|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
470-677 |
1.86e-107 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 330.96 E-value: 1.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 470 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 549
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 550 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 629
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131298187 630 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 677
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
371-560 |
3.52e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 371 IQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKesQREKEKLEAELATARSTNEDQRRHIEIRDQAL 450
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 451 SNAQ--AKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQG-NSQPTNVSE-- 525
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElq 205
|
170 180 190
....*....|....*....|....*....|....*
gi 1131298187 526 YNAAALMEILREKEERILALEADMTKWEQKYLEEN 560
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-652 |
1.27e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 327 ADPFAIVSraQQMV-EILS---DENRNLRQELEGcyekVARL--QKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLE 400
Cdd:TIGR02168 135 KRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYkeRRKETE-RKLERTRENLDRLEDILNELERQL-KSLE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 401 GEIR---RMHDFNRDLRDKE---SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKV 474
Cdd:TIGR02168 207 RQAEkaeRYKELKAELRELElalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 475 EKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAAALMEILREKEERILALEADMTKWEQ 554
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 555 KYLEenvmrhfaldaaatvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 634
Cdd:TIGR02168 366 ELEE-----------------------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
330
....*....|....*...
gi 1131298187 635 VLQQRSRKEPSKTEQLSS 652
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLK 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
326-628 |
2.71e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 326 PADPF--AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAM 395
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 396 RNKLEGEIRRMHDFNRDLRDKESQREK-EKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKV 474
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKlEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 475 EKMQQALVQLQAACEK-------REQLEHRLRtRLERELESLRiQQRQGnsqptnvseynAAALMEILREKEERILALEA 547
Cdd:PRK03918 279 EEKVKELKELKEKAEEyiklsefYEEYLDELR-EIEKRLSRLE-EEING-----------IEERIKELEEKEERLEELKK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 548 DMTKWEQKY--LEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEE--EEILMANKRCLDMEGRIKTLH 623
Cdd:PRK03918 346 KLKELEKRLeeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEieEEISKITARIGELKKEIKELK 425
|
....*
gi 1131298187 624 AQIIE 628
Cdd:PRK03918 426 KAIEE 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-548 |
1.12e-08 |
|
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: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 335 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRmhdfnR 411
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIAR-----L 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 412 DLRDKESQREKEKLEAELatarstnEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkvEKMQQALVQLQAACEKR 491
Cdd:COG1196 308 EERRRELEERLEELEEEL-------AELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAEL 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298187 492 EQLEHRLRTRLERELESLRiQQRQGNSQPTNVSEYNAAALMEILREKEERILALEAD 548
Cdd:COG1196 375 AEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
387-650 |
2.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 387 KREAlEKAMR-NKLEGEIRRMHDFNRDLRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 465
Cdd:COG1196 206 ERQA-EKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 466 KKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnvseynAAALMEILREKEERILAL 545
Cdd:COG1196 285 EAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE--------LEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 546 EADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQ 625
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260
....*....|....*....|....*
gi 1131298187 626 IIEKDAMIKVLQQRSRKEPSKTEQL 650
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-510 |
1.06e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 412
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 413 LRDK--ESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACE 489
Cdd:TIGR02168 822 LRERleSLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEaLALLRSELEELSE 901
|
170 180
....*....|....*....|.
gi 1131298187 490 KREQLEHRlRTRLERELESLR 510
Cdd:TIGR02168 902 ELRELESK-RSELRRELEELR 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-555 |
1.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 362 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAMR-----NKLEGEIRRMHDFNRDLRDKESQREKEKLEAELATARSTN 436
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPIRElaeryAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 437 EDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEKREqlehRLRTRLERELESLriqqrqG 516
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEERE----RRRARLEALLAAL------G 372
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131298187 517 NSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQK 555
Cdd:COG4913 373 LPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
332-515 |
1.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 332 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKR---EALEKAMRNkLEGEIRRMHD 408
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAE-LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 409 FNRDLRdkesqrekeKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQalVQLQAAC 488
Cdd:COG4913 683 SSDDLA---------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALL 751
|
170 180 190
....*....|....*....|....*....|...
gi 1131298187 489 EKR------EQLEHRLRTRLERELESLRIQQRQ 515
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARLNR 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
345-500 |
2.48e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 345 DENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFNRDLRD-KESQREKE 423
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEElRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 424 KLEAELATAR--------STNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLE 495
Cdd:COG4717 167 ELEAELAELQeeleelleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
....*
gi 1131298187 496 HRLRT 500
Cdd:COG4717 247 EARLL 251
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
372-700 |
9.05e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 372 QRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRD-----KESQREKEKLEAELATARSTNEDQRRHIEIR 446
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQlreelEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 447 DQALSNAQAKVVKLEEELKKKQ----VYVDKVEKMQQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQ 519
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQeeaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 520 PTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQ 599
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 600 KEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLSHSSTLTGT 679
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|.
gi 1131298187 680 PIMEEKRDDKSWKGSLGILLG 700
Cdd:COG4372 326 KKLELALAILLAELADLLQLL 346
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
417-652 |
1.31e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 417 ESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEH 496
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 497 RLRTRLERELESLRiQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQ 576
Cdd:TIGR02168 754 KELTELEAEIEELE-ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298187 577 RDTTVISHspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 652
Cdd:TIGR02168 833 IAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-654 |
1.95e-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: 51.99 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 338 QMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEirRMHDFNRDLRDK 416
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAE--RYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 417 ESQ---REKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAA--CEKR 491
Cdd:TIGR02169 224 EGYellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGelEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 492 EQLEHRLRTrLERELESLRIQQRQGnsqptnVSEYNaaALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAA 571
Cdd:TIGR02169 304 ASLERSIAE-KERELEDAEERLAKL------EAEID--KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 572 TVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR-----IKTLHAQIIEKDAMIKVLQQRSR 641
Cdd:TIGR02169 375 EVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELAdlnaaIAGIEAKINELEEEKEDKALEIK 451
|
330
....*....|...
gi 1131298187 642 KEPSKTEQLSSMR 654
Cdd:TIGR02169 452 KQEWKLEQLAADL 464
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
363-515 |
2.75e-06 |
|
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: 49.54 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 363 RLQKVETEIQRVSEAYENLvkssskrEALEKAMRNKLEGEIRRMHDFNRDLRDKEsqREKEKLEAELATARS-TNEDQRR 441
Cdd:COG1579 11 DLQELDSELDRLEHRLKEL-------PAELAELEDELAALEARLEAAKTELEDLE--KEIKRLELEIEEVEArIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 442 HIEIRD----QALS----NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQ 513
Cdd:COG1579 82 LGNVRNnkeyEALQkeieSLKRRISDLEDEILELM---ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
..
gi 1131298187 514 RQ 515
Cdd:COG1579 159 EE 160
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-515 |
6.45e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 341 EILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEayenlvksssKREALEKAmRNKLEGEIRRMhdfNRDLRDKESQR 420
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----------ELEELEAE-LEELREELEKL---EKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 421 EKEKLEAELAtarsTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVD---------KVEKMQQALVQLQAACEKR 491
Cdd:COG4717 133 ELEALEAELA----ELPERLEELEERLEELRELEEELEELEAELAELQEELEelleqlslaTEEELQDLAEELEELQQRL 208
|
170 180
....*....|....*....|....
gi 1131298187 492 EQLEHRLRtRLERELESLRIQQRQ 515
Cdd:COG4717 209 AELEEELE-EAQEELEELEEELEQ 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
333-550 |
8.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEGCYEKVARLqkvETEIQrvsEAYENLVKSSSKREALEKAMR------NKLEGEIRRM 406
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAEL---ESELE---EAREAVEDRREEIEELEEEIEelrerfGDAPVDLGNA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 407 HDFNRDLR-DKESQREKEK-LEAELATARSTNEDQRRHIE----------IRD----QALSNAQAKVVKLEEELKKKQVY 470
Cdd:PRK02224 411 EDFLEELReERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsphvETIEEDRERVEELEAELEDLEEE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 471 VDKVEKMQQALVQLQAAC-------EKREQLEHRL---RTRLERE---LESLRIQQRQGNSQpTNVSEYNAAALMEILRE 537
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEdrierleERREDLEELIaerRETIEEKrerAEELRERAAELEAE-AEEKREAAAEAEEEAEE 569
|
250
....*....|...
gi 1131298187 538 KEERILALEADMT 550
Cdd:PRK02224 570 AREEVAELNSKLA 582
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
387-648 |
1.20e-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: 49.58 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 387 KREALEKAMRnKLEGEIRRmhdfNRDLRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQALS----------NAQAK 456
Cdd:pfam02463 171 KKEALKKLIE-ETENLAEL----IIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklneeridLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 457 VVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQ------GNSQPTNVSEYNAAA 530
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKlerrkvDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 531 LMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntsydtaLEARIQKEEEEILMANK 610
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--------LESERLSSAAKLKEEEL 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 1131298187 611 RCLDMEGRIKTLHAQIIEKDAMI-KVLQQRSRKEPSKTE 648
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEE 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
352-509 |
1.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 352 QELEGCYEKVARLQKVETEIQRVSE----AYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLRDKESQREKEKLEA 427
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKelkkLEEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYEELREEYLELSR 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 428 ELATARSTNEDQRRHieiRDQALSNAQakvvKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELE 507
Cdd:PRK03918 674 ELAGLRAELEELEKR---REEIKKTLE----KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVG 746
|
..
gi 1131298187 508 SL 509
Cdd:PRK03918 747 EI 748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-517 |
1.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 335 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRvseayenlvksssKREALEKAMRNklegeirrmhdfnrdlr 414
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALRE-------------ELDELEAQIRG----------------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 415 dkESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE----- 489
Cdd:COG4913 335 --NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealae 409
|
170 180 190
....*....|....*....|....*....|.
gi 1131298187 490 ---KREQLEHRLRtRLERELESLRiqQRQGN 517
Cdd:COG4913 410 aeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
336-513 |
2.52e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 336 AQQMVEILSDENRNLRQElegcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 414
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 415 DK--ESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALvqlqaacekRE 492
Cdd:pfam01576 229 AQiaELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL---------GE 299
|
170 180
....*....|....*....|.
gi 1131298187 493 QLEhRLRTRLERELESLRIQQ 513
Cdd:pfam01576 300 ELE-ALKTELEDTLDTTAAQQ 319
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-556 |
2.69e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 335 RAQQMVEILSDENRNLRQELEGCYEKVARLQK-----------VETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEI 403
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEeleeaeeeleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 404 RRMHDFNRDLRDKESQ-----REKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkvekmQ 478
Cdd:COG1196 393 RAAAELAAQLEELEEAeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---------E 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131298187 479 QALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnvsEYNAAALMEILREKEERILALEADMTKWEQKY 556
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE-----GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
345-657 |
3.98e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 345 DENRNLRQELEGCYEKVARLQKVETEiqrvseayenlvKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKESQREKEK 424
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTE------------KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 425 LEAELATARSTNEDQRRHIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLER 504
Cdd:pfam10174 536 LENQLKKAHNAEEAVRTNPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 505 ELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVIS 583
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQS 684
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131298187 584 HSPNTSYDTALEARIQKEEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 657
Cdd:pfam10174 685 LAEKDGHLTNLRAERRKQLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| TMEM108 |
pfam15759 |
TMEM108 family; This family of proteins is found in eukaryotes. Proteins in this family are ... |
88-249 |
4.39e-05 |
|
TMEM108 family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 258 and 575 amino acids in length.
Pssm-ID: 464851 [Multi-domain] Cd Length: 511 Bit Score: 47.37 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 88 MQMSLATSGVKAHPPVTSAP-LSPPQPNDLYKNPTSSSDFYKAQGPPPsqhslkgmehrgpPPEYPFKGMPPQSIVCKPQ 166
Cdd:pfam15759 57 AAMATTESHSEGRPPGEAVPtILLTKPTGATSRPTTAPTRSTTRRPPR-------------PPGSSRKGASSSSRPVSPA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 167 EPGHYysehrlnqpGRTEGQLMRYQHPPEYGAARPTQDI----------SLPLSARNSQPHSPT---SSLTSGGSLPLLQ 233
Cdd:pfam15759 124 PSGHL---------GRKEGQRGRNQSSTHLGQKRPLGKIfqiykgnftgSVEPDPSALTPRTPLwgySSSPQPQTVSTTT 194
|
170
....*....|....*.
gi 1131298187 234 SPPSTRLSPAQHPLVP 249
Cdd:pfam15759 195 APPSTSWRPPTNPLVP 210
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
335-542 |
4.44e-05 |
|
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: 47.41 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 335 RAQQMVEILSDENRNLRQELEGCYEK-VARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEG----------EI 403
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkkqienknkNI 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 404 RRMHDFNRDLRDKESQREKE---------KLEAELATARS-----TNEDQRrhiEIRDQALSNAqakvvKLEEELKKKQV 469
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQlnayeikvnKLELELASAKQkfeeiIDNYQK---EIEDKKISEE-----KLLEEVEKAKA 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 470 YVDKVEKMQQ--------ALVQLQAACEK---------------------REQLEHRLRTRLERELESLRIQQRQGNSQp 520
Cdd:pfam05483 683 IADEAVKLQKeidkrcqhKIAEMVALMEKhkhqydkiieerdselglyknKEQEQSSAKAALEIELSNIKAELLSLKKQ- 761
|
250 260
....*....|....*....|..
gi 1131298187 521 tnvseynaaalMEILREKEERI 542
Cdd:pfam05483 762 -----------LEIEKEEKEKL 772
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
368-482 |
7.44e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 368 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDK--ESQREKEKLEAELATARSTNEDQ---RRH 442
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEleEKDERIERLERELSEARSEERREirkDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1131298187 443 IEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 482
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELK---RKLERLKELWK 503
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
105-237 |
8.22e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 105 SAPLSPPQPNDLYKNPTsssdfykaQGPPPSQHSLKGMEHRGPPPEY--PFKGMPPQSIVCKPQEPghYYSEHRLNQPGR 182
Cdd:PRK10263 753 QQPQQPVAPQQQYQQPQ--------QPVAPQPQYQQPQQPVAPQPQYqqPQQPVAPQPQYQQPQQP--VAPQPQYQQPQQ 822
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131298187 183 TEGQLMRYQHPPEYGAARPTQDISLPLSARN--SQP-HSPTSSLTSggsLPLLQSPPS 237
Cdd:PRK10263 823 PVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNgdSRPlHKPTTPLPS---LDLLTPPPS 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-547 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 343 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKR--EALEkamrnKLEGEIRRMHDF-NRDLRDKESQ 419
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVE-----ELEERLKELEPFyNEYLELKDAE 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 420 REKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVvkleEELKKK---QVYVDKVEKMQQALVQLQAACEKREQLEH 496
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----EELEKKyseEEYEELREEYLELSRELAGLRAELEELEK 687
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131298187 497 RLRTrLERELESLRIQQRQGNSQPTNVSEYNAA-ALMEILREKEERILALEA 547
Cdd:PRK03918 688 RREE-IKKTLEKLKEELEEREKAKKELEKLEKAlERVEELREKVKKYKALLK 738
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
349-554 |
1.25e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 349 NLRQELEgcyEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRmhdfNRDLRDKESQREKEKLEAE 428
Cdd:pfam12128 351 SWQSELE---NLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE----ARDRQLAVAEDDLQALESE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 429 L-----ATARSTNEDQRRhIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE 503
Cdd:pfam12128 424 LreqleAGKLEFNEEEYR-LKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131298187 504 RELESLRIQQRQGNSQPTNVSEynaaaLMEILREKEERILA-LEADMTKWEQ 554
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDE-----LELQLFPQAGTLLHfLRKEAPDWEQ 549
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
412-559 |
2.33e-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: 43.76 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 412 DLRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAcekR 491
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVRNN---K 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131298187 492 EQlehrlrTRLERELESLRIQQRQgnsqptnvSEYNAAALMEILREKEERILALEADMTKWEQKYLEE 559
Cdd:COG1579 90 EY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
333-655 |
2.56e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALekAMRNKLEGEIRRMHDFNRD 412
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM--AMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 413 LRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQAlsnAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAacekRE 492
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL---EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA----RQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 493 QLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAA---ALMEILREKEERILA-------LEADMTKWEQKYLEENVM 562
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 563 RHFaldaAATVAAQRDTTVISHSPNTSYDTalEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQ-QRSR 641
Cdd:pfam17380 515 RKL----LEKEMEERQKAIYEEERRREAEE--ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVEsEKAR 588
|
330
....*....|....
gi 1131298187 642 KEPSKTEQLSSMRP 655
Cdd:pfam17380 589 AEYEATTPITTIKP 602
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-644 |
2.70e-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: 45.05 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 359 EKVARLQKVETEIQR-VSEAYENLVKSSSKREALEKAMRNKLEgeirRMHDFNRDLrdKESQREKEKLEAELATARSTNE 437
Cdd:TIGR02168 239 EELEELQEELKEAEEeLEELTAELQELEEKLEELRLEVSELEE----EIEELQKEL--YALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 438 DQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQG 516
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 517 NSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEA 596
Cdd:TIGR02168 392 ELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1131298187 597 RIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVLQQRSRKEP 644
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFS 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
418-647 |
3.10e-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: 44.37 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 418 SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQAL-VQLQAACEKREQLEH 496
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 497 RLRTRLERELESLRIQQRQGNSQPTNV---------SEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFAL 567
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 568 DAAATVAAQRdttvishspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKT 647
Cdd:COG4942 178 ALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
350-509 |
4.96e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 42.73 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 350 LRQELEGCYEKVARLQKvetEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKESQREKEKLE 426
Cdd:cd07596 16 LEEQLKKLSKQAQRLVK---RRRELGSALGEFgkaLIKLAKCEEEVGGELGEALSKLGKAAEELSSLSEAQANQELVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 427 AEL----ATARSTNE--DQR----RHIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEH 496
Cdd:cd07596 93 EPLkeylRYCQAVKEtlDDRadalLTLQSLKKDLASKKAQLEKLKAAPGIKP---AKVEELEEELEEAESALEEARKRYE 169
|
170
....*....|...
gi 1131298187 497 RLRTRLERELESL 509
Cdd:cd07596 170 EISERLKEELKRF 182
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
333-540 |
6.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQkveteiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDfnrd 412
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLE------EELEELNEQLQAAQAELAQAQEEL-ESLQEEAEELQE---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 413 lRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM--QQALVQLQAACEK 490
Cdd:COG4372 116 -ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQALDELLKEANR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1131298187 491 REQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 540
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-652 |
6.30e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYEN-----------LVKSSSKREALEKAMrNKLEG 401
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEIN---EKTTEISNTQTQLNQLKDEQNKikkqlsekqkeLEQNNKKIKELEKQL-NQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 402 EI-----RRMHDFNRDLRD--KESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKV 474
Cdd:TIGR04523 296 EIsdlnnQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 475 EKMQQALVQ-LQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQPTNVSEYNAAALMEIlREKEERILALEA 547
Cdd:TIGR04523 376 KKENQSYKQeIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI-KDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 548 DMTKWEQ--KYLEENVmrhfaldaaatvaaqrDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQ 625
Cdd:TIGR04523 455 IIKNLDNtrESLETQL----------------KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
330 340
....*....|....*....|....*..
gi 1131298187 626 IIEKDAMIKVLQQRSRKEPSKTEQLSS 652
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-515 |
7.38e-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: 42.83 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 331 AIVSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFN 410
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIA---ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 411 RDLRDKE--SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAac 488
Cdd:COG4942 118 RQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA-- 195
|
170 180
....*....|....*....|....*..
gi 1131298187 489 eKREQLEHRLRTRLERELESLRIQQRQ 515
Cdd:COG4942 196 -ERQKLLARLEKELAELAAELAELQQE 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-650 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 359 EKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKESQREKEKLEAElaTARSTNE- 437
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEa 1521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 438 ---DQRRHIEIRDQALSNAQAKVVKLEEELKKKQvYVDKVEKMQQAlvqlqaacEKREQLEHRLRTRLERELESLRIQQR 514
Cdd:PTZ00121 1522 kkaDEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKA--------EEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 515 QGNSQPTNVSEYNAAALMEILREKEERIlaleadmtKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTAL 594
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKI--------KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131298187 595 EARiQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKV--LQQRSRKEPSKTEQL 650
Cdd:PTZ00121 1665 EEA-KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEEL 1721
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
395-521 |
1.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 395 MRNKLEGEIRRMHDFNRDLRDKESQREK--EKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVKLEE 462
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQEELEArlESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALARLRE 617
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298187 463 ----ELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGNSQPT 521
Cdd:PRK04863 618 qsgeEFEDSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGSEDPR 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
348-509 |
1.17e-03 |
|
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: 42.75 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 348 RNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKES--QREKEKL 425
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGdlKKERDEL 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 426 EAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvdKVEKMQQALVQLQAACEKREQLEHRLRtRLERE 505
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-------EIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEE 966
|
....
gi 1131298187 506 LESL 509
Cdd:TIGR02169 967 IRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-650 |
1.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 350 LRQELEGCYEKVARLQKVETEIQRVSEAYEnlVKSSSKREALEKAMRNKLEGEIRRMHDFNR--DLRDKESQR---EKEK 424
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELKkaeEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 425 LEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE- 503
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEe 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 504 -RELESLRIQQRQGN---SQPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDT 579
Cdd:PTZ00121 1646 kKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131298187 580 TVishspntsYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHaqiIEKDAMIKVLQQRSRKEPSKTEQL 650
Cdd:PTZ00121 1726 EE--------NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH---LKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
348-546 |
1.29e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 348 RNLRQELEGCYEKVARLQKVETEI---QRVSEAYENLVKSS----SKREALEKAMRNKLEGEIrrmhDFNRDLRD--KES 418
Cdd:COG5185 343 AEIEQGQESLTENLEAIKEEIENIvgeVELSKSSEELDSFKdtieSTKESLDEIPQNQRGYAQ----EILATLEDtlKAA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 419 QREKEKLEAELATARSTNEDQRRHIeirdQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRL 498
Cdd:COG5185 419 DRQIEELQRQIEQATSSNEEVSKLL----NELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1131298187 499 RTrLERELESLRIQ-QRQGNSQPTNVSEYNAAALMEILREKEERILALE 546
Cdd:COG5185 495 ST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
387-555 |
1.30e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 387 KREALEKAMRNKLEGEIRRmhdfnrDLRDKESQREKEKLEAELAtarstnedQRRHIEIRDQALSNAQAKVVKLEEELKk 466
Cdd:COG2268 192 RKIAEIIRDARIAEAEAER------ETEIAIAQANREAEEAELE--------QEREIETARIAEAEAELAKKKAEERRE- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 467 kqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgnsqptnvseynAAALMEILREKEERILAL 545
Cdd:COG2268 257 ----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADVRKPA 314
|
170
....*....|
gi 1131298187 546 EADMTKWEQK 555
Cdd:COG2268 315 EAEKQAAEAE 324
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-548 |
1.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 340 VEILSDENRNLRQELEGCYEKVAR---LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEgeirrmhdfnrdlrdk 416
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERaedLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE---------------- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 417 ESQREKEKLEAELATARSTNEDQRRHIEirdqalsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEH 496
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAE-------EAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1131298187 497 RLRTRLERELESlriqqrqgnsqptnvseynaaalMEILREKEERILALEAD 548
Cdd:PRK02224 614 KREALAELNDER-----------------------RERLAEKRERKRELEAE 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-445 |
2.48e-03 |
|
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: 41.98 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 334 SRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKREALEKAMRNkLEGEIRRMHDfnrd 412
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEK---- 483
|
90 100 110
....*....|....*....|....*....|...
gi 1131298187 413 lRDKESQREKEKLEAELATARSTNEDQRRHIEI 445
Cdd:TIGR02169 484 -ELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
474-649 |
2.73e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 474 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTKWE 553
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 554 QKYLEenvmrhfaldaaatVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 633
Cdd:COG1579 80 EQLGN--------------VRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 1131298187 634 KVLQQRSRKEPSKTEQ 649
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
337-556 |
2.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 337 QQMVEILSDENRNLRQELEGcyekvaRLQKVETEIQRVSEAYENLvksssKREALEKAMRNKLEGEIRRMHDFNRDLRdk 416
Cdd:COG3206 163 EQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLA-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 417 ESQREKEKLEAELATARSTNEDQRRHIE--IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQLQAACEKREQ 493
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298187 494 LEHRLRTRLERELESLRIQQRQGNSQptnVSEYNAAALMeiLREKEERILALEADMTKWEQKY 556
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
416-504 |
2.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 416 KESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKreqLE 495
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE---KELEQKQQELEKKEEELEE---LI 137
|
....*....
gi 1131298187 496 HRLRTRLER 504
Cdd:PRK12704 138 EEQLQELER 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
333-551 |
3.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRN----LRQELEGCYEK--VARLQKVETEIQRVSEAYENLvksSSKREAlEKAMRNKLEGEIRRM 406
Cdd:PRK02224 171 ASDARLGVERVLSDQRGsldqLKAQIEEKEEKdlHERLNGLESELAELDEEIERY---EEQREQ-ARETRDEADEVLEEH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 407 hdfnrdlrdKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQALVQLQA 486
Cdd:PRK02224 247 ---------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDDADAEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131298187 487 ACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTK 551
Cdd:PRK02224 312 VEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-629 |
3.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 337 QQMVEILSDENR--NLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKR------------EALEKAM------R 396
Cdd:PRK03918 328 ERIKELEEKEERleELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpeklekelEELEKAKeeieeeI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 397 NKLEGEIRRMHDFNRDLRDKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEE---ELKKKQVYVDK 473
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEkerKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 474 VEKMQQALVQLQAACEKREQLEHRLRT--------------RLERELESLRIQQRQGNSQPTNVSEYNA--AALMEILRE 537
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKynleelekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKklAELEKKLDE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 538 KEERILALEadmtkweqKYLEEnvmRHFALDAAATVAAQRDTTV----ISHSPNTSYDTALEARIQKEEEEILMANKRCL 613
Cdd:PRK03918 568 LEEELAELL--------KELEE---LGFESVEELEERLKELEPFyneyLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
330
....*....|....*.
gi 1131298187 614 DMEGRIKTLHAQIIEK 629
Cdd:PRK03918 637 ETEKRLEELRKELEEL 652
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
416-509 |
4.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 416 KESQREKE--KLEAELAtARSTNEDQRRHIE----IRDQALSNAQAKVVKLEEELKKKQVYVDK----VEKMQQALVQLQ 485
Cdd:PRK12704 45 EEAKKEAEaiKKEALLE-AKEEIHKLRNEFEkelrERRNELQKLEKRLLQKEENLDRKLELLEKreeeLEKKEKELEQKQ 123
|
90 100
....*....|....*....|....
gi 1131298187 486 AACEKREQLEHRLRTRLERELESL 509
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERI 147
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
340-493 |
5.11e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 340 VEILSDENRNLRQELEGCYEKVARLQK---------------VETEIQRVSEAYENLV-KSSSKREALEKAMrnKLEGEI 403
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNElgeqlieeghpdaeeIQERLEELNQRWEELReLAEERRQRLEEAL--DLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 404 RRMHDFNRDLRDKESQREKEKLEAELATARS---TNEDQRRHIEIRDQALSNAQAKVVKLEEE--LKKKQVYVDKVEKMQ 478
Cdd:cd00176 113 RDADDLEQWLEEKEAALASEDLGKDLESVEEllkKHKELEEELEAHEPRLKSLNELAEELLEEghPDADEEIEEKLEELN 192
|
170
....*....|....*
gi 1131298187 479 QALVQLQAACEKREQ 493
Cdd:cd00176 193 ERWEELLELAEERQK 207
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
353-544 |
5.24e-03 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 39.53 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 353 ELEGCYEKVARLQ-KVETEIQ--RVSEAyenlVKSSSKREALEKAMRNkLEGEIRRMHDFNRDLRD---KESQREKEKLE 426
Cdd:pfam06705 6 KLSNMNERVSGFHdKMENEIEvkRVDED----TRVKMIKEAIAHLEKL-IQTESKKRQESFEDIQEefkKEIDNMQETIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 427 AELAT--------ARSTNE-------DQRRHIEIRDQALSNAQAKVVK---------LEEELKKKQVYVDKVEKMQQALV 482
Cdd:pfam06705 81 EEIDDmaanfrkaLAELNDtinnvetNLQNEIAIHNDAIEALRKEALKslndletgiATENAERKKMYDQLNKKVAEGFA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298187 483 QLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTN-VSEYNAAALMEILREKEERILA 544
Cdd:pfam06705 161 RISAAIDTEKNARDSAVSAATTELTNTKLVEKCVNEQFENaVLSEIAAIKEELDREKAERKAA 223
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
100-288 |
5.30e-03 |
|
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: 40.91 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 100 HPPVTSAPLSPPQPNDLYK-NPTSSSDFYKAQGPPPSQhslkgmehrgPPPEYPFKGMPPQSIVckpqEPGHYYSEHRLN 178
Cdd:pfam03154 178 SGAASPPSPPPPGTTQAATaGPTPSAPSVPPQGSPATS----------QPPNQTQSTAAPHTLI----QQTPTLHPQRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 179 QPgrtegqlmryqHPPEYGAARPTqdislPLSARNSQPHSPTSSLTSGGSLP-LLQSPPSTRLSP-AQHPLVPNQGDHSA 256
Cdd:pfam03154 244 SP-----------HPPLQPMTQPP-----PPSQVSPQPLPQPSLHGQMPPMPhSLQTGPSHMQHPvPPQPFPLTPQSSQS 307
|
170 180 190
....*....|....*....|....*....|..
gi 1131298187 257 HLPRPQQHFLPNQAHQGDHYRLPQPGLSQQQP 288
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQP 339
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
421-547 |
5.77e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.42 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 421 EKEKLEAELATARSTNEDQRRHIEirdQALSNAQ---AKVVkleeeLKKKQVYVDKVEKMQQALVQLQAACEKREQLEHR 497
Cdd:COG1842 52 NQKRLERQLEELEAEAEKWEEKAR---LALEKGRedlAREA-----LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131298187 498 LRTRLE---RELESLRIQ------QRQGNSQPTNVSEYNAAALMEILrekEERILALEA 547
Cdd:COG1842 124 LESKLEelkAKKDTLKARakaakaQEKVNEALSGIDSDDATSALERM---EEKIEEMEA 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
359-509 |
5.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 359 EKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDKESQREKEKLEAE----LATARS 434
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaalLAEAGV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 435 TNEDQRRHIEIRDQALSNAQAKVVKLEEELKKK-------QVYVDKV---EKMQQALVQLQAACEKREQLEHRLRtRLER 504
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleelLEALDEEeleEELEELEEELEELEEELEELREELA-ELEA 460
|
....*
gi 1131298187 505 ELESL 509
Cdd:COG4717 461 ELEQL 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-465 |
7.48e-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: 40.43 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 333 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 412
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 413 LRDK---------ESQREKEKLEAELAT--------ARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 465
Cdd:TIGR02168 913 LRREleelreklaQLELRLEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
399-474 |
8.73e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.85 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298187 399 LEGEIRRmHDFNrDLRDKESQREKEKLEAELATARSTNEDQRRHIEI-------RDQALSNAQAKVVKLEEELKKKQVYV 471
Cdd:PLN02316 237 IEGGMDE-HSFE-DFLLEEKRRELEKLAKEEAERERQAEEQRRREEEkaameadRAQAKAEVEKRREKLQNLLKKASRSA 314
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...
gi 1131298187 472 DKV 474
Cdd:PLN02316 315 DNV 317
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