|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
555-761 |
2.25e-112 |
|
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: 342.52 E-value: 2.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 555 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADM 634
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 635 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 714
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 666335625 715 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 761
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-644 |
4.74e-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: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 386 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 465
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 466 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 545
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 546 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEE 625
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 666335625 626 RILALEADMTKWEQKYLEE 644
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-725 |
1.94e-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: 61.61 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 380 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 454
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 455 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeghyasqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 534
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 535 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHgNGQPANMPEYNAP 614
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-LESKLDELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 615 ALLELVREKEERILALEADMTKWEQKYLE-ESTIR----HFAMNAAATAAAERDTTIINH--SRNGSYGEsSLEAHIWQE 687
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEElESRLEeleeQLETLRSKVAQLELQIASLNNeiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 666335625 688 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 725
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-715 |
9.26e-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: 56.22 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 427 QRISEAYESLVKSTTKRESLDKAmRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQN------ 500
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 501 -KEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKREQM 579
Cdd:TIGR02168 756 lTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLR---ERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 580 ERRLRTWlERELDALRTQQKHGNGQPANmpeyNAPALLELVREKEErilaLEADMTKWEQKYLEESTIRHfamnAAATAA 659
Cdd:TIGR02168 830 ERRIAAT-ERRLEDLEEQIEELSEDIES----LAAEIEELEELIEE----LESELEALLNERASLEEALA----LLRSEL 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 666335625 660 AERDTTIINHSRNGSYGESSLEAhiwqEEEEVVQANRRCQDMEYTIKNLHAKIIEK 715
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-575 |
1.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 407 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 486
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 487 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 566
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 666335625 567 TQLQSACEK 575
Cdd:PRK03918 721 ERVEELREK 729
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-598 |
2.31e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 414 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 489
Cdd:pfam01576 145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 490 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 569
Cdd:pfam01576 224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298
|
170 180
....*....|....*....|....*....
gi 666335625 570 qsacekrEQMErRLRTWLERELDALRTQQ 598
Cdd:pfam01576 299 -------EELE-ALKTELEDTLDTTAAQQ 319
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
533-594 |
1.70e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.78 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 666335625 533 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 594
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
417-589 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 417 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 496
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 497 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 566
Cdd:cd07596 82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158
|
170 180
....*....|....*....|...
gi 666335625 567 TQLQSACEKREQMERRLRTWLER 589
Cdd:cd07596 159 SALEEARKRYEEISERLKEELKR 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
555-761 |
2.25e-112 |
|
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: 342.52 E-value: 2.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 555 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADM 634
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 635 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 714
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 666335625 715 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 761
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-644 |
4.74e-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: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 386 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 465
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 466 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 545
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 546 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEE 625
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 666335625 626 RILALEADMTKWEQKYLEE 644
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-725 |
1.94e-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: 61.61 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 380 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 454
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 455 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeghyasqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 534
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 535 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHgNGQPANMPEYNAP 614
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-LESKLDELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 615 ALLELVREKEERILALEADMTKWEQKYLE-ESTIR----HFAMNAAATAAAERDTTIINH--SRNGSYGEsSLEAHIWQE 687
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEElESRLEeleeQLETLRSKVAQLELQIASLNNeiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 666335625 688 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 725
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-644 |
1.95e-09 |
|
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: 61.62 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 383 DAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 461
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 462 HDFNRDLRDRLETANRQLSSREYEGHedkaaeghYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 540
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 541 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTWLE---RELDALRTQQKHGNGQPANMPEYna 613
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEEELSL-- 953
|
250 260 270
....*....|....*....|....*....|.
gi 666335625 614 PALLELVREKEERILALEADMTKWEQKYLEE 644
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
386-632 |
4.21e-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: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 386 AIVERAQQMVEILTEENRVLHQELQGYYDN-----------ADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKL 454
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQleeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 455 EGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYA--SQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILD 532
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 533 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTwlerELDALRTQQKHGNGQPANMpeyn 612
Cdd:TIGR02168 454 EELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL---- 522
|
250 260
....*....|....*....|
gi 666335625 613 aPALLELVREKEERILALEA 632
Cdd:TIGR02168 523 -GVLSELISVDEGYEAAIEA 541
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
389-645 |
8.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 389 ERAQQmveiLTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 468
Cdd:COG1196 213 ERYRE----LKEELKELEAELLLL-----KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 469 RDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 548
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 549 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanmpeynapALLELVREKEERIL 628
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424
|
250
....*....|....*..
gi 666335625 629 ALEADMTKWEQKYLEES 645
Cdd:COG1196 425 ELEEALAELEEEEEEEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-598 |
1.58e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 414 DNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETAnrqlssREYEGHEDKAAE 493
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 494 ghyASQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 573
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 666335625 574 EKR------EQMERRLRTWLERELDALRTQQ 598
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
383-622 |
2.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 383 DAFAIVERAQQMVEilteenrvlH-QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDkAMRNKL-----EG 456
Cdd:COG4913 219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 457 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDK--AAEGHYASQNkefLKEKEKLEMELAAVRTASEDHRRHIEILD 532
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELErlEARLDALREEldELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 533 QALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYN 612
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250
....*....|
gi 666335625 613 APALLELVRE 622
Cdd:COG4913 443 LALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-715 |
9.26e-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: 56.22 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 427 QRISEAYESLVKSTTKRESLDKAmRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQN------ 500
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA-LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 501 -KEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKREQM 579
Cdd:TIGR02168 756 lTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLR---ERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 580 ERRLRTWlERELDALRTQQKHGNGQPANmpeyNAPALLELVREKEErilaLEADMTKWEQKYLEESTIRHfamnAAATAA 659
Cdd:TIGR02168 830 ERRIAAT-ERRLEDLEEQIEELSEDIES----LAAEIEELEELIEE----LESELEALLNERASLEEALA----LLRSEL 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 666335625 660 AERDTTIINHSRNGSYGESSLEAhiwqEEEEVVQANRRCQDMEYTIKNLHAKIIEK 715
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-575 |
1.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 407 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 486
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 487 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 566
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 666335625 567 TQLQSACEK 575
Cdd:PRK03918 721 ERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
386-595 |
1.21e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 386 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 457
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 458 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEGHyaSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 532
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE--KELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 666335625 533 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 595
Cdd:PRK03918 285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
408-589 |
4.10e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 408 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 483
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 484 YEG--HEDKAAEghyasqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 560
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 666335625 561 KLQQALTQLQSACEK-REQMERRLRTWLER 589
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
426-602 |
2.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 426 LQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAEGHYASQN 500
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 501 KEFLKEKEKLEMELAAVRTASEDHRRHIEI---LDQALSNAQARVIKLEEELREKQAY------------VEKVEKLQQA 565
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 666335625 566 LTQLQsacEKREQMERRLRTwLERELDALRTQQKHGN 602
Cdd:COG4717 208 LAELE---EELEEAQEELEE-LEEELEQLENELEAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-625 |
5.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 417 DKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEghy 496
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKE--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 497 asqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 576
Cdd:PRK03918 285 ----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 666335625 577 EQMERRLRTwLERELDALRTQQKhgngqpANMPEYNAPALLELVREKEE 625
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-598 |
2.31e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 414 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 489
Cdd:pfam01576 145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 490 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 569
Cdd:pfam01576 224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298
|
170 180
....*....|....*....|....*....
gi 666335625 570 qsacekrEQMErRLRTWLERELDALRTQQ 598
Cdd:pfam01576 299 -------EELE-ALKTELEDTLDTTAAQQ 319
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
423-562 |
7.58e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 423 EKELQRISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEghyasqNK 501
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666335625 502 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 562
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
423-649 |
9.81e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 423 EKELQRISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANrqLSSREYEgheDKAAEghyasqnKE 502
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEE---ELEEE-------RR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 503 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK--- 575
Cdd:COG0497 217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElrr 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 576 -REQME---RRLRTWLEReLDALRT-QQKHGnGQPANMPEY--NAPALLELVREKEERILALEADMTKWEQKYLEE---- 644
Cdd:COG0497 287 yLDSLEfdpERLEEVEER-LALLRRlARKYG-VTVEELLAYaeELRAELAELENSDERLEELEAELAEAEAELLEAaekl 364
|
....*
gi 666335625 645 STIRH 649
Cdd:COG0497 365 SAARK 369
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
389-645 |
1.46e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 389 ERAQQMVEIlteENRVLHQELQgyydnadkLHKFEKELQRISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 465
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 466 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 530
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 531 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKREQM----ERRLRTwLERELDALR 595
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQ 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 666335625 596 TQQKHGNGQPANMPEY------------NAPALLE-LVREKEERILALEADMTKWEQKYLEES 645
Cdd:pfam10174 408 EQLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
533-594 |
1.70e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.78 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 666335625 533 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 594
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
416-599 |
1.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 416 ADKLHKFEKELQRISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 483
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 484 YEGHEDKAAE---GHYASQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 554
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 666335625 555 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQK 599
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
417-589 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 417 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 496
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 497 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 566
Cdd:cd07596 82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158
|
170 180
....*....|....*....|...
gi 666335625 567 TQLQSACEKREQMERRLRTWLER 589
Cdd:cd07596 159 SALEEARKRYEEISERLKEELKR 181
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
442-636 |
3.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 442 KRESLDKamrnkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYEGHEDKAAEGHYASQN-----KEFLKEKEKLE 511
Cdd:PRK02224 185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEvleehEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 512 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREqmerrlrTWLEREL 591
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-------EELRDRL 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 666335625 592 DALRTQQKHGNGQPANMPEyNAPALLELVREKEERILALEADMTK 636
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
497-742 |
3.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 497 ASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKR 576
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELE---KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 577 EQMERRLRTWLERELDALRTQQKHG---------NGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTI 647
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 648 RHFAMNAAATAAAERDttiinhsrngsygesSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSR 727
Cdd:COG4942 173 RAELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|....*
gi 666335625 728 KDAGKTDSSSLRPAR 742
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
398-583 |
4.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 398 LTEENRvlhQELQGYYdnADKLHKFEKELQRISEAYESLVKSTTKresLDKAMRNklEGEIRRLH---DFNRDLRDRLET 474
Cdd:PRK03918 445 LTEEHR---KELLEEY--TAELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 475 ANRQ---LSSREYEGHEDKAA--EGHYASQNKEfLKEKEKLEMELAAVRTASED-HRRHIEILDQALSNAQARVIKLEEE 548
Cdd:PRK03918 515 YNLEeleKKAEEYEKLKEKLIklKGEIKSLKKE-LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEER 593
|
170 180 190
....*....|....*....|....*....|....*
gi 666335625 549 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 583
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-579 |
5.12e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 386 AIVERAQQMVEILTEENRVLHQE-LQGYYDNADKLHKFEKELQRISEAYESLVKS----TTKRESLDKAMRNKLEGEIRR 460
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKhqdvTAKYNRRRSKIKEQNNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 461 LHDfnrDLRDRLETANRQLSSRE--YEGHEDKAAEGHYAsQNKEFLKEKEKLEMELAAVR------TASEDHRRHIEILD 532
Cdd:pfam12128 395 IKD---KLAKIREARDRQLAVAEddLQALESELREQLEA-GKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLENFD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 666335625 533 QALSNAQ-------ARVIKLEEELRE-KQAYVEKVEKLQQA---LTQLQSACEKREQM 579
Cdd:pfam12128 471 ERIERAReeqeaanAEVERLQSELRQaRKRRDQASEALRQAsrrLEERQSALDELELQ 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-732 |
5.73e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 393 QMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESL-VKSTTKRESLDKAMRNKLEGEIRRlhdfnrDLRDR 471
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 472 LetanrqlssREYEGhedkaaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELRE 551
Cdd:TIGR02169 220 K---------REYEG--------------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 552 KQAYVEKV--EKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpaNMPEYNapALLELVREKEERILA 629
Cdd:TIGR02169 277 LNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-------LEAEID--KLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 630 LEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHS----RNGSYGE--SSLEAHIWQEEEEVVQANRRCQDMEY 703
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKReiNELKRELDRLQEELQRLSEELADLNA 427
|
330 340
....*....|....*....|....*....
gi 666335625 704 TIKNLHAKIIEKDAMIKVLQQRSRKDAGK 732
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
389-564 |
6.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 389 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLHDFNR-- 466
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----------REELEKLEKLLQLLPLYQEle 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 467 DLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELA--------AVRTASEDHRRH---IEILDQAL 535
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELqqrLAELEEEL 215
|
170 180
....*....|....*....|....*....
gi 666335625 536 SNAQARVIKLEEELREKQAYVEKVEKLQQ 564
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
491-601 |
6.23e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 43.43 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 491 AAEGHYASQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 562
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 666335625 563 QQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHG 601
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
503-641 |
7.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 503 FLKEKEKLEMELAAVRTASEDHRRHIEILDQAlsnaQARVIKLEEELREKQAYVEKVEKLQQALT----------QLQSA 572
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPlyqelealeaELAEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666335625 573 CEKREQMERRLRTW--LERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKY 641
Cdd:COG4717 145 PERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-649 |
7.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 389 ERAQQMVEILTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvkstTKRESLDKAMRNKLEGEIRRLhdfnRDL 468
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEI----EEEISKITARIGELKKEIKEL----KKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 469 RDRLETANRQ--LSSREYEGHEDKAAEGHY-------ASQNKEFLKEKEKLEMELAAVRTASEDHRRHI---EILDQaLS 536
Cdd:PRK03918 428 IEELKKAKGKcpVCGRELTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQ-LK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 537 NAQAR-----VIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQQKHGNGQPANMPey 611
Cdd:PRK03918 507 ELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELG-- 583
|
250 260 270
....*....|....*....|....*....|....*...
gi 666335625 612 napalLELVREKEERILALEadmtKWEQKYLEESTIRH 649
Cdd:PRK03918 584 -----FESVEELEERLKELE----PFYNEYLELKDAEK 612
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
404-644 |
9.14e-04 |
|
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: 43.17 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 404 VLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 483
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 484 YEGHEDkaaEGHYASQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 558
Cdd:pfam05483 434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 559 VEKLQQALTQLQSACEKREQMERRLR---------TWLERELDALRTQQKHGNGQ---PANMPEYNAPALLELVREKEER 626
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 666335625 627 ILALEADMTKWEQ------KYLEE 644
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
395-579 |
9.55e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 395 VEILTEENRVLHQELQGYYDNADKLHKFEKEL---------------QRISEAYESLVKSTTKResldkamRNKLEgEIR 459
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 460 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 536
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 666335625 537 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKREQM 579
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
498-644 |
1.31e-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: 41.45 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 498 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekRE 577
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN---KE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666335625 578 QMErrlrtwLERELDALRTQQKHGngqpanmpEYNAPALLELVREKEERILALEADMTKWEQKYLEE 644
Cdd:COG1579 91 YEA------LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
498-761 |
2.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 498 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEEL----REKQAYVEKVEKLQQALTQLQSAC 573
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslqEEAEELQEELEELQKERQDLEQQR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 574 EKREQMERRLRTWL---ERELDALRTQQKHGNGQ-------PANMPEYNAPALLELVREKEERILALEADMTKWEQKYLE 643
Cdd:COG4372 132 KQLEAQIAELQSEIaerEEELKELEEQLESLQEElaaleqeLQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 644 ESTIRHFAMNAAATAAAER----DTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMI 719
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKlglaLSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 666335625 720 KVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLT 761
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-575 |
3.55e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 388 VERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQR-ISEAYESLVKSTTKRESLDKAMRNkLEGEIRRLHDFNR 466
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEE-LSEELRELESKRS 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 467 DLRDRLETANRQLSS--REYEGHEDKAAeghyasQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIK 544
Cdd:TIGR02168 912 ELRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKR 976
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 666335625 545 LE-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 575
Cdd:TIGR02168 977 LEnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
416-598 |
3.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 416 ADKLHKFEKELQRISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAE 493
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 494 ghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL----------------------------SNAQARVIKL 545
Cdd:PRK02224 354 --LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedfleelreerDELREREAEL 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 666335625 546 EEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKREQMERrlrtwLERELDALRTQQ 598
Cdd:PRK02224 432 EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE-----LEAELEDLEEEV 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-589 |
3.99e-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: 40.52 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 391 AQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRD 470
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 471 RLETANRQLSSREY-----------------EGHEDKAAEGHYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILD 532
Cdd:COG4942 98 ELEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 666335625 533 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLER 589
Cdd:COG4942 178 ALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
526-702 |
5.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 526 RHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLEREldALRTQQKHGngqp 605
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAEL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 606 anmpeynaPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW 685
Cdd:COG4717 145 --------PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170
....*....|....*..
gi 666335625 686 QEEEEVVQANRRCQDME 702
Cdd:COG4717 217 EAQEELEELEEELEQLE 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
400-644 |
5.95e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 400 EENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 479
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 480 SSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 559
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 560 EKLQQAlTQLQSACEKREQMERRlRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQ 639
Cdd:PTZ00121 1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
....*
gi 666335625 640 KYLEE 644
Cdd:PTZ00121 1633 KKVEQ 1637
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
384-739 |
6.37e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 384 AFAIVERAQQMVEILTEENRVLHQELQGYYdNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMR--NKLEGEIRR 460
Cdd:COG5185 54 DSLRVTLRSVINVLDGLNYQNDVKKSESSV-KARKFLKEKKLDTKILQEYVNSLIKLPNYEwSADILISllYLYKSEIVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 461 LHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 540
Cdd:COG5185 133 LKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESET 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 541 RVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDaLRTQQKHGNGQPANMPEYNAPALLELV 620
Cdd:COG5185 213 GNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTD-LRLEKLGENAESSKRLNENANNLIKQF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 621 REKEERILALEAD-MTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW--QEEEEVVQANRR 697
Cdd:COG5185 292 ENTKEKIAEYTKSiDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaiKEEIENIVGEVE 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 666335625 698 CQDMEYTIKNLHAKI---IEKDAMIKVLQQRSRKDAGKTDSSSLR 739
Cdd:COG5185 372 LSKSSEELDSFKDTIestKESLDEIPQNQRGYAQEILATLEDTLK 416
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
447-587 |
7.34e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 447 DKAMrNKLEGEIRRLHDF-------NRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRT 519
Cdd:PRK09039 52 DSAL-DRLNSQIAELADLlslerqgNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 520 ASEDHRRHIEILDQALSNAQARVIKLEEEL-------REKQAyvekveKLQQALTQLQSACEKR-EQMER-------RLR 584
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQA------KIADLGRRLNVALAQRvQELNRyrseffgRLR 204
|
...
gi 666335625 585 TWL 587
Cdd:PRK09039 205 EIL 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
407-578 |
7.67e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 407 QELQGYYDN--------ADKLHKFEKELQRISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 461
Cdd:pfam01576 415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666335625 462 HDFNRDLRDRLETanrqlssreyEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 541
Cdd:pfam01576 495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 666335625 542 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKREQ 578
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKKQK 604
|
|
| |
