|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
615-821 |
5.59e-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: 332.50 E-value: 5.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 615 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 694
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 695 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 774
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720433107 775 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 821
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-704 |
5.29e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 446 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 525
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 526 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 605
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 606 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 685
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 1720433107 686 RILALEADMTKWEQKYLEE 704
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-704 |
1.45e-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: 58.93 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 443 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 521
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 522 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 600
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 601 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 675
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955
|
250 260
....*....|....*....|....*....
gi 1720433107 676 LMELVREKEERILALEADMTKWEQKYLEE 704
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-635 |
1.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 467 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 546
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 547 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 626
Cdd:PRK03918 662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1720433107 627 TQLQSACEK 635
Cdd:PRK03918 721 ERVEELREK 729
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
449-631 |
5.48e-05 |
|
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: 47.12 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 525
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 526 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 590
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720433107 591 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 631
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
593-654 |
1.38e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 44.17 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720433107 593 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 654
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
477-649 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 477 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 555
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 556 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 629
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1720433107 630 QSACEKRGQMERRLRTWLER 649
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
513-775 |
1.71e-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: 45.82 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 513 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 592
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 593 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 670
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 671 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 740
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270
....*....|....*....|....*....|....*
gi 1720433107 741 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 775
Cdd:TIGR02168 918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| LIM1_Prickle_1 |
cd09483 |
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three ... |
16-51 |
3.39e-03 |
|
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three C-terminal LIM domains and a N-terminal PET domain Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in mainly expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. In addition, Prickle 1 regulates cell movements during gastrulation and neuronal migration through interaction with the noncanonical Wnt11/Wnt5 pathway in zebrafish. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.
Pssm-ID: 188867 Cd Length: 59 Bit Score: 36.82 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720433107 16 RAPPPICYSPSSPV-----QILEDPAYFYPDLQLYSGRHEA 51
Cdd:cd09483 19 RAGPGVCWHPSCFVcftcnELLVDLIYFYQDGKIHCGRHHA 59
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
615-821 |
5.59e-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: 332.50 E-value: 5.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 615 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 694
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 695 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 774
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720433107 775 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 821
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-704 |
5.29e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 446 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 525
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 526 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 605
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 606 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 685
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456
|
250
....*....|....*....
gi 1720433107 686 RILALEADMTKWEQKYLEE 704
Cdd:COG1196 457 EEEALLELLAELLEEAALL 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-704 |
1.45e-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: 58.93 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 443 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 521
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 522 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 600
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 601 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 675
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955
|
250 260
....*....|....*....|....*....
gi 1720433107 676 LMELVREKEERILALEADMTKWEQKYLEE 704
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
474-658 |
3.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 474 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEgEIRRLHDFNRDLRDRLETAnrqlssREYDGHEDKAAE 553
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 554 shyVSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 633
Cdd:COG4913 680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751
|
170 180 190
....*....|....*....|....*....|.
gi 1720433107 634 EKR------GQMERRLRTWLERELDALRTQQ 658
Cdd:COG4913 752 EERfaaalgDAVERELRENLEERIDALRARL 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
447-692 |
1.12e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 447 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNR 526
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 527 DLRDRLETANRQLSSREYDGHEDKAAESH--YVSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 604
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRreRLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 605 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGTGPPVSLpecnaPALMELVREKE 684
Cdd:TIGR02168 466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533
|
....*...
gi 1720433107 685 ERILALEA 692
Cdd:TIGR02168 534 GYEAAIEA 541
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
440-785 |
1.52e-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: 55.45 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 440 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMRtKL 514
Cdd:TIGR02168 133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQLK-SL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 515 EGEIRRLHDFnRDLRDRLETANRQLSSREYDGHEDKAAE-----SHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIE 589
Cdd:TIGR02168 206 ERQAEKAERY-KELKAELRELELALLVLRLEELREELEElqeelKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 590 ILDQALSNAQARVIKLEEELREKQayvekvEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppVSLP 669
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILR------ERLANLERQLEELEAQLEELESKLDE-LAEELAELEEKLE------ELKE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 670 ECNapALMELVREKEERILALEADMTKWEQKYLEESTIRHfamsaaaaATAERDTTISNH-SRNGSYGEsSLEAHIWPEE 748
Cdd:TIGR02168 352 ELE--SLEAELEELEAELEELESRLEELEEQLETLRSKVA--------QLELQIASLNNEiERLEARLE-RLEDRRERLQ 420
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720433107 749 EEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 785
Cdd:TIGR02168 421 QEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
443-659 |
2.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 443 DAFAIVERAQQMVEILTEENRvLHQELQGCYDNADKLhkfeKELQSISEAYESlvksTTKRESLDKAMRtKLEGEIRRLH 522
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE-LAERYAAARERLAEL----EYLRAALRLWFA----QRRLELLEAELE-ELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 523 DFNRDLRDRLETANRQLSS--REYDGHEdkaaeshyvsqnkefLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 600
Cdd:COG4913 309 AELERLEARLDALREELDEleAQIRGNG---------------GDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720433107 601 RVIKLEEELREKQAyveKVEKLQQALTQLQSACE--------KRGQMERRLRTwLERELDALRTQQK 659
Cdd:COG4913 374 PLPASAEEFAALRA---EAAALLEALEEELEALEealaeaeaALRDLRRELRE-LEAEIASLERRKS 436
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
456-647 |
9.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 456 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRTKLEGEIRRLHDF--NRDLRDRLE 533
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 534 TANRQLSS--REYDGHEDKAAESHYVSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 609
Cdd:COG4717 136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720433107 610 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 647
Cdd:COG4717 216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-635 |
1.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 467 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 546
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 547 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 626
Cdd:PRK03918 662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720
|
....*....
gi 1720433107 627 TQLQSACEK 635
Cdd:PRK03918 721 ERVEELREK 729
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
468-649 |
1.40e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 468 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 543
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 544 YDG--HEDKAAEshyvsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 620
Cdd:COG1579 91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 1720433107 621 KLQQALTQLQSACEK-RGQMERRLRTWLER 649
Cdd:COG1579 153 ELEAELEELEAEREElAAKIPPELLALYER 182
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
449-659 |
2.49e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLhdfnRDL 528
Cdd:COG1196 210 EKAERYRELKEELKELEAELL------LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEEL----RLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 529 RDRLETANRQLSSREYdghedkaaeshyvsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 608
Cdd:COG1196 276 LEELELELEEAQAEEY-----------------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720433107 609 LREKQA--------YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 659
Cdd:COG1196 339 LEELEEeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
477-685 |
9.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 477 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREydgheDKAAEShy 556
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKEL-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 557 vsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 636
Cdd:PRK03918 286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720433107 637 GQMERRLRTwLERELDALRTQQKHGTgppvslPECNAPALMELVREKEE 685
Cdd:PRK03918 361 HELYEEAKA-KKEELERLKKRLTGLT------PEKLEKELEELEKAKEE 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-700 |
3.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 498 KSTTkRESLDKAMRTKLEGEIRRLHDFN----RDLRDRLETANRQLssreydgHEDKAAESHYvsqnKEFLKEKEKLEME 573
Cdd:COG4717 36 KSTL-LAFIRAMLLERLEKEADELFKPQgrkpELNLKELKELEEEL-------KEAEEKEEEY----AELQEELEELEEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 574 LAAVRTASEDHRRHIEILDQALsNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDA 653
Cdd:COG4717 104 LEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE-LQEELEE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720433107 654 LRTQqkhgtgppvsLPECNAPALMELVREKEE---RILALEADMTKWEQK 700
Cdd:COG4717 182 LLEQ----------LSLATEEELQDLAEELEElqqRLAELEEELEEAQEE 221
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
449-631 |
5.48e-05 |
|
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: 47.12 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 525
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 526 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 590
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720433107 591 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 631
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
446-705 |
7.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 446 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEG---E 517
Cdd:PRK03918 129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 518 IRRLHDFNRDLRDRLETANRQLssREYDGHEDKAAESHyvsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 597
Cdd:PRK03918 209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 598 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppvslpecNAPALM 677
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330
|
250 260 270
....*....|....*....|....*....|
gi 1720433107 678 ELVREKEERILALEADMTKWEQKY--LEES 705
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
474-658 |
7.88e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 474 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRTKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYDGHED 549
Cdd:pfam01576 145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 550 KAAESHYVSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 629
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
170 180
....*....|....*....|....*....
gi 1720433107 630 QSAcekrgqmerrLRTWLERELDALRTQQ 658
Cdd:pfam01576 301 LEA----------LKTELEDTLDTTAAQQ 319
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
593-654 |
1.38e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 44.17 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720433107 593 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 654
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
449-657 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRTkLEGEIRRLHDFNRDL 528
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 529 RDRLETANRQLSSREydgheDKAAESHYVSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 604
Cdd:COG3206 239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720433107 605 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 657
Cdd:COG3206 314 ILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
477-649 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 477 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 555
Cdd:cd07596 11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 556 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 629
Cdd:cd07596 83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161
|
170 180
....*....|....*....|
gi 1720433107 630 QSACEKRGQMERRLRTWLER 649
Cdd:cd07596 162 EEARKRYEEISERLKEELKR 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
513-775 |
1.71e-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: 45.82 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 513 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 592
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 593 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 670
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 671 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 740
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270
....*....|....*....|....*....|....*
gi 1720433107 741 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 775
Cdd:TIGR02168 918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
464-704 |
2.06e-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: 45.10 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 464 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLeGEIRRLHDFNRdlrdRLETANRQLSSRE 543
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKK----QFEKIAEELKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 544 ydghedkaAESHYVSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 618
Cdd:pfam05483 439 --------QELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 619 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALR---TQQKHGTGPPVSLPECNAPALMELVREKEER 686
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVReefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588
|
250 260
....*....|....*....|....
gi 1720433107 687 ILALEADMTKWEQ------KYLEE 704
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-659 |
2.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 476 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 543
Cdd:COG4942 19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 544 YDGHEDKAAE---SHYVSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 614
Cdd:COG4942 99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720433107 615 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 659
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
483-622 |
3.16e-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: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 483 EKELQSISEAYESLVKST-TKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAEshyvsqNK 561
Cdd:COG2433 387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720433107 562 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 622
Cdd:COG2433 460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
449-686 |
3.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLDKAMRtKLEGEIRRLH-DFNR- 526
Cdd:PRK03918 480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLI-KLKGEIKSLKkELEKl 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 527 -DLRDRLETANRQLssreyDGHEDKAAESHYVSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 599
Cdd:PRK03918 552 eELKKKLAELEKKL-----DELEEELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 600 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGTgppvSLPECNAPALMEL 679
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699
|
....*..
gi 1720433107 680 VREKEER 686
Cdd:PRK03918 700 KEELEER 706
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
440-704 |
4.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 440 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRTK 513
Cdd:COG1196 133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 514 LEgeirRLHDFNRDLRDRLETANRQlssREydghedkAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 593
Cdd:COG1196 188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 594 ALSNAQARVIKLEEELRE-KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecn 672
Cdd:COG1196 254 ELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE------------- 320
|
250 260 270
....*....|....*....|....*....|..
gi 1720433107 673 apaLMELVREKEERILALEADMTKWEQKYLEE 704
Cdd:COG1196 321 ---LEEELAELEEELEELEEELEELEEELEEA 349
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-785 |
4.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 448 VERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLVkstTKRESLDKAMRTkLEGEIRRLHDFNRD 527
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL------VLRLEELREELEELQEELKEAE---EELEELTAELQE-LEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 528 LRDRLETANRQLssreydghedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEE 607
Cdd:TIGR02168 279 LEEEIEELQKEL---------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 608 ELREKQAYVEKVEKLQQALT-QLQSACEKRGQMERRLRTwLERELDALRTQqkhgtgppVSLPECNAPALMELVREKEER 686
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSK--------VAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 687 ILALEADMTKWEQkyleesTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEE---EEVVQANRRCQDMEY 763
Cdd:TIGR02168 409 LERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAER 482
|
330 340
....*....|....*....|..
gi 1720433107 764 TIKNLHAKIiekdAMIKVLQQR 785
Cdd:TIGR02168 483 ELAQLQARL----DSLERLQEN 500
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
483-709 |
5.01e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 483 EKELQSISEAYESLVKSTTKRESLDKAMRtklegEIRRLHDFNRDLRDRLETANrqLSSREYdghEDKAAEshyvsqnKE 562
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEE---EELEEE-------RR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 563 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 637
Cdd:COG0497 217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 638 QMER------RLRTWLEReLDALRT-QQKHGtgppVSLPEcnAPALMELVREK-------EERILALEADMTKWEQKYLE 703
Cdd:COG0497 287 YLDSlefdpeRLEEVEER-LALLRRlARKYG----VTVEE--LLAYAEELRAElaelensDERLEELEAELAEAEAELLE 359
|
250
....*....|
gi 1720433107 704 E----STIRH 709
Cdd:COG0497 360 AaeklSAARK 369
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
455-639 |
5.27e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.43 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 455 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRTKLEgEIR 519
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 520 RLHDFNRDLRD---RLETANRQLSSREYDGHEDKAaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 596
Cdd:cd00176 107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720433107 597 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 639
Cdd:cd00176 178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
558-704 |
1.04e-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: 41.83 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 558 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 637
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720433107 638 qmeRRLRTwLERELDALRTQQkhgtgppvSLPECNAPALMELVREKEERILALEADMTKWEQKYLEE 704
Cdd:COG1579 89 ---KEYEA-LQKEIESLKRRI--------SDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
502-696 |
1.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 502 KRESLDKamrtkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYDGHEDKAAE-----SHYVSQNKEFLKEKEKLE 571
Cdd:PRK02224 185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQAREtrdeaDEVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 572 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRgqmerrlRTWLEREL 651
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR-------DEELRDRL 330
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720433107 652 DALRTQQKHGTGPPVSLPEcNAPALMELVREKEERILALEADMTK 696
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-635 |
2.54e-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: 41.97 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 448 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLHDFNRD 527
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELE-ELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 528 LRDRLETANRQLSS--REYDGHEDKaaeshyVSQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 605
Cdd:TIGR02168 913 LRRELEELREKLAQleLRLEGLEVR------IDNLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720433107 606 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 635
Cdd:TIGR02168 978 EnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
|
|
| LIM1_Prickle_1 |
cd09483 |
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three ... |
16-51 |
3.39e-03 |
|
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three C-terminal LIM domains and a N-terminal PET domain Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in mainly expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. In addition, Prickle 1 regulates cell movements during gastrulation and neuronal migration through interaction with the noncanonical Wnt11/Wnt5 pathway in zebrafish. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.
Pssm-ID: 188867 Cd Length: 59 Bit Score: 36.82 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1720433107 16 RAPPPICYSPSSPV-----QILEDPAYFYPDLQLYSGRHEA 51
Cdd:cd09483 19 RAGPGVCWHPSCFVcftcnELLVDLIYFYQDGKIHCGRHHA 59
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
467-636 |
4.54e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 467 QELQGCYDN--------ADKLHKFEKELQSISEAYESLVKSTTK---------------RESLDKAMRTKLE--GEIRRL 521
Cdd:pfam01576 415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 522 HDFNRDLRDRLETanrqlssreyDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 601
Cdd:pfam01576 495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720433107 602 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKR 636
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKK 602
|
|
| Val_tRNA-synt_C |
pfam10458 |
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ... |
565-630 |
4.89e-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: 36.48 E-value: 4.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720433107 565 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 630
Cdd:pfam10458 4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
526-649 |
5.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 526 RDLRDRLETANRQLSS--------REYDGHEDKAAESHYvsqnkefLKEK---EKLEMELAAVRTASEDHRRHIEILDQA 594
Cdd:COG4913 238 ERAHEALEDAREQIELlepirelaERYAAARERLAELEY-------LRAAlrlWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 595 LSNAQARVIKLEEELRE-KQAY----VEKVEKLQQALTQLQSACEKRGQMERRLRTWLER 649
Cdd:COG4913 311 LERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
453-700 |
5.63e-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: 40.80 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 453 QMVEILTEENrvlhqelQGCYDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKAMRTK-------------LEGEI 518
Cdd:TIGR00606 667 QFITQLTDEN-------QSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 519 RRLHDFNRDLRDRLETANRQLSSREYD-----------GHEDKAAES-----HYVSQNKEFLKEKEKLEMELAAvRTASE 582
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDieeqetllgtiMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAA-KLQGS 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 583 DHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAL-----------TQLQSACEKRGQMERRLRTwLEREL 651
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLksktnelksekLQIGTNLQRRQQFEEQLVE-LSTEV 897
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720433107 652 DALRTQQKHGTGPPVSLpecnAPALMELVREKEERILALEADMTKWEQK 700
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPL----ETFLEKDQQEKEELISSKETSNKKAQDK 942
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
450-701 |
7.70e-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: 40.42 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 450 RAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLD----------------KAMRTK 513
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfergpfserqiknfhTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 514 LEGEIRRLHDFNRDLRDRLETANRQLssreyDGHEDKAAESHYVSQNKEFLKEKEKLEMelaavrtasedhrRHIEILDQ 593
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-----DEIRDEKKGLGRTIELKKEILEKKQEEL-------------KFVIKELQ 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 594 ALSNAQARVIKLEEELREKQAYVEKVEKlqQALTQLQSACEKRGQMERrlrtwlereLDALRTQQKhgtgppvsLPECNA 673
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKAEK--NSLTETLKKEVKSLQNEK---------ADLDRKLRK--------LDQEME 525
|
250 260 270
....*....|....*....|....*....|.
gi 1720433107 674 palmELVREKEER--ILALEAD-MTKWEQKY 701
Cdd:TIGR00606 526 ----QLNHHTTTRtqMEMLTKDkMDKDEQIR 552
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
449-658 |
8.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 449 ERAQQMVEILTEENRVLHQELQGCY----DNADKLHKFEKELQSISEAYESLVKSTtkreSLDKAMRTKLEGEIRRLHDF 524
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 525 NRDLRDRLETANRQLS--SREYDGHEDKAAESHyvSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL------- 595
Cdd:PRK02224 323 DEELRDRLEECRVAAQahNEEAESLREDADDLE--ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerf 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 596 ---------------------SNAQARVIKLEEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKRGQMERr 642
Cdd:PRK02224 401 gdapvdlgnaedfleelreerDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE- 479
|
250
....*....|....*.
gi 1720433107 643 lrtwLERELDALRTQQ 658
Cdd:PRK02224 480 ----LEAELEDLEEEV 491
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
481-645 |
8.72e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 481 KFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRL---HDFNRDLRDRLETANrqLSSREYDGHEDKAAESHYV 557
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGFKY--VSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 558 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEIL----------------DQALSNAQARVIKLE---EELREK-QAYVE 617
Cdd:PRK05771 164 SDVENVEYISTDKGYVYVVVVVLKELSDEVEEELkklgferleleeegtpSELIREIKEELEEIEkerESLLEElKELAK 243
|
170 180
....*....|....*....|....*...
gi 1720433107 618 KVEKLQQALTQLQSACEKRGQMERRLRT 645
Cdd:PRK05771 244 KYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
467-692 |
9.34e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 467 QELQGCYDN-ADKLHKFEKELQSISEAYESLVKsttKRESLDK---AMRTKLEgEIRRLHdfnrdLRDRLETANRQLSSR 542
Cdd:pfam05622 193 QELHGKLSEeSKKADKLEFEYKKLEEKLEALQK---EKERLIIerdTLRETNE-ELRCAQ-----LQQAELSQADALLSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 543 EYDGHEDKAAESHYVSqnkefLKEK-EKLEMELAAVRTASE-DHRRHIEILDQALSNAQARVIKLEEELREKQAYV---- 616
Cdd:pfam05622 264 SSDPGDNLAAEIMPAE-----IREKlIRLQHENKMLRLGQEgSYRERLTELQQLLEDANRRKNELETQNRLANQRIlelq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720433107 617 EKVEKLQQALTQLQSACEKRGQMERRLRTWLE--RELDALR---TQQKHGTGPPVSL-PECNAPALMELVREKEERILAL 690
Cdd:pfam05622 339 QQVEELQKALQEQGSKAEDSSLLKQKLEEHLEklHEAQSELqkkKEQIEELEPKQDSnLAQKIDELQEALRKKDEDMKAM 418
|
..
gi 1720433107 691 EA 692
Cdd:pfam05622 419 EE 420
|
|
| |
