|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
527-733 |
1.51e-108 |
|
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: 332.12 E-value: 1.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 527 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 606
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 607 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 686
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958798249 687 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 733
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-666 |
7.60e-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: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 358 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 437
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 438 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 517
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 518 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 597
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798249 598 RILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEEEEVVQA 666
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-697 |
4.17e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 352 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 426
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 427 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 506
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 507 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 586
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 587 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 659
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798249 660 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 697
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-547 |
3.48e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 379 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 458
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 459 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 538
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1958798249 539 TQLQSACEK 547
Cdd:PRK03918 721 ERVEELREK 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
425-687 |
4.56e-05 |
|
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: 47.36 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 425 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 504
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 505 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 580
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 581 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 647
Cdd:TIGR02168 833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798249 648 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 687
Cdd:TIGR02168 913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
389-561 |
1.11e-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: 44.27 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 389 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 467
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 468 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 541
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1958798249 542 QSACEKRGQMERRLRTWLER 561
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 181
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
505-566 |
2.03e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.40 E-value: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798249 505 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 566
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
386-570 |
2.67e-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: 44.78 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 386 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 461
Cdd:pfam01576 145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 462 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 541
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
170 180
....*....|....*....|....*....
gi 1958798249 542 QSAcekrgqmerrLRTWLERELDALRTQQ 570
Cdd:pfam01576 301 LEA----------LKTELEDTLDTTAAQQ 319
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
527-733 |
1.51e-108 |
|
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: 332.12 E-value: 1.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 527 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 606
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 607 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 686
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958798249 687 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 733
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-666 |
7.60e-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: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 358 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 437
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 438 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 517
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 518 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 597
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798249 598 RILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEEEEVVQA 666
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-697 |
4.17e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 352 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 426
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 427 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 506
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 507 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 586
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 587 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 659
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958798249 660 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 697
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-570 |
6.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 386 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDrLETANRQLSSREyeghedkaAE 465
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEID-VASAEREIAELE--------AE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 466 SHHMSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 545
Cdd:COG4913 677 LERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 1958798249 546 EKR------GQMERRLRTWLERELDALRTQQ 570
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-604 |
7.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 359 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR 438
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 439 DLRDRLETANRQLSSREYEGHEDKAAESHH--MSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 516
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRerLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 517 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGNGQPVNLpeynaPALMELVREKE 596
Cdd:TIGR02168 466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533
|
....*...
gi 1958798249 597 ERILALEA 604
Cdd:TIGR02168 534 GYEAAIEA 541
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
355-616 |
9.48e-08 |
|
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: 56.23 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 355 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 433
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 434 HDFNRDLRDRLETANRQLSSREYEghEDKAAEShhmSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQAR 513
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLE--KEYLEKE---IQELQ--EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 514 VIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GNGQPVNLPEYNAPAL 588
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLEDV 956
|
250 260
....*....|....*....|....*...
gi 1958798249 589 MELVREKEERILALEADMTKWEQKYLEE 616
Cdd:TIGR02169 957 QAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-617 |
1.26e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 361 ERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 440
Cdd:COG1196 210 EKAERYRELKEELKELEAELL------LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 441 RDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 520
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 521 LREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEERIL 600
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424
|
250
....*....|....*..
gi 1958798249 601 ALEADMTKWEQKYLEES 617
Cdd:COG1196 425 ELEEALAELEEEEEEEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-583 |
4.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 355 DAFAIVERAQQMVEilteenrvlH-QELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDkAMRNKL-----EG 428
Cdd:COG4913 219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 429 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAESHH-MSQNKefLKEKEKLEMELAAVRTASEDHRRHIEILDQ 505
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELErlEARLDALREELDELEAqIRGNG--GDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798249 506 ALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAC-EKRGQMERRLRTwLERELDALRTQQKHGNGQPVNLPEY 583
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALeEALAEAEAALRD-LRRELRELEAEIASLERRKSNIPAR 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-559 |
1.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 368 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRNKLEGEIRRLHDF--NRDLRDRLE 445
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 446 TANRQLSS--REYEGHEDKAAESHHMSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 521
Cdd:COG4717 136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798249 522 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 559
Cdd:COG4717 216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-547 |
3.48e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 379 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 458
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 459 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 538
Cdd:PRK03918 664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1958798249 539 TQLQSACEK 547
Cdd:PRK03918 721 ERVEELREK 729
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-561 |
6.05e-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: 48.38 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 380 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 455
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 456 YEG--HEDKAAEshhmsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 532
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 1958798249 533 KLQQALTQLQSACEK-RGQMERRLRTWLER 561
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-571 |
2.76e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 375 RVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSTTKResldKAMRNKLEGEIRRLHDFNRDLRDRLE-------TA 447
Cdd:TIGR02169 311 AEKERELE---DAEERLAKLEAEIDKLLAEIEELEREIEEE----RKRRDKLTEEYAELKEELEDLRAELEevdkefaET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 448 NRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAY 527
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958798249 528 VEKVEKLQQALTQLQSACEKRgqmerrlRTWLERELDALRTQQK 571
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKE-------LSKLQRELAEAEAQAR 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
389-597 |
4.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 389 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEShh 468
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKEL-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 469 msqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 548
Cdd:PRK03918 286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958798249 549 GQMERRLRTwLERELDALRTQQKhgngqpVNLPEYNAPALMELVREKEE 597
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
425-687 |
4.56e-05 |
|
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: 47.36 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 425 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 504
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 505 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 580
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 581 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 647
Cdd:TIGR02168 833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798249 648 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 687
Cdd:TIGR02168 913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
395-534 |
6.41e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 395 EKELQSISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKaaeshhMSQNK 473
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR------SEERR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798249 474 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 534
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
389-561 |
1.11e-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: 44.27 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 389 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 467
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 468 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 541
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1958798249 542 QSACEKRGQMERRLRTWLER 561
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 181
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
395-621 |
1.21e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 395 EKELQSISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANRQlssreyEGHEDKAAESHHMSQNKE 474
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAALQ------PGEEEELEEERRRLSNAE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 475 FLKEkeklemelaAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 549
Cdd:COG0497 223 KLRE---------ALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 550 QMER------RLRTWLEReLDALRT-QQKHGnGQPVNLPEYNAPALMEL--VREKEERILALEADMTKWEQKYLEE---- 616
Cdd:COG0497 287 YLDSlefdpeRLEEVEER-LALLRRlARKYG-VTVEELLAYAEELRAELaeLENSDERLEELEAELAEAEAELLEAaekl 364
|
....*
gi 1958798249 617 STIRH 621
Cdd:COG0497 365 SAARK 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
361-569 |
1.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 361 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRNkLEGEIRRLHDFNRDL 440
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 441 RDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 516
Cdd:COG3206 239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958798249 517 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 569
Cdd:COG3206 314 ILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-616 |
1.41e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 398 LQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAESHHMSQN 472
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 473 KEFLKEKEKLEMELAAVrtasedhrrhieildqalsnaQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEK----- 547
Cdd:COG4717 128 LPLYQELEALEAELAEL---------------------PERLEELEERLEELRELEEELEELEAELAELQEELEElleql 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798249 548 RGQMERRLRTWLErELDALRTQQKHgngqpvnlpeynapaLMELVREKEERILALEADMTKWEQKYLEE 616
Cdd:COG4717 187 SLATEEELQDLAE-ELEELQQRLAE---------------LEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-598 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 361 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLdKAMRNKLEGEIRRLH-DFNR- 438
Cdd:PRK03918 480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKL-KEKLIKLKGEIKSLKkELEKl 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 439 -DLRDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 511
Cdd:PRK03918 552 eELKKKLAELEKKLDELE-----EELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 512 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGNgqpvNLPEYNAPALMEL 591
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699
|
....*..
gi 1958798249 592 VREKEER 598
Cdd:PRK03918 700 KEELEER 706
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
505-566 |
2.03e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 43.40 E-value: 2.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798249 505 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 566
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
386-570 |
2.67e-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: 44.78 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 386 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 461
Cdd:pfam01576 145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 462 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 541
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
170 180
....*....|....*....|....*....
gi 1958798249 542 QSAcekrgqmerrLRTWLERELDALRTQQ 570
Cdd:pfam01576 301 LEA----------LKTELEDTLDTTAAQQ 319
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
372-607 |
3.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 372 EENRVLHQELQGcyDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKamRNKLEGEIRRLHDFNRDLRDRLETAnrq 450
Cdd:PRK02224 226 EEQREQARETRD--EADEVLEEHEERREELETLEAEIEDLReTIAETERE--REELAEEVRDLRERLEELEEERDDL--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 451 LSSREYEGHEDKAAESHHmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEildqalsNAQARVIKLEEELREKQayvEK 530
Cdd:PRK02224 299 LAEAGLDDADAEAVEARR----EELEDRDEELRDRLEECRVAAQAHNEEAE-------SLREDADDLEERAEELR---EE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798249 531 VEKLQQALTQLQSACEKRgqmeRRLRTWLERELDALRtqqKHGNGQPVNLPeyNAPALMELVREKEERILALEADMT 607
Cdd:PRK02224 365 AAELESELEEAREAVEDR----REEIEELEEEIEELR---ERFGDAPVDLG--NAEDFLEELREERDELREREAELE 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-617 |
5.90e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 358 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEG---E 429
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 430 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAESHhmsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 509
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 510 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgngqpvnlpeyNAPALM 589
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330
|
250 260 270
....*....|....*....|....*....|
gi 1958798249 590 ELVREKEERILALEADMTKWEQKY--LEES 617
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-621 |
7.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 352 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRNK 425
Cdd:COG1196 133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 426 LEgeirRLHDFNRDLRDRLETANRQlssREyeghedkAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 505
Cdd:COG1196 188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 506 ALSNAQARVIKLEEELREKQAYVE----KVEKLQQALTQLQS---ACEKRGQMERRLRTWLERELDALRTQQKHGNGQPV 578
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEelelELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958798249 579 NLPEyNAPALMELVREKEERILALEADMTKWEQKYLEESTIRH 621
Cdd:COG1196 334 ELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-697 |
9.19e-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: 43.12 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 360 VERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLVkstTKRESLDKAMrNKLEGEIRRLHDFNRD 439
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL------VLRLEELREELEELQEELKEAE---EELEELTAEL-QELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 440 LRDRLETANRQLssreyeghedkaaeshhmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEE 519
Cdd:TIGR02168 279 LEEEIEELQKEL---------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 520 ELREKQAYVEKVEKLQQALT-QLQSACEKRGQMERRLRTwLERELDALRTQqkhgngqpVNLPEYNAPALMELVREKEER 598
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSK--------VAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 599 ILALEADMTKWEQkyleesTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEE---EEVVQANRRCQDMEY 675
Cdd:TIGR02168 409 LERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAER 482
|
330 340
....*....|....*....|..
gi 1958798249 676 TIKNLHAKIiekdAMIKVLQQR 697
Cdd:TIGR02168 483 ELAQLQARL----DSLERLQEN 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
388-571 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 388 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 455
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 456 YEGHEDKAAE---SHHMSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 526
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958798249 527 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 571
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
470-616 |
1.56e-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: 41.06 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 470 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 549
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798249 550 qmeRRLRTwLERELDALRTQQKHGngqpvnlpEYNAPALMELVREKEERILALEADMTKWEQKYLEE 616
Cdd:COG1579 89 ---KEYEA-LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
361-543 |
2.12e-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: 41.73 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 361 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 437
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 438 RDLRDRLET--ANRQLSS--REYEGHEDKAAESHH--MSQNKEFLK-EKEKLEMELAAVRTASE-------DHRRHIEIL 503
Cdd:pfam10174 250 RDLEDEVQMlkTNGLLHTedREEEIKQMEVYKSHSkfMKNKIDQLKqELSKKESELLALQTKLEtltnqnsDCKQHIEVL 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958798249 504 DQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 543
Cdd:pfam10174 330 KESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
365-612 |
3.57e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 365 QMVEILTEENrvlhqelQGCYDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKAMRNK-------------LEGEI 430
Cdd:TIGR00606 667 QFITQLTDEN-------QSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 431 RRLHDFNRDLRDRLETANRQLSSR----------------EYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAvRTASE 494
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLkndieeqetllgtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA-KLQGS 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 495 DHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAL-----------TQLQSACEKRGQMERRLRTwLEREL 563
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLksktnelksekLQIGTNLQRRQQFEEQLVE-LSTEV 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958798249 564 DALRTQQKHGNGQPVNLpeynAPALMELVREKEERILALEADMTKWEQK 612
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPL----ETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-547 |
3.69e-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: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 360 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRNkLEGEIRRLHDFNRD 439
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELEE-LSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 440 LRDRLETANRQLSS--REYEGHEDKAAeshhmsQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 517
Cdd:TIGR02168 913 LRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958798249 518 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 547
Cdd:TIGR02168 978 EnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
367-551 |
4.68e-03 |
|
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: 39.35 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 367 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRNKLEgEIR 431
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 432 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDhrrhieiLDQALS 508
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESVEE--LLKKHKELEEELEAHEPRLKSLNELAEE-------LLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958798249 509 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 551
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
463-573 |
4.69e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.35 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 463 AAESHHMSQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 534
Cdd:PRK10361 22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958798249 535 QQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHG 573
Cdd:PRK10361 102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
376-616 |
6.13e-03 |
|
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: 40.48 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 376 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 455
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 456 YEGHEDkaaESHHMSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 530
Cdd:pfam05483 434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 531 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALRTQQKHGNGQ---PVNLPEYNAPALMELVREKEER 598
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 1958798249 599 ILALEADMTKWEQ------KYLEE 616
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
457-543 |
9.27e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 39.70 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 457 EGHEDKAAEShhmsqnKEFLKEKEKLEMELAAVRTasedhrrhieILDQA--LSNAQARVIklEEElREKQA-YVEKVEK 533
Cdd:PRK05729 804 EGLIDVEAEL------ARLEKELAKLEKEIERVEK----------KLSNEgfVAKAPEEVV--EKE-REKLAeYEEKLAK 864
|
90
....*....|
gi 1958798249 534 LQQALTQLQS 543
Cdd:PRK05729 865 LKERLARLKA 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-594 |
9.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 385 YDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR--DLRDRLETANRQLSSREYEGHEDK 462
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 463 AAEshhmsqNKEFLKEK-EKLEMELAAvrtasedhrrhieiLDQALSNAQARVIKLEEELREkqayVEKVEKLQQALTQL 541
Cdd:COG4717 423 EAL------DEEELEEElEELEEELEE--------------LEEELEELREELAELEAELEQ----LEEDGELAELLQEL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798249 542 QSACEKRGQMERR------LRTWLERELDALRtqqkhgngqpvnlpEYNAPALMELVRE 594
Cdd:COG4717 479 EELKAELRELAEEwaalklALELLEEAREEYR--------------EERLPPVLERASE 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-570 |
9.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 361 ERAQQMVEILTEENRVLHQELQGCY----DNADKLHKFEKELQSISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDF 436
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 437 NRDLRDRLETANRQLS--SREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL------- 507
Cdd:PRK02224 323 DEELRDRLEECRVAAQahNEEAESLREDADD--LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerf 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798249 508 ---------------------SNAQARVIKLEEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKRGQMERr 554
Cdd:PRK02224 401 gdapvdlgnaedfleelreerDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE- 479
|
250
....*....|....*.
gi 1958798249 555 lrtwLERELDALRTQQ 570
Cdd:PRK02224 480 ----LEAELEDLEEEV 491
|
|
| |
