLNlstrlrqLEDERNSLQEQLEEEeeakrnvERQLSTLQAQL----SDMKKKlEE 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 538 ELGRAKA---DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQarskLSQIQDSQHEISKNIEQ 604
Cdd:pfam01576 536 DAGTLEAleeGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDD----LLVDLDHQRQLVSNLEK 601
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
414-657 |
7.22e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQST---LAFTHWDTLREKYTLEQDIR----------ETEEAIRHKTTEVQEMQNDLDRETSSLQELE 480
Cdd:pfam15921 458 ESLEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 AQK---QDAQ---------------------DRLEEMDQ--------------QKAKLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:pfam15921 538 NEGdhlRNVQtecealklqmaekdkvieilrQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 523 TQIHSQE---SDLQSQEEELGRAKADLNR----LQQEEAQLEQSLQAGRIQL-------ETIIKSLKATQDEINQARSKL 588
Cdd:pfam15921 618 AKIRELEarvSDLELEKVKLVNAGSERLRavkdIKQERDQLLNEVKTSRNELnslsedyEVLKRNFRNKSEEMETTTNKL 697
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195109 589 S-QIQDSQHEisknIEQYSSTLN---GTHGGSMTNLADMSEGFPEKEnGGFGAMEDPFKVKPTVFNSAPQEMH 657
Cdd:pfam15921 698 KmQLKSAQSE----LEQTRNTLKsmeGSDGHAMKVAMGMQKQITAKR-GQIDALQSKIQFLEEAMTNANKEKH 765
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
414-610 |
7.54e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.92 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLqstlafthWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ--------ELEAQKQd 485
Cdd:PRK04778 282 EKNEEIQERIDQL--------YDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlnesELESVRQ- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 486 AQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:PRK04778 353 LEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 566 QLETII----KS------------LKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK04778 426 KLHEIKryleKSnlpglpedylemFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVE 486
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
446-592 |
8.17e-07 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment.
Pssm-ID: 341078 [Multi-domain] Cd Length: 180 Bit Score: 49.99 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 446 QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI 525
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 526 HSQESDLqsQEEELgrakADLNRLQQeEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:cd16853 91 EYVQKNL--TDEEL----ADWKRRQQ-IACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQ 150
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
414-598 |
9.26e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.53 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFThwdtlrekytleqDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEEL-------------DLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQ---EESQMISSLQTQIHSQESDLQSQEEELGRAKAD----LNRLQQEEAQLEQsLQAGRIQ 566
Cdd:PRK04778 323 KEQNKELKEEIDRVKQSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEIAyselQEELEEILKQLEE-IEKEQEK 401
|
170 180 190
....*....|....*....|....*....|..
gi 1207195109 567 LETIIKSLKatQDEiNQARSKLSQIQDSQHEI 598
Cdd:PRK04778 402 LSEMLQGLR--KDE-LEAREKLERYRNKLHEI 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
416-623 |
9.39e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEeairhktTEVQEMQNDLD-------RETSSLQELEAQKQDAqd 488
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQ-------TKLQEMQMERDamadirrRESQSQEDLRNQLQNT-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 489 rLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ--------------EEA 554
Cdd:pfam15921 151 -VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrslgsaiskilREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 555 QLEQSLQAGRI-----QLETiIKS---------LKATQDEINQ------------------ARSKLSQIQdSQHEIsknI 602
Cdd:pfam15921 230 DTEISYLKGRIfpvedQLEA-LKSesqnkiellLQQHQDRIEQliseheveitgltekassARSQANSIQ-SQLEI---I 304
|
250 260
....*....|....*....|.
gi 1207195109 603 EQYSSTLNGTHggsMTNLADM 623
Cdd:pfam15921 305 QEQARNQNSMY---MRQLSDL 322
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
418-625 |
1.05e-06 |
|
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: 52.42 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 418 DISQEIAQLqsTLAFTHWDTLREKYTLEQ--DIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQD------ 485
Cdd:pfam05483 187 DLNNNIEKM--ILAFEELRVQAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflle 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 486 -AQDRLEEMdQQKAKLEDmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGRAKADLNRLQQE-EAQLEQSL 560
Cdd:pfam05483 265 eSRDKANQL-EEKTKLQD--ENLKELIEKKDHLTKELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEkEAQMEELN 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 561 QAgRIQLETIIKSLKAT----QDEINQARSKLSQIQDSQHEISKNIEQYSSTLNgthggSMTNLADMSE 625
Cdd:pfam05483 342 KA-KAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQKKSSELE-----EMTKFKNNKE 404
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
415-630 |
1.06e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAfthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL------------QELEAQ 482
Cdd:pfam12128 242 EFTKLQQEFNTLESAEL--------RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLddqwkekrdelnGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 483 KQD-AQDR--LEEMDQQKAKLEDmlNDVRQKCQEESQMiSSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQleqs 559
Cdd:pfam12128 314 DAAvAKDRseLEALEDQHGAFLD--ADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---- 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 560 lqagriQLETIIKSLKATQDEINQARsklsqiqDSQH-EISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEK 630
Cdd:pfam12128 387 ------QNNRDIAGIKDKLAKIREAR-------DRQLaVAEDDLQALESELREQLEAGKLEFNEEEYRLKSR 445
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
443-631 |
1.24e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSL 521
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 522 QTQIHSQESDLQSQEEELGRAKADLNRL-------------------------QQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrrelddrnmevQRLEALLKAMKSECQGQMERQMAAIQG 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTlNGTHGGSMTNLADMSEGFPEKE 631
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKE 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
439-621 |
1.32e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 439 REKYTLEQDIRETEEaIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:TIGR00618 163 KEKKELLMNLFPLDQ-YTQLALMEFAKKKSLHGKAELLTlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEelgrakadlnrLQQEEAQLEqslqagriQLETIIKSLKATQDEINQARSKLSQIQDSQH- 596
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQL-----------LKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAHIKAv 302
|
170 180
....*....|....*....|....*.
gi 1207195109 597 -EISKNIEQYSSTLNGThggsMTNLA 621
Cdd:TIGR00618 303 tQIEQQAQRIHTELQSK----MRSRA 324
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
372-593 |
1.32e-06 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 51.62 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 372 SLSGYMTPVGSDMAALTEMRRAImfklwDSSSSVGSGEFTGIKELDDISQEIAQ-LQStlafthwdtlrekytLEQDIRE 450
Cdd:pfam04108 134 SLDSDLKRFDDDLRDLQKELESL-----SSPSESISLIPTLLKELESLEEEMASlLES---------------LTNHYDQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 451 TEEAIRHKTTEVQEMQNDLDRETsslQELEAQKQDAQDRLEEMDQQKAKLE---DMLNDVRQKCQEESQMISSLQTQIHS 527
Cdd:pfam04108 194 CVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQkllEQKNSLIDELLSALQLIAEIQSRLPE 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 528 QESDLQSQEEELGRAKAdlnRLQQEEAQLEQsLQAGRIQLETIIKSL-------KATQDEI----NQARSKLSQIQD 593
Cdd:pfam04108 271 YLAALKEFEERWEEEKE---TIEDYLSELED-LREFYEGFPSAYGSLlleverrREWAEKMkkilRKLAEELDRLQE 343
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
409-594 |
1.47e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 49.90 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 409 EFTGIKE---------LDDISQ---EIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDL---DRET 473
Cdd:pfam13851 9 AFNEIKNyynditrnnLELIKSlkeEIAELKKKEE----RNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyEKDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 474 SSLQELEAQKQDAQDRL-------EEMDQQKAKLEDMLNDVRQKCQeesQMISSLQtqihsQESDLQSQEEElgrakadl 546
Cdd:pfam13851 85 QSLKNLKARLKVLEKELkdlkwehEVLEQRFEKVERERDELYDKFE---AAIQDVQ-----QKTGLKNLLLE-------- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195109 547 NRLQQEEAQLEQSlqagRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:pfam13851 149 KKLQALGETLEKK----EAQLNEVLAAANLDPDALQAVTEKLEDVLES 192
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
413-605 |
1.66e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLafthwDTLREKytleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:COG1340 28 KEKRDELNEELKELAEKR-----DELNAQ------VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE------SDLQSQEEELGRAKaDLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG1340 97 LRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEeekelvEKIKELEKELEKAK-KALEKNEKLKELRAELKELRKE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195109 567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-567 |
1.77e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdQQKAKLEDMLNDVRQKCQEESQMISSLQt 523
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQ- 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207195109 524 qihSQESDLQSQEEELGRAKAdlnrlQQEEAQLEQSLQAGRIQL 567
Cdd:COG4942 220 ---QEAEELEALIARLEAEAA-----AAAERTPAAGFAALKGKL 255
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
443-589 |
2.17e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 49.68 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIRhkttevqEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDmlndvrqKCQE-----ESQM 517
Cdd:pfam04012 19 KAEDPEKMLEQAIR-------DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE-------KAQAaltkgNEEL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--TQDEINQARSKLS 589
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
532-604 |
2.30e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195109 532 LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
440-593 |
2.72e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETEEAIrhkttEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKL----------EDMLNDVRQ 509
Cdd:pfam13868 158 LEYLKEKAEREEEREA-----EREEIEEEKERE---IARLRAQQEKAQDEKAERDELRAKLyqeeqerkerQKEREEAEK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 510 KCQEESQMISSLQTQIHSQEsdlQSQEEELGRAKADLNRL---QQEEAQLEQSLQAGRIQLetiiksLKATQDEInqars 586
Cdd:pfam13868 230 KARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRMK------RLEHRREL----- 295
|
....*..
gi 1207195109 587 kLSQIQD 593
Cdd:pfam13868 296 -EKQIEE 301
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
414-610 |
2.85e-06 |
|
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: 51.20 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTT-------EVQEMQNDLDRETSSLQELEAQKQDA 486
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDR---------------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI--HSQESDLQSQEEELGRAKADLNRL 549
Cdd:TIGR00606 968 KDDylkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQM 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 550 Q-----QEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLS--QIQDSQ-------------HEISKNIEQYSSTL 609
Cdd:TIGR00606 1048 QvlqmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRepQFRDAEekyremmivmrttELVNKDLDIYYKTL 1127
|
.
gi 1207195109 610 N 610
Cdd:TIGR00606 1128 D 1128
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
476-608 |
2.89e-06 |
|
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: 50.02 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 476 LQELEAQKQDAQDRLEEMDQQKAKL---EDMLNDVRQKCQEESQMISSLQTQIHSQESDLQS-QEEELGRAKADLNRLQQ 551
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 552 E-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSST 608
Cdd:smart00787 219 EimikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKLKEQLKLL 283
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
436-610 |
2.95e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYTLEQDIreTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ------ 509
Cdd:TIGR01612 1621 DCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknye 1698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 510 -----KCQE----ESQMISSLQTQIHSQESDLQSQ-----------EEELGRAKADLNRLQQEEAQLeQSLQAGriQLET 569
Cdd:TIGR01612 1699 igiieKIKEiaiaNKEEIESIKELIEPTIENLISSfntndlegidpNEKLEEYNTEIGDIYEEFIEL-YNIIAG--CLET 1775
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195109 570 IIKSlKATQDEINQARSklsqiqDSQHEISKNIE---QYSSTLN 610
Cdd:TIGR01612 1776 VSKE-PITYDEIKNTRI------NAQNEFLKIIEiekKSKSYLD 1812
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
486-608 |
3.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 486 AQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 566 QLETIIKSL----------------KATQDEINQArSKLSQIQDSQHEIsknIEQYSST 608
Cdd:COG3883 87 ELGERARALyrsggsvsyldvllgsESFSDFLDRL-SALSKIADADADL---LEELKAD 141
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
441-605 |
3.02e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 441 KYTLEQDIRETEEAIRHKtteVQEMQNDLDrETSSLQELEAQkqdaqdrlEEMDQQKAKLEdmlNDVRQKCQEesqmISS 520
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLRNEFE---KELRERRNE----LQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--------TQDEinqARSKLSQ-- 590
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTAEE---AKEILLEkv 163
|
170
....*....|....*
gi 1207195109 591 IQDSQHEISKNIEQY 605
Cdd:PRK12704 164 EEEARHEAAVLIKEI 178
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
421-604 |
3.20e-06 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 49.32 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 421 QEIAQLQSTLafTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSS------LQELEAQKQDAQDRLEEMD 494
Cdd:pfam16591 9 TDISQLNDTL--TDLRIARLQYMLSNGDATAAQAVQKKLDELKQQLQQLKTTFTSpenvrlLQEQLQLIQAYRKSFNELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQI----------------------HSQ--------------ESDLQSQEEE 538
Cdd:pfam16591 87 AAYESRNASRQVMDSAAERALEAIDQLEAEVlqtpeadsrraaqyqaiselkrQVQmaryqvrgytftpnEDSEQAAYQQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 539 LGRAKADLNRLQQEEA--------QLEQSLQAGRIQLETiiksLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam16591 167 LDAALASLDQLRQALAgdpgaalqQLTSALQGYRDALDT----FKAAVAAIEQARQEMTSQGDEIVRISDELYQ 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
440-587 |
3.85e-06 |
|
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: 50.94 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETEEAI------------RHKTTE--VQEMQNDLDRE---TSSLQEL----EAQKQDAQDRL-------E 491
Cdd:pfam01576 125 EKVTTEAKIKKLEEDIllledqnsklskERKLLEerISEFTSNLAEEeekAKSLSKLknkhEAMISDLEERLkkeekgrQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRiQLETII 571
Cdd:pfam01576 205 ELEKAKRKLEGESTDLQEQ-------IAELQAQIAELRAQLAKKEEEL---QAALARLEEETAQKNNALKKIR-ELEAQI 273
|
170
....*....|....*.
gi 1207195109 572 KSLKATQDEINQARSK 587
Cdd:pfam01576 274 SELQEDLESERAARNK 289
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
431-605 |
5.33e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 431 AFTHWDTLREKYTLEQDIRETE-EAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------RLEEMDQQKA---- 498
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsIREISCQQHTltqh 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 499 --KLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgraKADLNRLQ-QEEAQLEQSLQAgRIQLETIIKSLK 575
Cdd:TIGR00618 381 ihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL----QGQLAHAKkQQELQQRYAELC-AAAITCTAQCEK 455
|
170 180 190
....*....|....*....|....*....|
gi 1207195109 576 ATQDEINQARSKLsqiqDSQHEISKNIEQY 605
Cdd:TIGR00618 456 LEKIHLQESAQSL----KEREQQLQTKEQI 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
414-604 |
5.79e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTT--EVQEMQNDLdrETSSLQELEAQKQDAQ---- 487
Cdd:PRK03918 459 AELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIKLKELaeQLKELEEKL--KKYNLEELEKKAEEYEklke 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 -------------DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEA 554
Cdd:PRK03918 533 kliklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 555 QLEQSLqagriqletiiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK03918 613 ELEREE-----------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
414-602 |
5.94e-06 |
|
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: 50.11 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAqkqdaqdrleem 493
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA------------ 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDmlndvRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKADLNRLQQEEAQLeqslqagRIQLETIIKS 573
Cdd:pfam05483 493 HCDKLLLEN-----KELTQEASDMTLELK----KHQEDIINCKKQEERMLKQIENLEEKEMNL-------RDELESVREE 556
|
170 180
....*....|....*....|....*....
gi 1207195109 574 LKATQDEInqaRSKLSQIQDSQHEISKNI 602
Cdd:pfam05483 557 FIQKGDEV---KCKLDKSEENARSIEYEV 582
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
411-598 |
6.45e-06 |
|
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: 49.04 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 411 TGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRE--TEEAIRHKTTEVQEMQNDLD---RETSSLQE-LEAQKQ 484
Cdd:pfam15905 112 AAVREKTSLSASVASLEKQLL----ELTRVNELLKAKFSEdgTQKKMSSLSMELMKLRNKLEakmKEVMAKQEgMEGKLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 485 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ---TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLeyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195109 562 AGRIQLETIIKSL--------KATQDEINQARSK----LSQIQDSQHEI 598
Cdd:pfam15905 268 EKEQELSKQIKDLnekcklleSEKEELLREYEEKeqtlNAELEELKEKL 316
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
415-594 |
6.85e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.31 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIA----------QLQSTLAfthwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQkQ 484
Cdd:PRK11637 48 QLKSIQQDIAakeksvrqqqQQRASLL----AQLKKQ---EEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQ-Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 485 DAQDRL--EEMDQ-----QKAKLEDM------------------LNDVRQKCQEE-SQMISSLQTQIHSQEsDLQSQEEE 538
Cdd:PRK11637 120 AAQERLlaAQLDAafrqgEHTGLQLIlsgeesqrgerilayfgyLNQARQETIAElKQTREELAAQKAELE-EKQSQQKT 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 539 LgrakadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:PRK11637 199 L------LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
416-585 |
8.12e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLAFT--HWDTLRE----KYTLEQDiRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK-----Q 484
Cdd:COG3096 895 LEELREELDAAQEAQAFIqqHGKALAQleplVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyE 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 485 DAQDRLEE----MDQQKAKLEDM----------LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG---------- 540
Cdd:COG3096 974 DAVGLLGEnsdlNEKLRARLEQAeearreareqLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaea 1053
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 541 --RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:COG3096 1054 eeRARIRRDELHEElsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
444-604 |
8.48e-06 |
|
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: 49.79 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTE-------VQEMQNDLDRETSSLQELEAQKQDAQDRLEEM--------DQQ------KAKLED 502
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEkkkmqqhIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLeedillleDQNsklskeRKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 503 MLNDVRQKCQEESQMISSLQTQIHSQE---SDLQ---SQEE----ELGRAK----ADLNRLQQEEAQLEQSLQAGRIQLE 568
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEerlKKEEkgrqELEKAKrkleGESTDLQEQIAELQAQIAELRAQLA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195109 569 TIIKSLKATQDEI-------NQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam01576 240 KKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLES 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
414-563 |
8.82e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAI-------------------------------------- 455
Cdd:COG4942 69 RRIRALEQELAALEAELA----ELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkyl 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 456 -RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLndvrqkcQEESQMISSLQTQIHSQESDLQS 534
Cdd:COG4942 145 aPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-------AERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*....
gi 1207195109 535 QEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
444-583 |
9.15e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 524 QIHSQESDLQSQEEELGRAKADLNRL------------QQEE------AQLEQsLQAGRIQLETIIKSL--------KAT 577
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEErydflsEQRED-LEEARETLEEAIEEIdretrerfLET 832
|
....*.
gi 1207195109 578 QDEINQ 583
Cdd:COG1196 833 FDAVNE 838
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
414-604 |
9.28e-06 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 46.83 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETE-EAIRhktTEVQEMQNdldretsslqELEAQKQDaqdrLEE 492
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQ-EKLEQKEELGEGLTMIDfLQLQ---IENQALNE----------KIEERNKE----LKR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslQAGRIQLETIIK 572
Cdd:pfam13870 68 LKLKVTNTVHALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQ--QGGLLHVPALLH 145
|
170 180 190
....*....|....*....|....*....|..
gi 1207195109 573 SLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam13870 146 DYDKTKAEVEEKRKSVKKLRRKVKILEMRIKE 177
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
417-594 |
1.05e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 417 DDISQEIAQLQSTLAFThwDTLREKYTLEQD----IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PRK04778 317 DFLEHAKEQNKELKEEI--DRVKQSYTLNESelesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHS-----QESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQL 567
Cdd:PRK04778 395 IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikrylEKSNLPGLPEDY---LEMFFEVSDEIEALAEELEEKPINM 471
|
170 180
....*....|....*....|....*..
gi 1207195109 568 ETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:PRK04778 472 EAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
438-625 |
1.09e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAI----RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 513
Cdd:TIGR00606 222 IRDQITSKEAQLESSREIvksyENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 514 EsqmissLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ------------SLQAGRIQLETIIKSLKATQdei 581
Cdd:TIGR00606 302 Q------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQektellveqgrlQLQADRHQEHIRARDSLIQS--- 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207195109 582 NQARSKLSQIQ---DSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:TIGR00606 373 LATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
414-552 |
1.10e-05 |
|
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: 48.48 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAirhkTTEVQEM-QNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:smart00787 158 EDYKLLMKELELLNSIK-----PKLRDRKdALEEELRQLKQL----EDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKCQEesqmissLQTQIHSQESDL-QSQ---EEELGRAKADLNRLQQE 552
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSE-------LNTEIAEAEKKLeQCRgftFKEIEKLKEQLKLLQSL 286
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
417-592 |
1.34e-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: 48.97 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 417 DDISQEIAQLQSTLAfTHWDtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EE 492
Cdd:pfam05557 279 EDLSRRIEQLQQREI-VLKE---ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDV---------RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKadlnrlqQEEAQLEQSLQAG 563
Cdd:pfam05557 355 RDGYRAILESYDKELtmsnyspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYK-------QQAQTLERELQAL 427
|
170 180
....*....|....*....|....*....
gi 1207195109 564 RIQLETiiKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam05557 428 RQQESL--ADPSYSKEEVDSLRRKLETLE 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
413-587 |
1.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQ-STLAFTHWDTLREKYTLE-QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:PRK03918 275 IEELEEKVKELKELKeKAEEYIKLSEFYEEYLDElREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 EEMdQQKAKLedmLNDVRQKcQEESQMISSLQTqIHSQEsDLQSQEEELGRAKadlnrlqqEEAQLEQSLQAGRI-QLET 569
Cdd:PRK03918 355 EEL-EERHEL---YEEAKAK-KEELERLKKRLT-GLTPE-KLEKELEELEKAK--------EEIEEEISKITARIgELKK 419
|
170
....*....|....*...
gi 1207195109 570 IIKSLKATQDEINQARSK 587
Cdd:PRK03918 420 EIKELKKAIEELKKAKGK 437
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
439-592 |
1.47e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 45.32 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 439 REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaqkqdAQDRLE-EMdQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-------AQQNYErEL-VLHAEDIKALQALREELNELKAE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEELgrakadlnrlQQEEAQLEQSLqagriqletiiKSLKATQDEIN-QARSKLSQIQ 592
Cdd:pfam07926 73 IAELKAEAESAKAELEESEESW----------EEQKKELEKEL-----------SELEKRIEDLNeQNKLLHDQLE 127
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
446-561 |
1.50e-05 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 44.87 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 446 QDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLqtqi 525
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQR---EEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEK---- 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207195109 526 hsqesdlqsqEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam13863 79 ----------EKEIKKLTAQIEELKSEISKLEEKLE 104
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
437-591 |
1.63e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 437 TLREKYT-LEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAkledmlndvrqKCQEEs 515
Cdd:COG3096 516 QLRAQLAeLEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA-----------EAVEQ- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 516 qmisslQTQIHSQESDLQSQEEELGR-------AKADLNRLQ-QEEAQLE--QSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:COG3096 580 ------RSELRQQLEQLRARIKELAArapawlaAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELAARK 653
|
....*..
gi 1207195109 586 SKL-SQI 591
Cdd:COG3096 654 QALeSQI 660
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
413-632 |
1.66e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAFTHWD-----TLRE---KYTLEQDI----RETEEAIRHKTTE-VQEMQNDLDRETSSLQEL 479
Cdd:pfam07111 189 AKQLAEAQKEAELLRKQLSKTQEEleaqvTLVEslrKYVGEQVPpevhSQTWELERQELLDtMQHLQEDRADLQATVELL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 480 EAQKQDAQDRL----EEMDQQKAKLEDMLNDVRQKCQE----ESQMISSLQTQIHSQE-------SDLQSQEEELgraKA 544
Cdd:pfam07111 269 QVRVQSLTHMLalqeEELTRKIQPSDSLEPEFPKKCRSllnrWREKVFALMVQLKAQDlehrdsvKQLRGQVAEL---QE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 545 DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA----RSKLSQIQDSQHEISKNIEQYSSTLNGTHgGSMTNL 620
Cdd:pfam07111 346 QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAqearRRQQQQTASAEEQLKFVVNAMSSTQIWLE-TTMTRV 424
|
250
....*....|..
gi 1207195109 621 ADMSEGFPEKEN 632
Cdd:pfam07111 425 EQAVARIPSLSN 436
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
436-588 |
1.99e-05 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 46.14 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYTLEQ----DIRETEEAIRHKTtevQEMQNDLDRETSSLQELEAQKQDaQDRLEEMDQQKAKLEDMLNDVR--- 508
Cdd:pfam16043 10 DQLQALILDLQeeleKLSETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASKVSrdq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 509 --QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslqagriqletIIKSLKATQDEINQARS 586
Cdd:pfam16043 86 fdETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKEL-----------LERRIKALQKLLQEGSE 154
|
..
gi 1207195109 587 KL 588
Cdd:pfam16043 155 EL 156
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
413-603 |
2.15e-05 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 47.93 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAFThWDTLRE----KYTLEQDIRETEEAIrHKTTEVQEMQND------------LDRETSSL 476
Cdd:pfam03148 122 LKEVELIEGIQELLQRTLEQA-WEQLRLlraaRHKLEKDLSDKKEAL-EIDEKCLSLNNTspnisykpgptrIPPNSSTP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 477 QE---------LEAQK--QDAQDRLEEMDQQkakLEDMLNDV-----------RQKCQEESQMISSLQTQ-------IHS 527
Cdd:pfam03148 200 EEwekftqdniERAEKerAASAQLRELIDSI---LEQTANDLraqadavnfalRKRIEETEDAKNKLEWQlkktlqeIAE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 528 QESDLQSQEEELGRAKADL--------NRLQ-------QEEAQ--LEQSLQagriQLETIIKSLkatQDEINQARSKLSQ 590
Cdd:pfam03148 277 LEKNIEALEKAIRDKEAPLklaqtrleNRTYrpnvelcRDEAQygLVDEVK----ELEETIEAL---KQKLAEAEASLQA 349
|
250
....*....|...
gi 1207195109 591 IQDSQHEISKNIE 603
Cdd:pfam03148 350 LERTRLRLEEDIA 362
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
444-547 |
2.32e-05 |
|
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: 46.56 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEK 204
|
90 100 110
....*....|....*....|....*....|.
gi 1207195109 524 QIHSQESDLQSQEE-------ELGRAKADLN 547
Cdd:pfam00261 205 EVDRLEDELEAEKEkykaiseELDQTLAELN 235
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
416-591 |
2.77e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLAFTHW---DTLREKY-TLEQDIRETEEAIRH------KTTEVQEMQNDLDRETSSLQELEAQKQD 485
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANLladETLADRLeELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSDPEQFEQLQADYLQ 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 486 AQDRLEEMDQQKakleDMLNDVRQKC-----QEESQMI---SSLQTQIHSQesdLQSQEEElgRAKADlNRLQQEEAQLE 557
Cdd:COG3096 946 AKEQQRRLKQQI----FALSEVVQRRphfsyEDAVGLLgenSDLNEKLRAR---LEQAEEA--RREAR-EQLRQAQAQYS 1015
|
170 180 190
....*....|....*....|....*....|....
gi 1207195109 558 QSLQAgRIQLETiikSLKATQDEINQARSKLSQI 591
Cdd:COG3096 1016 QYNQV-LASLKS---SRDAKQQTLQELEQELEEL 1045
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
472-609 |
2.87e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 472 ETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE----------------------SQMISSLQTQIH 526
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQqleRLRRErekaeryqallkekreyegyelLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ--AGRI---------QLETIIKSLKAtqdEINQARS----KLSQI 591
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIkdlgeeeqlRVKEKIGELEA---EIASLERsiaeKEREL 317
|
170
....*....|....*...
gi 1207195109 592 QDSQHEISKNIEQYSSTL 609
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLL 335
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
436-585 |
2.88e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYTlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEaqkQDAQDRLEEMDQQKAKLEDmlndvRQKCQEES 515
Cdd:pfam15709 336 DRLRAERA-EMRRLEVERKRREQEEQRRLQQEQLERAEKMREELE---LEQQRRFEEIRLRKQRLEE-----ERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 516 QMISSLQTQIHSQESDLQSQE--------------EELGRAKADLNRLQQEEAQL--EQSLQAGRIQlETIIKSLKATQD 579
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEfrrklqelqrkkqqEEAERAEAEKQRQKELEMQLaeEQKRLMEMAE-EERLEYQRQKQE 485
|
....*.
gi 1207195109 580 EINQAR 585
Cdd:pfam15709 486 AEEKAR 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
439-598 |
3.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 439 REKYT--------LE--QDIR-ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV 507
Cdd:pfam01576 632 REKETralslaraLEeaLEAKeELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 508 RQ-KCQEESQMiSSLQTQIhsqESDLQSQEEELGRAKADLNR-LQQEEAQLE----QSLQA--GRIQLETIIKSLKATQD 579
Cdd:pfam01576 712 EDaKLRLEVNM-QALKAQF---ERDLQARDEQGEEKRRQLVKqVRELEAELEderkQRAQAvaAKKKLELDLKELEAQID 787
|
170 180
....*....|....*....|....*..
gi 1207195109 580 EINQARS-------KL-SQIQDSQHEI 598
Cdd:pfam01576 788 AANKGREeavkqlkKLqAQMKDLQREL 814
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
440-606 |
3.23e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETEEAIRHKTtEVQEMQNDLDRETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsq 516
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKE-QMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRK-- 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 517 missLQTQIHSQESDLQSQ--EEELGRAKADLNRLQQEEAQLEQSLQAGRIQ------LETIIKSLKATQDEINQA---R 585
Cdd:TIGR00618 621 ----LQPEQDLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRvlpkelLASRQLALQKMQSEKEQLtywK 696
|
170 180
....*....|....*....|.
gi 1207195109 586 SKLSQIQDSQHEISKNIEQYS 606
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYD 717
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
415-593 |
3.25e-05 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 46.94 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAFThwDTLREKYTLEQDIRETEEA----IRHKTTE-----------VQEMQNDLDRETSSLQEL 479
Cdd:pfam04849 109 QLGSAREEILQLRHELSKK--DDLLQIYSNDAEESETESScstpLRRNESFsslhgcvqldaLQEKLRGLEEENLKLRSE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 480 EAQKQDAQDRLEEMDQQkakledMLNDVRQKCQEESQMISSLqtqihsqesdlqsqEEELGRaKADLNRLQQEE-----A 554
Cdd:pfam04849 187 ASHLKTETDTYEEKEQQ------LMSDCVEQLSEANQQMAEL--------------SEELAR-KMEENLRQQEEitsllA 245
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195109 555 Q---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam04849 246 QivdLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQD 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
526-610 |
3.66e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 526 HSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
....*
gi 1207195109 606 SSTLN 610
Cdd:COG4942 96 RAELE 100
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
421-604 |
3.69e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 421 QEIAQLQsTLAFTHWDTLREKytlEQDIRETEEAIR-----------------HKTTEVQEMQNDLDRETSSLQELE--- 480
Cdd:pfam15558 21 QRMRELQ-QQAALAWEELRRR---DQKRQETLERERrlllqqsqeqwqaekeqRKARLGREERRRADRREKQVIEKEsrw 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 ---AQKQDAQdRLEEMdqQKAKLEDMLndvRQKCQEESqmisslqtqihsqesdLQSQEEELgRAKADLNRLQQ----EE 553
Cdd:pfam15558 97 reqAEDQENQ-RQEKL--ERARQEAEQ---RKQCQEQR----------------LKEKEEEL-QALREQNSLQLqerlEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 554 AQLEQSLQAGRIQLETIIKSLKatqDEIN-QARSKL--SQIQDSQHEISKNIEQ 604
Cdd:pfam15558 154 ACHKRQLKEREEQKKVQENNLS---ELLNhQARKVLvdCQAKAEELLRRLSLEQ 204
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
435-594 |
3.73e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.33 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 435 WDTLREKY-TLEQDI-RETEEAIRHKTTEVQEMQNDLDretsslQELEAQKQDAQDRLEEMDQQ--------KAKLEDML 504
Cdd:pfam01442 6 LDELSTYAeELQEQLgPVAQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEELQAKlgqnveelRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 505 NDVRQKCQEESQmisSLQTQIHSQESDLQSQ-EEELGRAKADLN-RLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdein 582
Cdd:pfam01442 80 EELRKRLNADAE---ELQEKLAPYGEELRERlEQNVDALRARLApYAEELRQKLAERLEELKESLAPYAEEVQA------ 150
|
170
....*....|..
gi 1207195109 583 QARSKLSQIQDS 594
Cdd:pfam01442 151 QLSQRLQELREK 162
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
438-596 |
3.80e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LRE-KYTLEQdIRET---EEAIRHKTTEVQEM--------QNDLDRETSSLQELE-----AQKQ--DAQDRLEEMDQQKA 498
Cdd:COG3096 238 LREnRMTLEA-IRVTqsdRDLFKHLITEATNYvaadymrhANERRELSERALELRrelfgARRQlaEEQYRLVEMARELE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 499 KLEDMLNDVRQKCQEESQMISSLQTQIHSQESdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLEtiikslkATQ 578
Cdd:COG3096 317 ELSARESDLEQDYQAASDHLNLVQTALRQQEK-IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE-------AAE 388
|
170 180
....*....|....*....|.
gi 1207195109 579 DEINQARSKLSQIQ---DSQH 596
Cdd:COG3096 389 EEVDSLKSQLADYQqalDVQQ 409
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
413-511 |
3.90e-05 |
|
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.
Pssm-ID: 461756 [Multi-domain] Cd Length: 114 Bit Score: 43.73 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMqndldretsslqeleAQKQDAQDRLEE 492
Cdd:pfam05837 5 INRRDELSSAILKLSSE----LRELQEELTEVEKENLRLKRKNRELAAELLEL---------------AKEKESRREDPK 65
|
90
....*....|....*....
gi 1207195109 493 MDQQKAKLEDMLNDVRQKC 511
Cdd:pfam05837 66 LRAQLEKLEAELKKSRRRW 84
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
401-593 |
4.06e-05 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 45.76 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 401 SSSSVGSGEFTGIKElddisqeiaqlqstlAFthwDTLREkytleqdirETEEAIRHKTTEVQEMQNDL-DRETSSLQEL 479
Cdd:cd07651 46 SRKSLGGSEEGGLKN---------------SL---DTLRL---------ETESMAKSHLKFAKQIRQDLeEKLAAFASSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 480 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKadLNRLQqeeaqleQS 559
Cdd:cd07651 99 TQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKINSYT----LQSQLTWGKELEKNNAK--LNKAQ-------SS 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195109 560 LQAGRIQLETIIKSLKATQDEINQA-RSKLSQIQD 593
Cdd:cd07651 166 INSSRRDYQNAVKALRELNEIWNREwKAALDDFQD 200
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
413-604 |
4.71e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLD---RETSSLQELEAQKQDAQDR 489
Cdd:PRK01156 196 NLELENIKKQIADDEKS----HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmknRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 490 LEEMDQQKAKLEDMLNDVRQKCQEEsqmISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLEt 569
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRNY---INDYFKYK----NDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYI- 342
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195109 570 iikSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK01156 343 ---KKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
436-606 |
5.48e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE 514
Cdd:COG1340 11 EELEEKIEeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 515 SQMISSLQTQIhsqesdlqsqeEELGRAKADLNRLQQEEAQLEQSLQ------------AGRI-QLETIIKSLKA---TQ 578
Cdd:COG1340 91 REELDELRKEL-----------AELNKAGGSIDKLRKEIERLEWRQQtevlspeeekelVEKIkELEKELEKAKKaleKN 159
|
170 180
....*....|....*....|....*...
gi 1207195109 579 DEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELA 187
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
443-587 |
5.73e-05 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 46.17 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIRHKTTEVqemqNDLDRETSSLQELEAQ-KQDAQDRLEEMDQQKAKLEDML-----NDVRQkcQEEsq 516
Cdd:pfam04849 168 ALQEKLRGLEEENLKLRSEA----SHLKTETDTYEEKEQQlMSDCVEQLSEANQQMAELSEELarkmeENLRQ--QEE-- 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 517 mISSLQTQIhsqeSDLQSQEEELGRAKADLNR-LQQE---EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK 587
Cdd:pfam04849 240 -ITSLLAQI----VDLQHKCKELGIENEELQQhLQASkeaQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
293-366 |
5.94e-05 |
|
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: 42.75 E-value: 5.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 293 DGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSKGL-DPPQALTPDMIPPSER 366
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| bMERB_dom |
pfam12130 |
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ... |
476-595 |
6.99e-05 |
|
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.
Pssm-ID: 463467 [Multi-domain] Cd Length: 131 Bit Score: 43.27 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 476 LQELEAQkqdaqdrLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH------SQESDLQSQEEELgrakadlnRL 549
Cdd:pfam12130 2 LEEIEER-------QRELEERGVELEKALRGEMSGDEEEEQLLQEWFKLVNeknalvRRESELMYLAKEQ--------DL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 550 QQEEAQLEQSLQAgRIQLETIIKS---LKATQD------EINQARSKLSQIQDSQ 595
Cdd:pfam12130 67 EERQARLEQELRE-LMSKPDWLKTeedKQREEElleelvEIVEQRDALVDSLEED 120
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
438-590 |
7.21e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKY-TLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQ 516
Cdd:PRK04863 518 LRMRLsELEQRLRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 517 MISSLQTQ----IHSQE--SDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdEInqarSKLSQ 590
Cdd:PRK04863 594 RIQRLAARapawLAAQDalARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE---EI----ERLSQ 666
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
475-592 |
7.49e-05 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 43.54 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 475 SLQELEAQKQ--DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQ-MISSLQTQIHSQEsdlqsqeeELGRAKADLNRLQQ 551
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQrLYAEIQGKLVLLK--------ELEKVKQQVALLRE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207195109 552 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam07321 81 NEADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFA 121
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
415-625 |
7.52e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQStlafthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtSSLQELEAQKQDAQDRLEEMD 494
Cdd:PRK01156 491 EVKDIDEKIVDLKK----------RKEYLESEEINKSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLK 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQ--KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN--------RLQQEEAQLE---QSLQ 561
Cdd:PRK01156 560 LEdlDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksirEIENEANNLNnkyNEIQ 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 562 AGRIQLETIIKSLKATQDEInqarSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQI----AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
444-605 |
7.62e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqqkakLEDMLNDVRQKCQEES---QMISS 520
Cdd:PRK02224 192 LKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDE-------ADEVLEEHEERREELEtleAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISK 600
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
....*
gi 1207195109 601 NIEQY 605
Cdd:PRK02224 343 EAESL 347
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
414-588 |
9.33e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAftHWDTLREKYTLEqdirETEEAIRHKttEVQEMQNDLDRETSSLQELEAQKQDAQDRL-EE 492
Cdd:pfam13868 184 REIARLRAQQEKAQDEKA--ERDELRAKLYQE----EQERKERQK--EREEAEKKARQRQELQQAREEQIELKERRLaEE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKC---QEESQMISSLQTQiHSQEsdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqlet 569
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEeieQEEAEKRRMKRLE-HRRE--LEKQIEEREEQRAAEREEELEEGERLREEEAER----- 327
|
170
....*....|....*....
gi 1207195109 570 iikslkatQDEINQARSKL 588
Cdd:pfam13868 328 --------RERIEEERQKK 338
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
413-610 |
1.02e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNdldretsslqeleAQKQDAQDRLEE 492
Cdd:COG5325 76 EDEIDELSKKVNQDLQRCE----KILKTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKaKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEeLGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 572
Cdd:COG5325 139 VLQAK-FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFR 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195109 573 SLkatQDEINQarsklsqiqdsQHEISKNIEQYSSTLN 610
Cdd:COG5325 213 DL---GSLVGE-----------QGELVDRIDFNIENTS 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
422-595 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 422 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 501
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 502 dmlndvRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGR--------------AKADLNRLQQEEAQLEQSLQA-G 563
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEErR 552
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 564 RIQLETIIKSLKATQ-DEINQARSKLSQIQDSQ 595
Cdd:pfam17380 553 RIQEQMRKATEERSRlEAMEREREMMRQIVESE 585
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
481-609 |
1.09e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVrqkcqeESQmISSLQTQ---------IHSQESDLQSQEeelgrAKADLNRLQQ 551
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGEL------ERQ-LEPLERQaekaeryreLKEELKELEAEL-----LLLKLRELEA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195109 552 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
413-605 |
1.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEmqndLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PRK03918 185 IKRTENIEELIKEKEKELE----EVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIK 572
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----IEERIK 331
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 573 SLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
443-593 |
1.16e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKL--EDMLNDVRQkCQEESQMISS 520
Cdd:pfam06008 51 SLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLgeNDFALPSSD-LSRMLAEAQR 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 521 LQTQIHSQE--SDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAgriQLETIiksLKATQDEINQARSKLSQIQD 593
Cdd:pfam06008 130 MLGEIRSRDfgTQLQNAEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYEAKLSDLRE 194
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
413-613 |
1.19e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAFTHwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLD-KNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQE---------------ESQMISS------LQTQIHSQESDLQSQEEELGRAKADLNRLQQ 551
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKEnkknidkflteikkkEKELEKLnnkyndLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 552 EEAQLEQSLqagrIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 613
Cdd:TIGR04523 195 KLLKLELLL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-605 |
1.23e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEem 493
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASE----RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE-- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 dqqkakledMLNDVRQKCQeesQMISSLQTQIHSQESDLQSQE---EELGRAKADLN-RLQQEE-----------AQLEQ 558
Cdd:pfam01576 907 ---------LLNDRLRKST---LQVEQLTTELAAERSTSQKSEsarQQLERQNKELKaKLQEMEgtvkskfkssiAALEA 974
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207195109 559 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:pfam01576 975 KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQY 1021
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
516-610 |
1.25e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 516 QMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE----TIIKSLKATQDEI---------- 581
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkeaqQAIKEAKKEADEIikelrqlqkg 599
|
90 100
....*....|....*....|....*....
gi 1207195109 582 NQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
463-611 |
1.26e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 463 QEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqQKAKLEDMLNDVRQkcqeesqmISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 543 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK--------------------LSQIQDSQHEISKNI 602
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEKRL 316
|
....*....
gi 1207195109 603 EQYSSTLNG 611
Cdd:PRK03918 317 SRLEEEING 325
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
414-594 |
1.64e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.23 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFTHWDTlrekytleQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:pfam06160 305 EQNKELKEELERVQQSYTLNENEL--------ERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHS-----QESDL----QSQEEELGRAKADLNRLQQeeaQLEQSlqagR 564
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDEFKLELREikrlvEKSNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----P 449
|
170 180 190
....*....|....*....|....*....|
gi 1207195109 565 IQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:pfam06160 450 LNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
440-592 |
1.65e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 440 EKYTLEQDIRETeeairhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcQEESQMIS 519
Cdd:PRK11281 57 EDKLVQQDLEQT-----------LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 520 SLQTQIHSQESDLQSQEEELGRAKADL--NRLQQEEAQLEQSLQAGRIQ-LETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPSQRVLLQAE 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
402-584 |
1.79e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 402 SSSVGSGEFTGIKELDDISQEIAQLQSTLAFTHWDTlREKYTLEQDIRETEE---AIRHKTTEVQEMQNDLDRETSSLQe 478
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-RQKLNLSTRLRQLEDernSLQEQLEEEEEAKRNVERQLSTLQ- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 479 leAQKQDAQDRLEEM-------DQQKAKLEDMLNDVRQKCQEESqmisslqtqihsqesdlqSQEEELGRAKadlNRLQQ 551
Cdd:pfam01576 524 --AQLSDMKKKLEEDagtlealEEGKKRLQRELEALTQQLEEKA------------------AAYDKLEKTK---NRLQQ 580
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 552 EEAQLEQSLQAGRiqleTIIKSLKATQDEINQA 584
Cdd:pfam01576 581 ELDDLLVDLDHQR----QLVSNLEKKQKKFDQM 609
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
468-553 |
1.79e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 468 DLDREtssLQELEAQKQDA--------QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT------QIHSQESDLQ 533
Cdd:COG0542 415 ELERR---LEQLEIEKEALkkeqdeasFERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeeleQRYGKIPELE 491
|
90 100
....*....|....*....|
gi 1207195109 534 SQEEELGRAKADLNRLQQEE 553
Cdd:COG0542 492 KELAELEEELAELAPLLREE 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-574 |
1.82e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLqstlafthwdtLREKYTLEQDIR-ETE-----EAIR----HKTTEVQEMqndldretssLQELEAQK 483
Cdd:pfam01576 26 SELKELEKKHQQL-----------CEEKNALQEQLQaETElcaeaEEMRarlaARKQELEEI----------LHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170
....*....|....
gi 1207195109 564 RIQL---ETIIKSL 574
Cdd:pfam01576 165 TSNLaeeEEKAKSL 178
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
451-572 |
1.95e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 42.18 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 451 TEEAIRhKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEEsqmisslqtqihsqe 529
Cdd:pfam03938 7 MQKILE-ESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEE----REEKEQE--------------- 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207195109 530 sdLQSQEEELGRAKADLNR-LQQEEAQLEQSLQAgriQLETIIK 572
Cdd:pfam03938 67 --LQKKEQELQQLQQKAQQeLQKKQQELLQPIQD---KINKAIK 105
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
406-626 |
1.96e-04 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 406 GSGEFTGI--------KELDDISQEI-----AQLQSTLAFTHWDTLREKY--TLEQDIRETEEAIRHKTTEVQEMQNDLD 470
Cdd:pfam07902 69 GSGESTGLfksleemlSQLKELNLELtdtknSNLWSKIKLNNNGMLREYHndTIKTEIVESAEGIATRISEDTDKKLALI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 471 RETssLQELEAQKQDAQDRLEEMDQQ-----KAKLE----DMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelGR 541
Cdd:pfam07902 149 NET--ISGIRREYQDADRQLSSSYQAgieglKATMAsdkiGLQAEIQASAQGLSQRYDNEIRKLSAKITTTSS-----GT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 542 AKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD----EINQ-------ARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:pfam07902 222 TEAYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQstayQISQeisnregAVSRVQQDLDSYQRRLQDAEKNYSSLT 301
|
250
....*....|....*.
gi 1207195109 611 GTHGGSMTNLADMSEG 626
Cdd:pfam07902 302 QTVKGLQSTVSDPNSK 317
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
410-600 |
1.98e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 410 FTGIKELDD-ISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEA----IRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:PRK01156 134 FVGQGEMDSlISGDPAQRKKILDeILEINSLERNYDKLKDVIDMLRAeisnIDYLEEKLKSSNLELENIKKQIADDEKSH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 484 QDAQ---DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---DLNRLQQEEAQLE 557
Cdd:PRK01156 214 SITLkeiERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEleeRHMKIINDPVYKN 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 558 Q-------SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD--SQHEISK 600
Cdd:PRK01156 294 RnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyNDYIKKK 345
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
461-610 |
2.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 461 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEeel 539
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS--- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 540 grakADLNRLQQEEAQLEQSLQagriQLETIIK-------------SLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:PHA02562 255 ----AALNKLNTAAAKIKSKIE----QFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE 326
|
....
gi 1207195109 607 STLN 610
Cdd:PHA02562 327 EIMD 330
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
436-588 |
2.29e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYTLEQDIR-----ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA----QDRLEEMDQQKAKLEDMLND 506
Cdd:pfam12128 707 EQKREARTEKQAYWqvvegALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASlgvdPDVIAKLKREIRTLERKIER 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 507 VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARS 586
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERA---ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
..
gi 1207195109 587 KL 588
Cdd:pfam12128 864 GL 865
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
437-601 |
2.89e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 437 TLREKYTLEQDIRET-------EEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD---RLEEMDQQKAKLEDMLND 506
Cdd:COG5022 831 KLRETEEVEFSLKAEvliqkfgRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIdvkSISSLKLVNLELESEIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 507 VRQKCQ----EESQMISSLQT--QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDE 580
Cdd:COG5022 911 LKKSLSsdliENLEFKTELIArlKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE----EYEDLLKKSTILVRE 986
|
170 180
....*....|....*....|.
gi 1207195109 581 INQARSKLSQIQDSQHEISKN 601
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQ 1007
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
416-599 |
3.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLA-FTHWDTLREKY----TLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqeleaqkQDAQDRL 490
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqFQKVIKMYEKGgvcpTCTQQISEGPDRITKIKDKLKELQHSLEKL-----------DTAIDEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 491 EEmdqqkakLEDMLNDVRQKCQEesqmissLQTQIHSQESDLQSQEEELGRAKADLNRlqqeeaqleqsLQAGRIQLETI 570
Cdd:PHA02562 326 EE-------IMDEFNEQSKKLLE-------LKNKISTNKQSLITLVDKAKKVKAAIEE-----------LQAEFVDNAEE 380
|
170 180
....*....|....*....|....*....
gi 1207195109 571 IKSLKATQDEINQARSKLSQIQDSQHEIS 599
Cdd:PHA02562 381 LAKLQDELDKIVKTKSELVKEKYHRGIVT 409
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
457-606 |
3.24e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.01 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 457 HKTTEVQEMQndldretsslQELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLqtqihsqesdlqsqe 536
Cdd:pfam13863 3 EKKREMFLVQ----------LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKFDKF--------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 537 eelgrakadlnrLQQEEAQLEQSLQagRIQLETIIKSLKatQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:pfam13863 54 ------------LKENDAKRRRALK--KAEEETKLKKEK--EKEIKKLTAQIEELKSEISKLEEKLEEYK 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
413-580 |
3.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEA-------EEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEdmlnDVRQKCQEESQMISSLQT----------QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQA 562
Cdd:PTZ00121 1697 EAEEAKKAE----ELKKKEAEEKKKAEELKKaeeenkikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
170
....*....|....*...
gi 1207195109 563 GRIQLETIIKSLKATQDE 580
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDE 1790
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
452-609 |
3.59e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 452 EEAIRHKTTE---VQEMQNDLDRETSSL----QELEAQKQDAQDRL----------EEM----DQQKAKLEDMLNDVRQK 510
Cdd:pfam01576 4 EEEMQAKEEElqkVKERQQKAESELKELekkhQQLCEEKNALQEQLqaetelcaeaEEMrarlAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 511 CQEESQMISSLQTQ---IHSQESDLQSQEEElgrakadlnrlqqEEAQlEQSLQAGRIQLETIIKSLkatQDEINQARSK 587
Cdd:pfam01576 84 LEEEEERSQQLQNEkkkMQQHIQDLEEQLDE-------------EEAA-RQKLQLEKVTTEAKIKKL---EEDILLLEDQ 146
|
170 180
....*....|....*....|..
gi 1207195109 588 LSQIQDSQHEISKNIEQYSSTL 609
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNL 168
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
442-597 |
3.90e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 442 YTLEQDIRETEEAIRH---KTTEVQEMQNDL-DRET-----------SSLQELEAQKQDAQDRLEEMDQ-------QKAK 499
Cdd:COG5278 29 YLSLNRLREASEWVEHtyeVLRALEELLSALlDAETgqrgylltgdeSFLEPYEEARAEIDELLAELRSltadnpeQQAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 500 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLqsqeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 579
Cdd:COG5278 109 LDELEALIDQWLAELEQVIALRRAGGLEAALAL----VRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
170
....*....|....*...
gi 1207195109 580 EINQARSKLSQIQDSQHE 597
Cdd:COG5278 185 LLALAELLLLALARALAA 202
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
438-604 |
3.93e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA-------QKQDAQDRLEEMDQQKAKLEDMLNDVRQK 510
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrKKAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 511 -------------CQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT 577
Cdd:TIGR00618 517 rqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
|
170 180
....*....|....*....|....*....
gi 1207195109 578 QDEIN-QARSKLSQIQDSQ-HEISKNIEQ 604
Cdd:TIGR00618 597 QDLTEkLSEAEDMLACEQHaLLRKLQPEQ 625
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
415-604 |
3.97e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTL---------AFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQ 484
Cdd:PRK02224 315 RREELEDRDEELRDRLeecrvaaqaHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 485 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA-----------DLNRLQQEE 553
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegspHVETIEEDR 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 554 AQLEqSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQhEISKNIEQ 604
Cdd:PRK02224 475 ERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE-ERREDLEE 523
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
452-567 |
4.29e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.67 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 452 EEAIRHKttevQEMQndlDRetssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-------QKCQEESQMISSLQTQ 524
Cdd:pfam20492 2 EEAEREK----QELE---ER----LKQYEEETKKAQEELEESEETAEELEEERRQAEeeaerleQKRQEAEEEKERLEES 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 525 IHSQESDLQSQEEELGRAKADLNRLQQE------EA-QLEQSLQAGRIQL 567
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEverkeeEArRLQEELEEAREEE 120
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
414-584 |
4.38e-04 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 41.74 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlqeleaqkqdaqDRLEEM 493
Cdd:pfam16789 14 KRVEEAEKVVKDKKRALE-------KEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMLNDVRQKCQEESQmisslqtQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIiks 573
Cdd:pfam16789 75 KRYIKVVKERLKQEEKKVQDQKE-------QVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER--- 144
|
170
....*....|.
gi 1207195109 574 lkaTQDEINQA 584
Cdd:pfam16789 145 ---EQDEIGSA 152
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-591 |
4.45e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 449 RETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQkcQEESQMISSLQTQIHSQ 528
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE--QLEAEREELLEELLEEE 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195109 529 ESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQA-GRI---------QLETIIKSLKATQDEINQARSKLSQI 591
Cdd:COG1196 746 ELLEEEALEELPEP-PDLEELERELERLEREIEAlGPVnllaieeyeELEERYDFLSEQREDLEEARETLEEA 817
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
415-613 |
4.46e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTlafthwdtlrekytleqdIRETEEAIRHktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:TIGR00606 837 ELDTVVSKIELNRKL------------------IQDQQEQIQH----LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQ----IHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqleti 570
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------ 968
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195109 571 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 613
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
371-611 |
4.48e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 371 PSLSGYMTPVGSDMAALTEMRRAIMFKLWDSSSSVGS---GEFTGIKELDDISQEIAQLQSTLAFTHWDTLRE--KYTLE 445
Cdd:pfam12128 350 PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqnnRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelREQLE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 446 QDIRE-TEEAIRHKT-----------------TEVQEMQND--LDRETSSLQELEAQKQDAQDRLEEM----DQQKAKLE 501
Cdd:pfam12128 430 AGKLEfNEEEYRLKSrlgelklrlnqatatpeLLLQLENFDerIERAREEQEAANAEVERLQSELRQArkrrDQASEALR 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 502 DM---LNDVRQKCQE-ESQMISSLQTQIHSQESDLQSQEEELGR--AKADLNR------LQQEEAQLEQSLQAGRIQLET 569
Cdd:pfam12128 510 QAsrrLEERQSALDElELQLFPQAGTLLHFLRKEAPDWEQSIGKviSPELLHRtdldpeVWDGSVGGELNLYGVKLDLKR 589
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207195109 570 I-IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:pfam12128 590 IdVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
409-591 |
4.61e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 409 EFTGIKELDDISQEIAQ----LQSTLAFthwdtlrEKYTLEQDIRETEEAIRHKTTE-VQEMQNDLDRETSSLQ---ELE 480
Cdd:TIGR00618 709 LETHIEEYDREFNEIENasssLGSDLAA-------REDALNQSLKELMHQARTVLKArTEAHFNNNEEVTAALQtgaELS 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 560
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
170 180 190
....*....|....*....|....*....|.
gi 1207195109 561 QagriQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:TIGR00618 862 A----QLTQEQAKIIQLSDKLNGINQIKIQF 888
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
447-607 |
4.72e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 447 DIRETEEAIRHKTTEVQEMQNDLDRETSSLQELE----AQKQDaqdrLEEMDQQKAKLEDMLN------DVRQKCQEESQ 516
Cdd:pfam10174 110 TPELTEENFRRLQSEHERQAKELFLLRKTLEEMElrieTQKQT----LGARDESIKKLLEMLQskglpkKSGEEDWERTR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 517 MISSLQTQIHSQESDLQSQEEELGRAKADL---NRLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQ 590
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLL 265
|
170
....*....|....*..
gi 1207195109 591 IQDSQHEISKNIEQYSS 607
Cdd:pfam10174 266 HTEDREEEIKQMEVYKS 282
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
449-592 |
4.90e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 449 RETEEAIR--HKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE-EMDQQKAKLEDMLNDVRQKCQEESQMisslQTQI 525
Cdd:COG2268 210 RETEIAIAqaNREAEEAELEQEREIETARIAEAEAELAKKKAEERrEAETARAEAEAAYEIAEANAEREVQR----QLEI 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 526 HSQESD--LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT---QDEINQARSKLSQIQ 592
Cdd:COG2268 286 AEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEaegKRALAEAWNKLGDAA 357
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
415-588 |
5.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAI--------------RHKTTEVQEMQNDLDRETSSLQ--- 477
Cdd:pfam01576 862 ERDELADEIASGASGKSAL----QDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQkse 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 478 ----ELEAQKQDAQDRLEEMDQQ------------KAKLEDMLNDVRQKCQEESQMISSL-QTQIHSQESDLQSQEEelg 540
Cdd:pfam01576 938 sarqQLERQNKELKAKLQEMEGTvkskfkssiaalEAKIAQLEEQLEQESRERQAANKLVrRTEKKLKEVLLQVEDE--- 1014
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 541 RAKAD---------LNRLQQEEAQLE------QSLQAGR--IQ--LETIIKSLKATQDEINQARSKL 588
Cdd:pfam01576 1015 RRHADqykdqaekgNSRMKQLKRQLEeaeeeaSRANAARrkLQreLDDATESNESMNREVSTLKSKL 1081
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
444-610 |
5.10e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQ--NDLDRET----SSLQELEAQKQDAQDRLEEMD-------QQKAKLEDMLNDVRQK 510
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMstDALEQEIlqvsSQLLEKSRQAQQEQDRAREISdslsqlpQQQTEARRQLNEIERR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 511 CQ---------EESQMiSSLQTQIHSQESDLQSQE---------EELGRAKADLnrLQQEEAQLEQSLQAGRIQL----- 567
Cdd:PRK10929 160 LQtlgtpntplAQAQL-TALQAESAALKALVDELElaqlsannrQELARLRSEL--AKKRSQQLDAYLQALRNQLnsqrq 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 568 ---------------------ETIIKSLKATQD---EINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK10929 237 reaeralestellaeqsgdlpKSIVAQFKINRElsqALNQQAQRMDLIASQQRQAASQTLQVRQALN 303
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
415-610 |
5.46e-04 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 43.02 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLE 491
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEddEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKvTIKADAKDWRAHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKcqeesqmisslqtqihsqesdLQSQEEELGRAkadLNRLQQEEAQLEQslqagriQLETII 571
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195109 572 KSLKATQDEinqarskLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:pfam10498 275 QEYREAQDE-------LSEVQEKYKQLSEGVTERTRELA 306
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-597 |
5.65e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQStlAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAqdrleem 493
Cdd:pfam10174 528 QKKEECSKLENQLKK--AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDK------- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 494 DQQKAKLEDMlndVRQKCQEESQMISSLQtqiHSQesdlqsQEEELGRAKADLNRLQQEEAQLEQSLQagrIQLETIIKS 573
Cdd:pfam10174 599 DKKIAELESL---TLRQMKEQNKKVANIK---HGQ------QEMKKKGAQLLEEARRREDNLADNSQQ---LQLEELMGA 663
|
170 180
....*....|....*....|....
gi 1207195109 574 LKATQDEINQARSKLSQIQDSQHE 597
Cdd:pfam10174 664 LEKTRQELDATKARLSSTQQSLAE 687
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
500-610 |
5.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 500 LEDMLndvRQKCQEESQMISSLQ--------TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETII 571
Cdd:COG4717 43 IRAML---LERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREEL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207195109 572 KSLKATQD------EINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4717 119 EKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEE 163
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
438-597 |
6.10e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EEMDQQKaKLEDMLNDVRQKCQ- 512
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqTALRQQE-KIERYQADLEELEEr 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 513 -EESQMISSLQT-QIHSQESDLQSQEEELGRAK---ADLNR---LQQEEA-QLEQSLQA-GRIQ------------LETI 570
Cdd:PRK04863 364 lEEQNEVVEEADeQQEENEARAEAAEEEVDELKsqlADYQQaldVQQTRAiQYQQAVQAlERAKqlcglpdltadnAEDW 443
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 571 IKSLKATQDEI----NQARSKLSQIQD--SQHE 597
Cdd:PRK04863 444 LEEFQAKEQEAteelLSLEQKLSVAQAahSQFE 476
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
471-607 |
6.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 471 RETSSLQELEAQKQDAQDRLEEmdqqkAKLEdmLNDVRQKCQEESQ-MISSLQTQIhsqESDLQSQEEELGRAKadlNRL 549
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE-----AKKE--AEAIKKEALLEAKeEIHKLRNEF---EKELRERRNELQKLE---KRL 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 550 QQEEAQLE---QSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:PRK12704 92 LQKEENLDrklELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
415-598 |
6.70e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLafthwDTLREKYTLE--------QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKqDA 486
Cdd:PRK10246 683 ELTALQNRIQQLTPLL-----ETLPQSDDLPhseetvalDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-DT 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMDQQKAKLEDMLND--------VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ 558
Cdd:PRK10246 757 ALQASVFDDQQAFLAALLDEetltqleqLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQ 836
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207195109 559 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEI 598
Cdd:PRK10246 837 QLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQV 876
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
445-603 |
7.64e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSslqELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLQTQ 524
Cdd:pfam05701 285 KKTSTSIQAALASAKKELEEVKANIEKAKD---EVNCLRVAAASLRSELEKEKAELASL----RQREGMASIAVSSLEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 525 IHSQESDL---QSQEEELGRAKADLNRLQQEEAQ-LEQSLQAGRIQLETIIKSlkatQDEINQARSKLSQIQDSQHEISK 600
Cdd:pfam05701 358 LNRTKSEIalvQAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAREELRKA----KEEAEQAKAAASTVESRLEAVLK 433
|
...
gi 1207195109 601 NIE 603
Cdd:pfam05701 434 EIE 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
416-604 |
7.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIrETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:PRK02224 470 IEEDRERVEELEAELE-----DLEEEVeEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQAGRIQLETI---- 570
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeln 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195109 571 -------------IKSLKATQDE--INQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK02224 623 derrerlaekrerKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| PRK13735 |
PRK13735 |
conjugal transfer mating pair stabilization protein TraG; Provisional |
477-580 |
8.01e-04 |
|
conjugal transfer mating pair stabilization protein TraG; Provisional
Pssm-ID: 184287 [Multi-domain] Cd Length: 942 Bit Score: 43.20 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 477 QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEEL-----GRAKADLNRLQQ 551
Cdd:PRK13735 833 QDIIADHQGHQAIIEQRTQDSGIRNDVKHQVDNMVTEYEGNIGDTQNSIRGEENTVKGQYSELqnhhkTEALSQNNKYNE 912
|
90 100
....*....|....*....|....*....
gi 1207195109 552 EEAqlEQSLQAGRIQLETIIKSLKATQDE 580
Cdd:PRK13735 913 EKS--AQERMPGADSPEELMKRAKEYQDK 939
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
432-620 |
8.12e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 432 FTHWDTLREKYtleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQk 510
Cdd:PHA02562 165 LSEMDKLNKDK-----IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAKTIKAEIEE- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 511 CQEEsqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---------QSLQAGRIQLETIIKSLKATQ--- 578
Cdd:PHA02562 239 LTDE---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQhsl 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195109 579 DEINQARSKLSQIQDSQHEISKNIEQYSSTLNgTHGGSMTNL 620
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKIS-TNKQSLITL 356
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
435-539 |
8.30e-04 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 41.14 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 435 WDTLREKytLEQDIRETEEAiRHKTTEVQEMQNDLDRETSSLQELEAQKQ-----DAQDRLEEMDQQ----KAKLEDMLn 505
Cdd:pfam03280 84 LAALRAQ--LPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQraawQQRLDDYL- 159
|
90 100 110
....*....|....*....|....*....|....
gi 1207195109 506 dvrqkcQEESQMisslqTQIHSQESDLQSQEEEL 539
Cdd:pfam03280 160 ------AERQQI-----NAAGLSEQERQAAIAQL 182
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
415-607 |
8.55e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLAfthwdtLREKYTLEQDIRETEEairhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIK------TYNKNIEEQRKKNGEN--------IARKQNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE---------SDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQA 562
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207195109 563 GRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
448-590 |
8.58e-04 |
|
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: 40.76 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 448 IRETEEAIRHKT---TEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEMDQQKAKLedmlndvrqkcqeesqmiSSLQTQ 524
Cdd:pfam11559 44 LQQRDRDLEFREslnETIRTLEAEIERLQSKIERLKTQLEDLE---RELALLQAKE------------------RQLEKK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 525 IHSQESDLQSQEEELGRAKadlNRLQQEEAQLEQslqagriqletiikSLKATQDEINQARSKLSQ 590
Cdd:pfam11559 103 LKTLEQKLKNEKEELQRLK---NALQQIKTQFAH--------------EVKKRDREIEKLKERLAQ 151
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
459-610 |
8.91e-04 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 41.22 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 459 TTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ-KAKLEDM----LNDVRQ-------------KCQEESQMISS 520
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSyKKKYLQTrnelINELKQskklydnyyklysKYQQLKKISNE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 521 ---LQTQIHSQESDLQSQEEELGRAKADLN-RLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam15272 83 sldLQSTITNLESQLVDQAIDKDREIHNLNeKILSLELRnqeLETKREIDKMKYESRIDELERQLKEQEYPNVSSSSPYF 162
|
170
....*....|....*..
gi 1207195109 594 SQHEISKNIEQYSSTLN 610
Cdd:pfam15272 163 STSSYRDSSELFSTDYN 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-546 |
8.93e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAfthwdTLREKYT-----LEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQKQDAQ 487
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIE-----RLEARLErledrRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 488 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihsqesDLQSQEEELGRAKADL 546
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--------RLQENLEGFSEGVKAL 511
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
416-600 |
9.05e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 416 LDDISQEIAQLQStlafthwdtLREKYtleQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAqkqdAQ---DRLEE 492
Cdd:COG0497 147 LDAFAGLEELLEE---------YREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEA----AAlqpGEEEE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMlNDVRQKCQEESQMISSLQTQIHSQesdlqsqeeeLGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 569
Cdd:COG0497 211 LEEERRRLSNA-EKLREALQEALEALSGGEGGALDL----------LGQALRALERLAEYDPSLAelaERLESALIELEE 279
|
170 180 190
....*....|....*....|....*....|...
gi 1207195109 570 IIKSLKATQD--EINQARskLSQIQDSQHEISK 600
Cdd:COG0497 280 AASELRRYLDslEFDPER--LEEVEERLALLRR 310
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
461-614 |
9.18e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 461 EVQEMQNDLDRETSSlqeleaqkqdAQDRLEEMDQQKAKLEdmlndvrqkcQEESQMISslqtQIHSQESDLQSQEEELG 540
Cdd:TIGR00606 692 ELQEFISDLQSKLRL----------APDKLKSTESELKKKE----------KRRDEMLG----LAPGRQSIIDLKEKEIP 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 541 RAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQArSKLSQIQDSQHEISKNIEQYSSTLNGTHG 614
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
482-584 |
1.15e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 482 QKQDAQDRLE-EMDQQKAKLEDMLNDVR---QKCQEESQMISslqtqihsqESDLQSQEEELGRAKADLNRLQQEeaqLE 557
Cdd:COG2825 40 EGKAAQKKLEkEFKKRQAELQKLEKELQalqEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQE---AQ 107
|
90 100
....*....|....*....|....*..
gi 1207195109 558 QSLQAGRIQLetiiksLKATQDEINQA 584
Cdd:COG2825 108 QDLQKRQQEL------LQPILEKIQKA 128
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
508-607 |
1.21e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.53 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 508 RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQL--------------ETIIKS 573
Cdd:COG5283 13 KSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrqlsaaqRRLRSS 92
|
90 100 110
....*....|....*....|....*....|....
gi 1207195109 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:COG5283 93 LEQTNRQLERQQQRLARLGARQDRLKAARARLQR 126
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
442-538 |
1.29e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.85 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 442 YTLEQDIRETEEAIRHKttEVQEMQNDLdreTSSLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQMI 518
Cdd:smart00150 1 QQFLRDADELEAWLEEK--EQLLASEDL---GKDLESVEALLKKHEAFEAELEAHEERVEALNelgEQLIEEGHPDAEEI 75
|
90 100
....*....|....*....|
gi 1207195109 519 SSLQTQIHSQESDLQSQEEE 538
Cdd:smart00150 76 EERLEELNERWEELKELAEE 95
|
|
| Zwint |
pfam15556 |
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ... |
414-561 |
1.41e-03 |
|
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are typically between 127 and 281 amino acids in length.
Pssm-ID: 464766 [Multi-domain] Cd Length: 252 Bit Score: 41.50 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLAFT-HWDTLREKYtleqdiRETEEAIRHKTTEVQEMQNDLDRETSSLQE----LEAQKQDAQD 488
Cdd:pfam15556 46 QGLDPLASEDTSRQKAIAAKeQWKELKATY------QEHVEAITSALTQALPKMEEAQRKRAQLQEaleqLQAKKQMAME 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 489 RLEEMDQQkakledmlndvRQKCQEES-QMISSLQTQIHSQESDLQsqeEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam15556 120 KLRTAQKQ-----------WQLQQEKHlQHLAEVSAEVRERQTGTQ---QELERLYQELGTLKQQAGQERDKLQ 179
|
|
| CENP-Q |
pfam13094 |
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ... |
438-562 |
1.47e-03 |
|
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.
Pssm-ID: 432970 [Multi-domain] Cd Length: 159 Bit Score: 40.35 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam13094 25 LDRNKALEAQLSAELHSLELLEEEIEKEEALLESDEEYLEELEKNAKAEARERKEKLKKEHPLLQEDDSGVLSLPELSSD 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEELGRA-KADLNRLQQEEAQLEQSLQA 562
Cdd:pfam13094 105 LGLGDTDFSLFDPTLDEELLPLLEQlQKHLESMQGNLAQLEGLNEA 150
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
447-565 |
1.53e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.91 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 447 DIRETEEAIRHKTTEVQEMQNDL-DRETSSLQELEAQKQDAQDR-------LEEMDQQKAKLEDMLndvRQKCQEESQmI 518
Cdd:pfam14988 1 ENKFFLEYLAKKTEEKQKKIEKLwNQYVQECEEIERRRQELASRytqqtaeLQTQLLQKEKEQASL---KKELQALRP-F 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 519 SSLQTQihsQESDLQSQEEELGRAKADLN--------RLQQEEAQLEQSLQAGRI 565
Cdd:pfam14988 77 AKLKES---QEREIQDLEEEKEKVRAETAekdreahlQFLKEKALLEKQLQELRI 128
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
436-645 |
1.56e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKY-TLEQDIRETEEAIrhktTEVQEMQNDLDRETSSLQE-LEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 513
Cdd:pfam10174 418 AGLKERVkSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 514 ESQMISSLQTQIHSQESD-------LQSQEEELGRAKADLNRLQ---QEEAQLEQSLQAG-----RIQ-LETIIKSLK-- 575
Cdd:pfam10174 494 KESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLEnqlKKAHNAEEAVRTNpeindRIRlLEQEVARYKee 573
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 576 --ATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKENGGFGAMEDPFKVK 645
Cdd:pfam10174 574 sgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE 645
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
446-577 |
1.65e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 39.91 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 446 QDIRETEEAIR---HKTTEVQEMQNDLDRETSSLQELeaqkqdAQDRLEemdqqkakLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:pfam07200 9 QELLNDEDKLDafvHSLPQVKALQAEKEELLAENESL------AEENLS--------LEPELEELRSQLQELLEELKALK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 523 TQIHSQESDLQSQEEELGRAkADLNRLQ-----QEEA--QLEQSLQAGRIQLETIIKSLKAT 577
Cdd:pfam07200 75 SEYEEKEQELDELLSKFSPD-ALLARLQaaaaeAEEEseALAESFLEGEIDLDEFLKQFKEK 135
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
461-592 |
1.72e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 461 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ-KAKLEDmLNDVRQKCQEEsQMISSLQtqihSQESDLQS----- 534
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRyKEKTQQ-LADVKTICEQE-ARIKDLE----AQRAQLQAgqpcp 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195109 535 -------------QEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKatQDEiNQARSKLSQIQ 592
Cdd:PRK10246 508 lcgstshpaveayQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQ--RDE-SEAQSLRQEEQ 575
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
420-639 |
1.78e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 420 SQEIAQLQSTLA---FTHWDTLREkYTLEQDIR---ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-KQDAQDRLEE 492
Cdd:COG5185 277 SKRLNENANNLIkqfENTKEKIAE-YTKSIDIKkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEiEQGQESLTEN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVR-----QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAD-LNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG5185 356 LEAIKEEIENIVGEVElskssEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIEELQRQIEQATSS 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195109 567 LETIIKSLKATQDEINQAR-----SKLSQIQDSQHEISKNIEQYSSTLNGTHggsmTNLADMSEGFPEKENGGFGAME 639
Cdd:COG5185 436 NEEVSKLLNELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEEL----TQIESRVSTLKATLEKLRAKLE 509
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
438-575 |
1.80e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQndlDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsqm 517
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAER---AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEE--- 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195109 518 isslqtqihsqesdLQSQEEELGRAKAdlNRLQQEEAQLEQSLQAGRIQLETIIKSLK 575
Cdd:cd16269 250 --------------RENLLKEQERALE--SKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
415-546 |
1.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 415 ELDDISQEIAQLQSTLafthwDTLREKY---------TLEQDIRETEEAIRHKTTEVQEMQNDLDR----ETSSLQELEA 481
Cdd:COG4913 310 ELERLEARLDALREEL-----DELEAQIrgnggdrleQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 482 QKQDAQDRLEEMD-------QQKAKLEDMLNDVRQKCQEESQMISSLQTQ---IHSQESDLQSQ-EEELGRAKADL 546
Cdd:COG4913 385 LRAEAAALLEALEeelealeEALAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDAlAEALGLDEAEL 460
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
436-593 |
2.05e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKYTLEQDIRETEeairHKTTEVQEMQNDLDRETSSLQELEAQKQD--------------AQDRLEEMDQQKAKLE 501
Cdd:pfam05622 4 EAQEEKDELAQRCHELD----QQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyllLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 502 DMLNDVRQKCQEesqmissLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSlqAGRI-QLETIIKSLKATQDE 580
Cdd:pfam05622 80 TARDDYRIKCEE-------LEKEV----LELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLED 146
|
170
....*....|...
gi 1207195109 581 INQARSKLSQIQD 593
Cdd:pfam05622 147 LGDLRRQVKLLEE 159
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
459-587 |
2.25e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.93 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 459 TTEVQEMQndldretsSLQELEAQKQDAQDRLEemdQQKakledMLNDVrqkcQEESQMISSLQTQIHSQ--ESDLQSQE 536
Cdd:PTZ00491 660 TTKSQEAA--------ARHQAELLEQEARGRLE---RQK-----MHDKA----KAEEQRTKLLELQAESAavESSGQSRA 719
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 537 EELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD-EINQARSK 587
Cdd:PTZ00491 720 EALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKRQElELEYEQAQ 771
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
444-518 |
2.42e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQelEAQKQDAQDRLEEMDQQ-KAKLEDMLNDVRQKCQEESQMI 518
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQKLQQDLQKRQQEELQKI 96
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
462-608 |
2.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 462 VQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV---------RQKCQE------ESQMISSLQTQIH 526
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvaRELLRRlreqrhLAEQLQQLRMRLS 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 527 SQESDLQSQeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEISKNIEQYS 606
Cdd:PRK04863 524 ELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE---QLQARIQRLA 599
|
..
gi 1207195109 607 ST 608
Cdd:PRK04863 600 AR 601
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
413-614 |
2.43e-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: 41.57 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIaQLQSTLafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLdreTSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR00606 363 IRARDSLIQSL-ATRLEL-----DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL---CADLQSKERLKQEQADEIRD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE---EAQL--EQSLQAGRIQL 567
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKkeVKSLQNEKADL 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 568 ETIIKSLKATQDEINQARSKLSQIQ-------DSQHEISKNIEQYSSTLNGTHG 614
Cdd:TIGR00606 514 DRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmDKDEQIRKIKSRHSDELTSLLG 567
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
452-603 |
2.57e-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: 41.70 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 452 EEAIRHKTTEVQEMQNDLDRETSS--------------LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEDERKQraqavaakkkleldLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagRIQL-ETIIKSLK---ATQDEINQARSKLSQIQD 593
Cdd:pfam01576 821 RDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----RDELaDEIASGASgksALQDEKRRLEARIAQLEE 896
|
170
....*....|
gi 1207195109 594 SQHEISKNIE 603
Cdd:pfam01576 897 ELEEEQSNTE 906
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
478-593 |
2.58e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 478 ELEAQKQDAQDRLEEMDQQKAKledmlndvRQKCQEESQ-MISSLqtqihsqesdlqsqEEELGRAKADLNRLQQEEAQL 556
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKK--------AQEELEESEeTAEEL--------------EEERRQAEEEAERLEQKRQEA 60
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207195109 557 EQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam20492 61 EEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEE 97
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
428-604 |
2.92e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 40.68 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 428 STLAFTHWDTLReKY--TLEQdIRETEEAIRHKtteVQEMQNDLDRETSSLQELEAQ--KQDAQDRLEEMDQQKAKLEDM 503
Cdd:pfam13949 71 SELTATLRAEIR-KYreILEQ-ASESDSQVRSK---FREHEEDLELLSGPDEDLEAFlpSSRRAKNSPSVEEQVAKLREL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 504 LNDVRQKCQEESQMISSLQTQIH------------------SQESDLqsQEEELGRAKADLNRLQQ---EEAQLEQSLQA 562
Cdd:pfam13949 146 LNKLNELKREREQLLKDLKEKARnddispklllekarliapNQEEQL--FEEELEKYDPLQNRLEQnlhKQEELLKEITE 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195109 563 GRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam13949 224 ANNEFLQDKRVDSEKQRQREEALQKLENAYDKYKELVSNLQE 265
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
444-601 |
2.98e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 40.38 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQ----------NDLDRETSSLQ----ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ 509
Cdd:pfam14932 72 LEESLEEIREATEDLEAELQELQktkqlkinrlNKLQAQASSLSqglrALVAEEEEAAKQLEELQEELAALNAKTNNVLQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 510 KCQEESQMISSLQTQIH-----SQeSDLQ---SQEEELGRAkadLNRLQQEeaQLEQSLQA-------GRIQLETIIKSL 574
Cdd:pfam14932 152 SLQSEVKELASFFSASEppvflSQ-LPLEpylLQEEQFTKY---LTLYTKK--QFFQGISElvefsneERFQLLDLSDCS 225
|
170 180
....*....|....*....|....*....
gi 1207195109 575 KATQDE--INQARSKLSQIQdSQHEISKN 601
Cdd:pfam14932 226 ERDSDEvdVEHRRSELARLQ-SAYICAQL 253
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
463-592 |
3.14e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.09 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 463 QEMQNDLDRETSSLQEleaQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:cd21116 76 PDLIELADNLIKGDQG---AKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNAL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207195109 543 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:cd21116 153 KNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAF 202
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
487-609 |
3.15e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.55 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 487 QDRLEEMDQQKAKLEDMLNDVRQKcqeesqmissLQTQIhSQESDLQSQE--EELGRAKADLN-RLQQEEAQLEQSLQAG 563
Cdd:pfam01442 3 EDSLDELSTYAEELQEQLGPVAQE----------LVDRL-EKETEALRERlqKDLEEVRAKLEpYLEELQAKLGQNVEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1207195109 564 RIQLETIIKSLKATQD-EINQARSKLSQ-IQDSQHEISKNIEQYSSTL 609
Cdd:pfam01442 72 RQRLEPYTEELRKRLNaDAEELQEKLAPyGEELRERLEQNVDALRARL 119
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
413-604 |
3.25e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQL----------------QSTLAFTHWdtlREKYT---------LEQDIRETEEAIRhkTTEVQEMQN 467
Cdd:PRK04778 31 IDELEERKQELENLpvndelekvkklnltgQSEEKFEEW---RQKWDeivtnslpdIEEQLFEAEELND--KFRFRKAKH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 468 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEESQM----ISSLQTQIHSQESDLQSQE 536
Cdd:PRK04778 106 EINEIESLLDLIEEDIEQILEELQELLESEEKnreeveqLKDLYRELRKSLLANRFSfgpaLDELEKQLENLEEEFSQFV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 537 E--ELG---RAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKAT-QDEINQARS---KL-------------SQIQDS 594
Cdd:PRK04778 186 EltESGdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAgyrELveegyhldhldieKEIQDL 261
|
250
....*....|
gi 1207195109 595 QHEISKNIEQ 604
Cdd:PRK04778 262 KEQIDENLAL 271
|
|
| ING_ING3_Yng2p |
cd16858 |
Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar ... |
444-526 |
3.29e-03 |
|
Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar proteins; ING3, also termed p47ING3, is a member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). Yeast chromatin modification-related protein Yng2p, also termed ESA1-associated factor 4 or ING1 homolog 2, is a subunit of the NuA4 histone acetyltransferase (HAT) complex. It plays a critical role in intra-S-phase DNA damage response. Members of this family contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain.
Pssm-ID: 341091 Cd Length: 92 Bit Score: 37.57 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELeAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:cd16858 4 LPSELRHLLTEIREKDLQVQELLDRIQQRDAKLFKH-IKKNGSLTPNPKEEELYEKIREDYDKALELADEKVELANRLLD 82
|
...
gi 1207195109 524 QIH 526
Cdd:cd16858 83 LVD 85
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-625 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 414 KELDDISQEIAQLQSTLafthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:pfam10174 296 QELSKKESELLALQTKL-----ETLTNQNSdCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEE-------AQLEQSLQagri 565
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALS---- 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 566 QLETIIKSLKATQDEINQARskLSQIQDSQHEIsKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:pfam10174 447 EKERIIERLKEQREREDRER--LEELESLKKEN-KDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
444-593 |
3.33e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNdvrqkcqEESQMISSLQT 523
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLA-------ELAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 524 QIHSQESDLQSQEEELGRAKADLNRLQQeeaQLEqslqAGRIQLETIIKSLKATQDEInqaRSKLSQIQD 593
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQ---QIA----ALRRQLAALEAALDASEKRD---RESQAKIAD 176
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
417-569 |
3.35e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.60 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 417 DDISQEIAQlqstlafthwDTLRekyTLEQDIRETEEAIRHKTTEVQEMQN-----DLDRETSSLQ----ELEAQKQDAQ 487
Cdd:COG3524 168 NQLSERARE----------DAVR---FAEEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 drleemdQQKAKLEDMLND----VRQKcqeESQmISSLQTQIHSQESDL--QSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG3524 235 -------AELAALRSYLSPnspqVRQL---RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYT 303
|
....*...
gi 1207195109 562 AGRIQLET 569
Cdd:COG3524 304 SALAALEQ 311
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
482-585 |
3.53e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.71 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 482 QKQDAQDRLEEM-DQQKAKLEDMLNDVRQkcqeesqMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEeaqLEQSL 560
Cdd:pfam03938 16 EGKAAQAQLEKKfKKRQAELEAKQKELQK-------LYEELQKDGALLEEEREEKEQELQKKEQELQQLQQK---AQQEL 85
|
90 100
....*....|....*....|....*.
gi 1207195109 561 QAGRIQL-ETIIKSLKATQDEINQAR 585
Cdd:pfam03938 86 QKKQQELlQPIQDKINKAIKEVAKEK 111
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
444-591 |
3.70e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 39.70 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQT 523
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 524 QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAEssIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
537-610 |
3.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195109 537 EELGRAKADLNRLQQEE----AQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4372 6 EKVGKARLSLFGLRPKTgiliAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
439-539 |
4.16e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 439 REKYTLEQdirETEEAIRHKTT---EVQEMQNDLDRETSSLQELEA-------QKQDAQDRLEEMDQQKAKLE----DML 504
Cdd:pfam10473 31 RELEMSEE---NQELAILEAENskaEVETLKAEIEEMAQNLRDLELdlvtlrsEKENLTKELQKKQERVSELEslnsSLE 107
|
90 100 110
....*....|....*....|....*....|....*
gi 1207195109 505 NDVRQKCQEESQMISSLQTQIHSqesdLQSQEEEL 539
Cdd:pfam10473 108 NLLEEKEQEKVQMKEESKTAVEM----LQTQLKEL 138
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
436-600 |
4.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 436 DTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdqQKAKLEDMLND------VR 508
Cdd:PHA02562 216 ARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKMYEKggvcptCT 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 509 QKCQEESQMISSLQTQIHS---QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA- 584
Cdd:PHA02562 292 QQISEGPDRITKIKDKLKElqhSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELq 371
|
170 180
....*....|....*....|..
gi 1207195109 585 ------RSKLSQIQDSQHEISK 600
Cdd:PHA02562 372 aefvdnAEELAKLQDELDKIVK 393
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
495-593 |
4.27e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 495 QQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEE---------------------ELGRAKADLNRLQQEE 553
Cdd:pfam07926 1 AELSSLQSEIKRLKEE-------AADAEAQLQKLQEDLEKQAEiareaqqnyerelvlhaedikALQALREELNELKAEI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207195109 554 AQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL-SQIQD 593
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKELEKELSELeKRIED 114
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
465-590 |
4.43e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 37.95 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 465 MQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR------QKCQEESQMISSLQT-QIHSQESDLqsqEE 537
Cdd:COG1382 1 MMQNLPPE---VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEkaleelEKLPDDAEVYKSVGNlLVKTDKEEV---IK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 538 ELGRAKADLN-RLQQEEAQLEqslqagRIQletiiKSLKATQDEINQARSKLSQ 590
Cdd:COG1382 75 ELEEKKETLElRLKTLEKQEE------RLQ-----KQLEELQEKLQEALSGAGG 117
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
444-525 |
4.83e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-QDRLEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQ 522
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQQELQ------KKQQELLQPIQ 97
|
...
gi 1207195109 523 TQI 525
Cdd:pfam03938 98 DKI 100
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
463-555 |
4.94e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 463 QEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ 224
|
90
....*....|...
gi 1207195109 543 KAdlNRLQQEEAQ 555
Cdd:PRK11448 225 AA--KRLELSEEE 235
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
523-601 |
5.26e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 5.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195109 523 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKN 601
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATAQA 325
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
488-604 |
5.35e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 38.37 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 488 DRLEEMDQQKAKLEDMLNDVRQkCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQL 567
Cdd:pfam07200 6 EELQELLNDEDKLDAFVHSLPQ-VKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKSEYEEKEQEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207195109 568 ETIIK--SLKATQDEINQARSKlsqiqdsQHEISKNIEQ 604
Cdd:pfam07200 85 DELLSkfSPDALLARLQAAAAE-------AEEESEALAE 116
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
527-593 |
5.38e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.77 E-value: 5.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQE 67
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
472-605 |
5.40e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.22 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 472 ETSSLQELEAQKQDAQD--RLEEMDQQKAklEDMLNDVRQKCQEEsqmisslqtQIHSQESDLQSQEEELGRAKADLNRL 549
Cdd:COG3524 135 STSGIITLEVRAFDPEDaqAIAEALLAES--EELVNQLSERARED---------AVRFAEEEVERAEERLRDAREALLAF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 550 QQEE----------------AQLEQSLQAGRIQLETI----------IKSLK----ATQDEINQARSKLSQiQDSQHEIS 599
Cdd:COG3524 204 RNRNgildpeataeallqliATLEGQLAELEAELAALrsylspnspqVRQLRrriaALEKQIAAERARLTG-ASGGDSLA 282
|
....*.
gi 1207195109 600 KNIEQY 605
Cdd:COG3524 283 SLLAEY 288
|
|
| DivIC |
pfam04977 |
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ... |
527-588 |
5.53e-03 |
|
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.
Pssm-ID: 428231 [Multi-domain] Cd Length: 69 Bit Score: 36.43 E-value: 5.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195109 527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEI-NQARSKL 588
Cdd:pfam04977 3 NGLLTYYQLKQEIAQLQAEIAKLKQENEELEAE-----------IKDLKSDPDYIeERARSEL 54
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
413-515 |
5.77e-03 |
|
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: 39.62 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 413 IKELDDISQEIAQLQSTLAfthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:smart00787 188 LRQLKQLEDELEDCDPTEL----DRAKEKLKkLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
90 100
....*....|....*....|....
gi 1207195109 492 EMDQQKAKLEDMLNDVRQKCQEES 515
Cdd:smart00787 264 QCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
468-593 |
6.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 468 DLDRETSSLQELEAQKQDAQDRLEEMDQ---QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207195109 545 DLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEINQARSKLSQIQD 593
Cdd:PRK04863 580 RRMALRQQLEQLQAR-----------IQRLAARAPAWLAAQDALARLRE 617
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
141-188 |
6.17e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.85 E-value: 6.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1207195109 141 NGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMH 188
Cdd:COG5126 83 DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
456-561 |
6.29e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.43 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 456 RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQ--EESQmiSSLQTQIHSQ-ES-- 530
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELAslKESN--SLAETQLKCMaESye 754
|
90 100 110
....*....|....*....|....*....|.
gi 1207195109 531 DLQSQEEELgraKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam05911 755 DLETRLTEL---EAELNELRQKFEALEVELE 782
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
455-582 |
6.40e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 39.55 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 455 IRHKTTEVQEMQNDLDRETSSLQELeaqKQDAQDrleeMDQQKA-KLEDMLndvrQKcQEESQMISSL-----QTQIHSQ 528
Cdd:pfam15397 1 IRNRRTSLEELKKHEDFLTKLNLEL---IKAIQD----TEDSTAlKVRKLL----QQ-YEKFGTIISIleysnKKQLQQA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1207195109 529 ESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAgriqletiikslkaTQDEIN 582
Cdd:pfam15397 69 KAELQEWEEKE---ESKLNKLEQQLEQLNAKIQK--------------TQEELN 105
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
461-598 |
7.13e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 461 EVQEMQNDLDRETSSLQE---LEAqKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEE 537
Cdd:PRK00106 54 DAEHIKKTAKRESKALKKellLEA-KEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQ 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195109 538 ELGRAKADLNRLQQEEAQLEQSLQA--GRIQLETI--IKSLKATQDEINQARSKLSQIQDSQHEI 598
Cdd:PRK00106 133 SLTDKSKHIDEREEQVEKLEEQKKAelERVAALSQaeAREIILAETENKLTHEIATRIREAEREV 197
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
443-514 |
7.22e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.77 E-value: 7.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLndvrQKCQEE 514
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKL----RKLQEE 68
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
521-592 |
7.28e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.54 E-value: 7.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:COG0845 59 LQAALAQAQAQLAAAQAQLELAKAELERYK----ALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQAR 126
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
489-597 |
7.48e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 38.04 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 489 RLEEMDQQKAKLEDMLNDVRQKCQEESQ-------------MISSLQTQIHSQESDLQSQEEEL-----------GRA-K 543
Cdd:pfam17098 12 RLAEKEQEIQELKAQLQDLKQSLQPPSSqlrsllldpavnlEFLRLKKELEEKKKKLKEAQLELaawkftpdsttGKRlM 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195109 544 ADLNRLQQEEAQLEQSLQAGRIQ-LET-------IIKSLKATQDEINQARSKLSQIQDSQHE 597
Cdd:pfam17098 92 AKCRLLQQENEELGRQLSEGRIAkLEIelalqkkVVEELKKSLEELDEFLIELDEELEGLQS 153
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
438-568 |
8.06e-03 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 39.83 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQND----------LDRETSSLQELEAQKQDAQDRLEEMDQQkAKLEdmlndv 507
Cdd:PRK10865 353 LKERYELHHHVQITDPAIVAAATLSHRYIADrqlpdkaidlIDEAASSIRMQIDSKPEELDRLDRRIIQ-LKLE------ 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195109 508 RQKCQEES-----QMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagRIQLE 568
Cdd:PRK10865 426 QQALMKESdeaskKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQA----KIAIE 487
|
|
| HlyE-like |
cd22651 |
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, ... |
471-603 |
8.22e-03 |
|
alpha pore-forming toxin (alpha-PFT) hemolysin E (HlyE, ClyA or SheA) in Escherichia coli, Salmonella typhi, and Shigella flexneri, and similar proteins; This family of alpha pore-forming toxins (alpha-PFTs) includes hemolysin E (HlyE; also called cytolysin (ClyA) or silent hemolysin A (SheA)), produced by certain strains of Escherichia coli, as well as by Salmonella enterica and Shigella flexneri, among others. HlyE is responsible for the hemolytic activity of certain strains of E. coli, including the pathogenic strain E. coli O157. Distinct from many secreted toxins and effectors, HlyE is delivered by outer-membrane vesicles (OMVs). HlyE is unrelated to the well-characterized pore-forming E. coli hemolysins of the RTX (repeats in toxin) family, hemolysin A (HlyA), and the enterohemolysin encoded by the plasmid borne ehxA gene of E. coli 0157. However, they all have the common structural features of an elongated, entirely alpha-helical domain, except for a short hydrophobic beta-hairpin known as the beta-tongue. The HlyE is monomeric in the periplasm where it forms a disulfide bond to prevent oligomerization. In the OMVs, it oligomerizes via a sequential mechanism to form a circular dodecameric pore structure that is active. The pore structure concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. HlyE/ClyA represents a prototype of the structural ClyA family of alpha-PFT which includes toxins that share structural similarity with HlyE, and includes Bacillus cereus HblB, Aeromonas hydrophila AhlB, and Bacillus thuringiensis Cry6Aa. Expression of HlyE in the absence of the RTX toxins is sufficient to give a hemolytic phenotype in E. coli. HlyE is expressed during anaerobic growth of E. coli. Anaerobic expression is controlled by the transcription factor, FNR (regulator of fumarate and nitrate reduction), such that, upon ingestion and entry into the anaerobic mammalian intestine, HlyE is produced and may then contribute to the colonization of the host.
Pssm-ID: 439354 Cd Length: 247 Bit Score: 38.82 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 471 RETSSLQELEAQK----QDAQDRLEEMDQQKAKLEDmlndVRQKCQEESQMISSLQTQIHSqesDLQSQEEElGRAKADL 546
Cdd:cd22651 88 IQDYNLKDADAQKnilvKVLTDGIKKLGEALELLEV----VSNHFNEASGKLTALLHQLTN---DFGPKSFY-GKQQVDK 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195109 547 NRLQQEeaqLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIE 603
Cdd:cd22651 160 IRKAPE---LKEQLETIQTFFTTLTDKVKSASKIIDEAKSALEEEISNIGELKGTRE 213
|
|
| BBC |
smart00502 |
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains |
384-542 |
8.56e-03 |
|
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
Pssm-ID: 128778 Cd Length: 127 Bit Score: 37.24 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 384 MAALTEMRRAIMFKLWDSSSSvgsgeftgIKELDDISQEIaqlQSTLAfthwdtlrekyTLEQDIRETEEAIRhktTEVQ 463
Cdd:smart00502 2 REALEELLTKLRKKAAELEDA--------LKQLISIIQEV---EENAA-----------DVEAQIKAAFDELR---NALN 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 464 EmqndldRETSSLQELEAQKqdaQDRLEEMDQQKAKLEDMLNDVRQKCQE-ESQMISSLQTQI-HSQESDLQsQEEELGR 541
Cdd:smart00502 57 K------RKKQLLEDLEEQK---ENKLKVLEQQLESLTQKQEKLSHAINFtEEALNSGDPTELlLSKKLIIE-RLQNLLK 126
|
.
gi 1207195109 542 A 542
Cdd:smart00502 127 Q 127
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
444-563 |
9.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 444 LEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQE-----LEAQKQDAQDRLEEMdqqKAKLEDMLNDVRQKCQEEsqmi 518
Cdd:PRK00409 532 LEQKAEEAEALLK----EAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEA---KKEADEIIKELRQLQKGG---- 600
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207195109 519 sslQTQIHSQEsdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:PRK00409 601 ---YASVKAHE--LIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
421-656 |
9.77e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 39.81 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 421 QEIAQLQSTLAFTHWDTLREKYTLEqDIRETEEAIRHKTTEVQEMQ--------NDLDRETSSLQELEaqkqdaqdrlEE 492
Cdd:PTZ00440 638 QELLDELSHFLDDHKYLYHEAKSKE-DLQTLLNTSKNEYEKLEFMKsdnidniiKNLKKELQNLLSLK----------EN 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 493 MdqqkakLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE----EAQLEQSLQAGRIQLE 568
Cdd:PTZ00440 707 I------IKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEfilhLYENDKDLPDGKNTYE 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195109 569 TIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY---SSTLNGTHGGSMTNLADMSEGFPEK-ENGGFGAMEDPFKV 644
Cdd:PTZ00440 781 EFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYnilIQKLEAHTEKNDEELKQLLQKFPTEdENLNLKELEKEFNE 860
|
250
....*....|..
gi 1207195109 645 KPTVFNSAPQEM 656
Cdd:PTZ00440 861 NNQIVDNIIKDI 872
|
|
|