|
Name |
Accession |
Description |
Interval |
E-value |
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
214-309 |
4.33e-45 |
|
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: 155.13 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 214 EWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQ 293
Cdd:smart00027 1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
|
90
....*....|....*.
gi 160333280 294 PLPPVLPPEYIPPSFR 309
Cdd:smart00027 81 PIPASLPPSLIPPSKR 96
|
|
| EH |
smart00027 |
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
15-108 |
7.85e-36 |
|
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: 129.70 E-value: 7.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 15 WAITVEERAKHDQQFLSLKP-IAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQ 93
Cdd:smart00027 2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81
|
90
....*....|....*
gi 160333280 94 LPSTLPPVMKQQPVA 108
Cdd:smart00027 82 IPASLPPSLIPPSKR 96
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
225-291 |
7.01e-26 |
|
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: 100.76 E-value: 7.01e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333280 225 YRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMS 291
Cdd:cd00052 1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
26-90 |
2.60e-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: 99.22 E-value: 2.60e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 26 DQQFLSLKPI-AGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQ 90
Cdd:cd00052 2 DQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
224-307 |
7.76e-16 |
|
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: 73.56 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 224 KYRQLFNSHdKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSG--QPLPPVLPP 301
Cdd:pfam12763 11 KYWEIFSGL-KPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELPD 89
|
....*.
gi 160333280 302 EYIPPS 307
Cdd:pfam12763 90 WLVPGS 95
|
|
| EF-hand_4 |
pfam12763 |
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
21-99 |
4.05e-15 |
|
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: 71.25 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 21 ERAKHDQQFLSLKPIAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQ--LPSTL 98
Cdd:pfam12763 8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIadVPDEL 87
|
.
gi 160333280 99 P 99
Cdd:pfam12763 88 P 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-607 |
4.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQErlAQLERAEQERKERERQEQERKRQL-ELEKQLEKQRELERQREEERRKEIERREAAKRELE 441
Cdd:COG1196 221 ELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELaELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 442 R-QRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRI 520
Cdd:COG1196 299 RlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 521 AEIthlQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEID 600
Cdd:COG1196 379 EEL---EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
....*..
gi 160333280 601 VFNNQLK 607
Cdd:COG1196 456 EEEEALL 462
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-587 |
5.08e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 350 EDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKE 429
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 430 IERREAAKRElERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEI 509
Cdd:COG1196 345 ELEEAEEELE-EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160333280 510 ESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDE 587
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-607 |
6.39e-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: 68.93 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 347 VTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQER-----KRQLELEKQLEKQRELERQ 421
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 422 REEERrkeierreaaKRELERQRQLEWERNRRQELLNQRNKEQEgtvVLKARRKTLEFELEALNDKKHQLEGKLQDIRCR 501
Cdd:TIGR02168 314 LERQL----------EELEAQLEELESKLDELAEELAELEEKLE---ELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 502 LATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDsLLTLKRALEAKELARQQL 581
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-LEELEEELEELQEELERL 459
|
250 260
....*....|....*....|....*.
gi 160333280 582 REQLDEVERETRSKLQEIDVFNNQLK 607
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELA 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-600 |
2.37e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQERLAQLERAEQERkERERQEQERKRQlELEKQLEKQRELERQREEERRKEIERREAAKRELER 442
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 443 QRQLEWER---NRRQELLNQRNKEQEGTV-VLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSREL 518
Cdd:COG1196 318 LEELEEELaelEEELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 519 RIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSL-HRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQ 597
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
...
gi 160333280 598 EID 600
Cdd:COG1196 478 ALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-600 |
3.83e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQlEKQRELERQREEERRKEIERREAAKRELER 442
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 443 QRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAE 522
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160333280 523 ITHlqqqlqesqqmlgrlipEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEID 600
Cdd:COG1196 458 EEA-----------------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-587 |
4.77e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 358 ERGSVELEKRRQ-ALLEQQRKEQERLA------------QLERAEQERKERERQEQERKRQL-ELEKQLEK-QRELERQR 422
Cdd:TIGR02168 667 KTNSSILERRREiEELEEKIEELEEKIaelekalaelrkELEELEEELEQLRKELEELSRQIsALRKDLARlEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 423 EEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRL 502
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 503 ATQRQEIESTNKS---RELRIAEITHLQQQLQESQQMLGRLIPEKQI----LSDQLKQVQQN-SLHRDSLLTLKRALEAK 574
Cdd:TIGR02168 827 ESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEELESeleaLLNERASLEEAlALLRSELEELSEELREL 906
|
250
....*....|...
gi 160333280 575 ELARQQLREQLDE 587
Cdd:TIGR02168 907 ESKRSELRRELEE 919
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-600 |
5.39e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 350 EDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQE-RKERERQEQERKRQLELEKQLEKQRELerQREEERRK 428
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYElLAELARLEQDIARLEERRRELEERLEE--LEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 429 EIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQE 508
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 509 IESTNKSRE-LRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDE 587
Cdd:COG1196 409 EEALLERLErLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|...
gi 160333280 588 VERETRSKLQEID 600
Cdd:COG1196 489 AAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-556 |
8.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 352 KKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLE------LEKQLEKQRELERQREEE 425
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEeeleeaEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 426 RRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQ 505
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 160333280 506 RQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQ 556
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-600 |
5.86e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALlEQQRKEQERLAQLERAEQERKER----ERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKR 438
Cdd:COG1196 197 ELERQLEPL-ERQAEKAERYRELKEELKELEAEllllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 439 ELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSREL 518
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 519 RIAEITHLQQQLQESQQMLGRLIPE-KQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQ 597
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
...
gi 160333280 598 EID 600
Cdd:COG1196 436 EEE 438
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
330-516 |
9.70e-09 |
|
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: 58.04 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 330 PEEPSSEDEqqPEKKLPVTFEDKK-------RENFERGSVELEKRRQALLEQQRKEQErlaQLERAEQERKERERQEQER 402
Cdd:pfam15709 311 SEEERSEED--PSKALLEKREQEKasrdrlrAERAEMRRLEVERKRREQEEQRRLQQE---QLERAEKMREELELEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 403 KRQLELEKQlekQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELE 482
Cdd:pfam15709 386 FEEIRLRKQ---RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLA 462
|
170 180 190
....*....|....*....|....*....|....
gi 160333280 483 AlnDKKHQLEGKLQDircRLATQRQEIESTNKSR 516
Cdd:pfam15709 463 E--EQKRLMEMAEEE---RLEYQRQKQEAEEKAR 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
328-611 |
7.30e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 328 RLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGsvelEKRRQAllEQQRKEQE-RLAQLERAEQERKERERQEQERKRQL 406
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKA----EEKKKA--EEAKKAEEdKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 407 ELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELL------NQRNKEQEGTVVLKARRKTLEFE 480
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeeeNKIKAAEEAKKAEEDKKKAEEAK 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 481 LEALNDKK--HQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQML--GRLIPEKQILSDQLKQVQQ 556
Cdd:PTZ00121 1682 KAEEDEKKaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEedKKKAEEAKKDEEEKKKIAH 1761
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 160333280 557 NSLHRDslltlKRALEAKELARQQLREQLDEVERETRSKLQEI--DVFNNQLKVTPG 611
Cdd:PTZ00121 1762 LKKEEE-----KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKikDIFDNFANIIEG 1813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
328-599 |
5.05e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 328 RLPEEPSSEDEQQPEKKLPVTFEDKKRENFER--GSVELEKRRQALLEQQRKEQERLAQLERAEQERK--ERERQEQERK 403
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKadEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 404 RQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQlEWERNRRQELLNQRNKEQEGTVVLKARRKTLEF-ELE 482
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 483 ALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNslhrd 562
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA----- 1469
|
250 260 270
....*....|....*....|....*....|....*...
gi 160333280 563 slltlKRALEAKELARQQLR-EQLDEVERETRSKLQEI 599
Cdd:PTZ00121 1470 -----KKADEAKKKAEEAKKaDEAKKKAEEAKKKADEA 1502
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
326-414 |
5.97e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 52.82 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 326 DQRLPEEPSSEDEQQPEKKLPVTFEDKKR-ENFERGSVE-LEKRRQALLEQQRKEQERLAQlERAEQERKERERQEQ-ER 402
Cdd:PTZ00266 431 DKDHAERARIEKENAHRKALEMKILEKKRiERLEREERErLERERMERIERERLERERLER-ERLERDRLERDRLDRlER 509
|
90
....*....|...
gi 160333280 403 KRQLELEK-QLEK 414
Cdd:PTZ00266 510 ERVDRLERdRLEK 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
327-607 |
7.93e-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: 52.38 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 327 QRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERA------EQERKERERQEQ 400
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsriPEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 401 ERKRQ----LELEKQLEKQRELERQREEERRKEIERREAAK-RELERQRQLEwERNRRQELLNQRNKEQEGTVV------ 469
Cdd:TIGR02169 806 EVSRIearlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeQIKSIEKEIE-NLNGKKEELEEELEELEAALRdlesrl 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 470 --LKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKsrelRIAEIthlqqqlqESQQMLGRLIPEKQIL 547
Cdd:TIGR02169 885 gdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE----ELSEI--------EDPKGEDEEIPEEELS 952
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333280 548 SDQLKQVQQNSLHRDSLL---TLKRALEAKELARQQ--LREQLDEVERETRSKLQEIDVFNNQLK 607
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRALepvNMLAIQEYEEVLKRLdeLKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
364-522 |
1.58e-06 |
|
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: 51.11 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 364 LEKRRQALLEQQRKEQERlAQLERAEQERKERERQEQERKRQLELEKqlEKQRELERQREEERRKEIERREAAKRELERQ 443
Cdd:pfam15709 325 LEKREQEKASRDRLRAER-AEMRRLEVERKRREQEEQRRLQQEQLER--AEKMREELELEQQRRFEEIRLRKQRLEEERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 444 RQLEWERNRRQellnQRNKEQEgtvvlKARRKTLEF--ELEALNDKKHQLEGKlqdiRCRLATQRQeiestnKSRELRIA 521
Cdd:pfam15709 402 RQEEEERKQRL----QLQAAQE-----RARQQQEEFrrKLQELQRKKQQEEAE----RAEAEKQRQ------KELEMQLA 462
|
.
gi 160333280 522 E 522
Cdd:pfam15709 463 E 463
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
353-518 |
1.60e-06 |
|
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: 51.28 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 353 KRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERErQEQERKRQLElEKQLEKQRELERQREEERRKEIER 432
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQE-EERKRKKLELEKEKRDRKRAEEQR 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 433 REAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKtlEFELEALNDKKHQLEGKLQDIRCRLATQRQEIEST 512
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
....*.
gi 160333280 513 NKSREL 518
Cdd:pfam17380 572 EREREM 577
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-599 |
2.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 331 EEPSSEDEQQPEKKLPVTfeDKKRENFERGSVELEKRRQAL---LEQQRKEQERLAQLERAEQERKERERQEQERKRQLE 407
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 408 LEKQLEKQRELERQREEERRKEIERReaAKRELERQRQLEWERNRRQEllnqRNKEQEGTVVLKARRKTLEFELEALNDK 487
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEE----AKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 488 KHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLG----RLIPEKQILSDQLKQVQQNSLHRDS 563
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
250 260 270
....*....|....*....|....*....|....*.
gi 160333280 564 LLTLKRALEAKELARQQLREQLDEVERETRSKLQEI 599
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
337-600 |
2.99e-06 |
|
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: 50.51 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 337 DEQQPEKKLPVTFEDKKRENFERGSVELEKRRQAlleqQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQR 416
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKL----EEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 417 ELERQREEERRKEIERReaakRELERqrqLEWERNRRQELLNQRNKEQEGTVVLKA--RRKTLEFELEALNDKKHQLEGK 494
Cdd:pfam17380 361 ELERIRQEEIAMEISRM----RELER---LQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 495 LQDIRcRLATQR---------QEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQ---ILSDQLKQVQQNSLHRD 562
Cdd:pfam17380 434 QREVR-RLEEERaremervrlEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkILEKELEERKQAMIEEE 512
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 160333280 563 SlltlKRALEAKELARQQ---LREQLDEVERETRSKLQEID 600
Cdd:pfam17380 513 R----KRKLLEKEMEERQkaiYEEERRREAEEERRKQQEME 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-607 |
3.14e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 350 EDKKRENFERGSVELEK--RRQALLEQQRKEQ--ERLAQLERAEQERKERERQEQErkrqleLEKQLEKQRELERQREEE 425
Cdd:TIGR02169 193 IDEKRQQLERLRREREKaeRYQALLKEKREYEgyELLKEKEALERQKEAIERQLAS------LEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 426 RRKEIERREAAKREL-----ERQRQL---------EWERNRRQELLNQRNKEQ-EGTVV--------LKARRKTLEFELE 482
Cdd:TIGR02169 267 LEEIEQLLEELNKKIkdlgeEEQLRVkekigeleaEIASLERSIAEKERELEDaEERLAkleaeidkLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 483 ALNDKKHQLEGKLQDIRCRLATQRQEIESTNKS-RELRIA------EITHLQQQLQESQQMLGRLIPEKQILSDQLKQV- 554
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEfAETRDElkdyreKLEKLKREINELKRELDRLQEELQRLSEELADLn 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333280 555 --------QQNSLhRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLK 607
Cdd:TIGR02169 427 aaiagieaKINEL-EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
365-494 |
3.69e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.96 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 365 EKRRQALLEQQRKEQERLAQLERAEQERKE-RERQEQERKRQLELEKQLEKQRELERQREEERrkeierreaAKRELERQ 443
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEERLRKEElRRRAEEERARREEEARRLEEERRREEEERQRK---------AEEEAEER 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 160333280 444 RQLEWERNRRQEllnQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGK 494
Cdd:pfam05672 89 EQREQEEQERLQ---KQKEEAEAKAREEAERQRQEREKIMQQEEQERLERK 136
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-518 |
4.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELER 442
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333280 443 QRQLEWERNRRQELLNQRNKEQEGT-VVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSREL 518
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-599 |
5.34e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 331 EEPSSEDE--QQPEKKLPVTFEDKKRENFERGSVELEKRRQAL--LEQQRKEQE--RLAQLERAEQERKERE-RQEQERK 403
Cdd:PTZ00121 1467 EEAKKADEakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkADEAKKAEEakKADEAKKAEEAKKADEaKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 404 RQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLK---ARRKTLEFE 480
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeAKIKAEELK 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 481 LEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKsreLRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSlh 560
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-- 1701
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 160333280 561 rdslltlKRALEAKELARQQLR--EQLDEVERETRSKLQEI 599
Cdd:PTZ00121 1702 -------KKAEELKKKEAEEKKkaEELKKAEEENKIKAEEA 1735
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
354-476 |
8.25e-06 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 48.97 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 354 RENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKqLEKQRELerqreeerrkeierr 433
Cdd:PTZ00266 432 KDHAERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERER-LERERLE--------------- 495
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 160333280 434 eaaKRELERQRQLEWERNRRQELLNQRnkeqegtvVLKARRKT 476
Cdd:PTZ00266 496 ---RDRLERDRLDRLERERVDRLERDR--------LEKARRNS 527
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-517 |
1.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 328 RLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQ-EQERKRQL 406
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 407 ELEKQLEKQRELERQREeerrkeierreaAKRELERQRQLEWERNRRQELLNQRNKEQEGtvvLKARRKTLEFELEALND 486
Cdd:TIGR02168 404 RLEARLERLEDRRERLQ------------QEIEELLKKLEEAELKELQAELEELEEELEE---LQEELERLEEALEELRE 468
|
170 180 190
....*....|....*....|....*....|.
gi 160333280 487 KKHQLEGKLQDIRCRLATQRQEIESTNKSRE 517
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-594 |
1.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALL-EQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKqrelerqreeerrkeierreaakrELE 441
Cdd:COG4717 50 RLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE------------------------ELE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 442 RQRQLEWERNRRQELLNQRNKEQEgtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRcRLATQRQEIESTNKSRELRIA 521
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQLLP----LYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333280 522 EIthlqqqlqesqqMLGRLIPEKQILSDQLKQVQQnslHRDSLLTLKRALEAKELARQQLREQLDEVERETRS 594
Cdd:COG4717 181 EL------------LEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
351-600 |
1.24e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 351 DKKRENFERGSVELEkrrqalleQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEI 430
Cdd:pfam02463 152 PERRLEIEEEAAGSR--------LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 431 ERREAAKRELERQRQLEwernRRQELLNQRNKEQEgtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQrQEIE 510
Cdd:pfam02463 224 EYLLYLDYLKLNEERID----LLQELLRDEQEEIE----SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL-LAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 511 STNKSRELRIAEITHLQQQLQESQQMLgrlipEKQILSDQLKQVQQNSLHRDSLLTLKralEAKELARQQLREQLDEVER 590
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEK-----EKKKAEKELKKEKEEIEELEKELKEL---EIKREAEEEEEEELEKLQE 366
|
250
....*....|
gi 160333280 591 ETRSKLQEID 600
Cdd:pfam02463 367 KLEQLEEELL 376
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-591 |
1.47e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 349 FEDKKRENFErgsvELEKRRQALLEQQRKEQERLAQLERAEQER--KERERQEQERKRQLEL-EKQLEKQRELERQREEE 425
Cdd:TIGR02169 168 FDRKKEKALE----ELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYEGyELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 426 RRKEIERREAAKRELERQrQLEWERNRRQELLNQRNKE-----QEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDirc 500
Cdd:TIGR02169 244 RQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELED--- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 501 rLATQRQEIESTNKSRELRIAEIThlqqqlqesqqmlgRLIPEKQILSDQLKQVQQNSlhRDSLLTLKRALEAKELARQQ 580
Cdd:TIGR02169 320 -AEERLAKLEAEIDKLLAEIEELE--------------REIEEERKRRDKLTEEYAEL--KEELEDLRAELEEVDKEFAE 382
|
250
....*....|.
gi 160333280 581 LREQLDEVERE 591
Cdd:TIGR02169 383 TRDELKDYREK 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
328-599 |
1.56e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 328 RLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRqallEQQRKEQERLAQleRAEQERKERERQEQERKRQle 407
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA----EEAKKKADAAKK--KAEEAKKAAEAAKAEAEAA-- 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 408 lEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQ----RNKEQEGTVVLKARRKTLEFELEA 483
Cdd:PTZ00121 1356 -ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadelKKAAAAKKKADEAKKKAEEKKKAD 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 484 LNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDS 563
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
250 260 270
....*....|....*....|....*....|....*..
gi 160333280 564 LLTLKRALEAKELARQQLREQLDEVER-ETRSKLQEI 599
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKaEEKKKADEL 1551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
365-511 |
2.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 365 EKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE---------KQLEKQrelerqreeerrkeierREA 435
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrlEQLERE-----------------IER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 436 AKRELERQRQlewERNRRQELLNQ-------------RNKEQegtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRL 502
Cdd:COG4913 350 LERELEERER---RRARLEALLAAlglplpasaeefaALRAE-----AAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
....*....
gi 160333280 503 ATQRQEIES 511
Cdd:COG4913 422 RELEAEIAS 430
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
342-403 |
2.90e-05 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 47.42 E-value: 2.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 342 EKKLPVTFEDKKRENFERGSVE-LEKRR-------QALLEQQRKEQERLAQLERAEQERKERERQEQERK 403
Cdd:PTZ00266 456 EKKRIERLEREERERLERERMErIERERlererleRERLERDRLERDRLDRLERERVDRLERDRLEKARR 525
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
338-598 |
4.18e-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: 46.89 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 338 EQQPEKKLpvTFEDKKREnfergsvELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQ------ERKRQLELEKQ 411
Cdd:TIGR00618 238 TQQSHAYL--TQKREAQE-------EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 412 LEKQRELERQREEERRKEIERREAAKR---ELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKK 488
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKqqsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 489 HQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLK 568
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
250 260 270
....*....|....*....|....*....|
gi 160333280 569 RALEAKELARQQLREQLDEVERETRSKLQE 598
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-599 |
4.59e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 327 QRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQE------------RKE 394
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneeaANL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 395 RERQEQERKRQLELEKQLEK-QRELERQREEERRKEIERREAAKRELERQRQLEwernrrqELLNQRNKEQEGTVVLKAR 473
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEELESELE-------ALLNERASLEEALALLRSE 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 474 RKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTnksrELRIAEIthlQQQLQESQQMLGRLIPEKQILSDQLKQ 553
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGL----EVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333280 554 VQQNSLHRdslltLKRAL------------EAKEL----------------ARQQLREQLDEVERETRSKLQEI 599
Cdd:TIGR02168 969 EARRRLKR-----LENKIkelgpvnlaaieEYEELkerydfltaqkedlteAKETLEEAIEEIDREARERFKDT 1037
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-601 |
5.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 342 EKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQ 421
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 422 REEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKAR------RKT------LEFELEALNDKKH 489
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkRLTgltpekLEKELEELEKAKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 490 QLEGKLQDIRCRLATQRQEIESTNKS-RELRIAEITHLQQQLQESQQMLGRLIPE-KQILSDQLKQVQQNSLHRDSLLTL 567
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRELTEEHRKELLEEyTAELKRIEKELKEIEEKERKLRKE 481
|
250 260 270
....*....|....*....|....*....|....*...
gi 160333280 568 KRALEaKELARQQ----LREQLDEVeRETRSKLQEIDV 601
Cdd:PRK03918 482 LRELE-KVLKKESelikLKELAEQL-KELEEKLKKYNL 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
336-521 |
5.92e-05 |
|
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: 46.27 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 336 EDEQQPEKKLPVTFEDKKRENFERGSVE---LEKRRQALLEQQR-KEQERLAQLER-----AEQERKERERQEQERKRQL 406
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREvrrLEEERAREMERVRlEEQERQQQVERlrqqeEERKRKKLELEKEKRDRKR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 407 ELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEgtvvLKARRKTLEFELEALND 486
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE----MEERRRIQEQMRKATEE 564
|
170 180 190
....*....|....*....|....*....|....*
gi 160333280 487 KKhqlegKLQDIRCRLATQRQEIESTNKSRELRIA 521
Cdd:pfam17380 565 RS-----RLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
379-523 |
1.04e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 379 QERLAQLERAEQERKERERQEQERKRQLE-LEKQLEKQRELERQREEERRKEIERREAAKRELER-QRQLEWERNRRQel 456
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVRNNKE-- 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333280 457 LNQRNKEQEGtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEI 523
Cdd:COG1579 91 YEALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
371-600 |
1.12e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 371 LLEQQRKEQERLAQlERAEQERKERERQEQERK-RQLELEKQLEKqrelerqreeerrkeieRREAAKRELERQ------ 443
Cdd:pfam17380 277 IVQHQKAVSERQQQ-EKFEKMEQERLRQEKEEKaREVERRRKLEE-----------------AEKARQAEMDRQaaiyae 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 444 -RQLEWERNRRQELLNQRNKEQEGTVVlkaRRKTLEFELEALND-KKHQLEGKLQDIRCrlatqRQEIEStnkSRELRIA 521
Cdd:pfam17380 339 qERMAMERERELERIRQEERKRELERI---RQEEIAMEISRMRElERLQMERQQKNERV-----RQELEA---ARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 522 EithlqqqlqesqQMLGRLIPEKQILSDQLKQVQQNSLHRD-SLLTLKRALE-----AKELARQQLREQLDEVERETRSK 595
Cdd:pfam17380 408 E------------EERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRK 475
|
....*
gi 160333280 596 LQEID 600
Cdd:pfam17380 476 KLELE 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-556 |
1.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQERLAQLER----AEQERKERERQEQERKRQL-ELEKQLEKQRELERQREEERRKEIERREAAK 437
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKeekaLLKQLAALERRIAALARRIrALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 438 RELERQRQLEWERNRRQE---LLNQRNKEQEGTVV---------LKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQ 505
Cdd:COG4942 104 EELAELLRALYRLGRQPPlalLLSPEDFLDAVRRLqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 160333280 506 RQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQ 556
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
339-494 |
1.51e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 339 QQPEKKlpvtfeDKKRENFERGSVElEKRRQALLEQQRKEQERLAQLERA-EQERKERERQEQERKRQLELEKQLEKQRE 417
Cdd:PRK09510 67 QQQQQK------SAKRAEEQRKKKE-QQQAEELQQKQAAEQERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 418 LERQREEE---RRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTlefELEALNDKKHQLEGK 494
Cdd:PRK09510 140 KAAAAAKAkaeAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK---KAEAEAKKKAAAEAK 216
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
363-511 |
1.51e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 363 ELEKRRQALLEQQRKEQE---RLAQLERAEQERKERERQEQE-RKRQLELEKQLekqrelerqreeerrkeierreaaKR 438
Cdd:PRK12704 35 EAEEEAKRILEEAKKEAEaikKEALLEAKEEIHKLRNEFEKElRERRNELQKLE------------------------KR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333280 439 ELERQRQLEwernRRQELLNQRNKEqegtvvLKARRKTLEFELEALNDKKHQLEGKLQDircrlatQRQEIES 511
Cdd:PRK12704 91 LLQKEENLD----RKLELLEKREEE------LEKKEKELEQKQQELEKKEEELEELIEE-------QLQELER 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-606 |
2.11e-04 |
|
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: 44.67 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 375 QRKEQERLAQL-ERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRkeierreaakRELER-QRQLEWERNR 452
Cdd:TIGR02169 669 SRSEPAELQRLrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE----------KEIEQlEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 453 RQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQR--------QEIESTNKSRELRIAEIt 524
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREI- 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 525 hlqqqlqesQQMLGRLIPEKQILSDQLKQVQQnslhrdslltLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNN 604
Cdd:TIGR02169 818 ---------EQKLNRLTLEKEYLEKEIQELQE----------QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
..
gi 160333280 605 QL 606
Cdd:TIGR02169 879 DL 880
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
373-595 |
2.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 373 EQQRKEQERLAQLERA-EQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQR-QLEWER 450
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 451 NRRQELLN------QRNKEQEGTVVLKARRKTLEFE-----LEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELR 519
Cdd:COG4942 100 EAQKEELAellralYRLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 520 IAEITHLQQQLQesqqmlgRLIPEKQILSDQLKQvqqnslhrdSLLTLKRALEAKELARQQLREQLDEVERETRSK 595
Cdd:COG4942 180 LAELEEERAALE-------ALKAERQKLLARLEK---------ELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
335-523 |
2.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 335 SEDEQQPEKKLPVTFEDKKRENFE-RGSVELEKRRQAllEQQRKEQERLAQLERAEQERKERERQEQERKRQLE------ 407
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkae 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 408 -LEKQLEKQRELERQREEERRKEIERREAAKRELERQ-------RQLEWERNRRQELLNQRNKEQEGtvVLKARRKTLEF 479
Cdd:PTZ00121 1706 eLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkaeeaKKDEEEKKKIAHLKKEEEKKAEE--IRKEKEAVIEE 1783
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 160333280 480 ELEALNDKKH-QLEGKLQDIRCRLAT-QRQEIEST---NKSRELRIAEI 523
Cdd:PTZ00121 1784 ELDEEDEKRRmEVDKKIKDIFDNFANiIEGGKEGNlviNDSKEMEDSAI 1832
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
373-450 |
2.63e-04 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 42.35 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 373 EQQRKEQERLaQLERAEQERKERERQEQERKRQLE-----LEKQLEKqrelerqreEERRKEIERREAAKRELERQRQLE 447
Cdd:pfam15927 2 RLREEEEERL-RAEEEEAERLEEERREEEEEERLAaeqdrRAEELEE---------LKHLLEERKEALEKLRAEAREEAE 71
|
...
gi 160333280 448 WER 450
Cdd:pfam15927 72 WER 74
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
326-489 |
3.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 326 DQRLPEE--PSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQallEQQRKEQE-RLAQLERAEQERKERERQEQER 402
Cdd:PTZ00121 1673 DKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA---EELKKAEEeNKIKAEEAKKEAEEDKKKAEEA 1749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 403 KRQLELEKQLEKQRELERQREEERRKEIERREAAK-RELERQRQLEWERNRRQELLNQRNKEQ---EGTVVLKARRKTLE 478
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFDNFANIIEggkEGNLVINDSKEMED 1829
|
170
....*....|.
gi 160333280 479 FELEALNDKKH 489
Cdd:PTZ00121 1830 SAIKEVADSKN 1840
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
338-600 |
3.72e-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: 43.80 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 338 EQQPEKKLPVTFEDKKRENFERGSVEL--EKRRQALLEQQRKE-----QERLAQLERAEQERKERERQEQERKRQLELEK 410
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPLaaHIKAVTQIEQQAQRihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 411 QLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQ 490
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 491 LEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGrlipEKQILSDQLKQVQQNSLHRDSLL-TLKR 569
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRKKAVVLARLLELqEEPC 504
|
250 260 270
....*....|....*....|....*....|.
gi 160333280 570 ALEAKELARQQLREQLDEVERETRSKLQEID 600
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
331-595 |
3.79e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 331 EEPSSEDEQQPEKKLpVTFEDKKRENFERgSVELEKRRQALLEQQRKEQER-LAQLERAEQERKERERQEQERKRQLELE 409
Cdd:pfam02463 252 EIESSKQEIEKEEEK-LAQVLKENKEEEK-EKKLQEEELKLLAKEEEELKSeLLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 410 K--------QLEKQrelerqreeerrkeierreaaKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFEL 481
Cdd:pfam02463 330 LkkekeeieELEKE---------------------LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 482 EA-LNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLH 560
Cdd:pfam02463 389 AAkLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
250 260 270
....*....|....*....|....*....|....*
gi 160333280 561 RDSLLTLKRALEAKELARQQLREQLDEVERETRSK 595
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
224-283 |
4.23e-04 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 38.77 E-value: 4.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333280 224 KYRQLFNSHDKTMSGHLT----GPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAM 283
Cdd:pfam13499 3 KLKEAFKLLDSDGDGYLDveelKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
362-475 |
4.83e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 42.67 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 362 VELEKRRQALLEQQRKEQERLAQLERAEQERK------------ERERQEQERKRQLELEKQLEKqrelerqreeerrke 429
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAESAATAEAREEKRKtkaqrnkekrrkEEEREAKEEKALKKKLAQLER--------------- 273
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 160333280 430 ierreaAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRK 475
Cdd:pfam07767 274 ------LKEIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRPRK 313
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
90-410 |
5.42e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 43.22 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 90 QGYQLPSTLPPV----MKQQPVAISSAPAfgiggiaSMPPLTAvaPVPMGSIPVVGMSPPLVSSVPPAAVPPLANGAPPV 165
Cdd:pfam03154 308 QVPPGPSPAAPGqsqqRIHTPPSQSQLQS-------QQPPREQ--PLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 166 IQP----LPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAAEWAVPQSSrlkyrqlfnSHDKTMSGHLT 241
Cdd:pfam03154 379 SGPspfqMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQ---------SLPPPAASHPP 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 242 GPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAeefilamhlIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGMSVIS 321
Cdd:pfam03154 450 TSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTS---------TSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIK 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 322 SSSVDQrlPEEPSSEDEQQPEKKLPVTFEDKKR---------ENFERG---------------SVELEKRRQALLEQQRK 377
Cdd:pfam03154 521 EEALDE--AEEPESPPPPPRSPSPEPTVVNTPShasqsarfyKHLDRGynscartdlyfmplaGSKLAKKREEALEKAKR 598
|
330 340 350
....*....|....*....|....*....|...
gi 160333280 378 EQERLAQLERAEQERKERERqEQERKRQLELEK 410
Cdd:pfam03154 599 EAEQKAREEKEREKEKEKER-EREREREREAER 630
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
365-490 |
6.22e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 365 EKRRQALLEQQRKEQERLAQLERAEQ-ERKERERQEQ--ERKRQLELEKQLEKQRELERQREEERRKEIERREAAkrELE 441
Cdd:pfam13904 63 AKQRQRQKELQAQKEEREKEEQEAELrKRLAKEKYQEwlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 160333280 442 RQRQLEWERNRRQELLNQRNKEQEgtvvLKARRKTLEFELEALNDKKHQ 490
Cdd:pfam13904 141 KEVLQEWERKKLEQQQRKREEEQR----EQLKKEEEEQERKQLAEKAWQ 185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-598 |
7.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 327 QRLPEEPSSEDEQQPEKKLPVtfEDKKRENFERGSVE---LEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERK 403
Cdd:PTZ00121 1128 RKAEEARKAEDARKAEEARKA--EDAKRVEIARKAEDarkAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAA 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 404 RQLELEKQLEKqreLERQREEERRKEIERREAAKRELERQRQLEWERNRRQEllnqrNKEQEGTVVLKARRKTlefelea 483
Cdd:PTZ00121 1206 RKAEEERKAEE---ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI-----RKFEEARMAHFARRQA------- 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 484 lndkKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDS 563
Cdd:PTZ00121 1271 ----AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
250 260 270
....*....|....*....|....*....|....*
gi 160333280 564 LLTLKRALEAKELARQQLREQLDEVERETRSKLQE 598
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-606 |
8.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 436 AKR-----------------ELERQ--------------RQLEWERNRRQ--ELLNQRNKEQEGTVVLKARRKTLEFELE 482
Cdd:COG1196 177 AERkleateenlerledilgELERQleplerqaekaeryRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 483 ALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAE-------ITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQ 555
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElarleqdIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 160333280 556 QNSLH-RDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQL 606
Cdd:COG1196 337 EELEElEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-606 |
8.07e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 336 EDEQQPEKKLpvtfeDKKRENFERgsVElekrrqALLEQQRKEQERL-AQLERAEqerKERERQEQERKRQLELEKQ--L 412
Cdd:TIGR02168 172 ERRKETERKL-----ERTRENLDR--LE------DILNELERQLKSLeRQAEKAE---RYKELKAELRELELALLVLrlE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 413 EKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLE 492
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 493 GKLQdircRLATQRQEIESTNKSRELRIAEIthlqqqlqesqqmlgrlipEKQILSDqlkQVQQNSLhRDSLLTLKRALE 572
Cdd:TIGR02168 316 RQLE----ELEAQLEELESKLDELAEELAEL-------------------EEKLEEL---KEELESL-EAELEELEAELE 368
|
250 260 270
....*....|....*....|....*....|....
gi 160333280 573 AKELARQQLREQLDEVERETRSKLQEIDVFNNQL 606
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
212-284 |
8.57e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 8.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333280 212 AAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMH 284
Cdd:COG5126 58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
336-600 |
8.81e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 336 EDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKErERQEQERKRQLELEKQLEKQ 415
Cdd:pfam02463 193 EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 416 RELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEgtVVLKARRKTLEFELEALNDKKHQLEGKL 495
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK--EKKKAEKELKKEKEEIEELEKELKELEI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 496 QDIRCRLATQRQEiESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKE 575
Cdd:pfam02463 350 KREAEEEEEEELE-KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260
....*....|....*....|....*..
gi 160333280 576 LARQ--QLREQLDEVERETRSKLQEID 600
Cdd:pfam02463 429 LEILeeEEESIELKQGKLTEEKEELEK 455
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
224-284 |
8.87e-04 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 37.91 E-value: 8.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333280 224 KYRQLFNSHDKTMSGHLTGPQARTIL--MQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMH 284
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
131-202 |
9.71e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 41.36 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 131 PVPMGSIPVVGMSPPLVSSVPPAAvPPLANGAPPVIQPLPAFAHP---AATLPKSS----------SFSRS-GPGS---- 192
Cdd:PLN02983 142 PQPPPPAPVVMMQPPPPHAMPPAS-PPAAQPAPSAPASSPPPTPAsppPAKAPKSShpplkspmagTFYRSpAPGEppfv 220
|
90
....*....|
gi 160333280 193 QLNTKLQKAQ 202
Cdd:PLN02983 221 KVGDKVQKGQ 230
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
369-575 |
1.00e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 369 QALLEQQRKEQERL-AQLERAEQERKE--RERQEQERKRQLEL-------EKQLEKQRELERQREEERRKEIERREAAKR 438
Cdd:pfam17045 48 RNTLERKHKEIGLLrQQLEELEKGKQElvAKYEQQLQKLQEELsklkrsyEKLQRKQLKEAREEAKSREEDRSELSRLNG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 439 ELE--RQRQLEWERnrrqellnQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEG-----KLQDIRCRLATQRQEIES 511
Cdd:pfam17045 128 KLEefRQKSLEWEQ--------QRLQYQQQVASLEAQRKALAEQSSLIQSAAYQVQLegrkqCLEASQSEIQRLRSKLER 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333280 512 TNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQ-QNSLHRDSLLTLKRALEAKE 575
Cdd:pfam17045 200 AQDSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQrQLQVLQNELMELKATLQSQD 264
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
42-184 |
1.31e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 41.97 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 42 DQARNFFFQSglPQPVLAQIWALADMNNDGR---MDQVEFSIAMKLIKLKLqgyqlpSTLPPVMKQQ----------PVA 108
Cdd:PRK14959 311 DEARQWLGWA--KRFEPAHIHACWQMTLEGQrrvLTSLEPAMALELLLLNL------AMLPRLMPVEslrpsgggasAPS 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 109 ISSAPAFGIGGIASMPPLTAVApvPMGSIPVVGMSPplvSSVPPAAVPPLANGAPPV----IQPLPAF----AHPAATLP 180
Cdd:PRK14959 383 GSAAEGPASGGAATIPTPGTQG--PQGTAPAAGMTP---SSAAPATPAPSAAPSPRVpwddAPPAPPRsgipPRPAPRMP 457
|
....
gi 160333280 181 KSSS 184
Cdd:PRK14959 458 EASP 461
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
351-523 |
1.81e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 351 DKKRENFE--RGSVELEKRRQALLEQQRKE-------QERLAQLERAEQERKERERQEQERKRQL-----ELEKQLEKQR 416
Cdd:pfam05557 17 EKKQMELEhkRARIELEKKASALKRQLDREsdrnqelQKRIRLLEKREAEAEEALREQAELNRLKkkyleALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 417 ELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQegtvvlKARRKTLEFELEALNDKKHQL---EG 493
Cdd:pfam05557 97 SQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLL------KAKASEAEQLRQNLEKQQSSLaeaEQ 170
|
170 180 190
....*....|....*....|....*....|..
gi 160333280 494 KLQDIRCRLATQRQ--EIESTNKSRELRIAEI 523
Cdd:pfam05557 171 RIKELEFEIQSQEQdsEIVKNSKSELARIPEL 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-518 |
2.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 342 EKKLPVTFEdkKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQL-ELEKQLE--KQREL 418
Cdd:PRK03918 213 SSELPELRE--ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeELEEKVKelKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 419 ERQREEERRKEIERREAAKRELE-RQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALnDKKHQLegkLQD 497
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHEL---YEE 366
|
170 180
....*....|....*....|.
gi 160333280 498 IRcRLATQRQEIESTNKSREL 518
Cdd:PRK03918 367 AK-AKKEELERLKKRLTGLTP 386
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
373-596 |
2.31e-03 |
|
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: 40.79 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 373 EQQRKEQERLAQLERAEQERKERERQEQ-ERKRQLELEKQLE------KQRELERQREEERRKEIERREAAKRELERQRQ 445
Cdd:pfam15558 20 EQRMRELQQQAALAWEELRRRDQKRQETlERERRLLLQQSQEqwqaekEQRKARLGREERRRADRREKQVIEKESRWREQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 446 LEWERNRRQELLNQRNKEQEGTVVLKARR-KTLEFELEALNDKKHQLEGKLQDIRCRLATQR-----QEIESTNKSRELR 519
Cdd:pfam15558 100 AEDQENQRQEKLERARQEAEQRKQCQEQRlKEKEEELQALREQNSLQLQERLEEACHKRQLKereeqKKVQENNLSELLN 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160333280 520 IAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQvQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKL 596
Cdd:pfam15558 180 HQARKVLVDCQAKAEELLRRLSLEQSLQRSQENY-EQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-600 |
2.60e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 435 AAKRELER-QRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIestn 513
Cdd:COG4942 31 QLQQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 514 kSRELRIAEITHLQQQLQESQQMLG------RLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKelaRQQLREQLDE 587
Cdd:COG4942 107 -AELLRALYRLGRQPPLALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---RAELEALLAE 182
|
170
....*....|...
gi 160333280 588 VERETRSKLQEID 600
Cdd:COG4942 183 LEEERAALEALKA 195
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
332-607 |
2.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 332 EPSSEDEQQPEKKlpVTFEDKKREnfERGSVElEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQ 411
Cdd:PTZ00121 1085 EDNRADEATEEAF--GKAEEAKKT--ETGKAE-EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 412 LEKQRELERQREEERRKEIERREAAK--------RELERQRQLE----WERNRRQELLNQRNKEQEGTVVLKAR--RKTL 477
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEevrkaeelRKAEDARKAEaarkAEEERKAEEARKAEDAKKAEAVKKAEeaKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 478 EFELEALNDKKHQLEGKLQDIRCRLATQRQ---EIESTNKSRELRIAEITHLQQQLQESqqmlgrlipEKQILSDQLKQV 554
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKA---------EEKKKADEAKKK 1310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 160333280 555 QQNSLHRDSLltLKRALEAKELArQQLREQLDEVERETRSKLQEIDVFNNQLK 607
Cdd:PTZ00121 1311 AEEAKKADEA--KKKAEEAKKKA-DAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
336-600 |
3.01e-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: 40.72 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 336 EDEQQPEKKLPVTFEDKKRENFERGSVELEKR---RQALLEQQRKEQERlaQLERAEQERKERERQEQERKRQLELEKQL 412
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqdlQDVRLHLQQCSQEL--ALKLTALHALQLTLTQERVREHALSIRVL 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 413 EKQRELERQREEERRKEIERREAAKRELERQRQLEWeRNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNdkkhQLE 492
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL-RELETHIEEYDREFNEIENASSSLGSDLAAREDALN----QSL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 493 GKLQDIRcRLATQRQEIESTNKSRELRIAEIT-HLQQQLQESQQMLGRLIPEKQILSDQLK-QVQQNSLHRDSLLTLKRA 570
Cdd:TIGR00618 746 KELMHQA-RTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCE 824
|
250 260 270
....*....|....*....|....*....|
gi 160333280 571 LEAKElarqqlREQLDEVERETRSKLQEID 600
Cdd:TIGR00618 825 TLVQE------EEQFLSRLEEKSATLGEIT 848
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-484 |
3.21e-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: 40.81 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 352 KKRENFERGSVELEK------RRQALLEQQRKEQErlAQLERAEqERKER--ERQEQERKRQLELEKQLEKQRELERQRE 423
Cdd:TIGR02168 365 AELEELESRLEELEEqletlrSKVAQLELQIASLN--NEIERLE-ARLERleDRRERLQQEIEELLKKLEEAELKELQAE 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333280 424 EERRKEIERREAAKRElERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEAL 484
Cdd:TIGR02168 442 LEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-599 |
3.38e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 382 LAQLERAEQERKERERQeqerkrQLEL-EKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQ- 459
Cdd:pfam05483 361 LEELLRTEQQRLEKNED------QLKIiTMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEEl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 460 RNKEQEGTVVLKARRKT---LEFELEALNDKKHQLEGKLQDIRCRLATQR-QEIESTNKSRELRIAEithlqqqlqesqq 535
Cdd:pfam05483 435 KGKEQELIFLLQAREKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLEN------------- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160333280 536 mlGRLIPEKQILSDQLKQVQQ----NSLHRDSLLTLKRALEAKELarqQLREQLDEVERETRSKLQEI 599
Cdd:pfam05483 502 --KELTQEASDMTLELKKHQEdiinCKKQEERMLKQIENLEEKEM---NLRDELESVREEFIQKGDEV 564
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
355-481 |
3.44e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.49 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 355 ENFERGSVELEKRRQALLEQQRK--EQERLAQLE--RAEQERKERERQEQERKRQLELEKQLE----KQRELERQREEER 426
Cdd:pfam15346 26 EELEKRKDEIEAEVERRVEEARKimEKQVLEELEreREAELEEERRKEEEERKKREELERILEennrKIEEAQRKEAEER 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 427 RkeierreaakRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKAR-RKTLEFEL 481
Cdd:pfam15346 106 L----------AMLEEQRRMKEERQRREKEEEEREKREQQKILNKKNsRPKLSFSL 151
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
435-600 |
3.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 435 AAKRELERQRQLE-----WERNRRQELLNQRNKEqegtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLAT----Q 505
Cdd:COG4913 266 AARERLAELEYLRaalrlWFAQRRLELLEAELEE------LRAELARLEAELERLEARLDALREELDELEAQIRGnggdR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 506 RQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIP-EKQILSDQLKQVQQnslhrdSLLTLKRALEAKELARQQLREQ 584
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPaSAEEFAALRAEAAA------LLEALEEELEALEEALAEAEAA 413
|
170
....*....|....*.
gi 160333280 585 LDEVERETRSKLQEID 600
Cdd:COG4913 414 LRDLRRELRELEAEIA 429
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
99-214 |
3.45e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.47 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 99 PPVMKQQPVAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGMSPPLVSSVPPAAVPPLANGAPPVIQPLPAFAHPAAT 178
Cdd:PRK14951 373 AAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPP 452
|
90 100 110
....*....|....*....|....*....|....*.
gi 160333280 179 LPKSSSFSRSGPGSQLNTKLQKAQSfDVASAPPAAE 214
Cdd:PRK14951 453 AQAAPETVAIPVRVAPEPAVASAAP-APAAAPAAAR 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-498 |
3.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 350 EDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKE 429
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 430 IERREAAKRELERQRQLEWERNR-RQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDI 498
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAeREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
310-456 |
3.57e-03 |
|
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: 40.49 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 310 RVRSGSGMSVISSSSVDQRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERgsvELEKRRQALLEQQRK------------ 377
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK---ELEERKQAMIEEERKrkllekemeerq 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 378 ------EQERLAQLER-AEQERKERERQEQERKRQLELEKQLEkqrelerqreeerrkeierreAAKRELERQRQLEWER 450
Cdd:pfam17380 527 kaiyeeERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLE---------------------AMEREREMMRQIVESE 585
|
....*.
gi 160333280 451 NRRQEL 456
Cdd:pfam17380 586 KARAEY 591
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
95-214 |
3.62e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 40.53 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 95 PSTLPPVMKQQP-VAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGMSPPLVSSVPPAAVPPLANGAPPVIQPLPafa 173
Cdd:PRK14971 381 PVFTQPAAAPQPsAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKK--- 457
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 160333280 174 hpaATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAAE 214
Cdd:PRK14971 458 ---IPVSKVSSLGPSTLRPIQEKAEQATGNIKEAPTGTQKE 495
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
366-523 |
3.96e-03 |
|
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: 39.90 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 366 KRRQALLEQQRKEQERLAQLER----AEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELE 441
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEEReralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 442 RQRQLEWERNRRQELLNQRnkEQEGTVVLKARRKTLEFELEALNDKKhqLEGKLQDIRCRLATQRQEIESTNKSRELRIA 521
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLRE--EIDEFNEEQAEWKELEKEEEREEDER--ILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
..
gi 160333280 522 EI 523
Cdd:pfam13868 188 RL 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
444-600 |
3.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 444 RQLEWERNRRQELLNQRNKEQEGtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRI--A 521
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAA---LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333280 522 EITHLQQqlqesqqmlgrlipEKQILSDQLKQVQqnslhrDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEID 600
Cdd:COG1579 97 EIESLKR--------------RISDLEDEILELM------ERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
365-456 |
5.25e-03 |
|
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: 39.52 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 365 EKRRQALLEQQRKEQERLAQLER-AEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQ 443
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKqAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
90
....*....|...
gi 160333280 444 RQLEWERNRRQEL 456
Cdd:pfam13868 327 RRERIEEERQKKL 339
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
327-455 |
5.27e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.44 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 327 QRLPEEPSSEDEQQPEKKLPVTFEDKKREnfergsVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQL 406
Cdd:TIGR02794 55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQ------RAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 160333280 407 ELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQE 455
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-516 |
5.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 367 RRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQlELEKQLEKQRelerqreeerrkeierreaakrelERQRQL 446
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAELE------------------------EERAAL 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 447 EWERNRRQELLNQrnkeqegtvvLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSR 516
Cdd:COG4942 191 EALKAERQKLLAR----------LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
351-465 |
6.32e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 37.59 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 351 DKKRENFERGSVELEKRRQALleQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEI 430
Cdd:cd12923 25 DELYEKYNKLSQEIQLKRQAL--EAFEEAVKMFEEQLRTQEKFQKEAQPHEKQRLMENNELLKSRLKELEESKEQLEEDL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 160333280 431 ERREAAKRELERQR--------QLEWERNRRQELLNQRNKEQE 465
Cdd:cd12923 103 RKQVAYNRELEREMnslkpelmQLRKQKDQYLRWLKRKGVSQE 145
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
369-484 |
6.36e-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: 39.10 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 369 QALLEQQRKEQErlaqlERAEQERKERERQEQERKRQlELEKQLEKQRELERQREEERRkeierreaAKRELERQRQL-E 447
Cdd:cd16269 191 QALTEKEKEIEA-----ERAKAEAAEQERKLLEEQQR-ELEQKLEDQERSYEEHLRQLK--------EKMEEERENLLkE 256
|
90 100 110
....*....|....*....|....*....|....*..
gi 160333280 448 WERNRRQELLNQRNKEQEGtvvLKARRKTLEFELEAL 484
Cdd:cd16269 257 QERALESKLKEQEALLEEG---FKEQAELLQEEIRSL 290
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
351-414 |
6.70e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 38.33 E-value: 6.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333280 351 DKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKER-ER-----QEQERKRQL-ELEKQLEK 414
Cdd:pfam12072 95 DRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQElERisgltSEEAKEILLdEVEEELRH 165
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
338-413 |
7.19e-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: 38.71 E-value: 7.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 338 EQQPEKKLPVTFEDKKReNFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 413
Cdd:cd16269 217 LEEQQRELEQKLEDQER-SYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
365-500 |
7.34e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 38.10 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 365 EKRRQALLEQQRKEQERLAQleraEQERKERERQEQERKRQLELEKqlekqrelerqreeerrkeierreaAKRELERQR 444
Cdd:pfam09756 5 AKKRAKLELKEAKRQQREAE----EEEREEREKLEEKREEEYKERE-------------------------EREEEAEKE 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 445 QLEWERNRRQEllnQRNKEQEGTVVLKArrktlEFELEALNDKKHQLEGKLQDIRC 500
Cdd:pfam09756 56 KEEEERKQEEE---QERKEQEEYEKLKS-----QFVVEEEGTDKLSAEDESQLLED 103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-604 |
8.57e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 332 EPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALlEQQRKEQERLAQ-----LERAEQERKERERQEQERKRQL 406
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-ESKIQNQEKLNQqkdeqIKKLQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 407 ---------------ELEKQLEKQRELERQREEERRKEIERREAAKRELER-QRQLEwerNRRQEL--LNQRNKEQEGTV 468
Cdd:TIGR04523 436 iknnseikdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkQKELK---SKEKELkkLNEEKKELEEKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 469 -VLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLatqrQEIESTNKSRELRIaEITHLQQQLQESQQMLGRLIP---EK 544
Cdd:TIGR04523 513 kDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL----NKDDFELKKENLEK-EIDEKNKEIEELKQTQKSLKKkqeEK 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 545 QILSDQLKQVQQNslhrdslltLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNN 604
Cdd:TIGR04523 588 QELIDQKEKEKKD---------LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
95-213 |
8.99e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.54 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 95 PSTLPPVMKQQPVAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGmSPPLVSSVPPAAVPPLANGAPPVIQPLPAFAH 174
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA-RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
|
90 100 110
....*....|....*....|....*....|....*....
gi 160333280 175 PAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAA 213
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-601 |
9.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 366 KRRQALLEQQRKE-QERLAQLERAEQERKERERQEQERKRQLE-LEKQLEKQrelerqreeerrkeiERREAAKRELERQ 443
Cdd:COG4913 609 RAKLAALEAELAElEEELAEAEERLEALEAELDALQERREALQrLAEYSWDE---------------IDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333280 444 RQlewernRRQELLNQRNKEQEgtvvLKARRKTLEFELEALNDKKHQLEGKLQdircRLATQRQEIEstnksRELRIAEI 523
Cdd:COG4913 674 EA------ELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIG----RLEKELEQAE-----EELDELQD 734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333280 524 THLQQQLQESQQMLGRLIPE-KQILSDQLKQVQQNSLHRDslltLKRALEAKELARQQLREQLDEVERETRSKLQEIDV 601
Cdd:COG4913 735 RLEAAEDLARLELRALLEERfAAALGDAVERELRENLEER----IDALRARLNRAEEELERAMRAFNREWPAETADLDA 809
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
371-446 |
9.77e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.08 E-value: 9.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333280 371 LLEQQRKEQERLAQleraeqERKERERQEQErKRQLELEKQLEKQRELErqreeerrkeierreaAKRELERQRQL 446
Cdd:PLN02316 250 LLEEKRRELEKLAK------EEAERERQAEE-QRRREEEKAAMEADRAQ----------------AKAEVEKRREK 302
|
|
| |
