|
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 |
1.90e-105 |
|
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: 329.42 E-value: 1.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 578 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADM 657
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 658 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 737
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958810113 738 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLVHSSTLT 785
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-656 |
9.66e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 412 RAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYETL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 488
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 489 DLRDRLETANKQLAEKEYEGSEDTRKtISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 568
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 569 EEELKKKQVYVDKVEKMQQALVQLQAAC--EKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREK 646
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLeeELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|
gi 1958810113 647 EERILALEAD 656
Cdd:COG1196 472 AALLEAALAE 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-736 |
2.35e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 403 PADPF--AIVSRAQQMVEIL-SDENRN--LRQ--ELDGcYEKVAR-LQKVETEIQRVSEAYETLVKSSSKREALEKAMRN 474
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilGLDD-YENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 475 KLEGEIRRMHDFNRDLRDRLETANKqlAEKEYEGSEDTRKTISQLfakhkenQREKEKLEAELatarstnedqrRHIEIR 554
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEEL-------EKELESLEGSK-----------RKLEEK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 555 DQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacEKREQLEHRLRtRLERELESLRiQQRQGnsqptnasey 634
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS---EFYEEYLDELR-EIEKRLSRLE-EEING---------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 635 nAAALMELLREKEERILALEADMTKWEQKY--LEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEE-- 710
Cdd:PRK03918 326 -IEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEie 404
|
330 340
....*....|....*....|....*.
gi 1958810113 711 EEILMANKRCLDMEGRIKTLHAQIIE 736
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEE 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-664 |
7.96e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 439 ARLQKVETEIQRVSEAYETLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgSEDTRKTISQ 518
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 519 LFAKHKENQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 596
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958810113 597 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnaSEYNAAAlMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-667 |
1.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 464 KREALEK--AMRNKLEgeirRMHDFNRDLRDRLETANKQlAEK-----EYEGSEDTRKtISQLFAKHKENQREKEKLEAE 536
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 537 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 616
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958810113 617 LRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:COG1196 321 LEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-663 |
1.85e-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: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQR--------VSEAYETLVKSSSKREALEKAMRNkLEGEIRRM 483
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 484 HDFNRDLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 563
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 564 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQGNSQpTNASEYNAAALM 640
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEELSEE-LRELESKRSELR 914
|
250 260
....*....|....*....|...
gi 1958810113 641 ELLREKEERILALEADMTKWEQK 663
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-667 |
4.60e-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: 64.32 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDfnRD 489
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 490 LRDRLETANKQLAEKEYEGSEdTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 569
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSR-IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 570 EELKKKQVYVDKVEK------------------MQQALVQLQAACEKREQLEHRLRTRLERELESLR-IQQRQGNSQPTN 630
Cdd:TIGR02169 868 EELEELEAALRDLESrlgdlkkerdeleaqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIP 947
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958810113 631 ASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-664 |
9.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLR 491
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 492 DRLETANKQL--AEKEYEGSEDTRKTI----SQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKV 565
Cdd:COG1196 337 EELEELEEELeeAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 566 VKLEEELKKKQvyvdkvEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEynAAALMELLRE 645
Cdd:COG1196 417 ERLEEELEELE------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAE 488
|
250
....*....|....*....
gi 1958810113 646 KEERILALEADMTKWEQKY 664
Cdd:COG1196 489 AAARLLLLLEAEADYEGFL 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
405-625 |
1.04e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 405 DPFAIVSRAQQMVEILSDENRnLRQELDGCYEKVARLQkvetEIQRVSEAYETLVKSSSKREALEKAMR--------NKL 476
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALRlwfaqrrlELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 477 EGEIRRmhdfnrdLRDRLETANKQLAEKEyEGSEDTRKTISQLFAKHKENQ-REKEKLEAELATARSTNEDQRRHIEIRD 555
Cdd:COG4913 294 EAELEE-------LRAELARLEAELERLE-ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958810113 556 QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 625
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
404-760 |
1.51e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 404 ADPFAIVSraQQMV-EILS---DENRNLRQELDGcyekVARL--QKVETEiQRVSEAYETLVKSSSKREALEKAMrNKLE 477
Cdd:TIGR02168 135 KRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYkeRRKETE-RKLERTRENLDRLEDILNELERQL-KSLE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 478 GEIRRMHDFnRDLRDRLETANKQLAEKEYEgseDTRKTISQLFAKHKENQREKEKLEAELATArstnedqrrhieirDQA 557
Cdd:TIGR02168 207 RQAEKAERY-KELKAELRELELALLVLRLE---ELREELEELQEELKEAEEELEELTAELQEL--------------EEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 558 LSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEyNAA 637
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE-ELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 638 ALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaatvaaqrdttvishspntsydtaLEARIQKEEEEILMAN 717
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEE-----------------------------------LESRLEELEEQLETLR 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958810113 718 KRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 760
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-668 |
2.90e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 498 NKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 575
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 576 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NASEYNAAALMELLREKEERILA 652
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 1958810113 653 LEADMTKWEQKYLEEN 668
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-608 |
8.90e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 429 QELDGCYEKVARLQKVETEIQrvsEAYETLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRDRLETANKQLAE--K 504
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 505 EYEGSEDTRKTISQLFAKHKENQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 1958810113 584 KMQQALVQLQAACEKREQLEHRLRT 608
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
441-659 |
2.03e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 441 LQKVETEIQRVSEAyETLVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRDRLETANKQLAE-----KEYEGSED-- 511
Cdd:PRK02224 161 LGKLEEYRERASDA-RLGVERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 512 --TRKTISQLFAKHKENQREKEKLEAELATARST-NEDQRRHIEIRDQaLSNAQAKVVKLEEELKkkqvyvDKVEKMQQA 588
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETiAETEREREELAEE-VRDLRERLEELEEERD------DLLAEAGLD 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958810113 589 LVQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTK 659
Cdd:PRK02224 306 DADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-666 |
2.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 426 NLRQELDGCYEKVARLQKVETEIQRVSEAYETlvksssKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETANKQLAE 503
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRK------ELEELEEELEqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 504 KeyegSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 583
Cdd:TIGR02168 748 R----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 584 KMQQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNASEYNAAALMELLREKEERI 650
Cdd:TIGR02168 824 ERLESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*.
gi 1958810113 651 LALEADMTKWEQKYLE 666
Cdd:TIGR02168 904 RELESKRSELRRELEE 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
439-663 |
2.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 439 ARLQKVETEIQRVSEAYETLVKSSSKREALEKAmrnklegeirrmhdfnRDLRDRLETANKQLAEKEYEGSEdtrktisq 518
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYLRAA-------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 519 lfAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 598
Cdd:COG4913 281 --LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958810113 599 REqlehRLRTRLERELESLriqqrqGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQK 663
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
420-656 |
5.93e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 420 LSDENRNLRQELDGCYEKVARLQ-KVETEIQRVSEAYETL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 485
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 486 FNRDLRDRLETANK-QLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 564
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 565 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNASEYnaaa 638
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 1958810113 639 lmelLREKEERILALEAD 656
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
418-617 |
5.93e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 418 EILSDENRNLRQELDGCYEKVARLQK------------VETEIQRVSEAYE---TLVKSSSKREALEKAMRnKLEGEIRR 482
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKeleelgfesveeLEERLKELEPFYNeylELKDAEKELEREEKELK-KLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 483 MHDFNRDLRDRLETANKQLAEKEYEGSEDtrktisqlfaKHKENQREKEKLEAELATARSTNEDQRRHieiRDQALSNAQ 562
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEE----------EYEELREEYLELSRELAGLRAELEELEKR---REEIKKTLE 697
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958810113 563 akvvKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:PRK03918 698 ----KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
414-765 |
1.28e-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: 55.98 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 414 QQMVEILSDENRNLRQELDGCYEKVARLQkveTEIQRVSEAYETLVKSSSKREAL--------EKAMRNKLEgEIRRMHD 485
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQ---TDSSNTDTALTTLEEALSEKERIierlkeqrEREDRERLE-ELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 486 FNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKE-------------KLEAELATARSTNEDQRRHIE 552
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRTNPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 553 IRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNAS 632
Cdd:pfam10174 556 INDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMK 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 633 EYNAAALMELLREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQKEEE 711
Cdd:pfam10174 632 KKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRKQLE 704
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958810113 712 EILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 765
Cdd:pfam10174 705 EIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
440-623 |
2.47e-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: 53.00 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 440 RLQKVETEIQRVseayetlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRDRLETANKQLAEKEyEGSEDTRKTISQL 519
Cdd:COG1579 11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 520 FAKHKENQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 599
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....
gi 1958810113 600 EQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE 160
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
435-629 |
7.74e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 435 YEKVARL-QKVETEIQRvSEAY----ETLVKSSSKREALEK--AMRNKLeGEIRRMHDFNRDLRDRLETANKQLaEKEYE 507
Cdd:PRK04863 475 FEQAYQLvRKIAGEVSR-SEAWdvarELLRRLREQRHLAEQlqQLRMRL-SELEQRLRQQQRAERLLAEFCKRL-GKNLD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 508 GSEDtrktisqLFAKHKENQREKEKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVKLEE----ELK 573
Cdd:PRK04863 552 DEDE-------LEQLQEELEARLESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALARLREqsgeEFE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958810113 574 KKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGNSQPT 629
Cdd:PRK04863 625 DSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGSEDPR 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
418-658 |
8.91e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 418 EILSDENRNLRQELDGCYEkvaRLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRDRL 494
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 495 ETANKQL--AEKEYEGSEDTR---KTISQLFAKHKENQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 555
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 556 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRLRTRLER-ELESLRIQQRQGNS 626
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIAERRETiEEKRERAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958810113 627 QPTNAS----EYNAAALMELLREKEERILALEADMT 658
Cdd:PRK02224 547 AELEAEaeekREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
464-669 |
1.28e-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: 53.05 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 464 KREALEKAMR---------NKLEGEIR----------------------------------------RMHDFNRDLRDRL 494
Cdd:pfam02463 171 KKEALKKLIEetenlaeliIDLEELKLqelklkeqakkaleyyqlkekleleeeyllyldylklneeRIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 495 ET--ANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEEL 572
Cdd:pfam02463 251 EEieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 573 KKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEE---- 648
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqll 410
|
250 260
....*....|....*....|..
gi 1958810113 649 -RILALEADMTKWEQKYLEENV 669
Cdd:pfam02463 411 lELARQLEDLLKEEKKEELEIL 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-567 |
1.88e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 422 DENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 488
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 489 DLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 567
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
420-667 |
2.88e-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: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRDR 493
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 494 LETANKQLAEKEYEGSEDTRKTISQLF------AKHKENQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 559
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 560 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 619
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958810113 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 |
3.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 421 SDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQ 500
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 501 LAEKEYEGSEDTR---KTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 577
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958810113 578 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 623
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
409-637 |
5.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 409 IVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAmrnklEGEIRRmhdfNR 488
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 489 DLRDRLETANKQLAEkeyegsedtrktisqlfakhkenqrekekLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 568
Cdd:COG4913 675 AELERLDASSDDLAA-----------------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958810113 569 EEELKKKQVYVDKVEKMQQalVQLQAACEKR------EQLEHRLRTRLERELESLRIQQRQGNSQPTNA-SEYNAA 637
Cdd:COG4913 726 EEELDELQDRLEAAEDLAR--LELRALLEERfaaalgDAVERELRENLEERIDALRARLNRAEEELERAmRAFNRE 799
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
510-808 |
7.60e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 510 EDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 585
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 586 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQ 662
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 663 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 742
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958810113 743 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLVHSSTLTGVPIMEEKRDDKSWKGSLGILLG 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 |
8.26e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 413 AQQMVEILSDENRNLRQEldgcYEKVARLQKVETEIQRV-SEAYETLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 491
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 492 DRLETANKQLAEKEYE------GSEDTRKTISQLFAKHKENQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 558
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958810113 559 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 617
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-752 |
8.98e-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: 50.06 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 427 LRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKE 505
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 506 YEGSEDtRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 585
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 586 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnaseynAAALMELLREKEERILALEADMTKWEQKY 664
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 665 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 744
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 1958810113 745 QQRSRKEP 752
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-649 |
2.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 439 ARLQKVETEIQRVSEAYETLVKSSSKreaLEKAMRNklEGEIRRMH---DFNRDLRDRLETANKQLAEKEYEGSEDTR-- 513
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 514 ---------------KTISQLFAKHKENQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 557
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 558 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNSQptnaS 632
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKR----R 689
|
250
....*....|....*..
gi 1958810113 633 EYNAAALMELLREKEER 649
Cdd:PRK03918 690 EEIKKTLEKLKEELEER 706
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
413-654 |
2.62e-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: 48.42 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 413 AQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGE------IRRMHDF 486
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksSEELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 487 N---RDLRDRLETANKQLAEKEYEGSEDTRKTIsqlfakhKENQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 563
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 564 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRI---QQRQGNSQPTNASEYNAAALM 640
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAkleRQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|....
gi 1958810113 641 elLREKEERILALE 654
Cdd:COG5185 531 --RARGYAHILALE 542
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
420-760 |
2.68e-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: 48.48 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 420 LSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYETLvksSSKREALEKAMRNKlEGEIRRMHDFNRDLRDRLETANK 499
Cdd:TIGR04523 223 LKKQNNQLKDNIE---KKQQEINEKTTEISNTQTQLNQL---KDEQNKIKKQLSEK-QKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 500 QLAEKEYEGSEDTRKTI-SQLfakhKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVY 578
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELkSEL----KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 579 VDKVEKMQQALVQ---------------LQAACEKREQLEHRLRT------RLERELESLRIQQRQGNSQptnaseynaa 637
Cdd:TIGR04523 372 IEKLKKENQSYKQeiknlesqindleskIQNQEKLNQQKDEQIKKlqqekeLLEKEIERLKETIIKNNSE---------- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 638 almelLREKEERILALEADMTKWEQ--KYLEENVmrhfaldaaatvaaqrdtTVISHSPNtSYDTALEArIQKE----EE 711
Cdd:TIGR04523 442 -----IKDLTNQDSVKELIIKNLDNtrESLETQL------------------KVLSRSIN-KIKQNLEQ-KQKElkskEK 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958810113 712 EILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 760
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
412-672 |
3.87e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 412 RAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREAL---------EKAMRNKLEGEIRR 482
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 483 MHDFNR-------DLRDRLETANKQLAEKEYEGSEDTRkTISQLFAKHKENQREKEKLEAELATARSTNEDqrrhIEIRD 555
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 556 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL---------ESLRIQQR 622
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdEQIRKIKS 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958810113 623 QGNSQPTNASEY--NAAALMELLREKEERILALEADMTKWEQKYLEENVMRH 672
Cdd:TIGR00606 557 RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
455-652 |
4.06e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 455 YETLVKSSSKREALEKAMRNKLEGEIRrmhdfnrDLRDRLETANK------------QLAEKEYEGS-EDTRKTISQLFA 521
Cdd:pfam01576 754 LEAELEDERKQRAQAVAAKKKLELDLK-------ELEAQIDAANKgreeavkqlkklQAQMKDLQRElEEARASRDEILA 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 522 KHKENQREKEKLEAELATAR---STNEDQRRHI---------EIRDQALSNA---------QAKVVKLEEELKKKQVYV- 579
Cdd:pfam01576 827 QSKESEKKLKNLEAELLQLQedlAASERARRQAqqerdeladEIASGASGKSalqdekrrlEARIAQLEEELEEEQSNTe 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 580 ---DKVEKMQQALVQLQA-------ACEK----REQLEHR---LRTRLErELESlRIQQRQGNSqpTNASEYNAAALMEL 642
Cdd:pfam01576 907 llnDRLRKSTLQVEQLTTelaaersTSQKsesaRQQLERQnkeLKAKLQ-EMEG-TVKSKFKSS--IAALEAKIAQLEEQ 982
|
250
....*....|.
gi 1958810113 643 L-REKEERILA 652
Cdd:pfam01576 983 LeQESRERQAA 993
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-552 |
4.81e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 445 ETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHK 524
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE 466
|
90 100 110
....*....|....*....|....*....|
gi 1958810113 525 ENQREKE--KLEAELATARSTNEDQRRHIE 552
Cdd:COG2433 467 ISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
420-624 |
5.20e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 420 LSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLV-----------KSSSKREALEKAMR-NKLEGEIRRMHDFN 487
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekelveKIKELEKELEKAKKaLEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 488 RDLRDRLETANKQLAEKeYEGSEDTRKTISQLFakhkenqREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:COG1340 170 KELRKEAEEIHKKIKEL-AEEAQELHEEMIELY-------KEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958810113 568 LEEELKKKQVYVDKVEK-MQQALVQlqaacEKREQLEHRLRTRLERELESLRIQQRQG 624
Cdd:COG1340 242 LRKELKKLRKKQRALKReKEKEELE-----EKAEEIFEKLKKGEKLTTEELKLLQKSG 294
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
492-663 |
5.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 492 DRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEE 571
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 572 LKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER---ELESLRIQQRQGNSQptnaseynAAALMELLREKEE 648
Cdd:COG4372 82 LEELN---EQLQAAQAELAQAQEELESLQEEAEELQEELEElqkERQDLEQQRKQLEAQ--------IAELQSEIAEREE 150
|
170
....*....|....*
gi 1958810113 649 RILALEADMTKWEQK 663
Cdd:COG4372 151 ELKELEEQLESLQEE 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-762 |
6.66e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 415 QMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRDR 493
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 494 LEtankqlaekEYEGSEDTRktisqlfakhkenqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 573
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 574 KKQVYVDKVEKMQQALVQlqaacEKREQLEHRLRtRLERELESLRIQQRQGNSQPTNA-SEYNaaALMELLREKEERILA 652
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVK-----EKIGELEAEIA-SLERSIAEKERELEDAEERLAKLeAEID--KLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 653 LEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR- 726
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELAd 424
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958810113 727 ----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 762
Cdd:TIGR02169 425 lnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
376-600 |
7.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 376 LTPAQQQpGEAYSAMPRAQQAAAYQPMPADPFaivsRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQ-RVSEA 454
Cdd:COG4913 254 LEPIREL-AERYAAARERLAELEYLRAALRLW----FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 455 YETLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRDLRDRLETANKQLAEKEYEGSEDtrktisqlFAkhkENQREKEKL 533
Cdd:COG4913 329 EAQIRGNGGDRlEQLEREIER-LERELEER----ERRRARLEALLAALGLPLPASAEE--------FA---ALRAEAAAL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 534 EAELATARSTNEDQRRHIEirdQALSNAQAKVVKLEEE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 600
Cdd:COG4913 393 LEALEEELEALEEALAEAE---AALRDLRRELRELEAEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-667 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 412 RAQQMVEILSDENRNLRQELdGCYEKvarlQKVETEIQRVSEAYETLvkssskREALEK--AMRNKLEGEIRRMHDFNRD 489
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRL-TGLTP----EKLEKELEELEKAKEEI------EEEISKitARIGELKKEIKELKKAIEE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 490 L-----------RDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARS-----TNEDQRRHIEI 553
Cdd:PRK03918 431 LkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 554 R-------------------DQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacEKREQLEHRLRTR----- 609
Cdd:PRK03918 511 KlkkynleelekkaeeyeklKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE---EELAELLKELEELgfesv 587
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 610 --LERELESLRIQQRQGNSQPTNASEynaaalmelLREKEERILALEADMTKWEqKYLEE 667
Cdd:PRK03918 588 eeLEERLKELEPFYNEYLELKDAEKE---------LEREEKELKKLEEELDKAF-EELAE 637
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
414-592 |
1.71e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 414 QQMVEILSDENRNLRQELDG----CYEKVARLQKVETEIQRVSEAYETLVKSSSkrEALEKamRNKLEGEIRRMHDFNRD 489
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQkqkeLKSKEKELKKLNEEKKELEEKVKDLTKKIS--SLKEK--IEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 490 LRDRLETANKQLAEKEYEGSEDTR-KTISQLfaKH-----KENQREKEKLEAELATARStneDQRRHIEIRDQALSNAQA 563
Cdd:TIGR04523 543 LEDELNKDDFELKKENLEKEIDEKnKEIEEL--KQtqkslKKKQEEKQELIDQKEKEKK---DLIKEIEEKEKKISSLEK 617
|
170 180
....*....|....*....|....*....
gi 1958810113 564 KVVKLEEELKKKQVYVDKVEKMQQALVQL 592
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
404-662 |
1.95e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 404 ADPFAIVSRAQQMVEILSDENRNLRQELDGCYEKVARL-----------QKVETEIQRVSEAYETLVKSSSKREALEKAM 472
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELngelsaadaavAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 473 ----RNKLEGEIRRMHDFNRDLRD------RLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREK-EKLEAEL---- 537
Cdd:pfam12128 349 lpswQSELENLEERLKALTGKHQDvtakynRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlQALESELreql 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 538 -ATARSTNEDQRRhIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELES 616
Cdd:pfam12128 429 eAGKLEFNEEEYR-LKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA 507
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958810113 617 LRIQQRQGNSQPTNASEynaaaLMELLREKEERILA-LEADMTKWEQ 662
Cdd:pfam12128 508 LRQASRRLEERQSALDE-----LELQLFPQAGTLLHfLRKEAPDWEQ 549
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-667 |
2.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 511 DTRktISQLFAKHKENQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 590
Cdd:COG1579 16 DSE--LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958810113 591 QLQAAcekREQlehrlrTRLERELESLRIQQRQgnsqptnaSEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:COG1579 84 NVRNN---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1033-1066 |
2.49e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 42.54 E-value: 2.49e-04
10 20 30
....*....|....*....|....*....|....
gi 1958810113 1033 PATSAPVPSPASIPAPATAQASAPTPTQASTPAP 1066
Cdd:PRK05641 46 SAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAP 79
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
417-667 |
2.53e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 417 VEILSDENRNLRQELDgcyekvARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLET 496
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 497 --ANKQLAEKEYEGsedTRKTISQLFAKHKENQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 560
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 561 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgnsqptn 630
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958810113 631 aseynAAALMELLREKEER-----------ILALEADM--TKWE-QKYLEE 667
Cdd:pfam00038 240 -----KASLERQLAETEERyelqladyqelISELEAELqeTRQEmARQLRE 285
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-659 |
2.59e-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: 45.49 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 426 NLRQELDGCYEKVARLQKV----ETEIQRVSEayETLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRDRLeTANKQL 501
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEEL-TAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 502 AEkeyegseDTRKTISQLFAKHKENQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 575
Cdd:pfam15921 491 LE-------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 576 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnaseynaaalmelLREKEERI 650
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 1958810113 651 LALEADMTK 659
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
411-667 |
2.59e-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: 45.20 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 411 SRAQQMVEILSDENrNLRQELDgcyEKVARLQKVETEIQRVSEayetLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDL 490
Cdd:pfam10174 182 ERTRRIAEAEMQLG-HLEVLLD---QKEKENIHLREELHRRNQ----LQPDPAKTKALQTVIEMK-DTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 491 RDRLETANKQLAEkeyeGSEDTRKTISQL--------FAKHKENQREKE---------KLEAELATARSTNEDQRRHIEI 553
Cdd:pfam10174 253 EDEVQMLKTNGLL----HTEDREEEIKQMevykshskFMKNKIDQLKQElskkesellALQTKLETLTNQNSDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 554 -------RDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQ-------------------------LQaacEKREQ 601
Cdd:pfam10174 329 lkesltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEekstlageirdlkdmldvkerkinvLQ---KKIEN 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958810113 602 LEHRLRTRlERELESLRiQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEE 667
Cdd:pfam10174 406 LQEQLRDK-DKQLAGLK-ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEE 469
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
582-757 |
3.60e-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: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 582 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNASEyNAAALMELLREKEERILALEADMTKWE 661
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 662 QKyleenvmrhfaldaAATVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 741
Cdd:COG1579 80 EQ--------------LGNVRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 1958810113 742 KVLQQRSRKEPSKTEQ 757
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-656 |
4.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 436 EKVARLQKVEtEIQRVSEAY---ETLVKSSSKREALEKAMRNKLEgeiRRMHDFNRDLRDRLETANKQLAEK----EYEG 508
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAKKAEEAKikaeELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 509 SEDTRKTISQLFAKHKENQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVD 580
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 581 KVEKMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERI 650
Cdd:PTZ00121 1703 KAEELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA--EEIRKEKEAV 1780
|
....*.
gi 1958810113 651 LALEAD 656
Cdd:PTZ00121 1781 IEEELD 1786
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
436-652 |
4.74e-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: 43.38 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 436 EKVARLQ-KVETEIQ--RVSEAyetlVKSSSKREALEKAMRNkLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEgsedt 512
Cdd:pfam06705 12 ERVSGFHdKMENEIEvkRVDED----TRVKMIKEAIAHLEKL-IQTESKKRQESFEDIQEEFKKEIDNMQETIKE----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 513 rktisQLFAKHKENQREKEKLEAELATARSTNEDQRrhiEIRDQALSNAQAKVVK---------LEEELKKKQVYVDKVE 583
Cdd:pfam06705 82 -----EIDDMAANFRKALAELNDTINNVETNLQNEI---AIHNDAIEALRKEALKslndletgiATENAERKKMYDQLNK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 584 KMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALME-LLREKEERILA 652
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVEKCVNEQFENAVLSEIAAIKEeLDREKAERKAA 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
488-659 |
4.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 488 RDLRDRLETANKQLAEKEyegsedtrKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 567
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 568 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQpTNASEYNA 636
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAAL-RAELEAER 173
|
170 180
....*....|....*....|...
gi 1958810113 637 AALMELLREKEERILALEADMTK 659
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
436-617 |
5.52e-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: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 436 EKVARLQKVETEIQRVSEAYETLVKsssKREALEKAMrnklegeirrmHDFNRdlrdrletANKQLAEKEYEGSEDTRKT 515
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 516 ISQLFAKH-KENQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 577
Cdd:cd07596 66 LSKLGKAAeELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958810113 578 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 617
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-571 |
5.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 410 VSRAQQMVEILSDENRNLRQELDGCYEKVA-----RLQKVETEIQRVSEAYETLvksSSKREALEKAMRN---KLEGEIR 481
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 482 RMHDFNRDLRDRLETANKQLAEkeyegsedTRKTISQLFAKHKENQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 556
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 1958810113 557 ALSNAQAKV--------VKLEEE 571
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
439-612 |
5.83e-04 |
|
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: 42.71 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 439 ARLQKVETEIQrvsEAYETLVKSSSKREALEKAmRNKLEGEI----RRMHDFNRDLR---DRLETANKQL--AEKEYEGS 509
Cdd:pfam00261 1 KKMQQIKEELD---EAEERLKEAMKKLEEAEKR-AEKAEAEVaalnRRIQLLEEELErteERLAEALEKLeeAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 510 EDTRKTISQLFAKHKENQREkekLEAELATARSTNEDQRRHIE-------IRDQALSNA-------QAKVVKLEEELKkk 575
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEI---LEAQLKEAKEIAEEADRKYEevarklvVVEGDLERAeeraelaESKIVELEEELK-- 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958810113 576 qvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER 612
Cdd:pfam00261 152 ----VVGNNLKSLEASEEKASEREDKYEEQIRFLTEK 184
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
410-694 |
6.56e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVE-------TEIQRVSEAY--------------ETLVKSSSKREaL 468
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 469 EKAMRNKLEGEIRRMHDF----------NRDLRDRLETANKQ-LAEKEYEGSEDTRKTISQLFAKHKENQREKEkleael 537
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 538 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 606
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 607 RTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 686
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 1958810113 687 TTVISHSP 694
Cdd:pfam17380 595 TPITTIKP 602
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
425-749 |
7.52e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 425 RNLRQELDGCYEKVARLqkvETEIQRVSEAYETLvkssskREALekAMRNKLEGEIRRMHDfnRDLRDRLETANKQLAEk 504
Cdd:PRK04863 840 RQLNRRRVELERALADH---ESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 505 eyegSEDTRKTISQlfakhkeNQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvd 580
Cdd:PRK04863 906 ----AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF-- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 581 kveKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnASEYNA--AALMELLREKEERILALEADMT 658
Cdd:PRK04863 972 ---SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQ 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 659 KWEQKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKD 738
Cdd:PRK04863 1045 DLGVPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
330
....*....|.
gi 1958810113 739 AMIKVLQQRSR 749
Cdd:PRK04863 1116 AGWCAVLRLVK 1126
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
410-671 |
7.91e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 410 VSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 489
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 490 LRDRL-ETANKQLAEKEYEgsedtrktISQLFAKHKENQREKEKLEAELATARSTNEDQR-RHIEIRDQ-ALSNAQAKVV 566
Cdd:TIGR00606 960 IENKIqDGKDDYLKQKETE--------LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNlTLRKRENELK 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 567 KLEEELKK--KQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLR 644
Cdd:TIGR00606 1032 EVEEELKQhlKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
250 260
....*....|....*....|....*..
gi 1958810113 645 EKEERIlaleADMTKWeQKYLEENVMR 671
Cdd:TIGR00606 1112 TTELVN----KDLDIY-YKTLDQAIMK 1133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
420-553 |
8.30e-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: 43.52 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 420 LSDENRNLRQELDgcyEKVARLQKVETEIQrvseayETLVKSSSKREALEKAMR--NKLEGEIRRMHDFNRDLRDRLETA 497
Cdd:TIGR02169 355 LTEEYAELKEELE---DLRAELEEVDKEFA------ETRDELKDYREKLEKLKReiNELKRELDRLQEELQRLSEELADL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 498 NKQLA--------------EKEYEGSEDTRK--------------------TISQLFAKHKENQREKEKLEAELATARST 543
Cdd:TIGR02169 426 NAAIAgieakineleeekeDKALEIKKQEWKleqlaadlskyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEER 505
|
170
....*....|
gi 1958810113 544 NEDQRRHIEI 553
Cdd:TIGR02169 506 VRGGRAVEEV 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
447-664 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 447 EIQRVSEAY-ETLVKSS--SKREALEKAmRNKLEGEIRRmhdfnrdLRDRLETANKQLAE--KEY------EGSEDTRKT 515
Cdd:COG3206 149 LAAAVANALaEAYLEQNleLRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfrQKNglvdlsEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 516 ISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIE--IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQL 592
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958810113 593 QAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnASEYNAAALMelLREKEERILALEADMTKWEQKY 664
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
181-407 |
1.41e-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: 42.83 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 181 MSLATSGVKAHPPVTSAPLSP----PQPNDLYKNPTSSSEFYKAQGP-PPSQHSLKS----MEHRGPPPEYPFKGVPSQS 251
Cdd:pfam03154 228 HTLIQQTPTLHPQRLPSPHPPlqpmTQPPPPSQVSPQPLPQPSLHGQmPPMPHSLQTgpshMQHPVPPQPFPLTPQSSQS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 252 VVCKSQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARATQDIASLS---------FSARNSQPHSPTSSLTAGAASL 322
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqLPNPQSHKHPPHLSGPSPFQMN 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 323 PLLQSPPSTR-LSSgqhglVSNQGDHSAHLPRHQqhLLPnQSHQGDHYRHPQPSLTPAQQQPGEAYSAMPRA--QQAAAY 399
Cdd:pfam03154 388 SNLPPPPALKpLSS-----LSTHHPPSAHPPPLQ--LMP-QSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSglHQVPSQ 459
|
....*...
gi 1958810113 400 QPMPADPF 407
Cdd:pfam03154 460 SPFPQHPF 467
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
409-618 |
1.93e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 409 IVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREaLEK----AMRNKLEGEIRRMH 484
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ-LEKvtteAKIKKLEEDILLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 485 DFN-------RDLRDRLETANKQLAEKEyEGSEDTRK-------TISQLFAKHK-------ENQREKEKLEAELATARST 543
Cdd:pfam01576 145 DQNsklskerKLLEERISEFTSNLAEEE-EKAKSLSKlknkheaMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 544 NEDQRRHIEIRDQALSNA----QAKVVKLEEELKKKQVYVDKVEKMQQALVQLQ----AACEKREQLEHRLRTrLERELE 615
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKeeelQAALARLEEETAQKNNALKKIRELEAQISELQedleSERAARNKAEKQRRD-LGEELE 302
|
...
gi 1958810113 616 SLR 618
Cdd:pfam01576 303 ALK 305
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
415-663 |
2.07e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 415 QMVEILSDENRnlrqeldGCYEKVARLQKVETEIQRVSEAYETLVKSS-SKREALEKAMRNK-------------LEGEI 480
Cdd:TIGR00606 667 QFITQLTDENQ-------SCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 481 RRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRK-------------------TISQLFAKHKENQREKEKLEAELATA- 540
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesakvcltdvtIMERFQMELKDVERKIAQQAAKLQGSd 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 541 -RSTNEDQRRHIEIRDQALSNAQAKVVKL----EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELE 615
Cdd:TIGR00606 820 lDRTVQQVNQEKQEKQHELDTVVSKIELNrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE-LSTEVQ 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958810113 616 SL--RIQQRQGNSQPtnaseyNAAALMELLREKEERILALEADMTKWEQK 663
Cdd:TIGR00606 899 SLirEIKDAKEQDSP------LETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
443-663 |
2.11e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 443 KVETEIQRVSEAYETLvkSSSKREALEKAMRNKLEGEIR------RMHDFNRDlRDR-----LETANKQLAEKEYE---- 507
Cdd:COG2268 98 KVNSDPEDIANAAERF--LGRDPEEIEELAEEKLEGALRavaaqmTVEELNED-REKfaekvQEVAGTDLAKNGLElesv 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 508 ---GSEDT--------RKTISQLFAKHKENQREKEKlEAELATARSTNE------DQRRHIEIRDQALSNAQAKVVKLEE 570
Cdd:COG2268 175 aitDLEDEnnyldalgRRKIAEIIRDARIAEAEAER-ETEIAIAQANREaeeaelEQEREIETARIAEAEAELAKKKAEE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 571 ELKkkqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgnsqptnaseynAAALMELLREKEER 649
Cdd:COG2268 254 RRE-----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADV 310
|
250
....*....|....
gi 1958810113 650 ILALEADMTKWEQK 663
Cdd:COG2268 311 RKPAEAEKQAAEAE 324
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
489-655 |
2.91e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 489 DLRDRLETANKQLaEKEYEGSEDT----RKTISQLFAKHKENQREKEKLEAELATArstnEDQRRhieirdQALSNAQ-- 562
Cdd:COG1842 16 ALLDKAEDPEKML-DQAIRDMEEDlveaRQALAQVIANQKRLERQLEELEAEAEKW----EEKAR------LALEKGRed 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 563 -AKVVkleeeLKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE---RELESLRIQ------QRQGNSQPTNAS 632
Cdd:COG1842 85 lAREA-----LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEelkAKKDTLKARakaakaQEKVNEALSGID 159
|
170 180
....*....|....*....|...
gi 1958810113 633 EYNAAALMELLrekEERILALEA 655
Cdd:COG1842 160 SDDATSALERM---EEKIEEMEA 179
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
425-666 |
2.94e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 425 RNLRQELDGCYEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKL---EGEIRRMHDFNRDLRDRLETANKQL 501
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAEEEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 502 AEKEyEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQalsNAQAKVVKLEEELKKKQVYVDK 581
Cdd:pfam02029 157 EEEE-DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ---NGEEEVTKLKVTTKRRQGGLSQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 582 VEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGnsqptnaseynAAALMELLREKEERILALEADMTKWE 661
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEA-----------ELELEELKKKREERRKLLEEEEQRRK 301
|
....*
gi 1958810113 662 QKYLE 666
Cdd:pfam02029 302 QEEAE 306
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
392-661 |
3.16e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.82 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 392 RAQQAAAyQPMPADPFAIVSRAQQMVEILSDEN-------RNLRQELDgcyEKVARLQK-VETEIQRVSEAYETLVKSSS 463
Cdd:pfam15964 320 RSSLAEA-QQRESSAYEQVKQAVQMTEEANFEKtkaliqcEQLKSELE---RQKERLEKeLASQQEKRAQEKEALRKEMK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 464 K-REALEKAMRN------KLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLfakhkeNQREKEKLEAE 536
Cdd:pfam15964 396 KeREELGATMLAlsqnvaQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL------NQTKMKKDEAE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 537 lATARSTNEDQRRHIEIRDQalsnaqaKVVKLEEELKKkqvYVDKVEKMQQALVQLQAACEKREQL----EHRLR-TRLE 611
Cdd:pfam15964 470 -KEHREYRTKTGRQLEIKDQ-------EIEKLGLELSE---SKQRLEQAQQDAARAREECLKLTELlgesEHQLHlTRLE 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958810113 612 REleslRIQQRQGNsqptnasEYNAAALMELLREKE--ERILALEADMTKWE 661
Cdd:pfam15964 539 KE----SIQQSFSN-------EAKAQALQAQQREQEltQKMQQMEAQHDKTV 579
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
411-617 |
4.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 411 SRAQQmvEILSDENRNLRQELD------GCYEKV-ARLQKVETEIQRvSEAYETlvksssKREALE-----KAMRNKLEG 478
Cdd:COG3096 446 FRAKE--QQATEEVLELEQKLSvadaarRQFEKAyELVCKIAGEVER-SQAWQT------ARELLRryrsqQALAQRLQQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 479 EIRRMHDFNRDLRdRLETANKQLAE--KEYEGSEDTRKTISQLFAKHKEnqrEKEKLEAELATA---RSTNEDQRRHIEI 553
Cdd:COG3096 517 LRAQLAELEQRLR-QQQNAERLLEEfcQRIGQQLDAAEELEELLAELEA---QLEELEEQAAEAveqRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958810113 554 RDQALSN-------AQAKVVKLEEE----LKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESL 617
Cdd:COG3096 593 RIKELAArapawlaAQDALERLREQsgeaLADSQ---EVTAAMQQLLEREREATVERDELAAR-KQALESQIERL 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-667 |
5.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 436 EKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQlAEKEYEGSEDTRKT 515
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 516 iSQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAA 595
Cdd:PTZ00121 1394 -DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958810113 596 CEKREQLEHRlrtRLERELESLRIQQRQGNSQPTNASEYNAAAlmELLREKEERILALEADMTKwEQKYLEE 667
Cdd:PTZ00121 1473 DEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKAAEAKKKA--DEAKKAEEAKKADEAKKAE-EAKKADE 1538
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
410-739 |
6.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 410 VSRAQQMVEILSDENRNLRQELDgcyEKVARLQKVETEIQRVSEAYETLVKSSSKREALEKAMRNKLEgeirrmhdfnrd 489
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE------------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 490 lrdRLETANKQLAEKEyegsEDTRKTISQLFAKHKENQREKEKLEAELATARstNEDQRRHIEIRDQALSNAQAKVVKLE 569
Cdd:COG4372 119 ---ELQKERQDLEQQR----KQLEAQIAELQSEIAEREEELKELEEQLESLQ--EELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 570 EELKKKQVYVDKVEKMQQALVQLQAacEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEER 649
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPR--ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 650 ILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKT 729
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|
gi 1958810113 730 LHAQIIEKDA 739
Cdd:COG4372 348 VGLLDNDVLE 357
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
1031-1066 |
7.41e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 40.47 E-value: 7.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1958810113 1031 VAPATSAPVPSPASIPAPATAQASAPTPTQASTPAP 1066
Cdd:PRK06975 270 AQPATAAPAPSRMTDTNDSKSVTSQPAAAAAAPAPP 305
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1032-1119 |
8.03e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958810113 1032 APATSAPVPSPASIPAPATAQASAPTPTQASTPAPIEPPTAVPTPTPALVQAEGPASPGASSGPRRLSTPNLMCNPDKPD 1111
Cdd:PRK07764 415 AAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
|
....*...
gi 1958810113 1112 GPAFHSST 1119
Cdd:PRK07764 495 AAPAAPAA 502
|
|
| |
