|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
530-736 |
2.49e-107 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 329.04 E-value: 2.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 530 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 609
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 610 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 689
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907200898 690 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 736
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-669 |
8.98e-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: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 361 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 440
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 441 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 520
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 521 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 600
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200898 601 RILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEEEEVVQA 669
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-619 |
2.37e-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: 58.16 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 358 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 436
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 437 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 515
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 516 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 590
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955
|
250 260
....*....|....*....|....*....
gi 1907200898 591 LMELVREKEERILALEADMTKWEQKYLEE 619
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-550 |
2.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 382 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 461
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 462 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 541
Cdd:PRK03918 662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1907200898 542 TQLQSACEK 550
Cdd:PRK03918 721 ERVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
463-615 |
9.96e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 463 EDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALsNAQARVIKLEEELREKQAYVEKVEKLQQALT 542
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200898 543 QLQSACEKRGQMERRLRTwLERELDALRTQqkhgtgppvsLPECNAPALMELVREKEE---RILALEADMTKWEQK 615
Cdd:COG4717 157 ELRELEEELEELEAELAE-LQEELEELLEQ----------LSLATEEELQDLAEELEElqqRLAELEEELEEAQEE 221
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
364-546 |
1.80e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 364 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 440
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 441 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 505
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907200898 506 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 546
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-690 |
2.77e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 428 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 507
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 508 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 585
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 586 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 655
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270
....*....|....*....|....*....|....*
gi 1907200898 656 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 690
Cdd:TIGR02168 918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
392-564 |
4.48e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 42.73 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 392 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 470
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 471 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 544
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1907200898 545 QSACEKRGQMERRLRTWLER 564
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 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 ... |
530-736 |
2.49e-107 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 329.04 E-value: 2.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 530 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 609
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 610 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 689
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907200898 690 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 736
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-669 |
8.98e-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: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 361 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 440
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 441 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 520
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 521 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 600
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200898 601 RILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEEEEVVQA 669
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-619 |
2.37e-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: 58.16 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 358 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 436
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 437 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 515
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 516 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 590
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955
|
250 260
....*....|....*....|....*....
gi 1907200898 591 LMELVREKEERILALEADMTKWEQKYLEE 619
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-573 |
5.85e-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: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 389 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEgEIRRLHDFNRDLRDRLETAnrqlssREYDGHEDKAAE 468
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 469 shyVSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 548
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 1907200898 549 EKR------GQMERRLRTWLERELDALRTQQ 573
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-607 |
2.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 362 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNR 441
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 442 DLRDRLETANRQLSSREYDGHEDKAAESH--YVSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 519
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRreRLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 520 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGTGPPVSLpecnaPALMELVREKE 599
Cdd:TIGR02168 466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533
|
....*...
gi 1907200898 600 ERILALEA 607
Cdd:TIGR02168 534 GYEAAIEA 541
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
358-574 |
4.39e-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: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 358 DAFAIVERAQQMVEILTEENRvLHQELQGCYDNADKLhkfeKELQSISEAYESlvksTTKRESLDKAMRtKLEGEIRRLH 437
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE-LAERYAAARERLAEL----EYLRAALRLWFA----QRRLELLEAELE-ELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 438 DFNRDLRDRLETANRQLSS--REYDGHEdkaaeshyvsqnkefLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 515
Cdd:COG4913 309 AELERLEARLDALREELDEleAQIRGNG---------------GDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200898 516 RVIKLEEELREKQAyveKVEKLQQALTQLQSACE--------KRGQMERRLRTwLERELDALRTQQK 574
Cdd:COG4913 374 PLPASAEEFAALRA---EAAALLEALEEELEALEealaeaeaALRDLRRELRE-LEAEIASLERRKS 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-700 |
5.89e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 355 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMRtKL 429
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQLK-SL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 430 EGEIRRLHDFnRDLRDRLETANRQLSSREYDGHEDKAAE-----SHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIE 504
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLEELREELEElqeelKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 505 ILDQALSNAQARVIKLEEELREKQayvekvEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppVSLP 584
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILR------ERLANLERQLEELEAQLEELESKLDE-LAEELAELEEKLE------ELKE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 585 ECNapALMELVREKEERILALEADMTKWEQKYLEESTIRHfamsaaaaATAERDTTISNH-SRNGSYGEsSLEAHIWPEE 663
Cdd:TIGR02168 352 ELE--SLEAELEELEAELEELESRLEELEEQLETLRSKVA--------QLELQIASLNNEiERLEARLE-RLEDRRERLQ 420
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907200898 664 EEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 700
Cdd:TIGR02168 421 QEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-550 |
2.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 382 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 461
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 462 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 541
Cdd:PRK03918 662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1907200898 542 TQLQSACEK 550
Cdd:PRK03918 721 ERVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
371-562 |
2.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 371 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRTKLEGEIRRLHDF--NRDLRDRLE 448
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 449 TANRQLSS--REYDGHEDKAAESHYVSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 524
Cdd:COG4717 136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907200898 525 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 562
Cdd:COG4717 216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
383-564 |
3.92e-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: 49.15 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 383 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 458
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 459 YDG--HEDKAAEshyvsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 535
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 1907200898 536 KLQQALTQLQSACEK-RGQMERRLRTWLER 564
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
364-574 |
4.87e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 364 ERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLhdfnRDL 443
Cdd:COG1196 210 EKAERYRELKEELKELEAELL------LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEEL----RLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 444 RDRLETANRQLSSREYdghedkaaeshyvsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 523
Cdd:COG1196 276 LEELELELEEAQAEEY-----------------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200898 524 LREKQA--------YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 574
Cdd:COG1196 339 LEELEEeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
392-600 |
1.49e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 392 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREydgheDKAAEShy 471
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKEL-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 472 vsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 551
Cdd:PRK03918 286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907200898 552 GQMERRLRTwLERELDALRTQQKHGTgppvslPECNAPALMELVREKEE 600
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKRLTGLT------PEKLEKELEELEKAKEE 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
463-615 |
9.96e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 463 EDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALsNAQARVIKLEEELREKQAYVEKVEKLQQALT 542
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200898 543 QLQSACEKRGQMERRLRTwLERELDALRTQqkhgtgppvsLPECNAPALMELVREKEE---RILALEADMTKWEQK 615
Cdd:COG4717 157 ELRELEEELEELEAELAE-LQEELEELLEQ----------LSLATEEELQDLAEELEElqqRLAELEEELEEAQEE 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-620 |
1.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 361 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEG---E 432
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 433 IRRLHDFNRDLRDRLETANRQLssREYDGHEDKAAESHyvsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 512
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 513 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppvslpecNAPALM 592
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330
|
250 260 270
....*....|....*....|....*....|
gi 1907200898 593 ELVREKEERILALEADMTKWEQKY--LEES 620
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
508-569 |
1.80e-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: 1.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200898 508 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 569
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
364-546 |
1.80e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 364 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 440
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 441 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 505
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907200898 506 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 546
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
364-572 |
2.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 364 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRTkLEGEIRRLHDFNRDL 443
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 444 RDRLETANRQLSSREydgheDKAAESHYVSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 519
Cdd:COG3206 239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907200898 520 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 572
Cdd:COG3206 314 ILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
389-573 |
2.25e-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: 45.17 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 389 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRTKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYDGHED 464
Cdd:pfam01576 145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 465 KAAESHYVSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 544
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
170 180
....*....|....*....|....*....
gi 1907200898 545 QSAcekrgqmerrLRTWLERELDALRTQQ 573
Cdd:pfam01576 301 LEA----------LKTELEDTLDTTAAQQ 319
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-690 |
2.77e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 428 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 507
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 508 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 585
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 586 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 655
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270
....*....|....*....|....*....|....*
gi 1907200898 656 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 690
Cdd:TIGR02168 918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
398-537 |
3.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 398 EKELQSISEAYESLVKST-TKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAEshyvsqNK 476
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200898 477 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 537
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
392-564 |
4.48e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 42.73 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 392 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 470
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 471 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 544
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1907200898 545 QSACEKRGQMERRLRTWLER 564
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-574 |
5.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 391 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 458
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 459 YDGHEDKAAE---SHYVSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 529
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907200898 530 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 574
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
364-601 |
6.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 364 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLDKAMRtKLEGEIRRLH-DFNR- 441
Cdd:PRK03918 480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLI-KLKGEIKSLKkELEKl 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 442 -DLRDRLETANRQLssreyDGHEDKAAESHYVSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 514
Cdd:PRK03918 552 eELKKKLAELEKKL-----DELEEELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 515 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGTgppvSLPECNAPALMEL 594
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699
|
....*..
gi 1907200898 595 VREKEER 601
Cdd:PRK03918 700 KEELEER 706
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-619 |
8.12e-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: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 379 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLeGEIRRLHDFNRdlrdRLETANRQLSSRE 458
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKK----QFEKIAEELKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 459 ydghedkaAESHYVSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 533
Cdd:pfam05483 439 --------QELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 534 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALR---TQQKHGTGPPVSLPECNAPALMELVREKEER 601
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVReefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 1907200898 602 ILALEADMTKWEQ------KYLEE 619
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
398-624 |
8.82e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 398 EKELQSISEAYESLVKSTTKRESLDKAMRtklegEIRRLHDFNRDLRDRLETANrqLSSREYdghEDKAAEshyvsqnKE 477
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEE---EELEEE-------RR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 478 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 552
Cdd:COG0497 217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 553 QMER------RLRTWLEReLDALRT-QQKHGtgppVSLPEcnAPALMELVREK-------EERILALEADMTKWEQKYLE 618
Cdd:COG0497 287 YLDSlefdpeRLEEVEER-LALLRRlARKYG----VTVEE--LLAYAEELRAElaelensDERLEELEAELAEAEAELLE 359
|
250
....*....|
gi 1907200898 619 E----STIRH 624
Cdd:COG0497 360 AaeklSAARK 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
355-619 |
1.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 355 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRTK 428
Cdd:COG1196 133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 429 LEgeirRLHDFNRDLRDRLETANRQlssREydghedkAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 508
Cdd:COG1196 188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 509 ALSNAQARVIKLEEELRE-KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecn 587
Cdd:COG1196 254 ELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE------------- 320
|
250 260 270
....*....|....*....|....*....|..
gi 1907200898 588 apaLMELVREKEERILALEADMTKWEQKYLEE 619
Cdd:COG1196 321 ---LEEELAELEEELEELEEELEELEEELEEA 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
473-619 |
2.11e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 473 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 552
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200898 553 qmeRRLRTwLERELDALRTQQkhgtgppvSLPECNAPALMELVREKEERILALEADMTKWEQKYLEE 619
Cdd:COG1579 89 ---KEYEA-LQKEIESLKRRI--------SDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
417-611 |
2.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 417 KRESLDKamrtkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYDGHEDKAAE-----SHYVSQNKEFLKEKEKLE 486
Cdd:PRK02224 185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQAREtrdeaDEVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 487 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRgqmerrlRTWLEREL 566
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR-------DEELRDRL 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907200898 567 DALRTQQKHGTGPPVSLPEcNAPALMELVREKEERILALEADMTK 611
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
370-554 |
2.75e-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: 40.12 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 370 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRTKLEgEIR 434
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 435 RLHDFNRDLRD---RLETANRQLSSREYDGHEDKAaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 511
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907200898 512 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 554
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
363-550 |
6.18e-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: 40.43 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 363 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLHDFNRD 442
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELE-ELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 443 LRDRLETANRQLSS--REYDGHEDKaaeshyVSQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 520
Cdd:TIGR02168 913 LRRELEELREKLAQleLRLEGLEVR------IDNLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907200898 521 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 550
Cdd:TIGR02168 978 EnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
441-564 |
6.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 441 RDLRDRLETANRQLSS--------REYDGHEDKAAESHYvsqnkefLKEK---EKLEMELAAVRTASEDHRRHIEILDQA 509
Cdd:COG4913 238 ERAHEALEDAREQIELlepirelaERYAAARERLAELEY-------LRAAlrlWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 510 LSNAQARVIKLEEELRE-KQAY----VEKVEKLQQALTQLQSACEKRGQMERRLRTWLER 564
Cdd:COG4913 311 LERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
396-560 |
7.82e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 396 KFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRL---HDFNRDLRDRLETANrqLSSREYDGHEDKAAESHYV 472
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGFKY--VSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200898 473 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEIL----------------DQALSNAQARVIKLE---EELREK-QAYVE 532
Cdd:PRK05771 164 SDVENVEYISTDKGYVYVVVVVLKELSDEVEEELkklgferleleeegtpSELIREIKEELEEIEkerESLLEElKELAK 243
|
170 180
....*....|....*....|....*...
gi 1907200898 533 KVEKLQQALTQLQSACEKRGQMERRLRT 560
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
480-545 |
8.95e-03 |
|
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.
Pssm-ID: 431296 [Multi-domain] Cd Length: 66 Bit Score: 35.71 E-value: 8.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200898 480 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 545
Cdd:pfam10458 4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
|
|
| |
