|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
599-806 |
8.21e-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: 329.04 E-value: 8.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 599 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADM 678
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 679 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 758
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1905532658 759 DAMIKVLQQRSRKEPSKTEQLScMRPAKSLMSISNAGSGLLSHSSTLT 806
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQQS-LRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-677 |
1.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 509
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 510 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 589
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 590 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEE 669
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 1905532658 670 RILALEAD 677
Cdd:COG1196 472 AALLEAAL 479
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
423-688 |
1.54e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 423 VPADPF--AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKA 492
Cdd:PRK03918 121 IPYHVFlnAIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 493 MRNKLEG---EIRRMHDFNRDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQR 569
Cdd:PRK03918 198 KEKELEEvlrEINEISSELPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 570 RHI-EIRDQA-----LSNAQAKVVKLEEELKKKQVYVDKVEK----MQQALVQLQAACEKREQLEHRLRtRLERELESLr 639
Cdd:PRK03918 273 KEIeELEEKVkelkeLKEKAEEYIKLSEFYEEYLDELREIEKrlsrLEEEINGIEERIKELEEKEERLE-ELKKKLKEL- 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1905532658 640 iqQRQGNCQPTNVSEYN-AAALMELLREKEERILALEADMTKWEQKYLEE 688
Cdd:PRK03918 351 --EKRLEELEERHELYEeAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
433-685 |
3.91e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKV----ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFN 508
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELedaeERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 509 RDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKV 586
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 587 VKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRT---RLERELESLRIQQRQGNCQPTNVSEY--NAAALM 661
Cdd:TIGR02169 437 NELEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAEAEAQARASEERvrGGRAVE 513
|
250 260
....*....|....*....|....
gi 1905532658 662 ELLREKEERILALEADMTKWEQKY 685
Cdd:TIGR02169 514 EVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-685 |
6.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLR 512
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 513 ERLETANKQL--AEKEYEGSEDTRKTI----SQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKV 586
Cdd:COG1196 337 EELEELEEELeeAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 587 VKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQgncqpTNVSEYNAAALMELLRE 666
Cdd:COG1196 417 ERLEEELEELE---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE-----AALLEAALAELLEELAE 488
|
250
....*....|....*....
gi 1905532658 667 KEERILALEADMTKWEQKY 685
Cdd:COG1196 489 AAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
433-684 |
1.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 504
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 505 HDFNRDLRERLETANKQL--AEKEYEGSEDTRKTISQLFAKNKESQREKEK----LEAELATARSTNE-------DQRRH 571
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELaeAEAEIEELEAQIEQLKEELKALREALDELRAeltlLNEEAANLRERLEslerriaATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 572 IEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEHRLRtRLERELESLRIQQRQgncqptn 651
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALA-LLRSELEELSEELRE------- 905
|
250 260 270
....*....|....*....|....*....|...
gi 1905532658 652 vSEYNAAALMELLREKEERILALEADMTKWEQK 684
Cdd:TIGR02168 906 -LESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
485-779 |
2.70e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 485 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 557
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 558 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 637
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 638 LRIQQRQgncqptnvSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 717
Cdd:COG1196 321 LEEELAE--------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1905532658 718 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 779
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
450-629 |
6.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 450 QELEGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRERLETANKQLAE--K 525
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 526 EYEGSEDTRKTISQLFAKNKESQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 604
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 1905532658 605 KMQQALVQLQAACEKREQLEHRLRT 629
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
425-780 |
6.12e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 425 ADPFAIVSraQQMV-EILS---DENRNLRQELEGcyekVARL--QKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLE 498
Cdd:TIGR02168 135 KRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYkeRRKETE-RKLERTRENLDRLEDILNELERQL-KSLE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 499 GEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrhieirDQA 578
Cdd:TIGR02168 207 RQAEKAERY-KELKAELRELELALLVLRLE---ELREELEELQEELKEAEEELEELTAELQEL--------------EEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 579 LSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPtNVSEYNAA 658
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 659 ALMELLREKEERILALEADMTKWEQKYLEenvmrhfaldaaatvaaqrdttvishspntsydtaLEARIQKEEEEILMAN 738
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEE-----------------------------------LESRLEELEEQLETLR 385
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1905532658 739 KRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 780
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
426-646 |
7.01e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 426 DPFAIVSRAQQMVEILSDENRnLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 501
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 502 RRmhdfnrdLRERLETANKQLAEKEyEGSEDTRKTISQLF-AKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALS 580
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1905532658 581 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 646
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
519-689 |
4.38e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 519 NKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 596
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 597 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQR---QGNCQPTNVSEYNAAALMELLREKEERILA 673
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeelQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 1905532658 674 LEADMTKWEQKYLEEN 689
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-694 |
8.69e-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: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 428 FAIVSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENLV-----KSSSKREALEKamRNKLEGEIR 502
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRER--LANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 503 RMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNA 582
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 583 QAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLR-TRLERELESLRIQQRQGNCQptnvseynAAALM 661
Cdd:TIGR02168 399 NNEIERLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEA--------LEELR 467
|
250 260 270
....*....|....*....|....*....|....
gi 1905532658 662 ELLREKEERILALEADMTKWEQK-YLEENVMRHF 694
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARlDSLERLQENL 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
460-684 |
2.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 460 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRERLETANKQLAEKEYEgsedtRKTISQ 539
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYL-----RAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 540 LFAknkesQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 619
Cdd:COG4913 284 WFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905532658 620 REqlehRLRTRLERELESLRIQqrqgncQPTNVSEY--NAAALMELLREKEERILALEADMTKWEQK 684
Cdd:COG4913 357 RE----RRRARLEALLAALGLP------LPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-687 |
3.10e-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: 54.68 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 447 NLRQELEGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQlAEKE 526
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELE-QLRKELEELSRQISALRKDLARLEAE-VEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 527 YEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 606
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 607 QQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNCQPTNVSEYNAAALMELLREKEERILA 673
Cdd:TIGR02168 826 LESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEELRE 905
|
250
....*....|....
gi 1905532658 674 LEADMTKWEQKYLE 687
Cdd:TIGR02168 906 LESKRSELRRELEE 919
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
450-638 |
8.43e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 450 QELEGCYEKVARLQKVETEIQRVSEAYENLvkssskREALEKA--MRNKLEGEIRRmhdfnrdLRERLETANKQLAEKEY 527
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKAfeELAETEKRLEE-------LRKELEELEKKYSEEEY 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 528 EGSEDtrktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHieiRDQALSNAQakvvKLEEELKKKQVYVDKVEKMQ 607
Cdd:PRK03918 662 EELRE-----------------EYLELSRELAGLRAELEELEKR---REEIKKTLE----KLKEELEEREKAKKELEKLE 717
|
170 180 190
....*....|....*....|....*....|.
gi 1905532658 608 QALVQLQAACEKREQLEHRLRTRLERELESL 638
Cdd:PRK03918 718 KALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-644 |
1.21e-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: 52.07 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 442 SDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQ 521
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 522 LAEKEYEGSEDTR---KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 598
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1905532658 599 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 644
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
439-684 |
1.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 439 EILSDENRNLRQELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRERL 515
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 516 ETANKQL--AEKEYEGSEDTR---KTISQLFAKNKESQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 576
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 577 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrlereLESLRIQQRQGncqptnvsey 655
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED-----LEELIAERRET---------- 531
|
250 260
....*....|....*....|....*....
gi 1905532658 656 nAAALMELLREKEERILALEADMTKWEQK 684
Cdd:PRK02224 532 -IEEKRERAEELRERAAELEAEAEEKREA 559
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-773 |
1.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 448 LRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKE 526
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 527 YEGSEDtRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 606
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 607 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQgncqptnvSEYNAAALMELLREKEERILALEADMTKWEQKY 685
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQ--------LELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 686 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 765
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 1905532658 766 QQRSRKEP 773
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
461-633 |
1.60e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 461 RLQKVETEIQRVSEayenlvksssKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTIsql 540
Cdd:COG1579 11 DLQELDSELDRLEH----------RLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEARI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 541 fAKNKE------SQREKEKLEAELATA---RSTNEDQRRHIEIR----DQALSNAQAKVVKLEEELKKKQVYVDK-VEKM 606
Cdd:COG1579 76 -KKYEEqlgnvrNNKEYEALQKEIESLkrrISDLEDEILELMERieelEEELAELEAELAELEAELEEKKAELDEeLAEL 154
|
170 180
....*....|....*....|....*...
gi 1905532658 607 QQALVQLQAACEK-REQLEHRLRTRLER 633
Cdd:COG1579 155 EAELEELEAEREElAAKIPPELLALYER 182
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
435-789 |
2.65e-06 |
|
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: 51.75 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 435 QQMVEILSDENRNLRQELEGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 503
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 504 MHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKE-------------KLEAELATARSTNEDQRR 570
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 571 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPT 650
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 651 NVSEYNAAALMELLREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 729
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905532658 730 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQ-QRSRKEPSKTEQLSCMRPAKSLM 789
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLElSSSKKKKTQEEVMALKREKDRLV 753
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
434-675 |
3.24e-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: 51.11 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 434 AQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE------IRRMHDF 507
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksSEELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 508 N---RDLRERLETANKQLAEKEYEGSEDTRKTIsqlfaknKESQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 584
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 585 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQ-QRQGNCQPTNVSEYNAAALMEL 663
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|..
gi 1905532658 664 LREKEERILALE 675
Cdd:COG5185 531 RARGYAHILALE 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
441-677 |
3.89e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 441 LSDENRNLRQELEGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 506
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 507 FNRDLRERLETANK-QLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 585
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 586 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNCQPTNVSEYnaaa 659
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 1905532658 660 lmelLREKEERILALEAD 677
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
430-633 |
6.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 430 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKR---EALEKAMRNkLEGEIRRMHD 506
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAE-LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 507 FNRDLR---ERLETANKQLaekeyegsEDTRKTISQLfaknkesQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQ 583
Cdd:COG4913 683 SSDDLAaleEQLEELEAEL--------EELEEELDEL-------KGEIGRLEKELEQA----EEELDELQDRLEAAEDLA 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1905532658 584 AKVVKLEEELKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 633
Cdd:COG4913 744 RLELRALLEERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
443-772 |
1.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 443 DENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 509
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 510 DLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 588
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 589 LEE-----------------ELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHR---LRTRLERELESLRIQQRQGNCQ 648
Cdd:COG4717 247 EARlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGkeaEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 649 ----PTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENV---------------------MRHFALDAAATVA 703
Cdd:COG4717 327 alglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedeeelraaleqAEEYQELKEELEE 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905532658 704 AQRD----TTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQI--IEKDAMI-KVLQQRSRKE 772
Cdd:COG4717 407 LEEQleelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELaELLQELEELK 482
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
485-825 |
1.06e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 485 KREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKT------ISQLFAKNKESQREKEKLEAEL 558
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 559 ATARSTNEDQRRHIEIRDQALSNA--QAKVVKLEEE----------------LKKKQVYVDKVEKMQQALVQLQAAcEKR 620
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENkeEEKEKKLQEEelkllakeeeelkselLKLERRKVDDEEKLKESEKEKKKA-EKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 621 EQLEHRLRTRLERELESLRIQQrqgncQPTNVSEYNAAALMELLREKEERILALEADmtkwEQKYLEENVMRHFALDAAA 700
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKR-----EAEEEEEEELEKLQEKLEQLEEELLAKKKL----ESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 701 TVAAQRDTTVISHSPNtsYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAM----IKVLQQRSRKEPSK- 775
Cdd:pfam02463 401 SEEEKEAQLLLELARQ--LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKllkdELELKKSEDLLKETq 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1905532658 776 ----TEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLG 825
Cdd:pfam02463 479 lvklQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
434-638 |
1.84e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 434 AQQMVEILSDENRNLRQElegcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 512
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 513 ERLETANKQLAEKEYE------GSEDTRKTISQLFAKNKESQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 579
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905532658 580 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 638
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
456-646 |
2.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 456 YEKVARL-QKVETEIQRvSEAY----ENLVKSSSKREALEK--AMRNKLeGEIRRMHDFNRDLRERLETANKQLaEKEYE 528
Cdd:PRK04863 475 FEQAYQLvRKIAGEVSR-SEAWdvarELLRRLREQRHLAEQlqQLRMRL-SELEQRLRQQQRAERLLAEFCKRL-GKNLD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 529 GSEDtrktISQLFAknkESQREKEKLEAELATARSTNEDQRRHIE----------IRDQALSNAQAKVVKLEE----ELK 594
Cdd:PRK04863 552 DEDE----LEQLQE---ELEARLESLSESVSEARERRMALRQQLEqlqariqrlaARAPAWLAAQDALARLREqsgeEFE 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1905532658 595 KKQvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLriQQRQGN 646
Cdd:PRK04863 625 DSQ---DVTEYMQQLLERERELTVERDELAAR-KQALDEEIERL--SQPGGS 670
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-682 |
2.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 448 LRQELEGCYEKVAR---LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFN------RDLRERLETA 518
Cdd:PRK03918 271 LKKEIEELEEKVKElkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 519 NKQLAE-----KEYEGSEDTRKTISQLfaKNKESQREKEKLEAEL---ATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 590
Cdd:PRK03918 351 EKRLEEleerhELYEEAKAKKEELERL--KKRLTGLTPEKLEKELeelEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 591 EELKKKQVYV----------DKVEKMQQALVQLQAACEKREQLEHRLRtRLERELESLRIQQrqgNCQPTNVSEYNAAAL 660
Cdd:PRK03918 429 EELKKAKGKCpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKER-KLRKELRELEKVL---KKESELIKLKELAEQ 504
|
250 260
....*....|....*....|....
gi 1905532658 661 MELLREKEERILA--LEADMTKWE 682
Cdd:PRK03918 505 LKELEEKLKKYNLeeLEKKAEEYE 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
462-680 |
2.24e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 462 LQKVETEIQRVSEAYENlVKS--SSKREALEKamrnkLEGEIRRMHDfnRDLRERLETANKQLAE-----KEYEGSED-- 532
Cdd:PRK02224 161 LGKLEEYRERASDARLG-VERvlSDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 533 --TRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQAL 610
Cdd:PRK02224 233 reTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDD 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 611 VQLQAACEKREQLEHRlRTRLERELESLRIQQRQGNCQPTNVSEyNAAALMELLREKEERILALEADMTK 680
Cdd:PRK02224 307 ADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
433-639 |
3.68e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKVarlqkveteIQRVSEAYENLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDLR 512
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEF---------IQKGDEVKCKLDKSEENARSIEYEVLKK-EKQMKILENKCNNLK 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 513 ERLETANKQLAEKEYEGSEDTRKTIsqlfAKNKE---SQREKEKLEAELATARSTNED--QRRHIEIRDQALSNAqakvv 587
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGS----AENKQlnaYEIKVNKLELELASAKQKFEEiiDNYQKEIEDKKISEE----- 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 588 KLEEELKKKQVYVDKVEKMQQ--------ALVQLQAACEK---------------------REQLEHRLRTRLERELESL 638
Cdd:pfam05483 672 KLLEEVEKAKAIADEAVKLQKeidkrcqhKIAEMVALMEKhkhqydkiieerdselglyknKEQEQSSAKAALEIELSNI 751
|
.
gi 1905532658 639 R 639
Cdd:pfam05483 752 K 752
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
466-573 |
5.74e-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: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 466 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNK 545
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE-LSEARSEERREIRKDR 465
|
90 100 110
....*....|....*....|....*....|.
gi 1905532658 546 E---SQREKEKLEAELATARSTNEDQRRHIE 573
Cdd:COG2433 466 EisrLDREIERLERELEEERERIEELKRKLE 496
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
429-683 |
8.99e-05 |
|
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: 46.76 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 429 AIVSRAQQMVEILSDENRNLRQE-LEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRRMHD 506
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 507 FNRDLRERLETANKQLAEKE--YEGSEDTRKtiSQLFAKNKESQREKEKLEAELATARSTnedqrrhieirdqaLSNAQA 584
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEddLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLR--------------LNQATA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 585 KvvklEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELE-----SLRIQQRQGNCQptnvseynaaA 659
Cdd:pfam12128 459 T----PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEalrqaSRRLEERQSALD----------E 524
|
250 260
....*....|....*....|....*
gi 1905532658 660 LMELLREKEERILA-LEADMTKWEQ 683
Cdd:pfam12128 525 LELQLFPQAGTLLHfLRKEAPDWEQ 549
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
531-772 |
1.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 531 EDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 606
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 607 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQ 683
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 684 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 763
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
....*....
gi 1905532658 764 VLQQRSRKE 772
Cdd:COG4372 281 AALELEALE 289
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
435-613 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 435 QQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 511
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 512 RERLETANKQLAEKEYEGSEDTR-KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 590
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
170 180
....*....|....*....|...
gi 1905532658 591 EELKKKQVYVDKVEKMQQALVQL 613
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQE 646
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
441-688 |
1.75e-04 |
|
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: 45.45 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 441 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRER 514
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 515 LETANKQLAEKEYEGSEDTRKTISQLF------AKNKESQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 580
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 581 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 640
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1905532658 641 QQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKwEQKYLEE 688
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
191-328 |
1.83e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.85 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 191 HPPVTSAPLSPPQPNDlyKNPTSSSEFYKAQGPLPNQHSLKGMEHRGPPP---EYPFKGMPPQSVVCKPQEPghFYSEHR 267
Cdd:PRK10263 741 HEPLFTPIVEPVQQPQ--QPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQpqyQQPQQPVAPQPQYQQPQQP--VAPQPQ 816
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1905532658 268 LNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARN--SQP-HSPTSSLTSggsLPLLQSPPS 328
Cdd:PRK10263 817 YQQPQQPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNgdSRPlHKPTTPLPS---LDLLTPPPS 877
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
457-779 |
2.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 457 EKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEkEYEGSEDTRKt 536
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKK- 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 537 iSQLFAKNKESQREKEKLEAElaTARSTNEDQR---RHIEIRDQALSNAQAKVVKL-EEELKKKQVYVDKVEKMQQALVQ 612
Cdd:PTZ00121 1548 -ADELKKAEELKKAEEKKKAE--EAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 613 LQAACEKREQLEHRLRTRLE--RELESLRIQQRQGNC---QPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLE 687
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEekKKAEELKKAEEENKIkaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 688 ENVMRHFALDAAATVAAQRDTTVishspntsYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHaqiIEKDAMIKVLQQ 767
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEE--------NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH---LKKEEEKKAEEI 1773
|
330
....*....|..
gi 1905532658 768 RSRKEPSKTEQL 779
Cdd:PTZ00121 1774 RKEKEAVIEEEL 1785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
433-693 |
2.11e-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: 45.42 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 503
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 504 MHDFNR-------DLRERLETANKQLAEKEYEGSEDTRkTISQLFAKNKESQREKEKLEAELATARSTNEDqrrhIEIRD 576
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 577 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL---------ESLRIQQR 643
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdEQIRKIKS 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1905532658 644 QGNCQPTNVSEY--NAAALMELLREKEERILALEADMTKWEQKYLEENVMRH 693
Cdd:TIGR00606 557 RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
460-670 |
2.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 460 ARLQKVETEIQRVSEAYENLVKSSSKreaLEKAMRNklEGEIRRMH---DFNRDLRERLETANKQLAEKEYEGSEDTR-- 534
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKKYNLEELEKKAEEYEKLKek 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 535 ---------------KTISQLFAKNKESQREKEKLEAELA-------------------TARSTNEDQRRHIEIRD--QA 578
Cdd:PRK03918 534 liklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAellkeleelgfesveeleeRLKELEPFYNEYLELKDaeKE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 579 LSNAQAKVVKLEEELKKKQVYVDKVEK-MQQALVQLQAACEKREQLEHR----LRTRLERELESLRIQQRQGNcqptNVS 653
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKrLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELE----KRR 689
|
250
....*....|....*..
gi 1905532658 654 EYNAAALMELLREKEER 670
Cdd:PRK03918 690 EEIKKTLEKLKEELEER 706
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
438-688 |
2.41e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 438 VEILSDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLET 517
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 518 --ANKQLAEKEYEGsedTRKTISQLFAKNKESQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 581
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 582 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgncqptn 651
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1905532658 652 vseynAAALMELLREKEER-----------ILALEADM--TKWE-QKYLEE 688
Cdd:pfam00038 240 -----KASLERQLAETEERyelqladyqelISELEAELqeTRQEmARQLRE 285
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
436-783 |
2.55e-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: 45.44 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 436 QMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRER 514
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 515 LEtankqlaekEYEGSEDTRktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 594
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 595 KKQVYVDKVEKMQQALVQLQAA--CEKREQLEHRLRTrLERELESLRIQQRQGncqptnVSEYNaaALMELLREKEERIL 672
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIAE-KERELEDAEERLAKL------EAEID--KLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 673 ALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR 747
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELA 423
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1905532658 748 -----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMR 783
Cdd:TIGR02169 424 dlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
457-638 |
3.01e-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: 43.50 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 457 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrerletANKQLAEKEYEGSEDTRKT 536
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 537 ISQLFAK-NKESQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 598
Cdd:cd07596 66 LSKLGKAaEELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1905532658 599 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 638
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
470-685 |
3.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 470 QRVSEAY--ENLvksSSKREALEKAmRNKLEGEIRRmhdfnrdLRERLETANKQLAE-KEYEGSEDTRKTISQLFAKNKE 546
Cdd:COG3206 155 NALAEAYleQNL---ELRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 547 SQREKEKLEAELATARSTNEDQRRHIE---------IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQLQAA 616
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGsgpdalpelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905532658 617 CEKREQLEHRLRTRLERELESLRIQQRQGNcqpTNVSEYNAAALMelLREKEERILALEADMTKWEQKY 685
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQ---AQLAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
422-659 |
3.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 422 PVPADPFAIVSRAQQmveilsDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLvksSSKREALEKAMrNKLEGEI 501
Cdd:COG3883 11 PAFADPQIQAKQKEL------SELQAELEAAQ------AELDALQAELEELNEEYNEL---QAELEALQAEI-DKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 502 RRMhdfNRDLRERLETANKQLAEkEYE------------GSEDTRKTISQLFAKNKESQREKEKLEaELATARSTNEDQR 569
Cdd:COG3883 75 AEA---EAEIEERREELGERARA-LYRsggsvsyldvllGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 570 rhieirdQALSNAQAKVVKLEEELKKKQVYVD-KVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQ 648
Cdd:COG3883 150 -------AELEAKLAELEALKAELEAAKAELEaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250
....*....|.
gi 1905532658 649 PTNVSEYNAAA 659
Cdd:COG3883 223 AAAAAAAAAAA 233
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
460-633 |
4.11e-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: 43.09 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 460 ARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEI----RRMHDFNRDLR---ERLETANKQL--AEKEYEGS 530
Cdd:pfam00261 1 KKMQQIKEELD---EAEERLKEAMKKLEEAEKR-AEKAEAEVaalnRRIQLLEEELErteERLAEALEKLeeAEKAADES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 531 EDTRKTISQLFAKNKESQREkekLEAELATARSTNEDQRRHIE-------IRDQALSNA-------QAKVVKLEEELKkk 596
Cdd:pfam00261 77 ERGRKVLENRALKDEEKMEI---LEAQLKEAKEIAEEADRKYEevarklvVVEGDLERAeeraelaESKIVELEEELK-- 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1905532658 597 qvyvDKVEKMQQALVQLQAACEKREQLEHRLRTRLER 633
Cdd:pfam00261 152 ----VVGNNLKSLEASEEKASEREDKYEEQIRFLTEK 184
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
532-688 |
4.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 532 DTRktISQLFAKNKESQREKEKLEAELATARSTnedqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALV 611
Cdd:COG1579 16 DSE--LDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1905532658 612 QLQAAcekREQlehrlrTRLERELESLRIQQRQgncqptnvSEYNAAALMELLREKEERILALEADMTKWEQKYLEE 688
Cdd:COG1579 84 NVRNN---KEY------EALQKEIESLKRRISD--------LEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
431-594 |
4.66e-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: 44.28 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 431 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 510
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 511 LRERLETANKQLAEkeyegSEDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVKLE 590
Cdd:TIGR02168 913 LRRELEELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKRLE 978
|
....
gi 1905532658 591 EELK 594
Cdd:TIGR02168 979 NKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
433-621 |
5.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 433 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQ-RVSEAYENLVKSSSKR-EALEKAMRNkLEGEIRRMhdfnRD 510
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReELDELEAQIRGNGGDRlEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 511 LRERLETANKQLAEKEYEGSEDtrktisqlFAKN-KESQREKEKLEAELATARstnEDQRRHieirDQALSNAQAKVVKL 589
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FAALrAEAAALLEALEEELEALE---EALAEA----EAALRDLRRELREL 424
|
170 180 190
....*....|....*....|....*....|....*
gi 1905532658 590 EEE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 621
Cdd:COG4913 425 EAEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
464-684 |
5.74e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 464 KVETEIQRVSEAYENLvkSSSKREALEKAMRNKLEGEIR------RMHDFNRD----LRERLETANKQLAEKEYE----- 528
Cdd:COG2268 98 KVNSDPEDIANAAERF--LGRDPEEIEELAEEKLEGALRavaaqmTVEELNEDrekfAEKVQEVAGTDLAKNGLElesva 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 529 --GSEDT--------RKTISQLFAKNKESQREKEKlEAELATARSTNE------DQRRHIEIRDQALSNAQAKVVKLEEE 592
Cdd:COG2268 176 itDLEDEnnyldalgRRKIAEIIRDARIAEAEAER-ETEIAIAQANREaeeaelEQEREIETARIAEAEAELAKKKAEER 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 593 LKkkqvyVDKVEKMQQALVQLQAAcEKREQLEHRLR-TRLERELEslrIQQrqgncqptnvseynAAALMELLREKEERI 671
Cdd:COG2268 255 RE-----AETARAEAEAAYEIAEA-NAEREVQRQLEiAEREREIE---LQE--------------KEAEREEAELEADVR 311
|
250
....*....|...
gi 1905532658 672 LALEADMTKWEQK 684
Cdd:COG2268 312 KPAEAEKQAAEAE 324
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
509-680 |
6.94e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 509 RDLRERLETANKQLAEKEyegsedtrKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 588
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 589 LEEELKK-KQVYVDKVEKMQQ---------------------ALVQLQAACEKREQLEHRLRTRLErELESLRIQQRQgn 646
Cdd:COG4942 95 LRAELEAqKEELAELLRALYRlgrqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLA-ELAALRAELEA-- 171
|
170 180 190
....*....|....*....|....*....|....
gi 1905532658 647 cqptnvseyNAAALMELLREKEERILALEADMTK 680
Cdd:COG4942 172 ---------ERAELEALLAELEEERAALEALKAE 196
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
485-637 |
8.84e-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: 43.63 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 485 KREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAE-----KEYEGS-EDTRKTISQLFAKNKESQREKEKLEAEL 558
Cdd:pfam01576 763 KQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKlqaqmKDLQRElEEARASRDEILAQSKESEKKLKNLEAEL 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 559 ATAR---STNEDQRRHI---------EIRDQALSNA---------QAKVVKLEEELKKKQVYV----DKVEKMQQALVQL 613
Cdd:pfam01576 843 LQLQedlAASERARRQAqqerdeladEIASGASGKSalqdekrrlEARIAQLEEELEEEQSNTellnDRLRKSTLQVEQL 922
|
170 180 190
....*....|....*....|....*....|....*...
gi 1905532658 614 QA-------ACEK----REQLEHR---LRTRLErELES 637
Cdd:pfam01576 923 TTelaaersTSQKsesaRQQLERQnkeLKAKLQ-EMEG 959
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
447-680 |
9.44e-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: 43.57 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 447 NLRQELEGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRERLeTANKQL 522
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEEL-TAKKMT 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 523 AEkeyegseDTRKTISQLFAKNKESQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 596
Cdd:pfam15921 491 LE-------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 597 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNCQptnvseynaaalmelLREKEERI 671
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 1905532658 672 LALEADMTK 680
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
432-688 |
1.40e-03 |
|
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: 42.89 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 432 SRAQQMVEILSDEnrnlrQELEG-CYEKVARLQKVETEIQRVSEayenLVKSSSKREALEKAMRNKlEGEIRRMHDFNRD 510
Cdd:pfam10174 182 ERTRRIAEAEMQL-----GHLEVlLDQKEKENIHLREELHRRNQ----LQPDPAKTKALQTVIEMK-DTKISSLERNIRD 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 511 LRERLETANKQLAEkeyeGSEDTRKTISQL--------FAKNKESQREKE---------KLEAELATARSTNEDQRRHIE 573
Cdd:pfam10174 252 LEDEVQMLKTNGLL----HTEDREEEIKQMevykshskFMKNKIDQLKQElskkesellALQTKLETLTNQNSDCKQHIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 574 I-------RDQALSNAQAKVVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEHRLR-------------TRLER 633
Cdd:pfam10174 328 VlkesltaKEQRAAILQTEVDALRLRLEEKESFLNKKTK------QLQDLTEEKSTLAGEIRdlkdmldvkerkiNVLQK 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905532658 634 ELESLRIQQRQGNCQPTNVSEYNA-------------AALMELLREKEERILALEADMTKWEQKYLEE 688
Cdd:pfam10174 402 KIENLQEQLRDKDKQLAGLKERVKslqtdssntdtalTTLEEALSEKERIIERLKEQREREDRERLEE 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
547-776 |
1.49e-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: 42.06 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 547 SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQAL-VQLQAACEKREQLEH 625
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 626 RLRTRLERELESLRIQQRQGNCQPTNV---------SEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFAL 696
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 697 DAAATVAAQRdttvishspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKT 776
Cdd:COG4942 178 ALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
466-688 |
1.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 466 ETEIQRVSEAYENLVKSSSKREALEKAMRnklegEIRRMHDFNRDLRERLETANkqLAEKEYEGSEDTRKTISQLfaknk 545
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEEELEEERRRLSNA----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 546 esqrekEKLEAELATARST-NEDQRRHIEIRDQALSNAQaKVVKLEEELKkkqvyvDKVEKMQQALVQLQAACEkreQLE 624
Cdd:COG0497 222 ------EKLREALQEALEAlSGGEGGALDLLGQALRALE-RLAEYDPSLA------ELAERLESALIELEEAAS---ELR 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905532658 625 HRLRtRLE---RELEslRIQQRQG---------NCQPTNVSEYNAAALMEL--LREKEERILALEADMTKWEQKYLEE 688
Cdd:COG0497 286 RYLD-SLEfdpERLE--EVEERLAllrrlarkyGVTVEELLAYAEELRAELaeLENSDERLEELEAELAEAEAELLEA 360
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
431-715 |
1.76e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 431 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 489
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 490 EKAMRNKLEGEIRRMHDF----------NRDLRERLETANKQ-LAEKEYEGSEDTRKTISQLFAKNKESQREKEkleael 558
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 559 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 627
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 628 RTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 707
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 1905532658 708 TTVISHSP 715
Cdd:pfam17380 595 TPITTIKP 602
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
431-760 |
1.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 431 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQkveteiQRVSEAYENLVKSSSKREALEKamrnklegEIRRMHDFNRD 510
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLE------EELEELNEQLQAAQAELAQAQE--------ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 511 LRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARstNEDQRRHIEIRDQALSNAQAKVVKLE 590
Cdd:COG4372 113 LQEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEEQLESLQ--EELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 591 EELKKKQVYVDKVEKMQQALVQLQAacEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEER 670
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPR--ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 671 ILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKT 750
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|
gi 1905532658 751 LHAQIIEKDA 760
Cdd:COG4372 348 VGLLDNDVLE 357
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
510-644 |
1.93e-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: 39.60 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 510 DLRERLETANKQLAEKEYEgsedtrktISQLFAKNKESQREKEKLEAELATARSTNEDQrrhieirDQALSNAQA---KV 586
Cdd:pfam12718 18 ELEEKVKELEQENLEKEQE--------IKSLTHKNQQLEEEVEKLEEQLKEAKEKAEES-------EKLKTNNENltrKI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1905532658 587 VKLEEELKKKQVYV-DKVEKMQQALVQLQAACEKREQLEHRlRTRLERELESLRIQQRQ 644
Cdd:pfam12718 83 QLLEEELEESDKRLkETTEKLRETDVKAEHLERKVQALEQE-RDEWEKKYEELEEKYKE 140
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
431-592 |
2.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 431 VSRAQQMVEILSDENRNLRQELEGCYEKVA-----RLQKVETEIQRVSEAYENLvksSSKREALEKAMRN---KLEGEIR 502
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRgnggdRLEQLEREIERLERELEER---ERRRARLEALLAAlglPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 503 RMHDFNRDLRERLETANKQLAEkeyegsedTRKTISQLFAKNKESQREKEKLEAELA--TARSTNEDQRRHiEIRD---Q 577
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIAslERRKSNIPARLL-ALRDalaE 451
|
170 180
....*....|....*....|...
gi 1905532658 578 ALSNAQAKV--------VKLEEE 592
Cdd:COG4913 452 ALGLDEAELpfvgelieVRPEEE 474
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
441-645 |
2.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 441 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLV------------------KSSSKREALEKAMR-NKLEGEI 501
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspeeekelveKIKELEKELEKAKKaLEKNEKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 502 RRMHDFNRDLRERLETANKQLAEKeYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEirdqalsN 581
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKEL-AEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII-------E 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905532658 582 AQAKVVKLEEELKKKQVYVDKVEK-MQQALVQlqaacEKREQLEHRLRTRLERELESLRIQQRQG 645
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKReKEKEELE-----EKAEEIFEKLKKGEKLTTEELKLLQKSG 294
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
429-613 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 429 AIVSRAQQMVEILSDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKamrNKLEGEIRRMHDFN 508
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLS------EKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKEQDWNKELKSEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 509 RDLRERLETANKQLAEKEYEGSE------DTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-----IRD- 576
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQlneqisQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqINDl 396
|
170 180 190
....*....|....*....|....*....|....*...
gi 1905532658 577 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQL 613
Cdd:TIGR04523 397 eSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
603-778 |
6.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 603 VEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQQRQGNcqpTNVSEYNAA--ALMELLREKEERILALEADMTK 680
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKE-LPAELAELEDELAALE---ARLEAAKTEleDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 681 WEQKYLEenvmrhfaldaaatVAAQRDTTVISHSpntsyDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDA 760
Cdd:COG1579 78 YEEQLGN--------------VRNNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170
....*....|....*...
gi 1905532658 761 MIKVLQQRSRKEPSKTEQ 778
Cdd:COG1579 139 ELEEKKAELDEELAELEA 156
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
448-682 |
9.01e-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: 39.89 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 448 LRQELEgcyEKVARLQK-VETEIQRVSEAYENLVKSSSK-REALEKAMRN------KLEGEIRRMHDFNRDLRERLETAN 519
Cdd:pfam15964 361 LKSELE---RQKERLEKeLASQQEKRAQEKEALRKEMKKeREELGATMLAlsqnvaQLEAQVEKVTREKNSLVSQLEEAQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 520 KQLAEKEYegseDTRKTISQLFAKNKESQREKEKLEAELATARSTNEdqrRHIEIRDQalsnaqaKVVKLEEELKKkqvY 599
Cdd:pfam15964 438 KQLASQEM----DVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTG---RQLEIKDQ-------EIEKLGLELSE---S 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 600 VDKVEKMQQALVQLQAACEKREQL----EHRLR-TRLEREleslRIQQRQGNcqptnvsEYNAAALMELLREKE--ERIL 672
Cdd:pfam15964 501 KQRLEQAQQDAARAREECLKLTELlgesEHQLHlTRLEKE----SIQQSFSN-------EAKAQALQAQQREQEltQKMQ 569
|
250
....*....|
gi 1905532658 673 ALEADMTKWE 682
Cdd:pfam15964 570 QMEAQHDKTV 579
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
509-676 |
9.20e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 509 RDLRERLETANKQLAekeyegsedtrktisQLFAKNKESQREKEKLEAELATArstnEDQRRhieirdQALSNAQ---AK 585
Cdd:COG1842 33 RDMEEDLVEARQALA---------------QVIANQKRLERQLEELEAEAEKW----EEKAR------LALEKGRedlAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 586 VVkleeeLKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNCQ---PTNVSEYNAAA 659
Cdd:COG1842 88 EA-----LERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEelkAKKDTLKARAKAAKAQekvNEALSGIDSDD 162
|
170
....*....|....*..
gi 1905532658 660 LMELLREKEERILALEA 676
Cdd:COG1842 163 ATSALERMEEKIEEMEA 179
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
446-687 |
9.67e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.85 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 446 RNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKL---EGEIRRMHDFNRDLRERLETANKQL 522
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAEEEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 523 AEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQalsNAQAKVVKLEEELKKKQVYVDK 602
Cdd:pfam02029 157 EEEE-DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ---NGEEEVTKLKVTTKRRQGGLSQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905532658 603 VEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGncqptnvseynAAALMELLREKEERILALEADMTKWE 682
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEA-----------ELELEELKKKREERRKLLEEEEQRRK 301
|
....*
gi 1905532658 683 QKYLE 687
Cdd:pfam02029 302 QEEAE 306
|
|
| |
