|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
578-785 |
1.41e-104 |
|
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: 326.72 E-value: 1.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 578 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADM 657
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 658 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 737
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 590121980 738 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLAHSSTLT 785
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-656 |
1.29e-11 |
|
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: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 488
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 489 DLRDRLETANKQLAEKEYEGSEDTRKtISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 568
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 569 EEELKKKQVYVDKVEKMQQALVQLQAAC--EKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREK 646
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLeeELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|
gi 590121980 647 EERILALEAD 656
Cdd:COG1196 472 AALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-664 |
4.78e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 439 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQ 518
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 519 LFAKHKENQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 596
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 597 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnaSEYNAAAlMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-663 |
1.62e-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: 65.46 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 483
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 484 HDFNRDLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 563
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 564 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQGNSQpTNASEYNAAALM 640
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEELSEE-LRELESKRSELR 914
|
250 260
....*....|....*....|...
gi 590121980 641 ELLREKEERILALEADMTKWEQK 663
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVR 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-736 |
1.68e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 403 PADPF--AMVSRAQQMVEIL-SDENRN--LRQ--ELDGcYEKVAR-LQKVETEIQRVSEAYENLVKSSSKREALEKAMRN 474
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilGLDD-YENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 475 KLEGEIRRMHDFNRDLRDRLETANKqlAEKEYEGSEDTRKTISQLfakhkenQREKEKLEAELatarstnedqrRHIEIR 554
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEEL-------EKELESLEGSK-----------RKLEEK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 555 DQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacEKREQLEHRLRtRLERELESLRiQQRQGnsqptnasey 634
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS---EFYEEYLDELR-EIEKRLSRLE-EEING---------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 635 nAAALMELLREKEERILALEADMTKWEQKY--LEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEE-- 710
Cdd:PRK03918 326 -IEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEie 404
|
330 340
....*....|....*....|....*.
gi 590121980 711 EEILMANKRCLDMEGRIKTLHAQIIE 736
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEE 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-667 |
2.96e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 464 KREALEK--AMRNKLEgeirRMHDFNRDLRDRLETANKQlAEK-----EYEGSEDTRKtISQLFAKHKENQREKEKLEAE 536
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 537 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 616
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 590121980 617 LRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:COG1196 321 LEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
440-760 |
5.28e-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: 63.92 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 440 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRDRLETANKQLAEKEYEgseDTRKTISQL 519
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 520 FAKHKENQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 599
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 600 EQLEHRLRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 679
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 680 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 759
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 590121980 760 S 760
Cdd:TIGR02168 428 K 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-664 |
7.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLR 491
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 492 DRLETANKQL--AEKEYEGSEDTRKTI----SQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKV 565
Cdd:COG1196 337 EELEELEEELeeAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 566 VKLEEELKKKQvyvdkvEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynAAALMELLRE 645
Cdd:COG1196 417 ERLEEELEELE------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAE 488
|
250
....*....|....*....
gi 590121980 646 KEERILALEADMTKWEQKY 664
Cdd:COG1196 489 AAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-667 |
8.53e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 407 FAMVSRAQQMVEILSDEnrnlRQELDGCYEKVA-RLQKVETEIQRVSEAYENlVKSSSKREALEKAMR----NKLEGEIR 481
Cdd:TIGR02169 708 SQELSDASRKIGEIEKE----IEQLEQEEEKLKeRLEELEEDLSSLEQEIEN-VKSELKELEARIEELeedlHKLEEALN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 482 RMHDfnRDLRDRLETANKQLAEKEYEGSEdTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNA 561
Cdd:TIGR02169 783 DLEA--RLSHSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 562 QAKVVKLEEELKKKQVYVDKVEK------------------MQQALVQLQAACEKREQLEHRLRTRLERELESLR-IQQR 622
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESrlgdlkkerdeleaqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDP 939
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 590121980 623 QGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-625 |
2.15e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 405 DPFAMVSRAQQMVEILSDENRnLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 480
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 481 RRmhdfnrdLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQ-REKEKLEAELATARSTNEDQRRHIEIRDQALS 559
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 590121980 560 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 625
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-668 |
5.51e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 498 NKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 575
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 576 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NASEYNAAALMELLREKEERILA 652
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 590121980 653 LEADMTKWEQKYLEEN 668
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-608 |
2.15e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 429 QELDGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRDRLETANKQLAE--K 504
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 505 EYEGSEDTRKTISQLFAKHKENQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 590121980 584 KMQQALVQLQAACEKREQLEHRLRT 608
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
439-663 |
3.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 439 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRDRLETANKQLAEKEYEGSEdtrktisq 518
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYLRAA-------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 519 lfAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 598
Cdd:COG4913 281 --LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590121980 599 REqlehRLRTRLERELESLriqqrqGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQK 663
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-666 |
5.77e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 426 NLRQELDGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETANKQLAE 503
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 504 KeyegSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:TIGR02168 748 R----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 584 KMQQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNASEYNAAALMELLREKEERI 650
Cdd:TIGR02168 824 ERLESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*.
gi 590121980 651 LALEADMTKWEQKYLE 666
Cdd:TIGR02168 904 RELESKRSELRRELEE 919
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
420-617 |
1.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKS------------SSKREALEKAMRNKLE-----GEIRR 482
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesveelEERLKELEPFYNEYLElkdaeKELER 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 483 MHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQLFAK-----HKENQREKEKLEAELATARSTNEDQRRHieiRDQA 557
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKR---REEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 558 LSNAQakvvKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:PRK03918 693 KKTLE----KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
441-659 |
1.67e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 441 LQKVETEIQRVSEAYENlVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRDRLETANKQLAE-----KEYEGSED-- 511
Cdd:PRK02224 161 LGKLEEYRERASDARLG-VERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 512 --TRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQAL 589
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDD 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 590 VQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTK 659
Cdd:PRK02224 307 ADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
420-656 |
2.01e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 420 LSDENRNLRQELDGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 485
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 486 FNRDLRDRLETANK-QLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 564
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 565 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNASEYnaaa 638
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 590121980 639 lmelLREKEERILALEAD 656
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
351-629 |
2.51e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 351 LSRHQQHLLSSQSHQGdHYRHAQASLTSAQQQPGeaysAMPRAQQSASyqpmpadpfAMVSRAQQMVEILSDENRNLRQE 430
Cdd:PRK04863 399 LADYQQALDVQQTRAI-QYQQAVQALERAKQLCG----LPDLTADNAE---------DWLEEFQAKEQEATEELLSLEQK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 431 LD------GCYEKVARL-QKVETEIQRvSEAY----ENLVKSSSKREALEK--AMRNKLeGEIRRMHDFNRDLRDRLETA 497
Cdd:PRK04863 465 LSvaqaahSQFEQAYQLvRKIAGEVSR-SEAWdvarELLRRLREQRHLAEQlqQLRMRL-SELEQRLRQQQRAERLLAEF 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 498 NKQLaEKEYEGSEDtrktisqLFAKHKENQREKEKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVK 567
Cdd:PRK04863 543 CKRL-GKNLDDEDE-------LEQLQEELEARLESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALAR 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 568 LEE----ELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGNSQPT 629
Cdd:PRK04863 615 LREqsgeEFEDSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGSEDPR 674
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
440-623 |
4.64e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 440 RLQKVETEIQRVseayenlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRDRLETANKQLAEKEyEGSEDTRKTISQL 519
Cdd:COG1579 11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 520 FAKHKENQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 599
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....
gi 590121980 600 EQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE 160
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-765 |
6.54e-07 |
|
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: 53.67 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 414 QQMVEILSDENRNLRQELDGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 482
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 483 MHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKE-------------KLEAELATARSTNEDQRR 549
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 550 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 629
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 630 NASEYNAAALMELLREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 708
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 590121980 709 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 765
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
418-658 |
1.21e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 418 EILSDENRNLRQELDGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRDRL 494
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 495 ETANKQL--AEKEYEGSEDTR---KTISQLFAKHKENQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 555
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 556 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRLRTRLER-ELESLRIQQRQGNS 626
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIAERRETiEEKRERAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 590121980 627 QPTNAS----EYNAAALMELLREKEERILALEADMT 658
Cdd:PRK02224 547 AELEAEaeekREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-567 |
2.85e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 422 DENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 488
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 489 DLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 567
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
464-669 |
3.20e-06 |
|
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: 51.51 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 464 KREALEKAMR---------NKLEGEIR----------------------------------------RMHDFNRDLRDRL 494
Cdd:pfam02463 171 KKEALKKLIEetenlaeliIDLEELKLqelklkeqakkaleyyqlkekleleeeyllyldylklneeRIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 495 ET--ANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEEL 572
Cdd:pfam02463 251 EEieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 573 KKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEE---- 648
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqll 410
|
250 260
....*....|....*....|..
gi 590121980 649 -RILALEADMTKWEQKYLEENV 669
Cdd:pfam02463 411 lELARQLEDLLKEEKKEELEIL 432
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
420-667 |
3.22e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 51.23 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRDR 493
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 494 LETANKQLAEKEYEGSEDTRKTISQLF------AKHKENQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 559
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 560 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 619
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 590121980 620 QQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKwEQKYLEE 667
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
421-623 |
3.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 421 SDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQ 500
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 501 LAEKEYEGSEDTR---KTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 577
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 590121980 578 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-810 |
6.19e-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: 50.83 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 427 LRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKE 505
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 506 YEGSEDtRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 585
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 586 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnaseynAAALMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 665 LEENvmrhfaldaAATVAAQRDttvishspntsydtALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVL 744
Cdd:TIGR02168 424 EELL---------KKLEEAELK--------------ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 590121980 745 QQRSRKEPSKTEQLSSMRpaKSLMSISNAGSGLLAHSSTLTG--APIMEEKRDDKSWKGSLGVLLGGD 810
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQ--ENLEGFSEGVKALLKNQSGLSGilGVLSELISVDEGYEAAIEAALGGR 546
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
413-654 |
1.20e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.57 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 413 AQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE------IRRMHDF 486
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksSEELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 487 N---RDLRDRLETANKQLAEKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 563
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 564 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRI---QQRQGNSQPTNASEYNAAALM 640
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAkleRQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|....
gi 590121980 641 elLREKEERILALE 654
Cdd:COG5185 531 --RARGYAHILALE 542
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-637 |
1.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklEGEIRRmhdfNRDLR 491
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 492 DRLETANKQLAEkeyegsedtrktisqlfakhkenqrekekLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 571
Cdd:COG4913 678 ERLDASSDDLAA-----------------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 590121980 572 LKKKQVYVDKVEKMQQalVQLQAACEKR------EQLEHRLRTRLERELESLRIQQRQGNSQPTNA-SEYNAA 637
Cdd:COG4913 729 LDELQDRLEAAEDLAR--LELRALLEERfaaalgDAVERELRENLEERIDALRARLNRAEEELERAmRAFNRE 799
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
510-808 |
1.27e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 510 EDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 585
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 586 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQ 662
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 663 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 742
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 743 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLAHSSTLTGAPIMEEKRDDKSWKGSLGVLLG 808
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
413-617 |
2.11e-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: 49.02 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 413 AQQMVEILSDENRNLRQEldgcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 491
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 492 DRLETANKQLAEKEYE------GSEDTRKTISQLFAKHKENQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 558
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 590121980 559 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 617
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-649 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 439 ARLQKVETEIQRVSEAYENLVKSSSKreaLEKAMRNklEGEIRRMH---DFNRDLRDRLETANKQLAEKEYEGSEDTR-- 513
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 514 ---------------KTISQLFAKHKENQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 557
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 558 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNSQptnaS 632
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKR----R 689
|
250
....*....|....*..
gi 590121980 633 EYNAAALMELLREKEER 649
Cdd:PRK03918 690 EEIKKTLEKLKEELEER 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
410-760 |
5.42e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 410 VSRAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENLVKS-SSKREALEKAmrNKLegeirrmhdfNR 488
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEIN---EKTTEISNTQTQLNQLKDEQNKIKKQlSEKQKELEQN--NKK----------IK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 489 DLRDRLETANKQLAEKEYEGSEDTRKTI-SQLfakhKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKELkSEL----KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 568 LEEELKKKQVYVDKVEKMQQALVQ---------------LQAACEKREQLEHRLRT------RLERELESLRIQQRQGNS 626
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQeiknlesqindleskIQNQEKLNQQKDEQIKKlqqekeLLEKEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 627 QptnaseynaaalmelLREKEERILALEADMTKWEQ--KYLEENVmrhfaldaaatvaaqrDTTVISHSPNTSYDTALEA 704
Cdd:TIGR04523 441 E---------------IKDLTNQDSVKELIIKNLDNtrESLETQL----------------KVLSRSINKIKQNLEQKQK 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 705 RIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 760
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-552 |
6.11e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 445 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHK 524
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE 466
|
90 100 110
....*....|....*....|....*....|
gi 590121980 525 ENQREKE--KLEAELATARSTNEDQRRHIE 552
Cdd:COG2433 467 ISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
412-672 |
1.02e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 482
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 483 MHDFNR-------DLRDRLETANKQLAEKEYEGSEDTRkTISQLFAKHKENQREKEKLEAELATARSTNEDqrrhIEIRD 555
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 556 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL---------ESLRIQQR 622
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdEQIRKIKS 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 590121980 623 QGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQKYLEENVMRH 672
Cdd:TIGR00606 557 RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-592 |
1.12e-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: 46.55 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 414 QQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 490
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 491 RDRLETANKQLAEKEYEGSEDTR-KTISQLfaKH-----KENQREKEKLEAELATARStneDQRRHIEIRDQALSNAQAK 564
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEEL--KQtqkslKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKISSLEKE 618
|
170 180
....*....|....*....|....*...
gi 590121980 565 VVKLEEELKKKQVYVDKVEKMQQALVQL 592
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-762 |
1.13e-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: 46.60 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 415 QMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRDR 493
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 494 LEtankqlaekEYEGSEDTRktisqlfakhkenqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 573
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 574 KKQVYVDKVEKMQQALVQlqaacEKREQLEHRLRtRLERELESLRIQQRQGNSQPTNA-SEYNaaALMELLREKEERILA 652
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-----EKIGELEAEIA-SLERSIAEKERELEDAEERLAKLeAEID--KLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 653 LEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR- 726
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELAd 424
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 590121980 727 ----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 762
Cdd:TIGR02169 425 lnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
492-663 |
1.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 492 DRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 571
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 572 LKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER---ELESLRIQQRQGNSQptnaseynAAALMELLREKEE 648
Cdd:COG4372 82 LEELN---EQLQAAQAELAQAQEELESLQEEAEELQEELEElqkERQDLEQQRKQLEAQ--------IAELQSEIAEREE 150
|
170
....*....|....*
gi 590121980 649 RILALEADMTKWEQK 663
Cdd:COG4372 151 ELKELEEQLESLQEE 165
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
464-650 |
3.13e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 464 KREALEKAMRNKLEGEIRrmhdfnrDLRDRLETANK------------QLAEKEYEGS-EDTRKTISQLFAKHKENQREK 530
Cdd:pfam01576 763 KQRAQAVAAKKKLELDLK-------ELEAQIDAANKgreeavkqlkklQAQMKDLQRElEEARASRDEILAQSKESEKKL 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 531 EKLEAELATAR---STNEDQRRHI---------EIRDQALSNA---------QAKVVKLEEELKKKQVYV----DKVEKM 585
Cdd:pfam01576 836 KNLEAELLQLQedlAASERARRQAqqerdeladEIASGASGKSalqdekrrlEARIAQLEEELEEEQSNTellnDRLRKS 915
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 590121980 586 QQALVQLQA-------ACEKREQlehrLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERI 650
Cdd:pfam01576 916 TLQVEQLTTelaaersTSQKSES----ARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQL 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-667 |
3.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELdGCY--EKVAR-LQKVETEIQRVSEAYENLVKS----SSKREALEKAMrNKLEGEIRRMH 484
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRL-TGLtpEKLEKeLEELEKAKEEIEEEISKITARigelKKEIKELKKAI-EELKKAKGKCP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 485 DFNRDL--RDRLETANKQLAEkeyegSEDTRKTISQLFAKHKENQREKEKLEAELATARS-----TNEDQRRHIEIR--- 554
Cdd:PRK03918 440 VCGRELteEHRKELLEEYTAE-----LKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKlkk 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 555 ----------------DQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacEKREQLEHRLRTR-------LE 611
Cdd:PRK03918 515 ynleelekkaeeyeklKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE---EELAELLKELEELgfesveeLE 591
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 612 RELESLRIQQRQGNSQPTNASEynaaalmelLREKEERILALEADMTKWEqKYLEE 667
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKE---------LEREEKELKKLEEELDKAF-EELAE 637
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-667 |
3.39e-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: 43.37 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 511 DTRktISQLFAKHKENQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 590
Cdd:COG1579 16 DSE--LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590121980 591 QLQAAcekREQlehrlrTRLERELESLRIQQRQgnsqptnaSEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:COG1579 84 NVRNN---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
420-624 |
3.72e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLV-----------KSSSKREALEKAMR-NKLEGEIRRMHDFN 487
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekelveKIKELEKELEKAKKaLEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 488 RDLRDRLETANKQLAEKeYEGSEDTRKTISQLFakhkenqREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:COG1340 170 KELRKEAEEIHKKIKEL-AEEAQELHEEMIELY-------KEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 590121980 568 LEEELKKKQVYVDKVEK-MQQALVQlqaacEKREQLEHRLRTRLERELESLRIQQRQG 624
Cdd:COG1340 242 LRKELKKLRKKQRALKReKEKEELE-----EKAEEIFEKLKKGEKLTTEELKLLQKSG 294
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-656 |
4.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 436 EKVARLQKVEtEIQRVSEAY---ENLVKSSSKREALEKAMRNKLEgeiRRMHDFNRDLRDRLETANKQLAEK----EYEG 508
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAKKAEEAKikaeELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 509 SEDTRKTISQLFAKHKENQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVD 580
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 581 KVEKMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERI 650
Cdd:PTZ00121 1703 KAEELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA--EEIRKEKEAV 1780
|
....*.
gi 590121980 651 LALEAD 656
Cdd:PTZ00121 1781 IEEELD 1786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-600 |
5.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRD 489
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDELEAQIRGNGGDRlEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 490 LRDRLETANKQLAEKEYEGSEDtrktisqlFAkhkENQREKEKLEAELATARSTNEDQRRHIEirdQALSNAQAKVVKLE 569
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FA---ALRAEAAALLEALEEELEALEEALAEAE---AALRDLRRELRELE 425
|
170 180 190
....*....|....*....|....*....|....
gi 590121980 570 EE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 600
Cdd:COG4913 426 AEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-659 |
5.41e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 426 NLRQELDGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRDRLeTANKQL 501
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEEL-TAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 502 AEkeyegseDTRKTISQLFAKHKENQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 575
Cdd:pfam15921 491 LE-------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 576 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnaseynaaalmelLREKEERI 650
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 590121980 651 LALEADMTK 659
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
436-617 |
5.80e-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: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 436 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrdrletANKQLAEKEYEGSEDTRKT 515
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 516 ISQLFAKH-KENQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 577
Cdd:cd07596 66 LSKLGKAAeELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 590121980 578 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
582-757 |
5.83e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 582 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWE 661
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 662 QKyleenvmrhfaldaAATVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 741
Cdd:COG1579 80 EQ--------------LGNVRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 590121980 742 KVLQQRSRKEPSKTEQ 757
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
410-694 |
5.98e-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: 43.96 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 468
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 469 EKAMRNKLEGEIRRMHDF----------NRDLRDRLETANKQ-LAEKEYEGSEDTRKTISQLFAKHKENQREKEkleael 537
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 538 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 606
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 607 RTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 686
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 590121980 687 TTVISHSP 694
Cdd:pfam17380 595 TPITTIKP 602
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
411-667 |
7.01e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 411 SRAQQMVEILSDENrNLRQELDgcyEKVARLQKVETEIQRVSEayenLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDL 490
Cdd:pfam10174 182 ERTRRIAEAEMQLG-HLEVLLD---QKEKENIHLREELHRRNQ----LQPDPAKTKALQTVIEMK-DTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 491 RDRLETANKQLAEkeyeGSEDTRKTISQL--------FAKHKENQREKE---------KLEAELATARSTNEDQRRHIEI 553
Cdd:pfam10174 253 EDEVQMLKTNGLL----HTEDREEEIKQMevykshskFMKNKIDQLKQElskkesellALQTKLETLTNQNSDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 554 -------RDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQ-------------------------LQaacEKREQ 601
Cdd:pfam10174 329 lkesltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEekstlageirdlkdmldvkerkinvLQ---KKIEN 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 590121980 602 LEHRLRTRlERELESLRiQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:pfam10174 406 LQEQLRDK-DKQLAGLK-ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEE 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
488-659 |
7.31e-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: 43.21 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 488 RDLRDRLETANKQLAEKEyegsedtrKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 568 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQpTNASEYNA 636
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAAL-RAELEAER 173
|
170 180
....*....|....*....|...
gi 590121980 637 AALMELLREKEERILALEADMTK 659
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
436-652 |
9.50e-04 |
|
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: 42.23 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 436 EKVARLQ-KVETEIQ--RVSEAyenlVKSSSKREALEKAMRNkLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgsedt 512
Cdd:pfam06705 12 ERVSGFHdKMENEIEvkRVDED----TRVKMIKEAIAHLEKL-IQTESKKRQESFEDIQEEFKKEIDNMQETIKE----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 513 rktisQLFAKHKENQREKEKLEAELATARSTNEDQRrhiEIRDQALSNAQAKVVK---------LEEELKKKQVYVDKVE 583
Cdd:pfam06705 82 -----EIDDMAANFRKALAELNDTINNVETNLQNEI---AIHNDAIEALRKEALKslndletgiATENAERKKMYDQLNK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 584 KMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALME-LLREKEERILA 652
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVEKCVNEQFENAVLSEIAAIKEeLDREKAERKAA 223
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
417-667 |
1.05e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 417 VEILSDENRNLRQELDgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLET 496
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 497 --ANKQLAEKEYEGsedTRKTISQLFAKHKENQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 560
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 561 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgnsqptn 630
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 590121980 631 aseynAAALMELLREKEER-----------ILALEADM--TKWE-QKYLEE 667
Cdd:pfam00038 240 -----KASLERQLAETEERyelqladyqelISELEAELqeTRQEmARQLRE 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
410-671 |
1.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 489
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 490 LRDRL-ETANKQLAEKEYEgsedtrktISQLFAKHKENQREKEKLEAELATARSTNEDQR-RHIEIRDQ-ALSNAQAKVV 566
Cdd:TIGR00606 960 IENKIqDGKDDYLKQKETE--------LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNlTLRKRENELK 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 567 KLEEELKK--KQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLR 644
Cdd:TIGR00606 1032 EVEEELKQhlKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
250 260
....*....|....*....|....*..
gi 590121980 645 EKEERIlaleADMTKWeQKYLEENVMR 671
Cdd:TIGR00606 1112 TTELVN----KDLDIY-YKTLDQAIMK 1133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-571 |
1.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 410 VSRAQQMVEILSDENRNLRQELDGCYEKVA-----RLQKVETEIQRVSEAYENLvksSSKREALEKAMRN---KLEGEIR 481
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 482 RMHDFNRDLRDRLETANKQLAEkeyegsedTRKTISQLFAKHKENQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 556
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 590121980 557 ALSNAQAKV--------VKLEEE 571
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
447-664 |
1.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 447 EIQRVSEAY-ENLVKSS--SKREALEKAmRNKLEGEIRRmhdfnrdLRDRLETANKQLAE--KEY------EGSEDTRKT 515
Cdd:COG3206 149 LAAAVANALaEAYLEQNleLRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfrQKNglvdlsEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 516 ISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIE--IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQL 592
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 590121980 593 QAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnASEYNAAALMelLREKEERILALEADMTKWEQKY 664
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
439-612 |
1.30e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 439 ARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEI----RRMHDFNRDLR---DRLETANKQL--AEKEYEGS 509
Cdd:pfam00261 1 KKMQQIKEELD---EAEERLKEAMKKLEEAEKR-AEKAEAEVaalnRRIQLLEEELErteERLAEALEKLeeAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 510 EDTRKTISQLFAKHKENQREkekLEAELATARSTNEDQRRHIE-------IRDQALSNA-------QAKVVKLEEELKkk 575
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEI---LEAQLKEAKEIAEEADRKYEevarklvVVEGDLERAeeraelaESKIVELEEELK-- 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 590121980 576 qvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER 612
Cdd:pfam00261 152 ----VVGNNLKSLEASEEKASEREDKYEEQIRFLTEK 184
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1017-1049 |
1.31e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 40.62 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|...
gi 590121980 1017 PATSAPVPSPASIPAPATAQASAPTPTQASTPA 1049
Cdd:PRK05641 46 SAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPA 78
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
408-662 |
1.38e-03 |
|
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: 42.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 408 AMVSRAQQMVEILSDEnrnLRQELDGCYEKVA----RLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRR 482
Cdd:pfam12128 315 AAVAKDRSELEALEDQ---HGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 483 MHDFNRDLRDRLETANKQLAEKE--YEGSEdtrktiSQLfakhkenqreKEKLEAELATARstneDQRRHIEIRDQALSN 560
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEddLQALE------SEL----------REQLEAGKLEFN----EEEYRLKSRLGELKL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 561 AQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynaaaLM 640
Cdd:pfam12128 452 RLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LE 526
|
250 260
....*....|....*....|...
gi 590121980 641 ELLREKEERILA-LEADMTKWEQ 662
Cdd:pfam12128 527 LQLFPQAGTLLHfLRKEAPDWEQ 549
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
425-749 |
1.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 425 RNLRQELDGCYEKVARLqkvETEIQRVSEAYENLvkssskREALekAMRNKLEGEIRRMHDfnRDLRDRLETANKQLAEk 504
Cdd:PRK04863 840 RQLNRRRVELERALADH---ESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 505 eyegSEDTRKTISQlfakhkeNQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvd 580
Cdd:PRK04863 906 ----AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF-- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 581 kveKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnASEYNA--AALMELLREKEERILALEADMT 658
Cdd:PRK04863 972 ---SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQ 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 659 KWEQKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKD 738
Cdd:PRK04863 1045 DLGVPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
330
....*....|.
gi 590121980 739 AMIKVLQQRSR 749
Cdd:PRK04863 1116 AGWCAVLRLVK 1126
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
415-663 |
1.67e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 415 QMVEILSDENRnlrqeldGCYEKVARLQKVETEIQRVSEAYENLVKSS-SKREALEKAMRNK-------------LEGEI 480
Cdd:TIGR00606 667 QFITQLTDENQ-------SCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 481 RRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRK-------------------TISQLFAKHKENQREKEKLEAELATA- 540
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesakvcltdvtIMERFQMELKDVERKIAQQAAKLQGSd 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 541 -RSTNEDQRRHIEIRDQALSNAQAKVVKL----EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELE 615
Cdd:TIGR00606 820 lDRTVQQVNQEKQEKQHELDTVVSKIELNrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE-LSTEVQ 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 590121980 616 SL--RIQQRQGNSQPtnaseyNAAALMELLREKEERILALEADMTKWEQK 663
Cdd:TIGR00606 899 SLirEIKDAKEQDSP------LETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
372-507 |
1.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 372 AQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAMVSRAQQMVEILSDEN---RNLRQELDgcyekvARLQKVETEI 448
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIA------ALRAQLQQEA 311
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 590121980 449 QRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRdRLEtANKQLAEKEYE 507
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR-RLE-REVEVARELYE 368
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
410-573 |
2.56e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 489
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 490 LRDRLETANKQLA--EKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVK 567
Cdd:TIGR02168 913 LRRELEELREKLAqlELRLEGLEVRIDNL-------QERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKR 976
|
....*.
gi 590121980 568 LEEELK 573
Cdd:TIGR02168 977 LENKIK 982
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-599 |
2.88e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 358 LLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRAQQSAsyqpmpADPFAMVSRAQQMVEILSDENRNLRQELDGCYEK 437
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE------KALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 438 VARLQKVETEIQRVSEAYENLVKSSSKreALEKAMRNKLEGEIRRMHDFNRDLRDRleTANKQLAEKEYEGSEDTRKTIS 517
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 518 QLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACE 597
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
..
gi 590121980 598 KR 599
Cdd:COG4942 241 ER 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
409-618 |
4.00e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 409 MVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREaLEK----AMRNKLEGEIRRMH 484
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ-LEKvtteAKIKKLEEDILLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 485 DFN-------RDLRDRLETANKQLAEKEyEGSEDTRK-------TISQLFAKHK-------ENQREKEKLEAELATARST 543
Cdd:pfam01576 145 DQNsklskerKLLEERISEFTSNLAEEE-EKAKSLSKlknkheaMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 544 NEDQRRHIEIRDQALSNA----QAKVVKLEEELKKKQVYVDKVEKMQQALVQLQ----AACEKREQLEHRLRTrLERELE 615
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKeeelQAALARLEEETAQKNNALKKIRELEAQISELQedleSERAARNKAEKQRRD-LGEELE 302
|
...
gi 590121980 616 SLR 618
Cdd:pfam01576 303 ALK 305
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
443-663 |
4.17e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 443 KVETEIQRVSEAYENLvkSSSKREALEKAMRNKLEGEIR------RMHDFNRDlRDR-----LETANKQLAEKEYE---- 507
Cdd:COG2268 98 KVNSDPEDIANAAERF--LGRDPEEIEELAEEKLEGALRavaaqmTVEELNED-REKfaekvQEVAGTDLAKNGLElesv 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 508 ---GSEDT--------RKTISQLFAKHKENQREKEKlEAELATARSTNE------DQRRHIEIRDQALSNAQAKVVKLEE 570
Cdd:COG2268 175 aitDLEDEnnyldalgRRKIAEIIRDARIAEAEAER-ETEIAIAQANREaeeaelEQEREIETARIAEAEAELAKKKAEE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 571 ELKkkqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgnsqptnaseynAAALMELLREKEER 649
Cdd:COG2268 254 RRE-----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADV 310
|
250
....*....|....
gi 590121980 650 ILALEADMTKWEQK 663
Cdd:COG2268 311 RKPAEAEKQAAEAE 324
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
182-407 |
4.72e-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: 41.29 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 182 MSLATSGVKAHPPVTSAPLSP----PQPNDLYKNATSSSEFYKAQGP-PPSQHSLKG----MEHRGPPPEYPFKGVPSQS 252
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPlqpmTQPPPPSQVSPQPLPQPSLHGQmPPMPHSLQTgpshMQHPVPPQPFPLTPQSSQS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 253 VVCKSQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARAtqdisSLSLSARNSQPHSPTSSL-TAGASSLPLLQSPPS 331
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA-----PLSMPHIKPPPTTPIPQLpNPQSHKHPPHLSGPS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 332 -----TRLPPGQHL-----VSNQGDHSAHLSRHQqhlLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRA--QQSASY 399
Cdd:pfam03154 383 pfqmnSNLPPPPALkplssLSTHHPPSAHPPPLQ---LMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSglHQVPSQ 459
|
....*...
gi 590121980 400 QPMPADPF 407
Cdd:pfam03154 460 SPFPQHPF 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
420-553 |
5.48e-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: 40.82 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 420 LSDENRNLRQELDgcyEKVARLQKVETEIQRVSEayenlvKSSSKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETA 497
Cdd:TIGR02169 355 LTEEYAELKEELE---DLRAELEEVDKEFAETRD------ELKDYREKLEKLKReiNELKRELDRLQEELQRLSEELADL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 498 NKQLA--------------EKEYEGSEDTRK--------------------TISQLFAKHKENQREKEKLEAELATARST 543
Cdd:TIGR02169 426 NAAIAgieakineleeekeDKALEIKKQEWKleqlaadlskyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEER 505
|
170
....*....|
gi 590121980 544 NEDQRRHIEI 553
Cdd:TIGR02169 506 VRGGRAVEEV 515
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1014-1098 |
5.72e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 1014 QVAPATSAPVPSPASIPAPATAQASAPTPTQASTPAPTEPPSPVP-----TPTPALVQTEGPANPGASSGPRRLSTPNLM 1088
Cdd:PRK07764 409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGApspppAAAPSAQPAPAPAAAPEPTAAPAPAPPAAP 488
|
90
....*....|
gi 590121980 1089 CNPDKPDAPA 1098
Cdd:PRK07764 489 APAAAPAAPA 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-667 |
6.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 436 EKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQlAEKEYEGSEDTRKT 515
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 516 iSQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAA 595
Cdd:PTZ00121 1394 -DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 590121980 596 CEKREQLEHRlrtRLERELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERILALEADMTKwEQKYLEE 667
Cdd:PTZ00121 1473 DEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKAAEAKKKA--DEAKKAEEAKKADEAKKAE-EAKKADE 1538
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
425-666 |
7.05e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 425 RNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKL---EGEIRRMHDFNRDLRDRLETANKQL 501
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAEEEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 502 AEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQalsNAQAKVVKLEEELKKKQVYVDK 581
Cdd:pfam02029 157 EEEE-DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ---NGEEEVTKLKVTTKRRQGGLSQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 582 VEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGnsqptnaseynAAALMELLREKEERILALEADMTKWE 661
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEA-----------ELELEELKKKREERRKLLEEEEQRRK 301
|
....*
gi 590121980 662 QKYLE 666
Cdd:pfam02029 302 QEEAE 306
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
197-409 |
7.59e-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: 40.52 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 197 SAPLSPPQPNDLYKNATSSSEFYKAQGPPPSQHSLKG--------------MEHRGPPPEYPfkGVPSQSVVCKSQEPgh 262
Cdd:pfam03154 143 STSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGaasppsppppgttqAATAGPTPSAP--SVPPQGSPATSQPP-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 263 fysehrlNQPGRTEGQLMRYQHPPEYGAARAtqdisslslsarnSQPHSPTSSLTAGA-----SSLPLLQSPPSTRLPPG 337
Cdd:pfam03154 219 -------NQTQSTAAPHTLIQQTPTLHPQRL-------------PSPHPPLQPMTQPPppsqvSPQPLPQPSLHGQMPPM 278
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 590121980 338 QHLVSNQGDHSAHLSRHQQHLLSSQSHQGD--HYRHAQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAM 409
Cdd:pfam03154 279 PHSLQTGPSHMQHPVPPQPFPLTPQSSQSQvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
489-655 |
8.68e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 489 DLRDRLETANKQLaEKEYEGSEDT----RKTISQLFAKHKENQREKEKLEAELATArstnEDQRRhieirdQALSNAQ-- 562
Cdd:COG1842 16 ALLDKAEDPEKML-DQAIRDMEEDlveaRQALAQVIANQKRLERQLEELEAEAEKW----EEKAR------LALEKGRed 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 563 -AKVVkleeeLKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE---RELESLRIQ------QRQGNSQPTNAS 632
Cdd:COG1842 85 lAREA-----LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEelkAKKDTLKARakaakaQEKVNEALSGID 159
|
170 180
....*....|....*....|...
gi 590121980 633 EYNAAALMELLrekEERILALEA 655
Cdd:COG1842 160 SDDATSALERM---EEKIEEMEA 179
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-648 |
9.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 436 EKVARLQKVEtEIQRVSEAY--ENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDT 512
Cdd:PTZ00121 1534 KKADEAKKAE-EKKKADELKkaEELKKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590121980 513 RKTiSQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAqakvVKLEEELKKKQVYVDKVEKMQQALVQL 592
Cdd:PTZ00121 1613 KKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK----IKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 590121980 593 QAACE--KREQLEHRLRTRLERELEslriQQRQGNSQPTNASEYNAAALMELLREKEE 648
Cdd:PTZ00121 1688 KKAAEalKKEAEEAKKAEELKKKEA----EEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| |
