|
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: 141.65 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 120 WAVRPEEKSKFDGIFESLAP-VNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 198
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 1207195097 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 |
5.06e-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: 128.55 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 270 NWVVPVADRGRYDDIFLKTDSDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSkG 349
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79
|
90
....*....|....*..
gi 1207195097 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 |
1.81e-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: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 124 PEEKSKFDGIFESLAPVNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPS 201
Cdd:pfam12763 6 EWEIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPD 85
|
90
....*....|..
gi 1207195097 202 VLPSSLIPPSKR 213
Cdd:pfam12763 86 ELPDWLVPGSKA 97
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
130-195 |
5.84e-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: 5.84e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 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 |
4.78e-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: 4.78e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 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 |
1.79e-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: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 11 SSGNPVYENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQSGHDISIS 90
Cdd:smart00027 6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85
|
90
....*....|.
gi 1207195097 91 SLNLPVPPPKF 101
Cdd:smart00027 86 LPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
17-83 |
3.97e-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: 3.97e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 17 YENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQS 83
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-597 |
1.70e-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: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 411 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 489
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 490 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 569
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180
....*....|....*....|....*...
gi 1207195097 570 TQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
404-588 |
4.48e-19 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 90.35 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 404 TGIKELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 483
Cdd:COG4372 35 KALFELDKLQEELEQLREELE-----------QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagRIQLETI 563
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEA 181
|
170 180
....*....|....*....|....*
gi 1207195097 564 IKSLKATQDEINQARSKLSQIQDSQ 588
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAE 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-604 |
4.60e-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: 93.20 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTH--WDTLREK-YTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 483
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEkaLAELRKElEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETI 563
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207195097 564 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 604
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-603 |
5.05e-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: 89.73 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 411 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 489
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 490 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 569
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190
....*....|....*....|....*....|....
gi 1207195097 570 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-597 |
7.75e-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: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:COG1196 267 AELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 566
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190
....*....|....*....|....*....|.
gi 1207195097 567 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
441-599 |
4.56e-17 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 84.18 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 441 IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHS 520
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 521 QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 599
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-597 |
1.12e-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: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 566
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190
....*....|....*....|....*....|.
gi 1207195097 567 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-597 |
1.99e-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: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 487
Cdd:COG1196 275 ELEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSL 567
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190
....*....|....*....|....*....|
gi 1207195097 568 KATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-597 |
4.64e-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: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEm 486
Cdd:COG4942 27 AELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 dqQKAKLEDMLN-----------DVRQKCQEESQMISSLQ-------------TQIHSQESDLQSQEEELGRAKADLNRL 542
Cdd:COG4942 102 --QKEELAELLRalyrlgrqpplALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 543 QQEEAQLEQSLQAGRIQLETIIKSLKAtqdEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-597 |
5.68e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 385 AALTEMR------RDSSSSVGSGEFTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEM 458
Cdd:COG1196 267 AELEELRleleelELELEEAQAEEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 459 QNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAD 538
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 539 LNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-602 |
5.37e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.43 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAftHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQDAQDR 482
Cdd:COG4717 70 LKELKELEEELKEAEEKEE--EYAELQEELeELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDL-QSQEEELGRAKADLNRLQQEEAQLEQslqagriqle 561
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEE---------- 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195097 562 tiikSLKATQDEINQARSKLSQIQDSQ--HEISKNIEQYSSTL 602
Cdd:COG4717 214 ----ELEEAQEELEELEEELEQLENELeaAALEERLKEARLLL 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-597 |
8.13e-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: 79.33 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:TIGR02168 239 EELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADL----NRLQQEEAQLEQsLQAGRIQLEt 562
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeeleSRLEELEEQLET-LRSKVAQLE- 392
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195097 563 iiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:TIGR02168 393 --LQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
436-625 |
1.34e-14 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 76.48 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 515
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 516 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIqdSQHEISKNI 595
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL--SEAEAEQAL 185
|
170 180 190
....*....|....*....|....*....|
gi 1207195097 596 EQYSSTLNGTHGGSMTNLADMSEGFPEKEN 625
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
437-581 |
1.48e-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: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-----QKCQEEsqmI 511
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKE---I 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 512 SSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 581
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-597 |
1.24e-13 |
|
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: 75.48 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTH--WDTLR-EKYTLEQDIRETEEA-------IRHKTTEVQEMQNDLDRETSSLQELEAQK 476
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEekLEELRlEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 477 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAG 556
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195097 557 RIQLETIIKSLKATQDEINQARSKLS--QIQDSQHEISKNIEQ 597
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEE 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
406-599 |
2.39e-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: 74.33 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEE 485
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 562
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiQELQEQRIDLKE 847
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195097 563 IIKSLKATQDEIN-QARSKLSQIQDSQHEISKNIEQYS 599
Cdd:TIGR02169 848 QIKSIEKEIENLNgKKEELEEELEELEAALRDLESRLG 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-603 |
5.56e-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: 73.18 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 399 GSGEFTGIKE-LDDISQEIAQLQSTLAFTH---WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 474
Cdd:TIGR02169 285 GEEEQLRVKEkIGELEAEIASLERSIAEKErelEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 475 QKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLq 554
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195097 555 agriqletiikslKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:TIGR02169 444 -------------EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-597 |
1.93e-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: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAftHWDTLREKYTLEQDIRETEEAIRHKT--TEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 484
Cdd:COG4913 242 EALEDAREQIELLEPIRE--LAERYAAARERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 485 EMDQQKAKLEdmlndvRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ----L 560
Cdd:COG4913 320 ALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalL 393
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207195097 561 ETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
385-585 |
2.91e-12 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 70.43 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 385 AALTEMRRDSSSSVGSGEFTGI-KELDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIRETEEAIR--HKTTEVQEMQN 460
Cdd:COG3206 196 AALEEFRQKNGLVDLSEEAKLLlQQLSELESQLAEARAELA-----EAEARLaALRAQLGSGPDALPelLQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQTQI---HSQESDLQSQEEELGRAKA 537
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ------QEAQRILASLEAELealQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195097 538 DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-595 |
3.32e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQE-------LEAQKQDA 479
Cdd:TIGR02168 719 KELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeieeLEAQIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ 559
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207195097 560 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNI 595
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-597 |
9.44e-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: 68.89 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKakledmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKS 566
Cdd:TIGR04523 390 ESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV----KELIIKN 458
|
170 180 190
....*....|....*....|....*....|.
gi 1207195097 567 LKATQDEINQarsKLSQIQDSQHEISKNIEQ 597
Cdd:TIGR04523 459 LDNTRESLET---QLKVLSRSINKIKQNLEQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-597 |
1.92e-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: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQ-DRLE 484
Cdd:COG4913 262 ERYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETII 564
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 565 KSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-598 |
3.46e-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: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 424 AFTHWDT--LREKYTLEQDireTEEAIRHKTTEVQEMQNDLdretsslQELEAQKQDAQDRLEEMDQQKAKLEDMLNDvr 501
Cdd:COG4913 589 RHEKDDRrrIRSRYVLGFD---NRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEY-- 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 502 qkcQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 581
Cdd:COG4913 657 ---SWDEIDVASAEREI----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170
....*....|....*..
gi 1207195097 582 SQIQDSQHEISKNIEQY 598
Cdd:COG4913 730 DELQDRLEAAEDLARLE 746
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
407-555 |
6.96e-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: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK--QDAQDRLE 484
Cdd:COG1579 31 AELAELEDELAALEARLE-----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQA 555
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-597 |
8.81e-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: 66.24 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAIRHKTTE----VQEMQNDLDRETSSLQELEAQKQDAQd 481
Cdd:TIGR02169 244 RQLASLEEELEKLTEEI-----SELEKRLeEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKEREL- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 482 rlEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE 561
Cdd:TIGR02169 318 --EDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207195097 562 TIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-588 |
9.11e-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: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:COG1196 323 EELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH---SQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETI 563
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAeleEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180
....*....|....*....|....*
gi 1207195097 564 IKSLKATQDEINQARSKLSQIQDSQ 588
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-586 |
9.19e-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: 65.81 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQStlafthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:TIGR04523 376 KKENQSYKQEIKNLES-----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 565
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKIS 520
|
170 180
....*....|....*....|....*
gi 1207195097 566 SLKATQD----EINQARSKLSQIQD 586
Cdd:TIGR04523 521 SLKEKIEklesEKKEKESKISDLED 545
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
437-596 |
1.19e-10 |
|
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: 65.43 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 516
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 517 QIH------SQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQLET-------IIKSLKATQDEINQARSKLSQ 583
Cdd:TIGR04523 209 KIQknksleSQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNQlkdeqnkIKKQLSEKQKELEQNNKKIKE 285
|
170
....*....|...
gi 1207195097 584 IQDSQHEISKNIE 596
Cdd:TIGR04523 286 LEKQLNQLKSEIS 298
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
408-607 |
1.79e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqelEAQKQDAQDRLEEMD 487
Cdd:PRK02224 252 ELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakadlnrLQQEEAQLEQSLQAGRIQLETIIKSL 567
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEE----------LREEAAELESELEEAREAVEDRREEI 386
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207195097 568 KATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHG 607
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
459-597 |
3.38e-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: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 459 QNDLDRETSS-LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 537
Cdd:COG4942 18 QADAAAEAEAeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 538 DLNRLQQEEAQL-------------------EQSLQAGRI---------QLETIIKSLKATQDEINQARSKLSQIQDSQH 589
Cdd:COG4942 98 ELEAQKEELAELlralyrlgrqpplalllspEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
|
....*...
gi 1207195097 590 EISKNIEQ 597
Cdd:COG4942 178 ALLAELEE 185
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-597 |
4.33e-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: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEI-AQL-----QSTLAfthwdtlrEKYtleQDIRETEEAIrhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 482
Cdd:COG1196 191 LEDILGELeRQLeplerQAEKA--------ERY---RELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAdlnRLQQEEAQLEQSLQagriQLET 562
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEE----ELAE 327
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195097 563 IIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
428-597 |
4.55e-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: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 428 WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEeMDQQKAKLEDmLNDVRQKCQEE 507
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAE-LEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 508 SQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 587
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170
....*....|
gi 1207195097 588 QHEISKNIEQ 597
Cdd:COG4913 764 ERELRENLEE 773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-557 |
5.30e-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: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 403 FTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRhkTTEVQEMQNDLDRetssLQELEAQKQDAQDR 482
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELA----RLEAELERLEARLDALREELD--ELEAQIRGNGGDR----LEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQ----EEELGRAKADLNRLQQEEAQLEQ---SLQA 555
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEElealEEALAEAEAALRDLRRELRELEAeiaSLER 433
|
..
gi 1207195097 556 GR 557
Cdd:COG4913 434 RK 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
406-601 |
5.64e-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: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLafthwDTLREKY--------TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQE------ 471
Cdd:COG3883 29 QAELEAAQAELDALQAEL-----EELNEEYnelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 472 -----LEAQK-QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE 545
Cdd:COG3883 104 yldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 546 EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSST 601
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
469-597 |
7.59e-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: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 469 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---------DL 539
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEY 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 540 NRLQQEEA-------QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG1579 92 EALQKEIEslkrrisDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
438-588 |
1.03e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 438 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE-SQMISS 513
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 514 LQTQ------------------------------------IHSQESD---LQSQEEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:COG3883 95 LYRSggsvsyldvllgsesfsdfldrlsalskiadadadlLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|....
gi 1207195097 555 AGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 588
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
407-603 |
1.19e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 60.70 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAirhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRL- 483
Cdd:pfam00038 61 RQLDTLTVERARLQLELdnLRLAAEDFRQKYEDELNLRTSAEN------DLVGLRKDLDEATLARVDLEAKIESLKEELa 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 -------EEMDQQKAKLED-----------------MLNDVR-------QKCQEESQM-----ISSLQTQIHSQESDLQS 527
Cdd:pfam00038 135 flkknheEEVRELQAQVSDtqvnvemdaarkldltsALAEIRaqyeeiaAKNREEAEEwyqskLEELQQAAARNGDALRS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 528 QEEELgrakADLNR-LQQEEAQLeQSLQAGRIQLETIIKSLKATQD-EINQARSKLS----QIQDSQHEISKNIEQYSST 601
Cdd:pfam00038 215 AKEEI----TELRRtIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQEL 289
|
..
gi 1207195097 602 LN 603
Cdd:pfam00038 290 LN 291
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
474-603 |
1.29e-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: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 474 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 553
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195097 554 QAGRIQLETIIKS-----------LKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:COG4942 100 EAQKEELAELLRAlyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-597 |
2.18e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQnDLDRETSSLQE-------LEAQKQDA 479
Cdd:PRK03918 231 KELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEkaeeyikLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQM------ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEqSL 553
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKeerleeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-GL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207195097 554 QAGRI--QLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:PRK03918 385 TPEKLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-585 |
2.64e-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: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLA-----FTHWDTLREKYTLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 482
Cdd:COG4913 625 ELAEAEERLEALEAELDalqerREALQRLAEYSWDEIDVASAEREIA----ELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqlet 562
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE-------- 772
|
170 180
....*....|....*....|...
gi 1207195097 563 iiKSLKATQDEINQARSKLSQIQ 585
Cdd:COG4913 773 --ERIDALRARLNRAEEELERAM 793
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-598 |
2.94e-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: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL-- 483
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEE-----KLKERLEeLEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsh 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 ----------EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQES---DLQSQEEELGRAKADLN---------- 540
Cdd:TIGR02169 791 sripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNgkkeeleeel 870
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 541 -RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ-------ARSKLSQIQDSQHEISKNIEQY 598
Cdd:TIGR02169 871 eELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqiekKRKRLSELKAKLEALEEELSEI 936
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
433-624 |
3.19e-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: 59.39 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaQKQDAQDRLEEmdqQKAKLEDMLNDVRQKCQEESQMIS 512
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSRE---QLQELEEQLAT---ERSARREAEAELERLQEELRYLEE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 513 SLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQagriQL-ETIIKS---LKATQDEINQARSKL---- 581
Cdd:pfam09787 129 ELRRSKATLQSRIKDREAEIEKLRNQLTSKSQsssSQSELENRLH----QLtETLIQKqtmLEALSTEKNSLVLQLerme 204
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195097 582 SQIQDSQHEISKNIeqySSTLNGTHGGSMTNLADMSEGFPEKE 624
Cdd:pfam09787 205 QQIKELQGEGSNGT---SINMEGISDGEGTRLRNVPGLFSESD 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
407-588 |
3.51e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE----MQND-------------------LD 463
Cdd:COG3883 44 AELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGEraraLYRSggsvsyldvllgsesfsdfLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 464 RETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN 540
Cdd:COG3883 120 RLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195097 541 RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 588
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
469-604 |
3.68e-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: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 469 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqesDLQSQEEELGRAKADLNRLQQEEAQ 548
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 549 LEQsLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 604
Cdd:COG4913 687 LAA-LEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
415-593 |
3.98e-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: 60.52 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 415 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 494
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 495 DMLNDVRQKCQEES---QMISSLQTQIHSQESDlqsqEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETIIKSLKATQ 571
Cdd:pfam05557 153 QLRQNLEKQQSSLAeaeQRIKELEFEIQSQEQD----SEIVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLK 227
|
170 180
....*....|....*....|..
gi 1207195097 572 DEINQARSKLSQIQDSQHEISK 593
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAAT 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-597 |
5.94e-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: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQT 516
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 517 QIHSQESDLQ-------------------SQEE--ELGR--------AKADLNRLQQEEAQLEQsLQAGRIQLETIIKSL 567
Cdd:COG4942 98 ELEAQKEELAellralyrlgrqpplalllSPEDflDAVRrlqylkylAPARREQAEELRADLAE-LAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1207195097 568 KATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
407-590 |
5.96e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:COG3883 23 KELSELQAELEAAQAELD-----------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 --DQQKA-----KLEDMLNdvrqkcqeeSQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAG 556
Cdd:COG3883 92 arALYRSggsvsYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEaklAELEAL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1207195097 557 RIQLETIIKSLKATQDEINQARSKLSQIQDSQHE 590
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
406-602 |
6.01e-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: 59.98 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQDiRETEEAIRHKTTEVQEM---QNDLDRETSSLQELEAQKQDAQDR 482
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALH-------ALQLTLTQE-RVREHALSIRVLPKELLasrQLALQKMQSEKEQLTYWKEMLAQC 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI-----------HSQESDLQSQEEELGRAK----ADLNRLQQEEa 547
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdalnqslkelmHQARTVLKARTEAHFNNNeevtAALQTGAELS- 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 548 QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSSTL 602
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRL 837
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
419-606 |
6.27e-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: 60.08 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 419 LQSTLAFTHWDTLRE---KY---TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 492
Cdd:TIGR02169 620 FGDTLVVEDIEAARRlmgKYrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 493 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqleTIIKSLKATQD 572
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-------ELEARIEELEE 772
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195097 573 EINQARSKLSQIQDS-QHEISKNIEQYSSTLNGTH 606
Cdd:TIGR02169 773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEV 807
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-602 |
7.97e-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: 59.65 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQST------------LAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 474
Cdd:TIGR04523 426 KEIERLKETIIKNNSEikdltnqdsvkeLIIKNLDNTRES--LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 475 QKQDAQDRLEEMDQQKAKLEdmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA--KADLNRLQQEEAQLEQS 552
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLK-------EKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQT 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 553 lqagriqletiIKSLKATQDEINQarsKLSQIQDSQHEISKNIEQYSSTL 602
Cdd:TIGR04523 577 -----------QKSLKKKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKI 612
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
434-603 |
1.01e-08 |
|
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: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 434 KYTLEQDIRETEEAIRHKTTEVQEMQNDLD---------RETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKc 504
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 505 qeesqmISSLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQEEAQLEQSLQAG-------RIQLETIIKSLKATQDEI- 574
Cdd:COG3206 242 ------LAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRIl 315
|
170 180
....*....|....*....|....*....
gi 1207195097 575 NQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
407-582 |
1.24e-08 |
|
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: 58.37 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLafthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEM 486
Cdd:pfam07888 104 KELSASSEELSEEKDAL-------LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKS 566
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQER 245
|
170
....*....|....*.
gi 1207195097 567 LKATQDEINQARSKLS 582
Cdd:pfam07888 246 LNASERKVEGLGEELS 261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-596 |
1.25e-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: 58.88 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLafthwdtlrEKytLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqELEAQKQDAQDRLEEM 486
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI---------EK--LESEKKEKESKISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEEL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqLETIIKS 566
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQE 646
|
170 180 190
....*....|....*....|....*....|....
gi 1207195097 567 LKATQDEINQARSKLSQI----QDSQHEISKNIE 596
Cdd:TIGR04523 647 VKQIKETIKEIRNKWPEIikkiKESKTKIDDIIE 680
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
438-636 |
1.55e-08 |
|
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: 58.90 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 438 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------------RLEEMD----QQKAKLEDM---- 496
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtimerfqmELKDVErkiaQQAAKLQGSdldr 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 497 -LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ-AGRI--QLETIIKSLKATQD 572
Cdd:TIGR00606 823 tVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrRQQFeeQLVELSTEVQSLIR 902
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 573 EINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKenggFGAMEDPFK 636
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI----HGYMKDIEN 962
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
461-603 |
1.56e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-RAKA-- 537
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeRARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 538 --------------------------DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEI 591
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA---EL 173
|
170
....*....|..
gi 1207195097 592 SKNIEQYSSTLN 603
Cdd:COG3883 174 EAQQAEQEALLA 185
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
409-587 |
2.35e-08 |
|
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: 57.60 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQ 488
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 489 QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLK 568
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170
....*....|....*....
gi 1207195097 569 ATQDEINQARSKLSQIQDS 587
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDT 214
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
407-605 |
2.87e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLqstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMqNDLDRETSS-----LQELEAQKQDaqD 481
Cdd:PRK02224 579 SKLAELKERIESL---------ERIRTLLAAIADAEDEIERLREKREALAEL-NDERRERLAekrerKRELEAEFDE--A 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 482 RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelgrakadLNRLQQEEAQLEQSLQAgriqLE 561
Cdd:PRK02224 647 RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-----------LEELRERREALENRVEA----LE 711
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195097 562 TIIKSLKATQDEINQARSKLSQiqdsqheisKNIEQYSSTLNGT 605
Cdd:PRK02224 712 ALYDEAEELESMYGDLRAELRQ---------RNVETLERMLNET 746
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
407-597 |
3.35e-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: 57.17 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdtlrekytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:pfam06160 237 KEIQQLEEQLEENLALLE-------------NLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQ---EESQMISSLQTQIHSQESDLQSQEEELGRAKAD----LNRLQQEEAQLEQsLQAgriQ 559
Cdd:pfam06160 304 EEQNKELKEELERVQQSYTlneNELERVRGLEKQLEELEKRYDEIVERLEEKEVAyselQEELEEILEQLEE-IEE---E 379
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195097 560 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-554 |
3.60e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAFTHWDTLREKYT-------LEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQD 478
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEqaeeyqeLKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEE 443
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 479 AQDRLEEMDQQKAKLEDMLNDVrqkcqEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:COG4717 444 LEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
423-598 |
3.79e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 423 LAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR-------ETSSLQELEAQKQDAQDRLEEMDQQKAKLE- 494
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQl 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 495 ----------------DMLNDVRQKCQEESQMISsLQTQIHSQESDLQSQEEELGR--AKADLNRLQQEEAQLEQSLQAG 556
Cdd:COG4717 366 eeleqeiaallaeagvEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEEL 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195097 557 RIQLETIIKSLKATQDEINQARS--KLSQIQDSQHEISKNIEQY 598
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
481-597 |
3.80e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 DRLEEMDQqKAKLEdmLNDVRQKcqeESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE----EAQLEQS---L 553
Cdd:COG4372 2 DRLGEKVG-KARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207195097 554 QAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
407-563 |
4.58e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEiAQLQstlAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDR 482
Cdd:PRK12704 49 KEAEAIKKE-ALLE---AKEEIHKLRNE--FEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLET 562
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQA 197
|
.
gi 1207195097 563 I 563
Cdd:PRK12704 198 I 198
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-546 |
4.85e-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: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 378 TPVGSDMAALTEMRRDSSSSVGSGEftgiKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE 457
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVD----KEFAETRDELKDYREKLE----KLKREINELKRELDRLQEELQRLSEELAD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 458 MQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKA 537
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEA 497
|
....*....
gi 1207195097 538 DLNRLQQEE 546
Cdd:TIGR02169 498 QARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-585 |
4.86e-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: 57.37 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 439 QDI-RETEEAIRH------KTTEVQEMQNDLdrETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMI 511
Cdd:TIGR02168 192 EDIlNELERQLKSlerqaeKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 512 SSLQTQIHSQESDLQSQEEELGRAKADLNRL-------QQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQI 584
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
.
gi 1207195097 585 Q 585
Cdd:TIGR02168 350 K 350
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
431-618 |
5.85e-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: 56.72 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYtlEQDIRETEEAIRHKTTEVQEMQN---DLDRETSSLQEleaQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE 507
Cdd:pfam01576 181 LKNKH--EAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQE---QIAELQAQIAELRAQLAKKEEELQAALARLEEE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 508 SQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSlKATQDEINQAR-SKLSQIQD 586
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDT-TAAQQELRSKReQEVTELKK 334
|
170 180 190
....*....|....*....|....*....|..
gi 1207195097 587 SQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 618
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKHTQALEELTEQLE 366
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
438-544 |
7.21e-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: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 438 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE---SQM 510
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkDRE 466
|
90 100 110
....*....|....*....|....*....|....
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ 544
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-584 |
7.69e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAF---------THWDTLREKYTLEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQK 476
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESlaaeieeleELIEELESELEALLNERASLEEALALLrSELEELSEELRELESKRSELRREL 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 477 QDAQDRLEEMDQQKAKLEdmlndvrqkcqeesQMISSLQTQIHSQESD-LQSQEEELGRAKADLNRLQQEEAQLEQSLQA 555
Cdd:TIGR02168 918 EELREKLAQLELRLEGLE--------------VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195097 556 -GRIQLETI--IKSLK------ATQDE-INQARSKLSQI 584
Cdd:TIGR02168 984 lGPVNLAAIeeYEELKerydflTAQKEdLTEAKETLEEA 1022
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-633 |
1.01e-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: 55.95 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 414 QEIAQLQSTLAfthwdtlREKYTLEQDIRETEEaiRHkTTEVQEMQNDLD---RETSSL----QELEAQKQDAQDRLE-- 484
Cdd:pfam01576 327 QEVTELKKALE-------EETRSHEAQLQEMRQ--KH-TQALEELTEQLEqakRNKANLekakQALESENAELQAELRtl 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 485 -----EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR-- 557
Cdd:pfam01576 397 qqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQel 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 558 IQLETIIK-----SLKATQDEinqaRSKLSQIQDSQHEISKNIEQYSSTLNgthggsmTNLADMSEGFpEKENGGFGAME 632
Cdd:pfam01576 477 LQEETRQKlnlstRLRQLEDE----RNSLQEQLEEEEEAKRNVERQLSTLQ-------AQLSDMKKKL-EEDAGTLEALE 544
|
.
gi 1207195097 633 D 633
Cdd:pfam01576 545 E 545
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
433-594 |
1.15e-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: 53.22 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQ 509
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 510 MISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQAGRIQLETI------------IKSLKATQDEI 574
Cdd:cd00176 76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEdlgkdlesveelLKKHKELEEEL 155
|
170 180
....*....|....*....|
gi 1207195097 575 NQARSKLSQIQDSQHEISKN 594
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEE 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-598 |
1.30e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR---ETSSLQE-----------L 472
Cdd:COG4372 52 EELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAELAQAQEELESlqeEAEELQEeleelqkerqdL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 473 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEElgRAKADLNRLQQEEAQLEQS 552
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEK 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207195097 553 LQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 598
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
437-597 |
1.44e-07 |
|
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: 55.52 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE----------EMDQQKAKLED----MLNDVRQ 502
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAeaeealreqaELNRLKKKYLEalnkKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 503 KCQEESQMISSL-------QTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDEIN 575
Cdd:pfam05557 98 QLADAREVISCLknelselRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQSSLAEAEQRIK 173
|
170 180
....*....|....*....|..
gi 1207195097 576 QARSKLSQiQDSQHEISKNIEQ 597
Cdd:pfam05557 174 ELEFEIQS-QEQDSEIVKNSKS 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
408-602 |
1.58e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAFTHWDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDR---- 482
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksi 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 ----------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQ-------QE 545
Cdd:TIGR02169 853 ekeienlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEE 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 546 EAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQIQdsqheiSKNIEQYSSTL 602
Cdd:TIGR02169 933 LSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVN------MLAIQEYEEVL 985
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
372-586 |
1.58e-07 |
|
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: 54.32 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 372 SLSGYMTPVGSDMAALTEMRRDSSSSVGSGEFTG--IKELDDISQEIAQ-LQStlafthwdtlrekytLEQDIRETEEAI 448
Cdd:pfam04108 134 SLDSDLKRFDDDLRDLQKELESLSSPSESISLIPtlLKELESLEEEMASlLES---------------LTNHYDQCVTAV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 449 RHKTTEVQEMQNDLDRETsslQELEAQKQDAQDRLEEMDQQKAKLE---DMLNDVRQKCQEESQMISSLQTQIHSQESDL 525
Cdd:pfam04108 199 KLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQkllEQKNSLIDELLSALQLIAEIQSRLPEYLAAL 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 526 QSQEEELGRAKAdlnRLQQEEAQLEQsLQAGRIQLETIIKSL-------KATQDE----INQARSKLSQIQD 586
Cdd:pfam04108 276 KEFEERWEEEKE---TIEDYLSELED-LREFYEGFPSAYGSLlleverrREWAEKmkkiLRKLAEELDRLQE 343
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
402-585 |
1.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 402 EFTGIKE-LDDISQEIAQLQstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRET-SSLQELEAQKQ-- 477
Cdd:PRK03918 526 EYEKLKEkLIKLKGEIKSLK--------KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKel 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 478 -----------DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQ--EEELGRAKADLNRLQQ 544
Cdd:PRK03918 598 epfyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----EELEKKysEEEYEELREEYLELSR 673
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195097 545 EEAQLEQSLQAGRIQLETIIKS---LKATQDEINQARSKLSQIQ 585
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
414-586 |
2.02e-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: 53.07 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 414 QEIAQLQSTLAFthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlQELEAQKQDAQDRLEEMDQQKAKL 493
Cdd:pfam12795 17 KLLQDLQQALSL-----LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAK-AEAAPKEILASLSLEELEQRLLQT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 494 EDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADL-NRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 572
Cdd:pfam12795 91 SAQLQELQNQLAQLNSQLIELQTRP----ERAQQQLSEARQRLQQIrNRLNGPAPPGEPLSEAQRWALQAELAALKAQID 166
|
170
....*....|....
gi 1207195097 573 EINQARSKLSQIQD 586
Cdd:pfam12795 167 MLEQELLSNNNRQD 180
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
17-78 |
2.24e-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: 2.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 17 YENFYRQVDPGNtGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLV 78
Cdd:pfam12763 12 YWEIFSGLKPEN-NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-603 |
2.38e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 474 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQES--DLQSQEEELGRA--KADLNRLQQEEAQL 549
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykELKAELRELELAllVLRLEELREELEEL 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 550 EQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-600 |
2.69e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLA--FTHWDTL-REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQD---AQ 480
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEklNNKYNDLkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakaDLNRLQQEEAQLEQS------LQ 554
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL----NQLKDEQNK------IKKQLSEKQKELEQNnkkikeLE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 555 AGRIQLETIIKSLK--ATQDEINQARSKLS----QIQDSQHEISKNIEQYSS 600
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNKELKSELKnqekKLEEIQNQISQNNKIISQ 339
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
408-589 |
2.84e-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: 54.74 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIA----QLQSTLAFTHwdtLREK---YTLEQDIRETEEAIRHKTTeVQEMQNDLDRETSSLQELEAQKQDAQ 480
Cdd:pfam15921 364 ERDQFSQESGnlddQLQKLLADLH---KREKelsLEKEQNKRLWDRDTGNSIT-IDHLRRELDDRNMEVQRLEALLKAMK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 DRLE-EMDQQKAKLedmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiq 559
Cdd:pfam15921 440 SECQgQMERQMAAI--------QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-- 509
|
170 180 190
....*....|....*....|....*....|.
gi 1207195097 560 letiiKSLKATQDEINQARSKLS-QIQDSQH 589
Cdd:pfam15921 510 -----RAIEATNAEITKLRSRVDlKLQELQH 535
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
497-594 |
2.95e-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: 50.78 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 497 LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ 576
Cdd:pfam11559 40 IYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119
|
90
....*....|....*....
gi 1207195097 577 ARSKLSQIQDSQ-HEISKN 594
Cdd:pfam11559 120 LKNALQQIKTQFaHEVKKR 138
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
409-597 |
3.03e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.07 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQST-------LAFTHWDTLREKYTL-EQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQ 480
Cdd:PRK04778 214 MEEIPELLKELQTElpdqlqeLKAGYRELVEEGYHLdHLDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 DRLEEMDQQ-----KAKledmlNDVRQKCQEESQMISslqtqiHSQEsdlqsQEEELgraKADLNRLQQ------EEAQL 549
Cdd:PRK04778 289 ERIDQLYDIlerevKAR-----KYVEKNSDTLPDFLE------HAKE-----QNKEL---KEEIDRVKQsytlneSELES 349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195097 550 EQSLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:PRK04778 350 VRQLEK---QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
407-583 |
3.10e-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: 54.59 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLA-FTHWDT-LREKYTLEQDIRET---EEAIRHKTTEVQEMQNDLDRETSSLQELEAQK----- 476
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAyLTQKREaQEEQLKKQQLLKQLrarIEELRAQEAVLEETQERINRARKAAPLAAHIKavtqi 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 477 -QDAQDRLEEMDQQKAKLEDMLNDVR--QKCQEESQMISSLQTQIHSQESDLQSQ-------EEELGRAKADLNRLQQEE 546
Cdd:TIGR00618 306 eQQAQRIHTELQSKMRSRAKLLMKRAahVKQQSSIEEQRRLLQTLHSQEIHIRDAhevatsiREISCQQHTLTQHIHTLQ 385
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195097 547 AQLEQSLQAGRI--QLETIIKSLKATQDEINQARSKLSQ 583
Cdd:TIGR00618 386 QQKTTLTQKLQSlcKELDILQREQATIDTRTSAFRDLQG 424
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
407-596 |
3.58e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTHWDTLrEKYTLEQdireTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 486
Cdd:PRK11281 94 AKLRQAQAELEALKDDNDEETRETL-STLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDV-----------RQKCQEESQMissLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQeeAQLEQSL 553
Cdd:PRK11281 169 SQRLQQIRNLLKGGkvggkalrpsqRVLLQAEQAL---LNAQNDLQRKSLEgnTQLQDLLQKQRDYLTARI--QRLEHQL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 554 QAgriqLETII--KSLKATQDEINQARS--KLSQIQDS---QHEISKNIE 596
Cdd:PRK11281 244 QL----LQEAInsKRLTLSEKTVQEAQSqdEAARIQANplvAQELEINLQ 289
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
429-602 |
4.12e-07 |
|
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: 53.96 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTLE-QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-----------QDRLEEMDQQKA----- 491
Cdd:pfam05483 271 NQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAahsfv 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 492 ---------KLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQS----------QEEELGRAKADLNRLQQEEAQLEQS 552
Cdd:pfam05483 351 vtefeattcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAEDEKLLDEKKQFEKI 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 553 LQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 602
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
382-603 |
4.46e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.69 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 382 SDMAALTEMRRDSSSSVGSGEFTGIKE-LDDISQEIAQLqstlafthWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQN 460
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEkNEEIQERIDQL--------YDILEREVKARKYVEKNSDTLPDFLEHAKEQNK 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDRETSSLQ--------ELEAQKQdAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEEL 532
Cdd:PRK04778 328 ELKEEIDRVKqsytlnesELESVRQ-LEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 533 GRAKADLNRLQQEEAQLEQSLQAGRIQLETII----KS------------LKATQDEINQARSKLSQIQDSQHEISKNIE 596
Cdd:PRK04778 400 EKLSEMLQGLRKDELEAREKLERYRNKLHEIKryleKSnlpglpedylemFFEVSDEIEALAEELEEKPINMEAVNRLLE 479
|
....*..
gi 1207195097 597 QYSSTLN 603
Cdd:PRK04778 480 EATEDVE 486
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
407-599 |
5.92e-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: 53.32 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQST-------LAFTHWDTLREKYTLEQDirETEEairhkttEVQEMQNDLDRETSSLQELEAQkqDA 479
Cdd:pfam06160 193 ELMEDIPPLYEELKTElpdqleeLKEGYREMEEEGYALEHL--NVDK-------EIQQLEEQLEENLALLENLELD--EA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDRLEEMDQQKAKLEDMLN---DVRQKCQEESQMISSLQTQIHSQESDLQsqeEELGRAKadLN-RLQQEEAQLEQSLQA 555
Cdd:pfam06160 262 EEALEEIEERIDQLYDLLEkevDAKKYVEKNLPEIEDYLEHAEEQNKELK---EELERVQ--QSyTLNENELERVRGLEK 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195097 556 griQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 599
Cdd:pfam06160 337 ---QLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
406-585 |
5.95e-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: 51.53 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 483
Cdd:pfam12795 29 LDKIDASKQRAAAYQKALddAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 --------------EEMDQQKAKLEDMLN--DVRQKCQEESQM------ISSLQTQIHSQESDLQS--QEEELGRAKADL 539
Cdd:pfam12795 109 ielqtrperaqqqlSEARQRLQQIRNRLNgpAPPGEPLSEAQRwalqaeLAALKAQIDMLEQELLSnnNRQDLLKARRDL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 540 --NRLQQEEAQLE--QSLQAGRIQLETiIKSLKATQDEINQARSKLSQIQ 585
Cdd:pfam12795 189 ltLRIQRLEQQLQalQELLNEKRLQEA-EQAVAQTEQLAEEAAGDHPLVQ 237
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
410-630 |
6.40e-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: 52.37 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 410 DDISQEIAQLQSTLA-----FTHW--DTLREKYTLEQDIRE-TEEAIRHKTTEVQEMQNDLDR--ETSSLQELEAQKQDA 479
Cdd:cd22656 40 DKLSSDFDPLLDAYKsikdhCTDFkdDTYPSIVSLAGDIYNyAQNAGGTIDSYYAEILELIDDlaDATDDEELEEAKKTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDRLEEMD------QQKA-KLEDMLNDVRQKCQEESQMISSLQTQIHSQ----------------ESDLQSQEEELG-RA 535
Cdd:cd22656 120 KALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiarkeikdlQKELEKLNEEYAaKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 536 KADLNRLQQEEAQLEQSLQAG-RIQ--LETIIKSLKATQDEINQARSKLSQIQDSQHEISknieqysstlngthgGSMTN 612
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAAlRLIadLTAADTDLDNLLALIGPAIPALEKLQGAWQAIA---------------TDLDS 264
|
250
....*....|....*...
gi 1207195097 613 LADMSEGFPEKENGGFGA 630
Cdd:cd22656 265 LKDLLEDDISKIPAAILA 282
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
406-578 |
6.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAI---RHKTTEVQEMQNDLDRETSSLQELEAQK---- 476
Cdd:PRK04863 893 ADRVEEIREQLDEAEEAKRFvqQHGNALAQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFALTEVVQRRahfs 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 477 -QDAQD--------------RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-------- 533
Cdd:PRK04863 973 yEDAAEmlaknsdlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpads 1052
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 534 ----RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 578
Cdd:PRK04863 1053 gaeeRARARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
460-602 |
7.87e-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: 52.07 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 460 NDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDM---LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAK 536
Cdd:pfam09787 37 EGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLrteLQELEAQQQEEAESSREQLQELEEQLATERSARRE---AE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 537 ADLNRLQQEEAQLEQSLQAGRIQLETIIKSLkatQDEINQARSKL---SQIQDSQHEISKNIEQYSSTL 602
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKATLQSRIKDR---EAEIEKLRNQLtskSQSSSSQSELENRLHQLTETL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
417-602 |
8.88e-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: 53.05 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 417 AQLQSTLafTHWDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-------ELEAQKQDAQDRLEEMDQQ 489
Cdd:TIGR00618 549 HQLTSER--KQRASLKEQ---MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteklsEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 490 KAKLEDMLNDVRQKCQEESQmissLQTQIHSQESDLQSQEEELGRAkadlnRLQQEEAQLEQSLQAGRIQLETIIKSLKA 569
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQSEKEQLTY 694
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 570 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 602
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
425-597 |
8.91e-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: 50.91 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 425 FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-----------KQDAQDRLEEMDQQKAKL 493
Cdd:cd00176 12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlieeghpdAEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 494 EDMLNDVRQKCQE------ESQMISSLQTQIHSQESDLQSQeeELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKSL 567
Cdd:cd00176 92 RELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEA----HEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1207195097 568 KATQDEINQARSKLS--QIQDSQHEISKNIEQ 597
Cdd:cd00176 166 NELAEELLEEGHPDAdeEIEEKLEELNERWEE 197
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
311-624 |
1.14e-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: 52.81 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 311 HQNLLAHIWA-LADTRQM-GKLTREQFSLAMYLIQQ---KVSKGLdppqaltpdmippSERGTPGPSLSGYMTPVGSDMA 385
Cdd:pfam15921 182 HEGVLQEIRSiLVDFEEAsGKKIYEHDSMSTMHFRSlgsAISKIL-------------RELDTEISYLKGRIFPVEDQLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 386 ALtemrrdSSSSVGSGEFTGIKELDDISQEIAQLQ---STLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDL 462
Cdd:pfam15921 249 AL------KSESQNKIELLLQQHQDRIEQLISEHEveiTGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 463 DRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNR 541
Cdd:pfam15921 323 ESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 542 L-------------------------QQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIE 596
Cdd:pfam15921 403 LwdrdtgnsitidhlrrelddrnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVE 482
|
330 340
....*....|....*....|....*...
gi 1207195097 597 QYSSTlNGTHGGSMTNLADMSEGFPEKE 624
Cdd:pfam15921 483 ELTAK-KMTLESSERTVSDLTASLQEKE 509
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
389-650 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 389 EMRRDSSSSVGSGEftgikELDDISQEIAQLQST---LAFTHWDTLREKYTLEQDIR----------ETEEAIRHKTTEV 455
Cdd:pfam15921 445 QMERQMAAIQGKNE-----SLEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 456 QEMQNDLDRETSSLQELEAQK---QDAQ---------------------DRLEEMDQ--------------QKAKLEDML 497
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLKNEGdhlRNVQtecealklqmaekdkvieilrQQIENMTQlvgqhgrtagamqvEKAQLEKEI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 498 NDVRQKCQEESQMISSLQTQIHSQE---SDLQSQEEELGRAKADLNR----LQQEEAQLEQSLQAGRIQL-------ETI 563
Cdd:pfam15921 600 NDRRLELQEFKILKDKKDAKIRELEarvSDLELEKVKLVNAGSERLRavkdIKQERDQLLNEVKTSRNELnslsedyEVL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 564 IKSLKATQDEINQARSKLS-QIQDSQHEisknIEQYSSTLN---GTHGGSMTNLADMSEGFPEKEnGGFGAMEDPFKVKP 639
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKmQLKSAQSE----LEQTRNTLKsmeGSDGHAMKVAMGMQKQITAKR-GQIDALQSKIQFLE 754
|
330
....*....|.
gi 1207195097 640 TVFNSAPQEMH 650
Cdd:pfam15921 755 EAMTNANKEKH 765
|
|
| STAT3_CCD |
cd16853 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ... |
439-585 |
1.32e-06 |
|
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: 49.61 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 439 QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI 518
Cdd:cd16853 11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 519 HSQESDLqsQEEELgrakADLNRLQQeEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:cd16853 91 EYVQKNL--TDEEL----ADWKRRQQ-IACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQ 150
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
468-605 |
1.46e-06 |
|
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: 50.38 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 468 SLQELEAQK-------------QDAQDRLEEMDQQKAKLEDmlndVRQKCQEESQMISSLQTQIHSQEsdlQSQEEELgr 534
Cdd:pfam12795 1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAAA----YQKALDDAPAELRELRQELAALQ---AKAEAAP-- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195097 535 aKADLNRLQQEeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGT 605
Cdd:pfam12795 72 -KEILASLSLE--ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGP 139
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
436-582 |
1.47e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.21 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIrhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMdQQKAKL------EDMLNDVRQKCQEESQ 509
Cdd:COG1842 27 MLDQAIRDMEEDL-------VEARQALAQVIANQKRLERQLEELEAEAEKW-EEKARLalekgrEDLAREALERKAELEA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 510 MISSLQTQIhsqesdlQSQEEELGRAKADLNRLqqeEAQLEQsLQAGRIQLETIIKSLKATQdEINQARSKLS 582
Cdd:COG1842 99 QAEALEAQL-------AQLEEQVEKLKEALRQL---ESKLEE-LKAKKDTLKARAKAAKAQE-KVNEALSGID 159
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
413-591 |
1.50e-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: 51.46 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 413 SQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAirhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 492
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEK-------EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 493 LEDMLNDVRQKCQE-------ESQMISSLQTQIhsQESDLQSQE----------EELGRAKADLNRLQQEEAQLEQsLQA 555
Cdd:pfam13868 78 LEEQIEEREQKRQEeyeeklqEREQMDEIVERI--QEEDQAEAEeklekqrqlrEEIDEFNEEQAEWKELEKEEER-EED 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195097 556 GRI-----QLETIIKSLKATQDEINQA--------RSKLSQIQDSQHEI 591
Cdd:pfam13868 155 ERIleylkEKAEREEEREAEREEIEEEkereiarlRAQQEKAQDEKAER 203
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-560 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdQQKAKLEDMLNDVRQKCQEESQMISSLQt 516
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQ- 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1207195097 517 qihSQESDLQSQEEELGRAKAdlnrlQQEEAQLEQSLQAGRIQL 560
Cdd:COG4942 220 ---QEAEELEALIARLEAEAA-----AAAERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
525-597 |
2.47e-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: 2.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 525 LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
407-597 |
2.76e-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: 51.33 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETE----EAIRHKTT---EVQEMQNDLDRETSSLQE-------- 471
Cdd:pfam01576 384 SENAELQAELRTLQQAKQ----DSEHKRKKLEGQLQELQarlsESERQRAElaeKLSKLQSELESVSSLLNEaegknikl 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 472 ------LEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEE-------SQMISSLQTQIhsqeSDLQSQ-EE 530
Cdd:pfam01576 460 skdvssLESQLQDTQELLQEETRQKLNlstrlrqLEDERNSLQEQLEEEeeakrnvERQLSTLQAQL----SDMKKKlEE 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 531 ELGRAKA---DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQarskLSQIQDSQHEISKNIEQ 597
Cdd:pfam01576 536 DAGTLEAleeGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDD----LLVDLDHQRQLVSNLEK 601
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
408-623 |
2.80e-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: 51.38 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAfthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL------------QELEAQ 475
Cdd:pfam12128 242 EFTKLQQEFNTLESAEL--------RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLddqwkekrdelnGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 476 KQD-AQDR--LEEMDQQKAKLEDmlNDVRQKCQEESQMiSSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQleqs 552
Cdd:pfam12128 314 DAAvAKDRseLEALEDQHGAFLD--ADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---- 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 553 lqagriQLETIIKSLKATQDEINQARsklsqiqDSQH-EISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEK 623
Cdd:pfam12128 387 ------QNNRDIAGIKDKLAKIREAR-------DRQLaVAEDDLQALESELREQLEAGKLEFNEEEYRLKSR 445
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
429-603 |
3.19e-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: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTLEQDIreTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ------ 502
Cdd:TIGR01612 1621 DCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknye 1698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 503 -----KCQE----ESQMISSLQTQIHSQESDLQSQ-----------EEELGRAKADLNRLQQEEAQLeQSLQAGriQLET 562
Cdd:TIGR01612 1699 igiieKIKEiaiaNKEEIESIKELIEPTIENLISSfntndlegidpNEKLEEYNTEIGDIYEEFIEL-YNIIAG--CLET 1775
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207195097 563 IIKSlKATQDEINQARSklsqiqDSQHEISKNIE---QYSSTLN 603
Cdd:TIGR01612 1776 VSKE-PITYDEIKNTRI------NAQNEFLKIIEiekKSKSYLD 1812
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
434-598 |
3.25e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 434 KYTLEQDIRETEEAIRHKtteVQEMQNDLDrETSSLQELEAQkqdaqdrlEEMDQQKAKLEdmlNDVRQKCQEesqmISS 513
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLRNEFE---KELRERRNE----LQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 514 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--------TQDEinqARSKLSQ-- 583
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTAEE---AKEILLEkv 163
|
170
....*....|....*
gi 1207195097 584 IQDSQHEISKNIEQY 598
Cdd:PRK12704 164 EEEARHEAAVLIKEI 178
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
411-618 |
3.35e-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: 50.88 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 411 DISQEIAQLqsTLAFTHWDTLREKYTLEQ--DIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQD------ 478
Cdd:pfam05483 187 DLNNNIEKM--ILAFEELRVQAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflle 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 479 -AQDRLEEMdQQKAKLEDmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGRAKADLNRLQQE-EAQLEQSL 553
Cdd:pfam05483 265 eSRDKANQL-EEKTKLQD--ENLKELIEKKDHLTKELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEkEAQMEELN 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 554 QAgRIQLETIIKSLKAT----QDEINQARSKLSQIQDSQHEISKNIEQYSSTLNgthggSMTNLADMSE 618
Cdd:pfam05483 342 KA-KAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQKKSSELE-----EMTKFKNNKE 404
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
432-602 |
3.58e-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: 51.12 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 432 REKYTLEQDIRETEEaIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 510
Cdd:TIGR00618 163 KEKKELLMNLFPLDQ-YTQLALMEFAKKKSLHGKAELLTlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEelgrakadlnrLQQEEAQLEqslqagriQLETIIKSLKATQDEINQARSKLSQIQDSQH- 589
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQL-----------LKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAHIKAv 302
|
170
....*....|....
gi 1207195097 590 -EISKNIEQYSSTL 602
Cdd:TIGR00618 303 tQIEQQAQRIHTEL 316
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
409-616 |
3.91e-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: 50.89 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEeairhktTEVQEMQNDLD-------RETSSLQELEAQKQDAqd 481
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQ-------TKLQEMQMERDamadirrRESQSQEDLRNQLQNT-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 482 rLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ--------------EEA 547
Cdd:pfam15921 151 -VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrslgsaiskilREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 548 QLEQSLQAGRI-----QLETiIKS---------LKATQDEINQ------------------ARSKLSQIQdSQHEIsknI 595
Cdd:pfam15921 230 DTEISYLKGRIfpvedQLEA-LKSesqnkiellLQQHQDRIEQliseheveitgltekassARSQANSIQ-SQLEI---I 304
|
250 260
....*....|....*....|.
gi 1207195097 596 EQYSSTLNGTHggsMTNLADM 616
Cdd:pfam15921 305 QEQARNQNSMY---MRQLSDL 322
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
469-601 |
4.71e-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: 49.63 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 469 LQELEAQKQDAQDRLEEMDQQKAKL---EDMLNDVRQKCQEESQMISSLQTQIHSQESDLQS-QEEELGRAKADLNRLQQ 544
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 545 E-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSST 601
Cdd:smart00787 219 EimikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKLKEQLKLL 283
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
406-598 |
5.56e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLafthwDTLREKytleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:COG1340 28 KEKRDELNEELKELAEKR-----DELNAQ------VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE------SDLQSQEEELGRAKaDLNRLQQEEAQLEQSLQAGRIQ 559
Cdd:COG1340 97 LRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEeekelvEKIKELEKELEKAK-KALEKNEKLKELRAELKELRKE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195097 560 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 598
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
402-587 |
5.71e-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: 47.98 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 402 EFTGIKE---------LDDISQ---EIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDL---DRET 466
Cdd:pfam13851 9 AFNEIKNyynditrnnLELIKSlkeEIAELKKKEE----RNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyEKDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 467 SSLQELEAQKQDAQDRL-------EEMDQQKAKLEDMLNDVRQKCQeesQMISSLQtqihsQESDLQSQEEElgrakadl 539
Cdd:pfam13851 85 QSLKNLKARLKVLEKELkdlkwehEVLEQRFEKVERERDELYDKFE---AAIQDVQ-----QKTGLKNLLLE-------- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207195097 540 NRLQQEEAQLEQSlqagRIQLETIIKSLKATQDEINQARSKLSQIQDS 587
Cdd:pfam13851 149 KKLQALGETLEKK----EAQLNEVLAAANLDPDALQAVTEKLEDVLES 192
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
407-603 |
7.75e-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: 50.05 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTT-------EVQEMQNDLDRETSSLQELEAQKQDA 479
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDR---------------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI--HSQESDLQSQEEELGRAKADLNRL 542
Cdd:TIGR00606 968 KDDylkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQM 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 543 Q-----QEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLS--QIQDSQ-------------HEISKNIEQYSSTL 602
Cdd:TIGR00606 1048 QvlqmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRepQFRDAEekyremmivmrttELVNKDLDIYYKTL 1127
|
.
gi 1207195097 603 N 603
Cdd:TIGR00606 1128 D 1128
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
436-582 |
9.40e-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: 47.75 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIRhkttevqEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDmlndvrqKCQE-----ESQM 510
Cdd:pfam04012 19 KAEDPEKMLEQAIR-------DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE-------KAQAaltkgNEEL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--TQDEINQARSKLS 582
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
407-556 |
9.49e-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: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAI-------------------------------------- 448
Cdd:COG4942 69 RRIRALEQELAALEAELA----ELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkyl 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 449 -RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLndvrqkcQEESQMISSLQTQIHSQESDLQS 527
Cdd:COG4942 145 aPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-------AERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*....
gi 1207195097 528 QEEELGRAKADLNRLQQEEAQLEQSLQAG 556
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
437-576 |
9.86e-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: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 516
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 517 QIHSQESDLQSQEEELGRAKADLNRL------------QQEE------AQLEQsLQAGRIQLETIIKSL--------KAT 570
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEErydflsEQRED-LEEARETLEEAIEEIdretrerfLET 832
|
....*.
gi 1207195097 571 QDEINQ 576
Cdd:COG1196 833 FDAVNE 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-597 |
1.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTT--EVQEMQNDLdrETSSLQELEAQKQDAQ---- 480
Cdd:PRK03918 459 AELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIKLKELaeQLKELEEKL--KKYNLEELEKKAEEYEklke 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 -------------DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEA 547
Cdd:PRK03918 533 kliklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 548 QLEQSLqagriqletiiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:PRK03918 613 ELEREE-----------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
414-597 |
1.08e-05 |
|
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: 47.78 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 414 QEIAQLQSTLafTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSS------LQELEAQKQDAQDRLEEMD 487
Cdd:pfam16591 9 TDISQLNDTL--TDLRIARLQYMLSNGDATAAQAVQKKLDELKQQLQQLKTTFTSpenvrlLQEQLQLIQAYRKSFNELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQI----------------------HSQ--------------ESDLQSQEEE 531
Cdd:pfam16591 87 AAYESRNASRQVMDSAAERALEAIDQLEAEVlqtpeadsrraaqyqaiselkrQVQmaryqvrgytftpnEDSEQAAYQQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 532 LGRAKADLNRLQQEEA--------QLEQSLQAGRIQLETiiksLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:pfam16591 167 LDAALASLDQLRQALAgdpgaalqQLTSALQGYRDALDT----FKAAVAAIEQARQEMTSQGDEIVRISDELYQ 236
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
433-586 |
1.10e-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: 48.76 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETEEAIrhkttEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKL----------EDMLNDVRQ 502
Cdd:pfam13868 158 LEYLKEKAEREEEREA-----EREEIEEEKERE---IARLRAQQEKAQDEKAERDELRAKLyqeeqerkerQKEREEAEK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 503 KCQEESQMISSLQTQIHSQEsdlQSQEEELGRAKADLNRL---QQEEAQLEQSLQAGRIQLetiiksLKATQDEInqars 579
Cdd:pfam13868 230 KARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRMK------RLEHRREL----- 295
|
....*..
gi 1207195097 580 kLSQIQD 586
Cdd:pfam13868 296 -EKQIEE 301
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
409-578 |
1.48e-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: 49.18 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLAFT--HWDTLRE----KYTLEQDiRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK-----Q 477
Cdd:COG3096 895 LEELREELDAAQEAQAFIqqHGKALAQleplVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyE 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 478 DAQDRLEE----MDQQKAKLEDM----------LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG---------- 533
Cdd:COG3096 974 DAVGLLGEnsdlNEKLRARLEQAeearreareqLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaea 1053
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 534 --RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 578
Cdd:COG3096 1054 eeRARIRRDELHEElsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-601 |
1.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 479 AQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 558
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 559 QLETIIKSL----------------KATQDEINQArSKLSQIQDSQHEIsknIEQYSST 601
Cdd:COG3883 87 ELGERARALyrsggsvsyldvllgsESFSDFLDRL-SALSKIADADADL---LEELKAD 141
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
424-598 |
1.58e-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: 48.81 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 424 AFTHWDTLREKYTLEQDIRETE-EAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------RLEEMDQQKA---- 491
Cdd:TIGR00618 301 AVTQIEQQAQRIHTELQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsIREISCQQHTltqh 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 492 --KLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgraKADLNRLQ-QEEAQLEQSLQAgRIQLETIIKSLK 568
Cdd:TIGR00618 381 ihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL----QGQLAHAKkQQELQQRYAELC-AAAITCTAQCEK 455
|
170 180 190
....*....|....*....|....*....|
gi 1207195097 569 ATQDEINQARSKLsqiqDSQHEISKNIEQY 598
Cdd:TIGR00618 456 LEKIHLQESAQSL----KEREQQLQTKEQI 481
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
408-587 |
1.61e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIA----------QLQSTLAfthwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQkQ 477
Cdd:PRK11637 48 QLKSIQQDIAakeksvrqqqQQRASLL----AQLKKQ---EEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQ-Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 478 DAQDRL--EEMDQ-----QKAKLEDM------------------LNDVRQKCQEE-SQMISSLQTQIHSQEsDLQSQEEE 531
Cdd:PRK11637 120 AAQERLlaAQLDAafrqgEHTGLQLIlsgeesqrgerilayfgyLNQARQETIAElKQTREELAAQKAELE-EKQSQQKT 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 532 LgrakadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 587
Cdd:PRK11637 199 L------LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS 248
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
410-587 |
1.67e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 410 DDISQEIAQLQSTLAFThwDTLREKYTLEQD----IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:PRK04778 317 DFLEHAKEQNKELKEEI--DRVKQSYTLNESelesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHS-----QESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQL 560
Cdd:PRK04778 395 IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikrylEKSNLPGLPEDY---LEMFFEVSDEIEALAEELEEKPINM 471
|
170 180
....*....|....*....|....*..
gi 1207195097 561 ETIIKSLKATQDEINQARSKLSQIQDS 587
Cdd:PRK04778 472 EAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
407-597 |
1.97e-05 |
|
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: 46.06 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETE-EAIRhktTEVQEMQNdldretsslqELEAQKQDaqdrLEE 485
Cdd:pfam13870 6 NELSKLRLELITLKHTLAKIQ-EKLEQKEELGEGLTMIDfLQLQ---IENQALNE----------KIEERNKE----LKR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslQAGRIQLETIIK 565
Cdd:pfam13870 68 LKLKVTNTVHALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQ--QGGLLHVPALLH 145
|
170 180 190
....*....|....*....|....*....|..
gi 1207195097 566 SLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:pfam13870 146 DYDKTKAEVEEKRKSVKKLRRKVKILEMRIKE 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
433-580 |
1.98e-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: 48.63 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETEEAI------------RHKTTE--VQEMQNDLDRE---TSSLQEL----EAQKQDAQDRL-------E 484
Cdd:pfam01576 125 EKVTTEAKIKKLEEDIllledqnsklskERKLLEerISEFTSNLAEEeekAKSLSKLknkhEAMISDLEERLkkeekgrQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRiQLETII 564
Cdd:pfam01576 205 ELEKAKRKLEGESTDLQEQ-------IAELQAQIAELRAQLAKKEEEL---QAALARLEEETAQKNNALKKIR-ELEAQI 273
|
170
....*....|....*.
gi 1207195097 565 KSLKATQDEINQARSK 580
Cdd:pfam01576 274 SELQEDLESERAARNK 289
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
407-545 |
2.02e-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: 47.70 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAirhkTTEVQEM-QNDLDRETSSLQELEAQKQDAQDRLE 484
Cdd:smart00787 158 EDYKLLMKELELLNSIK-----PKLRDRKdALEEELRQLKQL----EDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKCQEesqmissLQTQIHSQESDL-QSQ---EEELGRAKADLNRLQQE 545
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSE-------LNTEIAEAEKKLeQCRgftFKEIEKLKEQLKLLQSL 286
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
404-591 |
2.07e-05 |
|
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: 47.50 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 404 TGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRE--TEEAIRHKTTEVQEMQNDLD---RETSSLQE-LEAQKQ 477
Cdd:pfam15905 112 AAVREKTSLSASVASLEKQLL----ELTRVNELLKAKFSEdgTQKKMSSLSMELMKLRNKLEakmKEVMAKQEgMEGKLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 478 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ---TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLeyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195097 555 AGRIQLETIIKSL--------KATQDEINQARSK----LSQIQDSQHEI 591
Cdd:pfam15905 268 EKEQELSKQIKDLnekcklleSEKEELLREYEEKeqtlNAELEELKEKL 316
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
406-596 |
2.31e-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: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAFThWDTLRE----KYTLEQDIRETEEAIrHKTTEVQEMQND------------LDRETSSL 469
Cdd:pfam03148 122 LKEVELIEGIQELLQRTLEQA-WEQLRLlraaRHKLEKDLSDKKEAL-EIDEKCLSLNNTspnisykpgptrIPPNSSTP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 470 QE---------LEAQK--QDAQDRLEEMDQQkakLEDMLNDV-----------RQKCQEESQMISSLQTQ-------IHS 520
Cdd:pfam03148 200 EEwekftqdniERAEKerAASAQLRELIDSI---LEQTANDLraqadavnfalRKRIEETEDAKNKLEWQlkktlqeIAE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 521 QESDLQSQEEELGRAKADL--------NRLQ-------QEEAQ--LEQSLQagriQLETIIKSLkatQDEINQARSKLSQ 583
Cdd:pfam03148 277 LEKNIEALEKAIRDKEAPLklaqtrleNRTYrpnvelcRDEAQygLVDEVK----ELEETIEAL---KQKLAEAEASLQA 349
|
250
....*....|...
gi 1207195097 584 IQDSQHEISKNIE 596
Cdd:pfam03148 350 LERTRLRLEEDIA 362
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
430-584 |
2.48e-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: 48.41 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 430 TLREKYT-LEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQkcQEEs 508
Cdd:COG3096 516 QLRAQLAeLEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ--QLE- 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 509 qmisslqtQIHSQESDLQSQEEELGRAKADLNRLQ-QEEAQLE--QSLQAGRIQLETIIKSLKATQDEINQARSKL-SQI 584
Cdd:COG3096 589 --------QLRARIKELAARAPAWLAAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELAARKQALeSQI 660
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
431-618 |
2.50e-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: 48.50 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYTLEQDIRETEEAI----RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 506
Cdd:TIGR00606 222 IRDQITSKEAQLESSREIvksyENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 507 EsqmissLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ------------SLQAGRIQLETIIKSLKATQdei 574
Cdd:TIGR00606 302 Q------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQektellveqgrlQLQADRHQEHIRARDSLIQS--- 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207195097 575 NQARSKLSQIQ---DSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 618
Cdd:TIGR00606 373 LATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
406-580 |
2.84e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQ-STLAFTHWDTLREKYTLE-QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 483
Cdd:PRK03918 275 IEELEEKVKELKELKeKAEEYIKLSEFYEEYLDElREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 EEMdQQKAKLedmLNDVRQKcQEESQMISSLQTqIHSQEsDLQSQEEELGRAKadlnrlqqEEAQLEQSLQAGRI-QLET 562
Cdd:PRK03918 355 EEL-EERHEL---YEEAKAK-KEELERLKKRLT-GLTPE-KLEKELEELEKAK--------EEIEEEISKITARIgELKK 419
|
170
....*....|....*...
gi 1207195097 563 IIKSLKATQDEINQARSK 580
Cdd:PRK03918 420 EIKELKKAIEELKKAKGK 437
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
389-625 |
2.99e-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: 47.82 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 389 EMRRdssssvgSGEftgIKELDDISQEIAQLQSTLAFTHWD-----TLRE---KYTLEQDI----RETEEAIRHKTTE-V 455
Cdd:pfam07111 182 ETKR-------AGE---AKQLAEAQKEAELLRKQLSKTQEEleaqvTLVEslrKYVGEQVPpevhSQTWELERQELLDtM 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 456 QEMQNDLDRETSSLQELEAQKQDAQDRL----EEMDQQKAKLEDMLNDVRQKCQEE----SQMISSLQTQIHSQESDLQS 527
Cdd:pfam07111 252 QHLQEDRADLQATVELLQVRVQSLTHMLalqeEELTRKIQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 528 QEEELGRAKADLNR----LQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA----RSKLSQIQDSQHEISKNIEQYS 599
Cdd:pfam07111 332 SVKQLRGQVAELQEqvtsQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAqearRRQQQQTASAEEQLKFVVNAMS 411
|
250 260
....*....|....*....|....*.
gi 1207195097 600 STLNGTHgGSMTNLADMSEGFPEKEN 625
Cdd:pfam07111 412 STQIWLE-TTMTRVEQAVARIPSLSN 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-603 |
3.93e-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: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 519 HSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 598
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
....*
gi 1207195097 599 SSTLN 603
Cdd:COG4942 96 RAELE 100
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
410-585 |
3.99e-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: 47.43 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 410 DDISQEIAQLQSTLAfTHWDtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EE 485
Cdd:pfam05557 279 EDLSRRIEQLQQREI-VLKE---ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDV---------RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKadlnrlqQEEAQLEQSLQAG 556
Cdd:pfam05557 355 RDGYRAILESYDKELtmsnyspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYK-------QQAQTLERELQAL 427
|
170 180
....*....|....*....|....*....
gi 1207195097 557 RIQLETiiKSLKATQDEINQARSKLSQIQ 585
Cdd:pfam05557 428 RQQESL--ADPSYSKEEVDSLRRKLETLE 454
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
406-504 |
4.19e-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: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMqndldretsslqeleAQKQDAQDRLEE 485
Cdd:pfam05837 5 INRRDELSSAILKLSSE----LRELQEELTEVEKENLRLKRKNRELAAELLEL---------------AKEKESRREDPK 65
|
90
....*....|....*....
gi 1207195097 486 MDQQKAKLEDMLNDVRQKC 504
Cdd:pfam05837 66 LRAQLEKLEAELKKSRRRW 84
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
437-597 |
4.25e-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: 47.48 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTE-------VQEMQNDLDRETSSLQELEAQKQDAQDRLEEM--------DQQ------KAKLED 495
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEkkkmqqhIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLeedillleDQNsklskeRKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 496 MLNDVRQKCQEESQMISSLQTQIHSQE---SDLQ---SQEE----ELGRAK----ADLNRLQQEEAQLEQSLQAGRIQLE 561
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEerlKKEEkgrqELEKAKrkleGESTDLQEQIAELQAQIAELRAQLA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195097 562 TIIKSLKATQDEI-------NQARSKLSQIQDSQHEISKNIEQ 597
Cdd:pfam01576 240 KKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLES 282
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
439-554 |
4.32e-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: 43.71 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 439 QDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLqtqi 518
Cdd:pfam13863 6 REMFLVQLALDAKREEIERLEELLKQR---EEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEK---- 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207195097 519 hsqesdlqsqEEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:pfam13863 79 ----------EKEIKKLTAQIEELKSEISKLEEKLE 104
|
|
| F-BAR_PombeCdc15_like |
cd07651 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ... |
394-586 |
4.35e-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: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 394 SSSSVGSGEFTGIKElddisqeiaqlqstlAFthwDTLREkytleqdirETEEAIRHKTTEVQEMQNDL-DRETSSLQEL 472
Cdd:cd07651 46 SRKSLGGSEEGGLKN---------------SL---DTLRL---------ETESMAKSHLKFAKQIRQDLeEKLAAFASSY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 473 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKadLNRLQqeeaqleQS 552
Cdd:cd07651 99 TQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKINSYT----LQSQLTWGKELEKNNAK--LNKAQ-------SS 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195097 553 LQAGRIQLETIIKSLKATQDEINQA-RSKLSQIQD 586
Cdd:cd07651 166 INSSRRDYQNAVKALRELNEIWNREwKAALDDFQD 200
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
409-584 |
4.45e-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: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLAFTHW---DTLREKY-TLEQDIRETEEAIRH------KTTEVQEMQNDLDRETSSLQELEAQKQD 478
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANLladETLADRLeELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSDPEQFEQLQADYLQ 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 479 AQDRLEEMDQQKakleDMLNDVRQKC-----QEESQMI---SSLQTQIHSQesdLQSQEEElgRAKADlNRLQQEEAQLE 550
Cdd:COG3096 946 AKEQQRRLKQQI----FALSEVVQRRphfsyEDAVGLLgenSDLNEKLRAR---LEQAEEA--RREAR-EQLRQAQAQYS 1015
|
170 180 190
....*....|....*....|....*....|....
gi 1207195097 551 QSLQAgRIQLETiikSLKATQDEINQARSKLSQI 584
Cdd:COG3096 1016 QYNQV-LASLKS---SRDAKQQTLQELEQELEEL 1045
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
429-581 |
4.77e-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: 44.99 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTLEQ----DIRETEEAIRHKTtevQEMQNDLDRETSSLQELEAQKQDaQDRLEEMDQQKAKLEDMLNDVR--- 501
Cdd:pfam16043 10 DQLQALILDLQeeleKLSETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASKVSrdq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 502 --QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslqagriqletIIKSLKATQDEINQARS 579
Cdd:pfam16043 86 fdETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKEL-----------LERRIKALQKLLQEGSE 154
|
..
gi 1207195097 580 KL 581
Cdd:pfam16043 155 EL 156
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
431-589 |
5.55e-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: 47.25 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LRE-KYTLEQdIRET---EEAIRHKTTEVQEM--------QNDLDRETSSLQELE-----AQKQ--DAQDRLEEMDQQKA 491
Cdd:COG3096 238 LREnRMTLEA-IRVTqsdRDLFKHLITEATNYvaadymrhANERRELSERALELRrelfgARRQlaEEQYRLVEMARELE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 492 KLEDMLNDVRQKCQEESQMISSLQTQIHSQESdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLEtiikslkATQ 571
Cdd:COG3096 317 ELSARESDLEQDYQAASDHLNLVQTALRQQEK-IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE-------AAE 388
|
170 180
....*....|....*....|.
gi 1207195097 572 DEINQARSKLSQIQ---DSQH 589
Cdd:COG3096 389 EEVDSLKSQLADYQqalDVQQ 409
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
382-587 |
5.57e-05 |
|
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: 46.77 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 382 SDMAALTEMRRDSSSSVGSGEFTGIKE-LDDISQEIAQLQSTL-----AF----THWDTLREK----------------- 434
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENLELDEAEEaLEEIEERIDQLYDLLekevdAKkyveKNLPEIEDYlehaeeqnkelkeeler 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 435 ----YTL----EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 506
Cdd:pfam06160 317 vqqsYTLneneLERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 507 ESQMISSLQTQIHS-----QESDL----QSQEEELGRAKADLNRLQQeeaQLEQSlqagRIQLETIIKSLKATQDEINQA 577
Cdd:pfam06160 397 AREKLDEFKLELREikrlvEKSNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----PLNMDEVNRLLDEAQDDVDTL 469
|
250
....*....|
gi 1207195097 578 RSKLSQIQDS 587
Cdd:pfam06160 470 YEKTEELIDN 479
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
437-540 |
5.85e-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: 45.40 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 516
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEK 204
|
90 100 110
....*....|....*....|....*....|.
gi 1207195097 517 QIHSQESDLQSQEE-------ELGRAKADLN 540
Cdd:pfam00261 205 EVDRLEDELEAEKEkykaiseELDQTLAELN 235
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
293-366 |
6.38e-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: 6.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 293 DGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSKGL-DPPQALTPDMIPPSER 366
Cdd:pfam12763 23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-602 |
7.79e-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: 46.60 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 465 ETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE----------------------SQMISSLQTQIH 519
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQqleRLRRErekaeryqallkekreyegyelLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 520 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ--AGRI---------QLETIIKSLKAtqdEINQARS----KLSQI 584
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIkdlgeeeqlRVKEKIGELEA---EIASLERsiaeKEREL 317
|
170
....*....|....*...
gi 1207195097 585 QDSQHEISKNIEQYSSTL 602
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLL 335
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
468-585 |
7.99e-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: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 468 SLQELEAQKQ--DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQ-MISSLQTQIHSQEsdlqsqeeELGRAKADLNRLQQ 544
Cdd:pfam07321 9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQrLYAEIQGKLVLLK--------ELEKVKQQVALLRE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207195097 545 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:pfam07321 81 NEADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFA 121
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
432-585 |
8.12e-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: 43.40 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 432 REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaqkqdAQDRLE-EMdQQKAKLEDMLNDVRQKCQEESQM 510
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-------AQQNYErEL-VLHAEDIKALQALREELNELKAE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEELgrakadlnrlQQEEAQLEQSLqagriqletiiKSLKATQDEIN-QARSKLSQIQ 585
Cdd:pfam07926 73 IAELKAEAESAKAELEESEESW----------EEQKKELEKEL-----------SELEKRIEDLNeQNKLLHDQLE 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
433-599 |
8.64e-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: 46.50 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETEEAIRHKTtEVQEMQNDLDRETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsq 509
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKE-QMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRK-- 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 510 missLQTQIHSQESDLQSQ--EEELGRAKADLNRLQQEEAQLEQSLQAGRIQ------LETIIKSLKATQDEINQA---R 578
Cdd:TIGR00618 621 ----LQPEQDLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRvlpkelLASRQLALQKMQSEKEQLtywK 696
|
170 180
....*....|....*....|.
gi 1207195097 579 SKLSQIQDSQHEISKNIEQYS 599
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYD 717
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
408-586 |
8.76e-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: 45.79 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAFThwDTLREKYTLEQDIRETEEA----IRHKTTE-----------VQEMQNDLDRETSSLQEL 472
Cdd:pfam04849 109 QLGSAREEILQLRHELSKK--DDLLQIYSNDAEESETESScstpLRRNESFsslhgcvqldaLQEKLRGLEEENLKLRSE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 473 EAQKQDAQDRLEEMDQQkakledMLNDVRQKCQEESQMISSLqtqihsqesdlqsqEEELGRaKADLNRLQQEE-----A 547
Cdd:pfam04849 187 ASHLKTETDTYEEKEQQ------LMSDCVEQLSEANQQMAEL--------------SEELAR-KMEENLRQQEEitsllA 245
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195097 548 Q---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 586
Cdd:pfam04849 246 QivdLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQD 287
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
429-578 |
9.15e-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: 46.10 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEaqkQDAQDRLEEMDQQKAKLEDmlndvRQKCQEES 508
Cdd:pfam15709 336 DRLRAERA-EMRRLEVERKRREQEEQRRLQQEQLERAEKMREELE---LEQQRRFEEIRLRKQRLEE-----ERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 509 QMISSLQTQIHSQESDLQSQE--------------EELGRAKADLNRLQQEEAQL--EQSLQAGRIQlETIIKSLKATQD 572
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEfrrklqelqrkkqqEEAERAEAEKQRQKELEMQLaeEQKRLMEMAE-EERLEYQRQKQE 485
|
....*.
gi 1207195097 573 EINQAR 578
Cdd:pfam15709 486 AEEKAR 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
406-597 |
1.02e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLD---RETSSLQELEAQKQDAQDR 482
Cdd:PRK01156 196 NLELENIKKQIADDEKS----HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmknRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 483 LEEMDQQKAKLEDMLNDVRQKCQEEsqmISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLEt 562
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRNY---INDYFKYK----NDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYI- 342
|
170 180 190
....*....|....*....|....*....|....*
gi 1207195097 563 iikSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:PRK01156 343 ---KKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
437-598 |
1.15e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqqkakLEDMLNDVRQKCQEES---QMISS 513
Cdd:PRK02224 192 LKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDE-------ADEVLEEHEERREELEtleAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 514 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISK 593
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
....*
gi 1207195097 594 NIEQY 598
Cdd:PRK02224 343 EAESL 347
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
474-602 |
1.18e-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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 474 AQKQDAQDRLEEMDQQKAKLEDMLNDVrqkcqeESQmISSLQTQ---------IHSQESDLQSQEeelgrAKADLNRLQQ 544
Cdd:COG1196 172 ERKEEAERKLEATEENLERLEDILGEL------ERQ-LEPLERQaekaeryreLKEELKELEAEL-----LLLKLRELEA 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195097 545 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 602
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
436-583 |
1.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 515
Cdd:PRK04863 524 ELEQRLRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 516 TQ----IHSQE--SDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdEInqarSKLSQ 583
Cdd:PRK04863 600 ARapawLAAQDalARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE---EI----ERLSQ 666
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
436-580 |
1.44e-04 |
|
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: 45.02 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIRHKTTEVqemqNDLDRETSSLQELEAQ-KQDAQDRLEEMDQQKAKLEDML-----NDVRQkcQEEsq 509
Cdd:pfam04849 168 ALQEKLRGLEEENLKLRSEA----SHLKTETDTYEEKEQQlMSDCVEQLSEANQQMAELSEELarkmeENLRQ--QEE-- 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 510 mISSLQTQIhsqeSDLQSQEEELGRAKADLNR-LQQE---EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK 580
Cdd:pfam04849 240 -ITSLLAQI----VDLQHKCKELGIENEELQQhLQASkeaQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
408-618 |
1.47e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQStlafthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtSSLQELEAQKQDAQDRLEEMD 487
Cdd:PRK01156 491 EVKDIDEKIVDLKK----------RKEYLESEEINKSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLK 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQ--KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN--------RLQQEEAQLE---QSLQ 554
Cdd:PRK01156 560 LEdlDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksirEIENEANNLNnkyNEIQ 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 555 AGRIQLETIIKSLKATQDEInqarSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 618
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQI----AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
444-587 |
1.59e-04 |
|
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: 43.41 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 444 TEEAIRHKTTEVQEMQNDLDretsslQELEAQKQDAQDRLEEMDQQ--------KAKLEDMLNDVRQKCQEESQmisSLQ 515
Cdd:pfam01442 24 AQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEELQAKlgqnveelRQRLEPYTEELRKRLNADAE---ELQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 516 TQIHSQESDLQSQ-EEELGRAKADLN-RLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdeinQARSKLSQIQDS 587
Cdd:pfam01442 95 EKLAPYGEELRERlEQNVDALRARLApYAEELRQKLAERLEELKESLAPYAEEVQA------QLSQRLQELREK 162
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
432-591 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 432 REKYT--------LE--QDIR-ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV 500
Cdd:pfam01576 632 REKETralslaraLEeaLEAKeELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 501 RQ-KCQEESQMiSSLQTQIhsqESDLQSQEEELGRAKADLNR-LQQEEAQLE----QSLQA--GRIQLETIIKSLKATQD 572
Cdd:pfam01576 712 EDaKLRLEVNM-QALKAQF---ERDLQARDEQGEEKRRQLVKqVRELEAELEderkQRAQAvaAKKKLELDLKELEAQID 787
|
170 180
....*....|....*....|....*..
gi 1207195097 573 EINQARS-------KL-SQIQDSQHEI 591
Cdd:pfam01576 788 AANKGREeavkqlkKLqAQMKDLQREL 814
|
|
| bMERB_dom |
pfam12130 |
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ... |
469-588 |
1.70e-04 |
|
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: 42.50 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 469 LQELEAQkqdaqdrLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH------SQESDLQSQEEELgrakadlnRL 542
Cdd:pfam12130 2 LEEIEER-------QRELEERGVELEKALRGEMSGDEEEEQLLQEWFKLVNeknalvRRESELMYLAKEQ--------DL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 543 QQEEAQLEQSLQAgRIQLETIIKS---LKATQD------EINQARSKLSQIQDSQ 588
Cdd:pfam12130 67 EERQARLEQELRE-LMSKPDWLKTeedKQREEElleelvEIVEQRDALVDSLEED 120
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
428-599 |
1.70e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 428 WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE 507
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 508 SQMISSLQTQIhsqesdlqsqeEELGRAKADLNRLQQEEAQLEQSLQ------------AGRI-QLETIIKSLKA---TQ 571
Cdd:COG1340 91 REELDELRKEL-----------AELNKAGGSIDKLRKEIERLEWRQQtevlspeeekelVEKIkELEKELEKAKKaleKN 159
|
170 180
....*....|....*....|....*...
gi 1207195097 572 DEINQARSKLSQIQDSQHEISKNIEQYS 599
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELA 187
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
509-603 |
1.72e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 509 QMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE----TIIKSLKATQDEI---------- 574
Cdd:PRK00409 520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkeaqQAIKEAKKEADEIikelrqlqkg 599
|
90 100
....*....|....*....|....*....
gi 1207195097 575 NQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
433-585 |
1.77e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 433 EKYTLEQDIRETeeairhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcQEESQMIS 512
Cdd:PRK11281 57 EDKLVQQDLEQT-----------LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLR 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 513 SLQTQIHSQESDLQSQEEELGRAKADL--NRLQQEEAQLEQSLQAGRIQ-LETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPSQRVLLQAE 200
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
415-588 |
1.82e-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: 45.50 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 415 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 494
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 495 dmlndvRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGR--------------AKADLNRLQQEEAQLEQSLQA-G 556
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEErR 552
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 557 RIQLETIIKSLKATQ-DEINQARSKLSQIQDSQ 588
Cdd:pfam17380 553 RIQEQMRKATEERSRlEAMEREREMMRQIVESE 585
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
406-598 |
1.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEmqndLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:PRK03918 185 IKRTENIEELIKEKEKELE----EVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIK 565
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----IEERIK 331
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 566 SLKATQDEINQARSKLSQIQDSQHEISKNIEQY 598
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
461-546 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDREtssLQELEAQKQDA--------QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT------QIHSQESDLQ 526
Cdd:COG0542 415 ELERR---LEQLEIEKEALkkeqdeasFERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeeleQRYGKIPELE 491
|
90 100
....*....|....*....|
gi 1207195097 527 SQEEELGRAKADLNRLQQEE 546
Cdd:COG0542 492 KELAELEEELAELAPLLREE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
456-604 |
2.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 456 QEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqQKAKLEDMLNDVRQkcqeesqmISSLQTQIHSQESDLQSQEEELGRA 535
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 536 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK--------------------LSQIQDSQHEISKNI 595
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEKRL 316
|
....*....
gi 1207195097 596 EQYSSTLNG 604
Cdd:PRK03918 317 SRLEEEING 325
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
414-597 |
2.35e-04 |
|
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: 44.64 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 414 QEIAQLQsTLAFTHWDTLREKytlEQDIRETEEAIR-----------------HKTTEVQEMQNDLDRETSSLQELE--- 473
Cdd:pfam15558 21 QRMRELQ-QQAALAWEELRRR---DQKRQETLERERrlllqqsqeqwqaekeqRKARLGREERRRADRREKQVIEKEsrw 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 474 ---AQKQDAQdRLEEMdqQKAKLEDMLndvRQKCQEESqmisslqtqihsqesdLQSQEEELgRAKADLNRLQQ----EE 546
Cdd:pfam15558 97 reqAEDQENQ-RQEKL--ERARQEAEQ---RKQCQEQR----------------LKEKEEEL-QALREQNSLQLqerlEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 547 AQLEQSLQAGRIQLETIIKSLKatqDEIN-QARSKL--SQIQDSQHEISKNIEQ 597
Cdd:pfam15558 154 ACHKRQLKEREEQKKVQENNLS---ELLNhQARKVLvdCQAKAEELLRRLSLEQ 204
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
406-603 |
2.57e-04 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 44.06 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNdldretsslqeleAQKQDAQDRLEE 485
Cdd:COG5325 76 EDEIDELSKKVNQDLQRCE----KILKTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKaKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEeLGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 565
Cdd:COG5325 139 VLQAK-FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFR 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207195097 566 SLkatQDEINQarsklsqiqdsQHEISKNIEQYSSTLN 603
Cdd:COG5325 213 DL---GSLVGE-----------QGELVDRIDFNIENTS 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
454-603 |
2.72e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 454 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEeel 532
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS--- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 533 grakADLNRLQQEEAQLEQSLQagriQLETIIK-------------SLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 599
Cdd:PHA02562 255 ----AALNKLNTAAAKIKSKIE----QFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE 326
|
....
gi 1207195097 600 STLN 603
Cdd:PHA02562 327 EIMD 330
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-606 |
3.05e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAFTHwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLD-KNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQE---------------ESQMISS------LQTQIHSQESDLQSQEEELGRAKADLNRLQQ 544
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKEnkknidkflteikkkEKELEKLnnkyndLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 545 EEAQLEQSLqagrIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 606
Cdd:TIGR04523 195 KLLKLELLL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
407-581 |
3.16e-04 |
|
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: 44.14 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAftHWDTLREKYTLEqdirETEEAIRHKttEVQEMQNDLDRETSSLQELEAQKQDAQDRL-EE 485
Cdd:pfam13868 184 REIARLRAQQEKAQDEKA--ERDELRAKLYQE----EQERKERQK--EREEAEKKARQRQELQQAREEQIELKERRLaEE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKC---QEESQMISSLQTQiHSQEsdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqlet 562
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEeieQEEAEKRRMKRLE-HRRE--LEKQIEEREEQRAAEREEELEEGERLREEEAER----- 327
|
170
....*....|....*....
gi 1207195097 563 iikslkatQDEINQARSKL 581
Cdd:pfam13868 328 --------RERIEEERQKK 338
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
399-619 |
3.16e-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: 44.56 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 399 GSGEFTGI--------KELDDISQEI-----AQLQSTLAFTHWDTLREKY--TLEQDIRETEEAIRHKTTEVQEMQNDLD 463
Cdd:pfam07902 69 GSGESTGLfksleemlSQLKELNLELtdtknSNLWSKIKLNNNGMLREYHndTIKTEIVESAEGIATRISEDTDKKLALI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 464 RETssLQELEAQKQDAQDRLEEMDQQ-----KAKLE----DMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelGR 534
Cdd:pfam07902 149 NET--ISGIRREYQDADRQLSSSYQAgieglKATMAsdkiGLQAEIQASAQGLSQRYDNEIRKLSAKITTTSS-----GT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 535 AKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD----EINQ-------ARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:pfam07902 222 TEAYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQstayQISQeisnregAVSRVQQDLDSYQRRLQDAEKNYSSLT 301
|
250
....*....|....*.
gi 1207195097 604 GTHGGSMTNLADMSEG 619
Cdd:pfam07902 302 QTVKGLQSTVSDPNSK 317
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
436-586 |
3.28e-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: 43.56 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 436 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKL--EDMLNDVRQkCQEESQMISS 513
Cdd:pfam06008 51 SLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLgeNDFALPSSD-LSRMLAEAQR 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 514 LQTQIHSQE--SDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAgriQLETIiksLKATQDEINQARSKLSQIQD 586
Cdd:pfam06008 130 MLGEIRSRDfgTQLQNAEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYEAKLSDLRE 194
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
435-590 |
4.19e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 435 YTLEQDIRETEEAIRH---KTTEVQEMQNDL-DRET-----------SSLQELEAQKQDAQDRLEEMDQ-------QKAK 492
Cdd:COG5278 29 YLSLNRLREASEWVEHtyeVLRALEELLSALlDAETgqrgylltgdeSFLEPYEEARAEIDELLAELRSltadnpeQQAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 493 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLqsqeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 572
Cdd:COG5278 109 LDELEALIDQWLAELEQVIALRRAGGLEAALAL----VRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
170
....*....|....*...
gi 1207195097 573 EINQARSKLSQIQDSQHE 590
Cdd:COG5278 185 LLALAELLLLALARALAA 202
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
403-593 |
4.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 403 FTGIKELDD-ISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEA----IRHKTTEVQEMQNDLDRETSSLQELEAQK 476
Cdd:PRK01156 134 FVGQGEMDSlISGDPAQRKKILDeILEINSLERNYDKLKDVIDMLRAeisnIDYLEEKLKSSNLELENIKKQIADDEKSH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 477 QDAQ---DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---DLNRLQQEEAQLE 550
Cdd:PRK01156 214 SITLkeiERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEleeRHMKIINDPVYKN 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 551 Q-------SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD--SQHEISK 593
Cdd:PRK01156 294 RnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyNDYIKKK 345
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
429-581 |
4.35e-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: 44.44 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTLEQDIR-----ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQ----DRLEEMDQQKAKLEDMLND 499
Cdd:pfam12128 707 EQKREARTEKQAYWqvvegALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIER 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 500 VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARS 579
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERA---ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
..
gi 1207195097 580 KL 581
Cdd:pfam12128 864 GL 865
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
430-594 |
4.59e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 430 TLREKYTLEQDIRET-------EEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD---RLEEMDQQKAKLEDMLND 499
Cdd:COG5022 831 KLRETEEVEFSLKAEvliqkfgRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIdvkSISSLKLVNLELESEIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 500 VRQKCQ----EESQMISSLQT--QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDE 573
Cdd:COG5022 911 LKKSLSsdliENLEFKTELIArlKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE----EYEDLLKKSTILVRE 986
|
170 180
....*....|....*....|.
gi 1207195097 574 INQARSKLSQIQDSQHEISKN 594
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQ 1007
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
409-592 |
4.75e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLA-FTHWDTLREKY----TLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqeleaqkQDAQDRL 483
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqFQKVIKMYEKGgvcpTCTQQISEGPDRITKIKDKLKELQHSLEKL-----------DTAIDEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 484 EEmdqqkakLEDMLNDVRQKCQEesqmissLQTQIHSQESDLQSQEEELGRAKADLNRlqqeeaqleqsLQAGRIQLETI 563
Cdd:PHA02562 326 EE-------IMDEFNEQSKKLLE-------LKNKISTNKQSLITLVDKAKKVKAAIEE-----------LQAEFVDNAEE 380
|
170 180
....*....|....*....|....*....
gi 1207195097 564 IKSLKATQDEINQARSKLSQIQDSQHEIS 592
Cdd:PHA02562 381 LAKLQDELDKIVKTKSELVKEKYHRGIVT 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
442-584 |
4.78e-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: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 442 RETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQkcQEESQMISSLQTQIHSQ 521
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE--QLEAEREELLEELLEEE 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 522 ESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQA-GRI---------QLETIIKSLKATQDEINQARSKLSQI 584
Cdd:COG1196 746 ELLEEEALEELPEP-PDLEELERELERLEREIEAlGPVnllaieeyeELEERYDFLSEQREDLEEARETLEEA 817
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-604 |
4.85e-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: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 383 DMAALTEMRRDSSSSVGSGEFTGIKELDDISQEIAQLQSTLAFTHWDTLRE--KYTLEQDIRE-TEEAIRHKT------- 452
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelREQLEAGKLEfNEEEYRLKSrlgelkl 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 453 ----------TEVQEMQND--LDRETSSLQELEAQKQDAQDRLEEM----DQQKAKLEDM---LNDVRQKCQE-ESQMIS 512
Cdd:pfam12128 452 rlnqatatpeLLLQLENFDerIERAREEQEAANAEVERLQSELRQArkrrDQASEALRQAsrrLEERQSALDElELQLFP 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 513 SLQTQIHSQESDLQSQEEELGR--AKADLNR------LQQEEAQLEQSLQAGRIQLETI-IKSLKATQDEINQARSKLSQ 583
Cdd:pfam12128 532 QAGTLLHFLRKEAPDWEQSIGKviSPELLHRtdldpeVWDGSVGGELNLYGVKLDLKRIdVPEWAASEEELRERLDKAEE 611
|
250 260
....*....|....*....|.
gi 1207195097 584 IQDSQHEISKNIEQYSSTLNG 604
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANG 632
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
451-565 |
4.88e-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: 41.41 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 451 KTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDvrqkcqeesqmisslqtqihsQESDLQSQE 529
Cdd:pfam03938 13 ESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEEREE---------------------KEQELQKKE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207195097 530 EELGRAKADLNR-LQQEEAQLEQSLQAgriQLETIIK 565
Cdd:pfam03938 72 QELQQLQQKAQQeLQKKQQELLQPIQD---KINKAIK 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
407-598 |
5.15e-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: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEem 486
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASE----RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE-- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 dqqkakledMLNDVRQKCQeesQMISSLQTQIHSQESDLQSQE---EELGRAKADLN-RLQQEE-----------AQLEQ 551
Cdd:pfam01576 907 ---------LLNDRLRKST---LQVEQLTTELAAERSTSQKSEsarQQLERQNKELKaKLQEMEgtvkskfkssiAALEA 974
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207195097 552 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 598
Cdd:pfam01576 975 KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQY 1021
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
442-585 |
5.26e-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: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 442 RETEEAIR--HKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE-EMDQQKAKLEDMLNDVRQKCQEESQMisslQTQI 518
Cdd:COG2268 210 RETEIAIAqaNREAEEAELEQEREIETARIAEAEAELAKKKAEERrEAETARAEAEAAYEIAEANAEREVQR----QLEI 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 519 HSQESD--LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT---QDEINQARSKLSQIQ 585
Cdd:COG2268 286 AEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEaegKRALAEAWNKLGDAA 357
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
437-603 |
5.49e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQ--NDLDRET----SSLQELEAQKQDAQDRLEEMD-------QQKAKLEDMLNDVRQK 503
Cdd:PRK10929 80 LSAELRQQLNNERDEPRSVPPNMstDALEQEIlqvsSQLLEKSRQAQQEQDRAREISdslsqlpQQQTEARRQLNEIERR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 504 CQ---------EESQMiSSLQTQIHSQESDLQSQE---------EELGRAKADLnrLQQEEAQLEQSLQAGRIQL----- 560
Cdd:PRK10929 160 LQtlgtpntplAQAQL-TALQAESAALKALVDELElaqlsannrQELARLRSEL--AKKRSQQLDAYLQALRNQLnsqrq 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 561 ---------------------ETIIKSLKATQD---EINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:PRK10929 237 reaeralestellaeqsgdlpKSIVAQFKINRElsqALNQQAQRMDLIASQQRQAASQTLQVRQALN 303
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
382-583 |
5.82e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 382 SDMAALTEMRRDSSSSVGSGEFTGIKELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQnD 461
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH-A 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 462 LDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNR 541
Cdd:PRK01156 327 IIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195097 542 LQQEEAQLEQSLQagriQLETIIKSLKATQDEINQARSKLSQ 583
Cdd:PRK01156 407 IKKELNEINVKLQ----DISSKVSSLNQRIRALRENLDELSR 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
493-603 |
6.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 493 LEDMLndvRQKCQEESQMISSLQ--------TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETII 564
Cdd:COG4717 43 IRAML---LERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREEL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207195097 565 KSLKATQD------EINQARSKLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:COG4717 119 EKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEE 163
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
408-597 |
6.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTL---------AFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQ 477
Cdd:PRK02224 315 RREELEDRDEELRDRLeecrvaaqaHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 478 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA-----------DLNRLQQEE 546
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegspHVETIEEDR 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207195097 547 AQLEqSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQhEISKNIEQ 597
Cdd:PRK02224 475 ERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE-ERREDLEE 523
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
464-600 |
7.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 464 RETSSLQELEAQKQDAQDRLEEmdqqkAKLEdmLNDVRQKCQEESQ-MISSLQTQIhsqESDLQSQEEELGRAKadlNRL 542
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE-----AKKE--AEAIKKEALLEAKeEIHKLRNEF---EKELRERRNELQKLE---KRL 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207195097 543 QQEEAQLE---QSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 600
Cdd:PRK12704 92 LQKEENLDrklELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
406-573 |
7.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEA-------EEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEdmlnDVRQKCQEESQMISSLQT----------QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQA 555
Cdd:PTZ00121 1697 EAEEAKKAE----ELKKKEAEEKKKAEELKKaeeenkikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
170
....*....|....*...
gi 1207195097 556 GRIQLETIIKSLKATQDE 573
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 ... |
407-553 |
7.23e-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: 43.63 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLqstlafthwdtLREKYTLEQDIR-ETE-----EAIR----HKTTEVQEMqndldretssLQELEAQK 476
Cdd:pfam01576 26 SELKELEKKHQQL-----------CEEKNALQEQLQaETElcaeaEEMRarlaARKQELEEI----------LHELESRL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 477 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 553
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
372-590 |
7.90e-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: 43.27 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 372 SLSGYMTPVGSDMAALTEmRRDSSSSVGSGEFTGIKELD-DISQ---EIAQLQSTLAFTH--WDTLREKYTLEQDIRETE 445
Cdd:pfam10174 486 ALQPELTEKESSLIDLKE-HASSLASSGLKKDSKLKSLEiAVEQkkeECSKLENQLKKAHnaEEAVRTNPEINDRIRLLE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 446 EAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAqdrleemDQQKAKLEDMlndVRQKCQEESQMISSLQtqiHSQesdl 525
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILREVENEKNDK-------DKKIAELESL---TLRQMKEQNKKVANIK---HGQ---- 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 526 qsQEEELGRAKADLNRLQQEEAQLEQSLQagrIQLETIIKSLKATQDEINQARSKLSQIQDSQHE 590
Cdd:pfam10174 628 --QEMKKKGAQLLEEARRREDNLADNSQQ---LQLEELMGALEKTRQELDATKARLSSTQQSLAE 687
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
395-577 |
7.94e-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: 43.24 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 395 SSSVGSGEFTGIKELDDISQEIAQLQSTLAFTHWDTlREKYTLEQDIRETEE---AIRHKTTEVQEMQNDLDRETSSLQe 471
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-RQKLNLSTRLRQLEDernSLQEQLEEEEEAKRNVERQLSTLQ- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 472 leAQKQDAQDRLEEM-------DQQKAKLEDMLNDVRQKCQEESqmisslqtqihsqesdlqSQEEELGRAKadlNRLQQ 544
Cdd:pfam01576 524 --AQLSDMKKKLEEDagtlealEEGKKRLQRELEALTQQLEEKA------------------AAYDKLEKTK---NRLQQ 580
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 545 EEAQLEQSLQAGRiqleTIIKSLKATQDEINQA 577
Cdd:pfam01576 581 ELDDLLVDLDHQR----QLVSNLEKKQKKFDQM 609
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
437-586 |
8.03e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNdvrqkcqEESQMISSLQT 516
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLA-------ELAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 517 QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLeqslqagRIQLETIIKSLKATQDEInqaRSKLSQIQD 586
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAAL-------RRQLAALEAALDASEKRD---RESQAKIAD 176
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
408-603 |
8.45e-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: 42.63 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLE 484
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEddEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKvTIKADAKDWRAHLE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKcqeesqmisslqtqihsqesdLQSQEEELGRAkadLNRLQQEEAQLEQslqagriQLETII 564
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207195097 565 KSLKATQDEinqarskLSQIQDSQHEISKNIEQYSSTLN 603
Cdd:pfam10498 275 QEYREAQDE-------LSEVQEKYKQLSEGVTERTRELA 306
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
408-606 |
9.30e-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: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTlafthwdtlrekytleqdIRETEEAIRHktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 487
Cdd:TIGR00606 837 ELDTVVSKIELNRKL------------------IQDQQEQIQH----LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQ----IHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqleti 563
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------ 968
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207195097 564 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 606
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
431-597 |
9.54e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA-------QKQDAQDRLEEMDQQKAKLEDMLNDVRQK 503
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrKKAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 504 -------------CQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT 570
Cdd:TIGR00618 517 rqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
|
170 180
....*....|....*....|....*....
gi 1207195097 571 QDEIN-QARSKLSQIQDSQ-HEISKNIEQ 597
Cdd:TIGR00618 597 QDLTEkLSEAEDMLACEQHaLLRKLQPEQ 625
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
409-593 |
9.73e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQStlafthwdtLREKYtleQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAqkqdAQ---DRLEE 485
Cdd:COG0497 147 LDAFAGLEELLEE---------YREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEA----AAlqpGEEEE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMlNDVRQKCQEESQMISSLQTQIHSQesdlqsqeeeLGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 562
Cdd:COG0497 211 LEEERRRLSNA-EKLREALQEALEALSGGEGGALDL----------LGQALRALERLAEYDPSLAelaERLESALIELEE 279
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 563 IIKSLKATQD--EINQARskLSQIQDSQHEISK 593
Cdd:COG0497 280 AASELRRYLDslEFDPER--LEEVEERLALLRR 310
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
440-600 |
1.03e-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: 42.89 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 440 DIRETEEAIRHKTTEVQEMQNDLDRETSSLQELE----AQKQDaqdrLEEMDQQKAKLEDMLN------DVRQKCQEESQ 509
Cdd:pfam10174 110 TPELTEENFRRLQSEHERQAKELFLLRKTLEEMElrieTQKQT----LGARDESIKKLLEMLQskglpkKSGEEDWERTR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 510 MISSLQTQIHSQESDLQSQEEELGRAKADL---NRLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQ 583
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLL 265
|
170
....*....|....*..
gi 1207195097 584 IQDSQHEISKNIEQYSS 600
Cdd:pfam10174 266 HTEDREEEIKQMEVYKS 282
|
|
| PRK13735 |
PRK13735 |
conjugal transfer mating pair stabilization protein TraG; Provisional |
470-573 |
1.05e-03 |
|
conjugal transfer mating pair stabilization protein TraG; Provisional
Pssm-ID: 184287 [Multi-domain] Cd Length: 942 Bit Score: 42.81 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 470 QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEEL-----GRAKADLNRLQQ 544
Cdd:PRK13735 833 QDIIADHQGHQAIIEQRTQDSGIRNDVKHQVDNMVTEYEGNIGDTQNSIRGEENTVKGQYSELqnhhkTEALSQNNKYNE 912
|
90 100
....*....|....*....|....*....
gi 1207195097 545 EEAqlEQSLQAGRIQLETIIKSLKATQDE 573
Cdd:PRK13735 913 EKS--AQERMPGADSPEELMKRAKEYQDK 939
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
402-584 |
1.06e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 402 EFTGIKELDDISQEIAQ----LQSTLAFthwdtlrEKYTLEQDIRETEEAIRHKTTE-VQEMQNDLDRETSSLQ---ELE 473
Cdd:TIGR00618 709 LETHIEEYDREFNEIENasssLGSDLAA-------REDALNQSLKELMHQARTVLKArTEAHFNNNEEVTAALQtgaELS 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 474 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 553
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
170 180 190
....*....|....*....|....*....|.
gi 1207195097 554 QagriQLETIIKSLKATQDEINQARSKLSQI 584
Cdd:TIGR00618 862 A----QLTQEQAKIIQLSDKLNGINQIKIQF 888
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
408-600 |
1.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAfthwdtLREKYTLEQDIRETEEairhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 487
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIK------TYNKNIEEQRKKNGEN--------IARKQNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE---------SDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQA 555
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207195097 556 GRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 600
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
425-613 |
1.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 425 FTHWDTLREKYtleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQk 503
Cdd:PHA02562 165 LSEMDKLNKDK-----IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAKTIKAEIEE- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 504 CQEEsqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---------QSLQAGRIQLETIIKSLKATQ--- 571
Cdd:PHA02562 239 LTDE---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQhsl 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207195097 572 DEINQARSKLSQIQDSQHEISKNIEQYSSTLNgTHGGSMTNL 613
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKIS-TNKQSLITL 356
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
408-591 |
1.25e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLafthwDTLREKYTLE--------QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKqDA 479
Cdd:PRK10246 683 ELTALQNRIQQLTPLL-----ETLPQSDDLPhseetvalDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-DT 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 480 QDRLEEMDQQKAKLEDMLND--------VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ 551
Cdd:PRK10246 757 ALQASVFDDQQAFLAALLDEetltqleqLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQ 836
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207195097 552 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEI 591
Cdd:PRK10246 837 QLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQV 876
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
441-583 |
1.27e-03 |
|
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: 40.38 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 441 IRETEEAIRHKT---TEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEMDQQKAKLedmlndvrqkcqeesqmiSSLQTQ 517
Cdd:pfam11559 44 LQQRDRDLEFREslnETIRTLEAEIERLQSKIERLKTQLEDLE---RELALLQAKE------------------RQLEKK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 518 IHSQESDLQSQEEELGRAKadlNRLQQEEAQLEQslqagriqletiikSLKATQDEINQARSKLSQ 583
Cdd:pfam11559 103 LKTLEQKLKNEKEELQRLK---NALQQIKTQFAH--------------EVKKRDREIEKLKERLAQ 151
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
450-599 |
1.29e-03 |
|
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: 39.47 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 450 HKTTEVQEMQndldretsslQELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLqtqihsqesdlqsqe 529
Cdd:pfam13863 3 EKKREMFLVQ----------LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKFDKF--------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 530 eelgrakadlnrLQQEEAQLEQSLQagRIQLETIIKSLKatQDEINQARSKLSQIQDSQHEISKNIEQYS 599
Cdd:pfam13863 54 ------------LKENDAKRRRALK--KAEEETKLKKEK--EKEIKKLTAQIEELKSEISKLEEKLEEYK 107
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
407-577 |
1.30e-03 |
|
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: 40.59 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlqeleaqkqdaqDRLEEM 486
Cdd:pfam16789 14 KRVEEAEKVVKDKKRALE-------KEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 487 DQQKAKLEDMLNDVRQKCQEESQmisslqtQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIiks 566
Cdd:pfam16789 75 KRYIKVVKERLKQEEKKVQDQKE-------QVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER--- 144
|
170
....*....|.
gi 1207195097 567 lkaTQDEINQA 577
Cdd:pfam16789 145 ---EQDEIGSA 152
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
409-597 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 409 LDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIrETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 487
Cdd:PRK02224 470 IEEDRERVEELEAELE-----DLEEEVeEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 488 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQAGRIQLETI---- 563
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeln 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207195097 564 -------------IKSLKATQDE--INQARSKLSQIQDSQHEISKNIEQ 597
Cdd:PRK02224 623 derrerlaekrerKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
501-600 |
1.30e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.53 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 501 RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQL--------------ETIIKS 566
Cdd:COG5283 13 KSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrqlsaaqRRLRSS 92
|
90 100 110
....*....|....*....|....*....|....
gi 1207195097 567 LKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 600
Cdd:COG5283 93 LEQTNRQLERQQQRLARLGARQDRLKAARARLQR 126
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
431-590 |
1.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EEMDQQKaKLEDMLNDVRQKCQ- 505
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqTALRQQE-KIERYQADLEELEEr 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 506 -EESQMISSLQT-QIHSQESDLQSQEEELGRAK---ADLNR---LQQEEA-QLEQSLQA-GRIQ------------LETI 563
Cdd:PRK04863 364 lEEQNEVVEEADeQQEENEARAEAAEEEVDELKsqlADYQQaldVQQTRAiQYQQAVQAlERAKqlcglpdltadnAEDW 443
|
170 180 190
....*....|....*....|....*....|...
gi 1207195097 564 IKSLKATQDEI----NQARSKLSQIQD--SQHE 590
Cdd:PRK04863 444 LEEFQAKEQEAteelLSLEQKLSVAQAahSQFE 476
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
445-583 |
1.41e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 445 EEAIRHKTTE---VQEMQNDLDRETSSL----QELEAQKQDAQDRL----------EEM----DQQKAKLEDMLNDVRQK 503
Cdd:pfam01576 4 EEEMQAKEEElqkVKERQQKAESELKELekkhQQLCEEKNALQEQLqaetelcaeaEEMrarlAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 504 CQEESQMISSLQTQIHSQESDLQSQEEELgrakadlnrlqQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQ 583
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQL-----------DEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
454-607 |
1.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 454 EVQEMQNDLDRETSSlqeleaqkqdAQDRLEEMDQQKAKLEdmlndvrqkcQEESQMIsslqTQIHSQESDLQSQEEELG 533
Cdd:TIGR00606 692 ELQEFISDLQSKLRL----------APDKLKSTESELKKKE----------KRRDEML----GLAPGRQSIIDLKEKEIP 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 534 RAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQArSKLSQIQDSQHEISKNIEQYSSTLNGTHG 607
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-539 |
1.88e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAfthwdTLREKYT-----LEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQKQDAQ 480
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIE-----RLEARLErledrRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 481 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihsqesDLQSQEEELGRAKADL 539
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--------RLQENLEGFSEGVKAL 511
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
452-605 |
1.93e-03 |
|
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: 40.45 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 452 TTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ-KAKLEDM----LNDVRQ-------------KCQEESQMISS 513
Cdd:pfam15272 3 TSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSyKKKYLQTrnelINELKQskklydnyyklysKYQQLKKISNE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 514 ---LQTQIHSQESDLQSQEEELGRAKADLN-RLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 586
Cdd:pfam15272 83 sldLQSTITNLESQLVDQAIDKDREIHNLNeKILSLELRnqeLETKREIDKMKYESRIDELERQLKEQEYPNVSSSSPYF 162
|
170
....*....|....*....
gi 1207195097 587 SQHEISKNIEQYSSTLNGT 605
Cdd:pfam15272 163 STSSYRDSSELFSTDYNLK 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-539 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLafthwDTLREKY---------TLEQDIRETEEAIRHKTTEVQEMQNDLDR----ETSSLQELEA 474
Cdd:COG4913 310 ELERLEARLDALREEL-----DELEAQIrgnggdrleQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 475 QKQDAQDRLEEMD-------QQKAKLEDMLNDVRQKCQEESQMISSLQTQ---IHSQESDLQSQ-EEELGRAKADL 539
Cdd:COG4913 385 LRAEAAALLEALEeelealeEALAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDAlAEALGLDEAEL 460
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
438-596 |
2.24e-03 |
|
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: 41.55 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 438 EQDIRETEEAIRHKTTEVQEMQNDLDRETSslqELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLQTQ 517
Cdd:pfam05701 285 KKTSTSIQAALASAKKELEEVKANIEKAKD---EVNCLRVAAASLRSELEKEKAELASL----RQREGMASIAVSSLEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 518 IHSQESDL---QSQEEELGRAKADLNRLQQEEAQ-LEQSLQAGRIQLETIIKSlkatQDEINQARSKLSQIQDSQHEISK 593
Cdd:pfam05701 358 LNRTKSEIalvQAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAREELRKA----KEEAEQAKAAASTVESRLEAVLK 433
|
...
gi 1207195097 594 NIE 596
Cdd:pfam05701 434 EIE 436
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
435-531 |
2.51e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.08 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 435 YTLEQDIRETEEAIRHKttEVQEMQNDLdreTSSLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQMI 511
Cdd:smart00150 1 QQFLRDADELEAWLEEK--EQLLASEDL---GKDLESVEALLKKHEAFEAELEAHEERVEALNelgEQLIEEGHPDAEEI 75
|
90 100
....*....|....*....|
gi 1207195097 512 SSLQTQIHSQESDLQSQEEE 531
Cdd:smart00150 76 EERLEELNERWEELKELAEE 95
|
|
| CENP-Q |
pfam13094 |
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ... |
431-555 |
2.54e-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: 39.58 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 510
Cdd:pfam13094 25 LDRNKALEAQLSAELHSLELLEEEIEKEEALLESDEEYLEELEKNAKAEARERKEKLKKEHPLLQEDDSGVLSLPELSSD 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEELGRA-KADLNRLQQEEAQLEQSLQA 555
Cdd:pfam13094 105 LGLGDTDFSLFDPTLDEELLPLLEQlQKHLESMQGNLAQLEGLNEA 150
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
475-577 |
2.58e-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: 39.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 475 QKQDAQDRLE-EMDQQKAKLEDMLNDVR---QKCQEESQMISslqtqihsqESDLQSQEEELGRAKADLNRLQQEeaqLE 550
Cdd:COG2825 40 EGKAAQKKLEkEFKKRQAELQKLEKELQalqEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQE---AQ 107
|
90 100
....*....|....*....|....*..
gi 1207195097 551 QSLQAGRIQLetiiksLKATQDEINQA 577
Cdd:COG2825 108 QDLQKRQQEL------LQPILEKIQKA 128
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
452-580 |
2.61e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.54 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 452 TTEVQEMQndldretsSLQELEAQKQDAQDRLEemdQQKakledMLNDVrqkcQEESQMISSLQTQIHSQ--ESDLQSQE 529
Cdd:PTZ00491 660 TTKSQEAA--------ARHQAELLEQEARGRLE---RQK-----MHDKA----KAEEQRTKLLELQAESAavESSGQSRA 719
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 530 EELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD-EINQARSK 580
Cdd:PTZ00491 720 EALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKRQElELEYEQAQ 771
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
445-560 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 445 EEAIRHKttevQEMQndlDRetssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-------QKCQEESQMISSLQTQ 517
Cdd:pfam20492 2 EEAEREK----QELE---ER----LKQYEEETKKAQEELEESEETAEELEEERRQAEeeaerleQKRQEAEEEKERLEES 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 518 IHSQESDLQSQEEELGRAKADLNRLQQE------EA-QLEQSLQAGRIQL 560
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEverkeeEArRLQEELEEAREEE 120
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
428-532 |
2.71e-03 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 39.99 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 428 WDTLREKytLEQDIRETEEAiRHKTTEVQEMQNDLDRETSSLQELEAQKQ-----DAQDRLEEMDQQ----KAKLEDMLn 498
Cdd:pfam03280 84 LAALRAQ--LPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQraawQQRLDDYL- 159
|
90 100 110
....*....|....*....|....*....|....
gi 1207195097 499 dvrqkcQEESQMisslqTQIHSQESDLQSQEEEL 532
Cdd:pfam03280 160 ------AERQQI-----NAAGLSEQERQAAIAQL 182
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
408-581 |
2.79e-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: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 408 ELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAI--------------RHKTTEVQEMQNDLDRETSSLQ--- 470
Cdd:pfam01576 862 ERDELADEIASGASGKSAL----QDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQkse 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 471 ----ELEAQKQDAQDRLEEMDQQ------------KAKLEDMLNDVRQKCQEESQMISSL-QTQIHSQESDLQSQEEelg 533
Cdd:pfam01576 938 sarqQLERQNKELKAKLQEMEGTvkskfkssiaalEAKIAQLEEQLEQESRERQAANKLVrRTEKKLKEVLLQVEDE--- 1014
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 534 RAKAD---------LNRLQQEEAQLE------QSLQAGR--IQ--LETIIKSLKATQDEINQARSKL 581
Cdd:pfam01576 1015 RRHADqykdqaekgNSRMKQLKRQLEeaeeeaSRANAARrkLQreLDDATESNESMNREVSTLKSKL 1081
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
454-585 |
3.34e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 454 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsQMISSLQtqihSQESDLQS------ 527
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQE-ARIKDLE----AQRAQLQAgqpcpl 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 528 ------------QEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKatQDEiNQARSKLSQIQ 585
Cdd:PRK10246 509 cgstshpaveayQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQ--RDE-SEAQSLRQEEQ 575
|
|
| Zwint |
pfam15556 |
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ... |
407-554 |
3.35e-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: 40.35 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLAFT-HWDTLREKYtleqdiRETEEAIRHKTTEVQEMQNDLDRETSSLQE----LEAQKQDAQD 481
Cdd:pfam15556 46 QGLDPLASEDTSRQKAIAAKeQWKELKATY------QEHVEAITSALTQALPKMEEAQRKRAQLQEaleqLQAKKQMAME 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 482 RLEEMDQQkakledmlndvRQKCQEES-QMISSLQTQIHSQESDLQsqeEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:pfam15556 120 KLRTAQKQ-----------WQLQQEKHlQHLAEVSAEVRERQTGTQ---QELERLYQELGTLKQQAGQERDKLQ 179
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
410-562 |
3.59e-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: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 410 DDISQEIAQlqstlafthwDTLRekyTLEQDIRETEEAIRHKTTEVQEMQN-----DLDRETSSLQ----ELEAQKQDAQ 480
Cdd:COG3524 168 NQLSERARE----------DAVR---FAEEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 481 drleemdQQKAKLEDMLND----VRQKcqeESQmISSLQTQIHSQESDL--QSQEEELGRAKADLNRLQQEEAQLEQSLQ 554
Cdd:COG3524 235 -------AELAALRSYLSPnspqVRQL---RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYT 303
|
....*...
gi 1207195097 555 AGRIQLET 562
Cdd:COG3524 304 SALAALEQ 311
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
431-568 |
3.68e-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: 40.25 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 431 LREKYTLEQDIRETEEAIRHKTTEVQEMQndlDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsqm 510
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAER---AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEE--- 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195097 511 isslqtqihsqesdLQSQEEELGRAKAdlNRLQQEEAQLEQSLQAGRIQLETIIKSLK 568
Cdd:cd16269 250 --------------RENLLKEQERALE--SKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
437-638 |
4.02e-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: 40.96 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIrhktTEVQEMQNDLDRETSSLQE-LEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 515
Cdd:pfam10174 427 LQTDSSNTDTAL----TTLEEALSEKERIIERLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 516 TQIHSQESD-------LQSQEEELGRAKADLNRLQ---QEEAQLEQSLQAG-----RIQ-LETIIKSLK----ATQDEIN 575
Cdd:pfam10174 503 EHASSLASSglkkdskLKSLEIAVEQKKEECSKLEnqlKKAHNAEEAVRTNpeindRIRlLEQEVARYKeesgKAQAEVE 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 576 QARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKENGGFGAMEDPFKVK 638
Cdd:pfam10174 583 RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE 645
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
456-585 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 456 QEMQNDLDRETSSLQEleaQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 535
Cdd:cd21116 76 PDLIELADNLIKGDQG---AKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNAL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207195097 536 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:cd21116 153 KNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAF 202
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
455-601 |
4.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 455 VQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV---------RQKCQE------ESQMISSLQTQIH 519
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvaRELLRRlreqrhLAEQLQQLRMRLS 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 520 SQESDLQSQeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEISKNIEQYS 599
Cdd:PRK04863 524 ELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE---QLQARIQRLA 599
|
..
gi 1207195097 600 ST 601
Cdd:PRK04863 600 AR 601
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
429-586 |
4.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKYTLEQDIRETEeairHKTTEVQEMQNDLDRETSSLQELEAQKQD--------------AQDRLEEMDQQKAKLE 494
Cdd:pfam05622 4 EAQEEKDELAQRCHELD----QQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyllLQKQLEQLQEENFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 495 DMLNDVRQKCQEesqmissLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSlqAGRI-QLETIIKSLKATQDE 573
Cdd:pfam05622 80 TARDDYRIKCEE-------LEKEV----LELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLED 146
|
170
....*....|...
gi 1207195097 574 INQARSKLSQIQD 586
Cdd:pfam05622 147 LGDLRRQVKLLEE 159
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
437-511 |
4.75e-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: 38.33 E-value: 4.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQelEAQKQDAQDRLEEMDQQ-KAKLEDMLNDVRQKCQEESQMI 511
Cdd:smart00935 23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQKLQQDLQKRQQEELQKI 96
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
440-558 |
4.83e-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: 39.37 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 440 DIRETEEAIRHKTTEVQEMQNDL-DRETSSLQELEAQKQDAQDR-------LEEMDQQKAKLEDMLndvRQKCQEESQmI 511
Cdd:pfam14988 1 ENKFFLEYLAKKTEEKQKKIEKLwNQYVQECEEIERRRQELASRytqqtaeLQTQLLQKEKEQASL---KKELQALRP-F 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1207195097 512 SSLQTQihsQESDLQSQEEELGRAKADLN--------RLQQEEAQLEQSLQAGRI 558
Cdd:pfam14988 77 AKLKES---QEREIQDLEEEKEKVRAETAekdreahlQFLKEKALLEKQLQELRI 128
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
439-570 |
4.86e-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: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 439 QDIRETEEAIR---HKTTEVQEMQNDLDRETSSLQELeaqkqdAQDRLEemdqqkakLEDMLNDVRQKCQEESQMISSLQ 515
Cdd:pfam07200 9 QELLNDEDKLDafvHSLPQVKALQAEKEELLAENESL------AEENLS--------LEPELEELRSQLQELLEELKALK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 516 TQIHSQESDLQSQEEELGRAkADLNRLQ-----QEEA--QLEQSLQAGRIQLETIIKSLKAT 570
Cdd:pfam07200 75 SEYEEKEQELDELLSKFSPD-ALLARLQaaaaeAEEEseALAESFLEGEIDLDEFLKQFKEK 135
|
|
| ING_ING3_Yng2p |
cd16858 |
Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar ... |
437-519 |
5.18e-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: 37.18 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELeAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 516
Cdd:cd16858 4 LPSELRHLLTEIREKDLQVQELLDRIQQRDAKLFKH-IKKNGSLTPNPKEEELYEKIREDYDKALELADEKVELANRLLD 82
|
...
gi 1207195097 517 QIH 519
Cdd:cd16858 83 LVD 85
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
406-607 |
5.41e-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: 40.80 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIaQLQSTLafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLdreTSSLQELEAQKQDAQDRLEE 485
Cdd:TIGR00606 363 IRARDSLIQSL-ATRLEL-----DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL---CADLQSKERLKQEQADEIRD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE---EAQL--EQSLQAGRIQL 560
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKkeVKSLQNEKADL 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207195097 561 ETIIKSLKATQDEINQARSKLSQIQ-------DSQHEISKNIEQYSSTLNGTHG 607
Cdd:TIGR00606 514 DRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmDKDEQIRKIKSRHSDELTSLLG 567
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
437-584 |
5.58e-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: 39.32 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQT 516
Cdd:cd21116 82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 517 QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQI 584
Cdd:cd21116 155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAEssIDAAFLQADLKAAKADWNQLYEQAKSL 224
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
413-632 |
5.63e-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: 40.33 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 413 SQEIAQLQSTLA---FTHWDTLREkYTLEQDIR---ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-KQDAQDRLEE 485
Cdd:COG5185 277 SKRLNENANNLIkqfENTKEKIAE-YTKSIDIKkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEiEQGQESLTEN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVR-----QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAD-LNRLQQEEAQLEQSLQAGRIQ 559
Cdd:COG5185 356 LEAIKEEIENIVGEVElskssEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIEELQRQIEQATSS 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207195097 560 LETIIKSLKATQDEINQAR-----SKLSQIQDSQHEISKNIEQYSSTLNGTHggsmTNLADMSEGFPEKENGGFGAME 632
Cdd:COG5185 436 NEEVSKLLNELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEEL----TQIESRVSTLKATLEKLRAKLE 509
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
456-548 |
5.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 456 QEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 535
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ 224
|
90
....*....|...
gi 1207195097 536 KAdlNRLQQEEAQ 548
Cdd:PRK11448 225 AA--KRLELSEEE 235
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
465-598 |
5.79e-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: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 465 ETSSLQELEAQKQDAQD--RLEEMDQQKAklEDMLNDVRQKCQEEsqmisslqtQIHSQESDLQSQEEELGRAKADLNRL 542
Cdd:COG3524 135 STSGIITLEVRAFDPEDaqAIAEALLAES--EELVNQLSERARED---------AVRFAEEEVERAEERLRDAREALLAF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 543 QQEE----------------AQLEQSLQAGRIQLETI----------IKSLK----ATQDEINQARSKLSQiQDSQHEIS 592
Cdd:COG3524 204 RNRNgildpeataeallqliATLEGQLAELEAELAALrsylspnspqVRQLRrriaALEKQIAAERARLTG-ASGGDSLA 282
|
....*.
gi 1207195097 593 KNIEQY 598
Cdd:COG3524 283 SLLAEY 288
|
|
| DivIC |
pfam04977 |
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ... |
520-581 |
5.88e-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: 5.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 520 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEI-NQARSKL 581
Cdd:pfam04977 3 NGLLTYYQLKQEIAQLQAEIAKLKQENEELEAE-----------IKDLKSDPDYIeERARSEL 54
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
429-593 |
6.25e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdqQKAKLEDMLND------VR 501
Cdd:PHA02562 216 ARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKMYEKggvcptCT 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 502 QKCQEESQMISSLQTQIHS---QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA- 577
Cdd:PHA02562 292 QQISEGPDRITKIKDKLKElqhSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELq 371
|
170 180
....*....|....*....|..
gi 1207195097 578 ------RSKLSQIQDSQHEISK 593
Cdd:PHA02562 372 aefvdnAEELAKLQDELDKIVK 393
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
520-586 |
7.31e-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: 7.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207195097 520 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 586
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQE 67
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
475-578 |
7.40e-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: 37.94 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 475 QKQDAQDRLEEM-DQQKAKLEDMLNDVRQkcqeesqMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEeaqLEQSL 553
Cdd:pfam03938 16 EGKAAQAQLEKKfKKRQAELEAKQKELQK-------LYEELQKDGALLEEEREEKEQELQKKEQELQQLQQK---AQQEL 85
|
90 100
....*....|....*....|....*.
gi 1207195097 554 QAGRIQL-ETIIKSLKATQDEINQAR 578
Cdd:pfam03938 86 QKKQQELlQPIQDKINKAIKEVAKEK 111
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
406-597 |
7.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQL----------------QSTLAFTHWdtlREKYT---------LEQDIRETEEAIRhkTTEVQEMQN 460
Cdd:PRK04778 31 IDELEERKQELENLpvndelekvkklnltgQSEEKFEEW---RQKWDeivtnslpdIEEQLFEAEELND--KFRFRKAKH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEESQM----ISSLQTQIHSQESDLQSQE 529
Cdd:PRK04778 106 EINEIESLLDLIEEDIEQILEELQELLESEEKnreeveqLKDLYRELRKSLLANRFSfgpaLDELEKQLENLEEEFSQFV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 530 E--ELG---RAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKAT-QDEINQARS---KL-------------SQIQDS 587
Cdd:PRK04778 186 EltESGdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAgyrELveegyhldhldieKEIQDL 261
|
250
....*....|
gi 1207195097 588 QHEISKNIEQ 597
Cdd:PRK04778 262 KEQIDENLAL 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
445-596 |
7.58e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 445 EEAIRHKTTEVQEMQNDLDRETSS--------------LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 510
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELEDERKQraqavaakkkleldLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 511 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagRIQL-ETIIKSLK---ATQDEINQARSKLSQIQD 586
Cdd:pfam01576 821 RDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----RDELaDEIASGASgksALQDEKRRLEARIAQLEE 896
|
170
....*....|
gi 1207195097 587 SQHEISKNIE 596
Cdd:pfam01576 897 ELEEEQSNTE 906
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
429-597 |
7.63e-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: 39.53 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 429 DTLREKY--------------TLEQDIRETEEAIRHKTT-------EVQEMQNDLDRETSSLQELEAQ--KQDAQDRLEE 485
Cdd:pfam13949 55 EQLRAKYgtrwtrppsseltaTLRAEIRKYREILEQASEsdsqvrsKFREHEEDLELLSGPDEDLEAFlpSSRRAKNSPS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH------------------SQESDLqsQEEELGRAKADLNRLQQ--- 544
Cdd:pfam13949 135 VEEQVAKLRELLNKLNELKREREQLLKDLKEKARnddispklllekarliapNQEEQL--FEEELEKYDPLQNRLEQnlh 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207195097 545 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 597
Cdd:pfam13949 213 KQEELLKEITEANNEFLQDKRVDSEKQRQREEALQKLENAYDKYKELVSNLQE 265
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
407-618 |
7.68e-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: 40.19 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 407 KELDDISQEIAQLQSTLafthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 485
Cdd:pfam10174 296 QELSKKESELLALQTKL-----ETLTNQNSdCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 486 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEE-------AQLEQSLQagri 558
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALS---- 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 559 QLETIIKSLKATQDEinQARSKLSQIQDSQHEIsKNIEQYSSTLNGTHGGSMTNLADMSE 618
Cdd:pfam10174 447 EKERIIERLKEQRER--EDRERLEELESLKKEN-KDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
141-188 |
7.73e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 37.85 E-value: 7.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1207195097 141 NGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMH 188
Cdd:COG5126 83 DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
437-594 |
7.77e-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: 39.22 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQ----------NDLDRETSSLQ----ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ 502
Cdd:pfam14932 72 LEESLEEIREATEDLEAELQELQktkqlkinrlNKLQAQASSLSqglrALVAEEEEAAKQLEELQEELAALNAKTNNVLQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 503 KCQEESQMISSLQTQIH-----SQeSDLQ---SQEEELGRAkadLNRLQQEeaQLEQSLQA-------GRIQLETIIKSL 567
Cdd:pfam14932 152 SLQSEVKELASFFSASEppvflSQ-LPLEpylLQEEQFTKY---LTLYTKK--QFFQGISElvefsneERFQLLDLSDCS 225
|
170 180
....*....|....*....|....*....
gi 1207195097 568 KATQDE--INQARSKLSQIQdSQHEISKN 594
Cdd:pfam14932 226 ERDSDEvdVEHRRSELARLQ-SAYICAQL 253
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
514-585 |
7.81e-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: 7.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207195097 514 LQTQIHSQESDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 585
Cdd:COG0845 59 LQAALAQAQAQLAAAQAQLELAKAELERYK----ALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQAR 126
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
516-594 |
7.92e-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: 39.71 E-value: 7.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207195097 516 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKN 594
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATAQA 325
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
406-508 |
8.34e-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: 39.23 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 406 IKELDDISQEIAQLQSTLAfthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 484
Cdd:smart00787 188 LRQLKQLEDELEDCDPTEL----DRAKEKLKkLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263
|
90 100
....*....|....*....|....
gi 1207195097 485 EMDQQKAKLEDMLNDVRQKCQEES 508
Cdd:smart00787 264 QCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
437-518 |
8.70e-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: 37.56 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 437 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-QDRLEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQ 515
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQQELQ------KKQQELLQPIQ 97
|
...
gi 1207195097 516 TQI 518
Cdd:pfam03938 98 DKI 100
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
461-586 |
9.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207195097 461 DLDRETSSLQELEAQKQDAQDRLEEMDQ---QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 537
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1207195097 538 DLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEINQARSKLSQIQD 586
Cdd:PRK04863 580 RRMALRQQLEQLQAR-----------IQRLAARAPAWLAAQDALARLRE 617
|
|
| |
