|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
592-799 |
2.21e-106 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 330.58 E-value: 2.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 592 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 671
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 672 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 751
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1542976327 752 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 799
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
426-670 |
3.45e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 502
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 503 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 582
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 583 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 662
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 1542976327 663 RILALEAD 670
Cdd:COG1196 472 AALLEAAL 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-750 |
4.13e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 417 PADPF--AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAM 486
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 487 RNKLEGEIRRMHDFN---RDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRR 563
Cdd:PRK03918 199 EKELEEVLREINEISselPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 564 HIEirdqalsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacekreQLEHRLrTRLERELESLRIQQRQGNSQPT 643
Cdd:PRK03918 274 EIE-------ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRL-SRLEEEINGIEERIKELEEKEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 644 NVSEynaaaLMEILREKEERILALEADMTKWEQ-KYLEENVMRHFALDAAAtvaaqrdttvishSPNTSYDTALEARIQK 722
Cdd:PRK03918 339 RLEE-----LKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKRLTGL-------------TPEKLEKELEELEKAK 400
|
330 340 350
....*....|....*....|....*....|
gi 1542976327 723 EE--EEILMANKRCLDMEGRIKTLHAQIIE 750
Cdd:PRK03918 401 EEieEEISKITARIGELKKEIKELKKAIEE 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
426-678 |
8.82e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKV----ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFN 501
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELedaeERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 502 RDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKV 579
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 580 VKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnvSEYNAA 651
Cdd:TIGR02169 437 NELEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRA 511
|
250 260
....*....|....*....|....*..
gi 1542976327 652 AlMEILREKEERILALEADMTKWEQKY 678
Cdd:TIGR02169 512 V-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-774 |
3.18e-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: 64.69 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 418 ADPFAIVSraQQMV-EILS---DENRNLRQELEGcyekVARL--QKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLE 491
Cdd:TIGR02168 135 KRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYkeRRKETE-RKLERTRENLDRLEDILNELERQL-KSLE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 492 GEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrhieirDQA 571
Cdd:TIGR02168 207 RQAEKAERY-KELKAELRELELALLVLRLE---ELREELEELQEELKEAEEELEELTAELQEL--------------EEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 572 LSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAA 651
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 652 ALMEILREKEERILALEADMTKWEQKYLEenvmrhfaldaaatvaaqrdttvishspntsydtaLEARIQKEEEEILMAN 731
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEE-----------------------------------LESRLEELEEQLETLR 385
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1542976327 732 KRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSS 774
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
478-772 |
8.96e-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: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 478 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 550
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 551 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 630
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 631 LRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 710
Cdd:COG1196 321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542976327 711 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 772
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-673 |
9.83e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 497
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 498 HDFNRDLRERLETANKQLAEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 577
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 578 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQgnsqptnvseynaaaLM 654
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEE---------------LS 900
|
250
....*....|....*....
gi 1542976327 655 EILREKEERILALEADMTK 673
Cdd:TIGR02168 901 EELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
443-622 |
3.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 443 QELEGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRERLETANKQLAE--K 518
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 519 EYEGSEDTRKTISQLFAKNKESQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 597
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 1542976327 598 KMQQALVQLQAACEKREQLEHRLRT 622
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
419-639 |
5.49e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 419 DPFAIVSRAQQMVEILSDENRnLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 494
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 495 RRmhdfnrdLRERLETANKQLAEKEyEGSEDTRKTISQLF-AKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALS 573
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542976327 574 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 639
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
512-682 |
3.28e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 512 NKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 589
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 590 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQG-NSQPTNVSE--YNAAALMEILREKEERILA 666
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEElqQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 1542976327 667 LEADMTKWEQKYLEEN 682
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
421-687 |
9.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 421 FAIVSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENLV-----KSSSKREALEKamRNKLEGEIR 495
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRER--LANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 496 RMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNA 575
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 576 QAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLR-TRLERELESLRIQQRQGNSQptnvseynAAALM 654
Cdd:TIGR02168 399 NNEIERLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEA--------LEELR 467
|
250 260 270
....*....|....*....|....*....|....
gi 1542976327 655 EILREKEERILALEADMTKWEQK-YLEENVMRHF 687
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARlDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
440-680 |
1.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 440 NLRQELEGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMR--NKLEGEIRRMHDFNRDLRERLETANKQLAE 517
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELEqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 518 KeyegSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 597
Cdd:TIGR02168 748 R----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 598 KMQQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNVSEYNAAALMEILREKEERI 664
Cdd:TIGR02168 824 ERLESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|....*.
gi 1542976327 665 LALEADMTKWEQKYLE 680
Cdd:TIGR02168 904 RELESKRSELRRELEE 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
453-677 |
3.78e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 453 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRERLETANKQLAEKEYEgsedtRKTISQ 532
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYL-----RAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 533 LFAknkesQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 612
Cdd:COG4913 284 WFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 613 REqlehRLRTRLERELESLriqqrqGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQK 677
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-631 |
3.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 443 QELEGCYEKVARLQKVETEIQRVSEAYENLvkssskREALEKA--MRNKLEGEIRRmhdfnrdLRERLETANKQLAEKEY 520
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKAfeELAETEKRLEE-------LRKELEELEKKYSEEEY 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 521 EGSEDtrktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHieiRDQALSNAQakvvKLEEELKKKQVYVDKVEKMQ 600
Cdd:PRK03918 662 EELRE-----------------EYLELSRELAGLRAELEELEKR---REEIKKTLE----KLKEELEEREKAKKELEKLE 717
|
170 180 190
....*....|....*....|....*....|.
gi 1542976327 601 QALVQLQAACEKREQLEHRLRTRLERELESL 631
Cdd:PRK03918 718 KALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
428-779 |
4.20e-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: 54.06 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 428 QQMVEILSDENRNLRQELEGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 496
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 497 MHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKE-------------KLEAELATARSTNEDQRR 563
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 564 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 643
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 644 NVSEYNAAALMEILREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 722
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 723 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 779
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
432-672 |
4.21e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 432 EILSDENRNLRQELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRERL 508
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 509 ETANKQL--AEKEYEGSEDTR---KTISQLFAKNKESQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 569
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 570 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRL---RTRLERE---LESLRIQQ 635
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIaerRETIEEKrerAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*..
gi 1542976327 636 RQGNSQpTNVSEYNAAALMEILREKEERILALEADMT 672
Cdd:PRK02224 547 AELEAE-AEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
441-766 |
4.99e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 441 LRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKE 519
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 520 YEGSEDtRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 599
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 600 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKY 678
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 679 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 758
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 1542976327 759 QQRSRKEP 766
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-626 |
8.57e-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: 51.46 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 454 RLQKVETEIQRVSEayenlvksssKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTIsql 533
Cdd:COG1579 11 DLQELDSELDRLEH----------RLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 534 fAKNKE------SQREKEKLEAELATA---RSTNEDQRRHIEIR----DQALSNAQAKVVKLEEELKKKQVYVDK-VEKM 599
Cdd:COG1579 76 -KKYEEqlgnvrNNKEYEALQKEIESLkrrISDLEDEILELMERieelEEELAELEAELAELEAELEEKKAELDEeLAEL 154
|
170 180
....*....|....*....|....*...
gi 1542976327 600 QQALVQLQAACEK-REQLEHRLRTRLER 626
Cdd:COG1579 155 EAELEELEAEREElAAKIPPELLALYER 182
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
434-670 |
1.04e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 434 LSDENRNLRQELEGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 499
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 500 FNRDLRERLETANK-QLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 578
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 579 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNVSEYnaaa 652
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 1542976327 653 lmeiLREKEERILALEAD 670
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
435-637 |
1.40e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 435 SDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQ 514
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 515 LAEKEYEGSEDTR---KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 591
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1542976327 592 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 637
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
427-668 |
2.58e-06 |
|
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: 51.50 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 427 AQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE------IRRMHDF 500
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksSEELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 501 N---RDLRERLETANKQLAEKEYEGSEDTRKTIsqlfaknKESQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 577
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 578 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQ-QRQGNSQPTNVSEYNAAALMEI 656
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|..
gi 1542976327 657 LREKEERILALE 668
Cdd:COG5185 531 RARGYAHILALE 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
455-673 |
3.65e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 455 LQKVETEIQRVSEAYENlVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRERLETANKQLAE-----KEYEGSED-- 525
Cdd:PRK02224 161 LGKLEEYRERASDARLG-VERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 526 --TRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQAL 603
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDD 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 604 VQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTK 673
Cdd:PRK02224 307 ADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
423-626 |
5.37e-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: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 423 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKR---EALEKAMRNkLEGEIRRMHD 499
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAE-LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 500 FNRDLR---ERLETANKQLaekeyegsEDTRKTISQLfaknkesQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQ 576
Cdd:COG4913 683 SSDDLAaleEQLEELEAEL--------EELEEELDEL-------KGEIGRLEKELEQA----EEELDELQDRLEAAEDLA 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1542976327 577 AKVVKLEEELKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 626
Cdd:COG4913 744 RLELRALLEERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
441-675 |
6.23e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 441 LRQELEGCYEKVAR---LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFN------RDLRERLETA 511
Cdd:PRK03918 271 LKKEIEELEEKVKElkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 512 NKQLAE-----KEYEGSEDTRKTISQLfaKNKESQREKEKLEAEL---ATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 583
Cdd:PRK03918 351 EKRLEEleerhELYEEAKAKKEELERL--KKRLTGLTPEKLEKELeelEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 584 EELKKKQVYV----------DKVEKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQrqgNSQPTNVSEYNAAAL 653
Cdd:PRK03918 429 EELKKAKGKCpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKVL---KKESELIKLKELAEQ 504
|
250 260
....*....|....*....|....
gi 1542976327 654 MEILREKEERILA--LEADMTKWE 675
Cdd:PRK03918 505 LKELEEKLKKYNLeeLEKKAEEYE 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
434-581 |
7.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 434 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE------KAMRNKLEgEIRRMHDFNRDLRER 507
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperlEELEERLE-ELRELEEELEELEAE 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542976327 508 LETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 581
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
478-683 |
9.13e-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: 49.97 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 478 KREALEKAMR---------NKLEGEIR----------------------------------------RMHDFNRDLRERL 508
Cdd:pfam02463 171 KKEALKKLIEetenlaeliIDLEELKLqelklkeqakkaleyyqlkekleleeeyllyldylklneeRIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 509 ET--ANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEEL 586
Cdd:pfam02463 251 EEieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 587 KKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE---- 662
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqll 410
|
250 260
....*....|....*....|..
gi 1542976327 663 -RILALEADMTKWEQKYLEENV 683
Cdd:pfam02463 411 lELARQLEDLLKEEKKEELEIL 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
427-631 |
1.09e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 427 AQQMVEILSDENRNLRQElegcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 505
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 506 ERLETANKQLAEKEYE------GSEDTRKTISQLFAKNKESQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 572
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542976327 573 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 631
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
426-664 |
1.62e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKVarlqkveteIQRVSEAYENLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDLR 505
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEF---------IQKGDEVKCKLDKSEENARSIEYEVLKK-EKQMKILENKCNNLK 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 506 ERLETANKQLAEKEYEGSEDTRKTIsqlfAKNKE---SQREKEKLEAELATARS-----TNEDQRrhiEIRDQALSNAqa 577
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGS----AENKQlnaYEIKVNKLELELASAKQkfeeiIDNYQK---EIEDKKISEE-- 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 578 kvvKLEEELKKKQVYVDKVEKMQQ--------ALVQLQAACEK---------------------REQLEHRLRTRLEREL 628
Cdd:pfam05483 672 ---KLLEEVEKAKAIADEAVKLQKeidkrcqhKIAEMVALMEKhkhqydkiieerdselglyknKEQEQSSAKAALEIEL 748
|
250 260 270
....*....|....*....|....*....|....*.
gi 1542976327 629 ESLRIQQRQGNSQptnvseynaaalMEILREKEERI 664
Cdd:pfam05483 749 SNIKAELLSLKKQ------------LEIEKEEKEKL 772
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
436-765 |
1.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 436 DENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 502
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 503 DLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 581
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 582 LEE-----------------ELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHR---LRTRLERELESLRIQQRQGNSQ 641
Cdd:COG4717 247 EARlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGkeaEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 642 PTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDT-------------------- 701
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleqaeeyqelkeelee 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542976327 702 ---------TVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQI--IEKDAMI-KVLQQRSRKE 765
Cdd:COG4717 407 leeqleellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELaELLQELEELK 482
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
524-822 |
4.03e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 524 EDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 599
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 600 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQ 676
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 677 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 756
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542976327 757 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLSHSSTLTGTPIMEEKRDDKSWKGSLGILLG 822
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| TMEM108 |
pfam15759 |
TMEM108 family; This family of proteins is found in eukaryotes. Proteins in this family are ... |
179-340 |
5.07e-05 |
|
TMEM108 family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 258 and 575 amino acids in length.
Pssm-ID: 464851 [Multi-domain] Cd Length: 511 Bit Score: 47.37 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 179 MQMSLATSGVKAHPPVTSAP-LSPPQPNDLYKNPTSSSDFYKAQGPPPsqhslkgmehrgpPPEYPFKGMPPQSIVCKPQ 257
Cdd:pfam15759 57 AAMATTESHSEGRPPGEAVPtILLTKPTGATSRPTTAPTRSTTRRPPR-------------PPGSSRKGASSSSRPVSPA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 258 EPGHYysehrlnqpGRTEGQLMRYQHPPEYGAARPTQDI----------SLPLSARNSQPHSPT---SSLTSGGSLPLLQ 324
Cdd:pfam15759 124 PSGHL---------GRKEGQRGRNQSSTHLGQKRPLGKIfqiykgnftgSVEPDPSALTPRTPLwgySSSPQPQTVSTTT 194
|
170
....*....|....*.
gi 1542976327 325 SPPSTRLSPAQHPLVP 340
Cdd:pfam15759 195 APPSTSWRPPTNPLVP 210
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
459-566 |
5.24e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 459 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNK 538
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE-LSEARSEERREIRKDR 465
|
90 100 110
....*....|....*....|....*....|.
gi 1542976327 539 E---SQREKEKLEAELATARSTNEDQRRHIE 566
Cdd:COG2433 466 EisrLDREIERLERELEEERERIEELKRKLE 496
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
434-681 |
7.01e-05 |
|
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: 46.61 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 434 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRER 507
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 508 LETANKQLAEKEYEGSEDTRKTISQLF------AKNKESQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 573
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 574 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 633
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1542976327 634 QQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKwEQKYLEE 681
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
453-663 |
9.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 453 ARLQKVETEIQRVSEAYENLVKSSSKreaLEKAMRNklEGEIRRMH---DFNRDLRERLETANKQLAEKEYEGSEDTR-- 527
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 528 ---------------KTISQLFAKNKESQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 571
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 572 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNSQPTNVs 646
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEI- 692
|
250
....*....|....*..
gi 1542976327 647 eynAAALMEILREKEER 663
Cdd:PRK03918 693 ---KKTLEKLKEELEER 706
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
196-328 |
1.04e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 196 SAPLSPPQPNDLYKNPTsssdfykaQGPPPSQHSLKGMEHRGPPPEY--PFKGMPPQSIVCKPQEPghYYSEHRLNQPGR 273
Cdd:PRK10263 753 QQPQQPVAPQQQYQQPQ--------QPVAPQPQYQQPQQPVAPQPQYqqPQQPVAPQPQYQQPQQP--VAPQPQYQQPQQ 822
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1542976327 274 TEGQLMRYQHPPEYGAARPTQDISLPLSARN--SQP-HSPTSSLTSggsLPLLQSPPS 328
Cdd:PRK10263 823 PVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNgdSRPlHKPTTPLPS---LDLLTPPPS 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
461-678 |
1.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 461 EIQRVSEAY-ENLVKSS--SKREALEKAmRNKLEGEIRRmhdfnrdLRERLETANKQLAE-KEYEGSEDTRKTISQLFAK 536
Cdd:COG3206 149 LAAAVANALaEAYLEQNleLRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 537 NKESQREKEKLEAELATARSTNEDQRRHIE---------IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQL 606
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGsgpdalpelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542976327 607 QAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnVSEYNAAALMeiLREKEERILALEADMTKWEQKY 678
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
429-776 |
1.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 429 QMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRER 507
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 508 LEtankqlaekEYEGSEDTRktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 587
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 588 KKQVYVDKVEKMQQALVQLQAA--CEKREQLEHRLRTrLERELESLRIQQRQGnsqptnVSEYNaaALMEILREKEERIL 665
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIAE-KERELEDAEERLAKL------EAEID--KLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 666 ALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR 740
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELA 423
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1542976327 741 -----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 776
Cdd:TIGR02169 424 dlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
426-686 |
1.18e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 496
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 497 MHDFNR-------DLRERLETANKQLAEKEYEGSEDTRkTISQLFAKNKESQREKEKLEAELATARSTNEDqrrhIEIRD 569
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 570 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL---------ESLRIQQR 636
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdEQIRKIKS 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1542976327 637 QGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQKYLEENVMRH 686
Cdd:TIGR00606 557 RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
428-606 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 428 QQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 504
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 505 RERLETANKQLAEKEYEGSEDTR-KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 583
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
170 180
....*....|....*....|...
gi 1542976327 584 EELKKKQVYVDKVEKMQQALVQL 606
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQE 646
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
431-681 |
1.49e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 431 VEILSDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLET 510
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 511 --ANKQLAEKEYEGsedTRKTISQLFAKNKESQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 574
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 575 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgnsqptn 644
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1542976327 645 vseynAAALMEILREKEER-----------ILALEADM--TKWE-QKYLEE 681
Cdd:pfam00038 240 -----KASLERQLAETEERyelqladyqelISELEAELqeTRQEmARQLRE 285
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
424-753 |
1.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 424 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQkveteiQRVSEAYENLVKSSSKREALEKamrnklegEIRRMHDFNRD 503
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLE------EELEELNEQLQAAQAELAQAQE--------ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 504 LRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARstNEDQRRHIEIRDQALSNAQAKVVKLE 583
Cdd:COG4372 113 LQEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEEQLESLQ--EELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 584 EELKKKQVYVDKVEKMQQALVQLQAacEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEER 663
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPR--ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 664 ILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKT 743
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|
gi 1542976327 744 LHAQIIEKDA 753
Cdd:COG4372 348 VGLLDNDVLE 357
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
450-631 |
1.95e-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: 43.88 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 450 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrerletANKQLAEKEYEGSEDTRKT 529
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 530 ISQLFAK-NKESQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 591
Cdd:cd07596 66 LSKLGKAaEELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1542976327 592 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 631
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
453-626 |
2.03e-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: 44.25 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 453 ARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEI----RRMHDFNRDLR---ERLETANKQL--AEKEYEGS 523
Cdd:pfam00261 1 KKMQQIKEELD---EAEERLKEAMKKLEEAEKR-AEKAEAEVaalnRRIQLLEEELErteERLAEALEKLeeAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 524 EDTRKTISQLFAKNKESQREkekLEAELATARSTNEDQRRHIE-------IRDQALSNA-------QAKVVKLEEELKkk 589
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEI---LEAQLKEAKEIAEEADRKYEevarklvVVEGDLERAeeraelaESKIVELEEELK-- 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1542976327 590 qvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER 626
Cdd:pfam00261 152 ----VVGNNLKSLEASEEKASEREDKYEEQIRFLTEK 184
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
422-676 |
2.25e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 422 AIVSRAQQMVEILSDENRNLRQE-LEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRRMHD 499
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 500 FNRDLRERLETANKQLAEKE--YEGSEDTRKtiSQLFAKNKESQREKEKLEAELATARSTnedqrrhieirdqaLSNAQA 577
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEddLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLR--------------LNQATA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 578 KvvklEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEynaaaLMEIL 657
Cdd:pfam12128 459 T----PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQL 529
|
250 260
....*....|....*....|
gi 1542976327 658 REKEERILA-LEADMTKWEQ 676
Cdd:pfam12128 530 FPQAGTLLHfLRKEAPDWEQ 549
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
509-631 |
2.39e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 509 ETANKQLAEKEYEGSEDTRKTISQlfAKnKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKK 588
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLE--AK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1542976327 589 KQvyvDKVEKMQQALVQLQAACEKreqlehrLRTRLERELESL 631
Cdd:PRK12704 115 KE---KELEQKQQELEKKEEELEE-------LIEEQLQELERI 147
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
525-681 |
2.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 525 DTRktISQLFAKNKESQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 604
Cdd:COG1579 16 DSE--LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 605 QLQAAcekREQlehrlrTRLERELESLRIQQRQgnsqptnvSEYNAAALMEILREKEERILALEADMTKWEQKYLEE 681
Cdd:COG1579 84 NVRNN---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
440-673 |
3.64e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 440 NLRQELEGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRERLeTANKQL 515
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEEL-TAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 516 AEkeyegseDTRKTISQLFAKNKESQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 589
Cdd:pfam15921 491 LE-------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 590 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnvseynaaalmeiLREKEERI 664
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 1542976327 665 LALEADMTK 673
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
426-614 |
3.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRD 503
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDELEAQIRGNGGDRlEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 504 LRERLETANKQLAEKEYEGSEDtrktisqlFAKN-KESQREKEKLEAELATARstnEDQRRHieirDQALSNAQAKVVKL 582
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FAALrAEAAALLEALEEELEALE---EALAEA----EAALRDLRRELREL 424
|
170 180 190
....*....|....*....|....*....|....*
gi 1542976327 583 EEE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 614
Cdd:COG4913 425 EAEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
425-681 |
4.17e-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: 44.43 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 425 SRAQQMVEILSDEnrnlrQELEG-CYEKVARLQKVETEIQRVSEayenLVKSSSKREALEKAMRNKlEGEIRRMHDFNRD 503
Cdd:pfam10174 182 ERTRRIAEAEMQL-----GHLEVlLDQKEKENIHLREELHRRNQ----LQPDPAKTKALQTVIEMK-DTKISSLERNIRD 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 504 LRERLETANKQLAEkeyeGSEDTRKTISQL--------FAKNKESQREKE---------KLEAELATARSTNEDQRRHIE 566
Cdd:pfam10174 252 LEDEVQMLKTNGLL----HTEDREEEIKQMevykshskFMKNKIDQLKQElskkesellALQTKLETLTNQNSDCKQHIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 567 I-------RDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQ-------------------------LQaacEKRE 614
Cdd:pfam10174 328 VlkesltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEekstlageirdlkdmldvkerkinvLQ---KKIE 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 615 QLEHRLRTRlERELESLRiQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEE 681
Cdd:pfam10174 405 NLQEQLRDK-DKQLAGLK-ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEE 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
424-587 |
4.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 424 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 503
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 504 LRERLETANKQLAEkeyegSEDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVKLE 583
Cdd:TIGR02168 913 LRRELEELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKRLE 978
|
....
gi 1542976327 584 EELK 587
Cdd:TIGR02168 979 NKIK 982
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
444-666 |
4.53e-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: 43.00 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 444 ELEGCYEKVARLQ-KVETEIQ--RVSEAyenlVKSSSKREALEKAMRNkLEGEIRRMHDFNRDLRERLETANKQLAEKEY 520
Cdd:pfam06705 6 KLSNMNERVSGFHdKMENEIEvkRVDED----TRVKMIKEAIAHLEKL-IQTESKKRQESFEDIQEEFKKEIDNMQETIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 521 EgsedtrktisQLFAKNKESQREKEKLEAELATARSTNEDQRrhiEIRDQALSNAQAKVVK---------LEEELKKKQV 591
Cdd:pfam06705 81 E----------EIDDMAANFRKALAELNDTINNVETNLQNEI---AIHNDAIEALRKEALKslndletgiATENAERKKM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542976327 592 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTN-VSEYNAAALMEILREKEERILA 666
Cdd:pfam06705 148 YDQLNKKVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVEKCVNEQFENaVLSEIAAIKEELDREKAERKAA 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
540-769 |
4.79e-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: 43.60 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 540 SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQAL-VQLQAACEKREQLEH 618
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 619 RLRTRLERELESLRIQQRQGNSQPTNV---------SEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFAL 689
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 690 DAAATVAAQRdttvishspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKT 769
Cdd:COG4942 178 ALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
450-664 |
5.08e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 450 EKVARLQKVEtEIQRVSEAY---ENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANK-QLAEKEYEGSED 525
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 526 TRKTISQLFAKNKESQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVDKVE 597
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAKKAE 1705
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 598 KMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNVSEYNAAAlMEILREKEERI 664
Cdd:PTZ00121 1706 ELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA-EEIRKEKEAVI 1781
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
457-677 |
7.34e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 457 KVETEIQRVSEAYENLvkSSSKREALEKAMRNKLEGEIR------RMHDFNRD----LRERLETANKQLAEKEYE----- 521
Cdd:COG2268 98 KVNSDPEDIANAAERF--LGRDPEEIEELAEEKLEGALRavaaqmTVEELNEDrekfAEKVQEVAGTDLAKNGLElesva 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 522 --GSEDT--------RKTISQLFAKNKESQREKEKlEAELATARSTNE------DQRRHIEIRDQALSNAQAKVVKLEEE 585
Cdd:COG2268 176 itDLEDEnnyldalgRRKIAEIIRDARIAEAEAER-ETEIAIAQANREaeeaelEQEREIETARIAEAEAELAKKKAEER 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 586 LKkkqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgnsqptnvseynAAALMEILREKEERI 664
Cdd:COG2268 255 RE-----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADVR 311
|
250
....*....|...
gi 1542976327 665 LALEADMTKWEQK 677
Cdd:COG2268 312 KPAEAEKQAAEAE 324
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
424-708 |
8.42e-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: 43.57 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 424 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 482
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 483 EKAMRNKLEGEIRRMHDF----------NRDLRERLETANKQ-LAEKEYEGSEDTRKTISQLFAKNKESQREKEkleael 551
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 552 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 620
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 621 RTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 700
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 1542976327 701 TTVISHSP 708
Cdd:pfam17380 595 TPITTIKP 602
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
423-632 |
9.90e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 423 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENlVKSSSKREALEK----AMRNKLEGEIRRMH 498
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKvtteAKIKKLEEDILLLE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 499 DFN-------RDLRERLETANKQLAEKEyEGSEDTRK-------TISQLFAKNK-------ESQREKEKLEAELATARST 557
Cdd:pfam01576 145 DQNsklskerKLLEERISEFTSNLAEEE-EKAKSLSKlknkheaMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 558 NEDQRRHIEIRDQALSNA----QAKVVKLEEELKKKQVYVDKVEKMQQALVQLQ----AACEKREQLEHRLRTrLERELE 629
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKeeelQAALARLEEETAQKNNALKKIRELEAQISELQedleSERAARNKAEKQRRD-LGEELE 302
|
...
gi 1542976327 630 SLR 632
Cdd:pfam01576 303 ALK 305
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
502-669 |
1.22e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 502 RDLRERLETANKQLAekeyegsedtrktisQLFAKNKESQREKEKLEAELATArstnEDQRRhieirdQALSNAQ---AK 578
Cdd:COG1842 33 RDMEEDLVEARQALA---------------QVIANQKRLERQLEELEAEAEKW----EEKAR------LALEKGRedlAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 579 VVkleeeLKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE---RELESLRIQ------QRQGNSQPTNVSEYN 649
Cdd:COG1842 88 EA-----LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEelkAKKDTLKARakaakaQEKVNEALSGIDSDD 162
|
170 180
....*....|....*....|
gi 1542976327 650 AAALMEILrekEERILALEA 669
Cdd:COG1842 163 ATSALERM---EEKIEEMEA 179
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
503-637 |
1.27e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.37 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 503 DLRERLETANKQLAEKEYEgsedtrktISQLFAKNKESQREKEKLEAELATARSTNEDQrrhieirDQALSNAQA---KV 579
Cdd:pfam12718 18 ELEEKVKELEQENLEKEQE--------IKSLTHKNQQLEEEVEKLEEQLKEAKEKAEES-------EKLKTNNENltrKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1542976327 580 VKLEEELKKKQVYV-DKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLRIQQRQ 637
Cdd:pfam12718 83 QLLEEELEESDKRLkETTEKLRETDVKAEHLERKVQALEQE-RDEWEKKYEELEEKYKE 140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
502-673 |
1.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 502 RDLRERLETANKQLAEKEyegsedtrKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 581
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 582 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQPTNVSEyNA 650
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEA-ER 173
|
170 180
....*....|....*....|...
gi 1542976327 651 AALMEILREKEERILALEADMTK 673
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-613 |
1.31e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 426 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKreALEKAMRNKLEGEIRRMHDFNRDLR 505
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 506 --ERLETANKQLAEKEyegsEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 583
Cdd:COG4942 137 rlQYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
170 180 190
....*....|....*....|....*....|
gi 1542976327 584 EELKKKQVYVDKVEKMQQALVQLQAACEKR 613
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
434-638 |
1.50e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 434 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLV------------------KSSSKREALEKAMR-NKLEGEI 494
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspeeekelveKIKELEKELEKAKKaLEKNEKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 495 RRMHDFNRDLRERLETANKQLAEKeYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEirdqalsN 574
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKEL-AEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII-------E 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542976327 575 AQAKVVKLEEELKKKQVYVDKVEK-MQQALVQlqaacEKREQLEHRLRTRLERELESLRIQQRQG 638
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKReKEKEELE-----EKAEEIFEKLKKGEKLTTEELKLLQKSG 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-585 |
1.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 424 VSRAQQMVEILSDENRNLRQELEGCYEKVA-----RLQKVETEIQRVSEAYENLvksSSKREALEKAMRN---KLEGEIR 495
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 496 RMHDFNRDLRERLETANKQLAEkeyegsedTRKTISQLFAKNKESQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 570
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 1542976327 571 ALSNAQAKV--------VKLEEE 585
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
401-675 |
1.62e-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: 42.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 401 SAMPRAQQSSASYQPMPADPFAIVSRAQQMVEILSDEN-------RNLRQELEgcyEKVARLQK-VETEIQRVSEAYENL 472
Cdd:pfam15964 314 SALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKtkaliqcEQLKSELE---RQKERLEKeLASQQEKRAQEKEAL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 473 VKSSSK-REALEKAMRN------KLEGEIRRMHDFNRDLRERLETANKQLAEKEYegseDTRKTISQLFAKNKESQREKE 545
Cdd:pfam15964 391 RKEMKKeREELGATMLAlsqnvaQLEAQVEKVTREKNSLVSQLEEAQKQLASQEM----DVTKVCGEMRYQLNQTKMKKD 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 546 KLEAELATARSTNEdqrRHIEIRDQalsnaqaKVVKLEEELKKkqvYVDKVEKMQQALVQLQAACEKREQL----EHRLR 621
Cdd:pfam15964 467 EAEKEHREYRTKTG---RQLEIKDQ-------EIEKLGLELSE---SKQRLEQAQQDAARAREECLKLTELlgesEHQLH 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1542976327 622 -TRLEREleslRIQQRQGNsqptnvsEYNAAALMEILREKE--ERILALEADMTKWE 675
Cdd:pfam15964 534 lTRLEKE----SIQQSFSN-------EAKAQALQAQQREQEltQKMQQMEAQHDKTV 579
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
453-652 |
1.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 453 ARLQKVETEIQRVSEAYENLvksSSKREALEKAMrNKLEGEIRRMhdfNRDLRERLETANKQLAEkEYE----------- 521
Cdd:COG3883 37 AELDALQAELEELNEEYNEL---QAELEALQAEI-DKLQAEIAEA---EAEIEERREELGERARA-LYRsggsvsyldvl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 522 -GSEDTRKTISQLFAKNKESQREKEKLEaELATARSTNEDQRRHIEirdQALSNAQAKVVKLEEELKKKQvyvDKVEKMQ 600
Cdd:COG3883 109 lGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELE---AKLAELEALKAELEAAKAELE---AQQAEQE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1542976327 601 QALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAA 652
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
596-771 |
3.39e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 596 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTKWE 675
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 676 QKyleenvmrhfaldaAATVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 755
Cdd:COG1579 80 EQ--------------LGNVRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170
....*....|....*.
gi 1542976327 756 KVLQQRSRKEPSKTEQ 771
Cdd:COG1579 141 EEKKAELDEELAELEA 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
422-606 |
3.85e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 422 AIVSRAQQMVEILSDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKamrNKLEGEIRRMHDFN 501
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLS------EKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKEQDWNKELKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 502 RDLRERLETANKQLAEKEYEGSE------DTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-----IRD- 569
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQlneqisQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqINDl 396
|
170 180 190
....*....|....*....|....*....|....*...
gi 1542976327 570 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQL 606
Cdd:TIGR04523 397 eSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
450-778 |
4.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 450 EKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKT 529
Cdd:TIGR00618 167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ-LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 530 ISQLFAKNKESQREK---------EKLEAELATARSTNE--DQRRH-----------IEIRDQA---LSNAQAKVVKLEE 584
Cdd:TIGR00618 246 TQKREAQEEQLKKQQllkqlrariEELRAQEAVLEETQEriNRARKaaplaahikavTQIEQQAqriHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 585 ELKKKQVYVDK---VEKMQQALVQLQAACEKREQ---LEHRLRTRLERELESL-RIQQRQGNSQPTNVSEYNAAALMEIL 657
Cdd:TIGR00618 326 LLMKRAAHVKQqssIEEQRRLLQTLHSQEIHIRDaheVATSIREISCQQHTLTqHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 658 REKEERILALEAdmtkweqkylEENVMRHFALDAAATVAAQRDTTVI--SHSPNTSYDTALEARIQ-------KEEEEIL 728
Cdd:TIGR00618 406 QREQATIDTRTS----------AFRDLQGQLAHAKKQQELQQRYAELcaAAITCTAQCEKLEKIHLqesaqslKEREQQL 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1542976327 729 MANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPA 778
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
424-685 |
4.68e-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: 41.19 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 424 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 503
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKD 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 504 LRERL-ETANKQLAEKEYEgsedtrktISQLFAKNKESQREKEKLEAELATARSTNEDQR-RHIEIRDQ-ALSNAQAKVV 580
Cdd:TIGR00606 960 IENKIqDGKDDYLKQKETE--------LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiQERWLQDNlTLRKRENELK 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 581 KLEEELKK--KQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILR 658
Cdd:TIGR00606 1032 EVEEELKQhlKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
250 260
....*....|....*....|....*..
gi 1542976327 659 EKEERIlaleADMTKWeQKYLEENVMR 685
Cdd:TIGR00606 1112 TTELVN----KDLDIY-YKTLDQAIMK 1133
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
459-681 |
5.75e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 459 ETEIQRVSEAYENLVKSSSKREALEKAMRnklegEIRRMHDFNRDLRERLETANkqLAEKEYEGSEDTRKTISQLfaknk 538
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEEELEEERRRLSNA----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 539 esqrekEKLEAELATARST-NEDQRRHIEIRDQALSNAQaKVVKLEEELKkkqvyvDKVEKMQQALVQLQAACEkreQLE 617
Cdd:COG0497 222 ------EKLREALQEALEAlSGGEGGALDLLGQALRALE-RLAEYDPSLA------ELAERLESALIELEEAAS---ELR 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1542976327 618 HRLRtRLE---RELEslRIQQRQG---------NSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQKYLEE 681
Cdd:COG0497 286 RYLD-SLEfdpERLE--EVEERLAllrrlarkyGVTVEELLAYaeELRAELAELENSDERLEELEAELAEAEAELLEA 360
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
191-379 |
6.10e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 191 HPPVTSAPLSPPQPNDLYK-NPTSSSDFYKAQGPPPSQhslkgmehrgPPPEYPFKGMPPQSIVckpqEPGHYYSEHRLN 269
Cdd:pfam03154 178 SGAASPPSPPPPGTTQAATaGPTPSAPSVPPQGSPATS----------QPPNQTQSTAAPHTLI----QQTPTLHPQRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 270 QPgrtegqlmryqHPPEYGAARPTqdislPLSARNSQPHSPTSSLTSGGSLP-LLQSPPSTRLSP-AQHPLVPNQGDHSA 347
Cdd:pfam03154 244 SP-----------HPPLQPMTQPP-----PPSQVSPQPLPQPSLHGQMPPMPhSLQTGPSHMQHPvPPQPFPLTPQSSQS 307
|
170 180 190
....*....|....*....|....*....|..
gi 1542976327 348 HLPRPQQHFLPNQAHQGDHYRLPQPGLSQQQP 379
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQP 339
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
442-763 |
6.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 442 RQELEgcyekvARLQKVETEIQRVSEAYENLvkssskREALekAMRNKLEGEIRRMHDfnRDLRERLETANKQLAEkeye 521
Cdd:PRK04863 846 RVELE------RALADHESQEQQQRSQLEQA------KEGL--SALNRLLPRLNLLAD--ETLADRVEEIREQLDE---- 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 522 gSEDTRKTISQlfaknkeSQREKEKLEAELATARSTNED----QRRHIEIrDQALSNAQAKVVKLEEELKKKQVYvdkve 597
Cdd:PRK04863 906 -AEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQfeqlKQDYQQA-QQTQRDAKQQAFALTEVVQRRAHF----- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 598 KMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQRQGNSQptnVSEYNA--AALMEILREKEERILALEADMTKWE 675
Cdd:PRK04863 972 SYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQLRQAQAQ---LAQYNQvlASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 676 QKYLEENVMRhfaldaaatVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMI 755
Cdd:PRK04863 1048 VPADSGAEER---------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGW 1118
|
....*...
gi 1542976327 756 KVLQQRSR 763
Cdd:PRK04863 1119 CAVLRLVK 1126
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
428-589 |
7.66e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 428 QQMVEIlSDENRNLRQELEGCYEKVARLQKveteiqrvseayeNLVKSSSKREALE--KAMRNKLEGEIRRMHDFNRDLR 505
Cdd:pfam13851 47 KLMSEI-QQENKRLTEPLQKAQEEVEELRK-------------QLENYEKDKQSLKnlKARLKVLEKELKDLKWEHEVLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 506 ERLEtanKQLAEKE--YEGSEDTRKTISQ--------LFAKNKESQREKEKLEAELATARSTNedqrrhiEIRDQALSNA 575
Cdd:pfam13851 113 QRFE---KVERERDelYDKFEAAIQDVQQktglknllLEKKLQALGETLEKKEAQLNEVLAAA-------NLDPDALQAV 182
|
170
....*....|....
gi 1542976327 576 QakvVKLEEELKKK 589
Cdd:pfam13851 183 T---EKLEDVLESK 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-591 |
9.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 422 AIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSskREALEKAMRNKLEGEIRRMHDFN 501
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL--EELLEALDEEELEEELEELEEEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542976327 502 RDLRERLETANKQLAEKEYEgsedtrktISQLfaknkESQREKEKLEAELATARStnedQRRHIEIRDQALSNAQAKVVK 581
Cdd:COG4717 442 EELEEELEELREELAELEAE--------LEQL-----EEDGELAELLQELEELKA----ELRELAEEWAALKLALELLEE 504
|
170
....*....|
gi 1542976327 582 LEEELKKKQV 591
Cdd:COG4717 505 AREEYREERL 514
|
|
| |
