|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
39-306 |
1.38e-94 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 301.14 E-value: 1.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 39 TQTVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRY 117
Cdd:pfam07651 1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 118 RNELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECEL 196
Cdd:pfam07651 81 RRRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 197 NLFQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLK 270
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLK 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 206729937 271 DLFYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
814-1012 |
3.15e-94 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 297.36 E-value: 3.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 814 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 893
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 894 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 972
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 206729937 973 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 1012
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
9.90e-84 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 265.75 E-value: 9.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 40 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 119
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 206729937 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 153
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
1.02e-69 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 227.55 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 40 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 119
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 206729937 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 153
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
864-1010 |
2.07e-59 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 200.12 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 864 KNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVN 943
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 944 QATAGVVASTISGKSQIEE--TDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYE 1010
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
5.80e-57 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 191.62 E-value: 5.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 40 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 119
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 206729937 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 153
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
40-153 |
5.54e-41 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 146.37 E-value: 5.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 40 QTVSINKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAVLCWKFCHVFHKLLRDGHP--NVLKDSLR 116
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 206729937 117 -YRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 153
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
38-160 |
1.03e-38 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 140.46 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 38 RTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVLKDSL 115
Cdd:smart00273 1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 206729937 116 RYRNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTKMEYHTKNPRFP 160
Cdd:smart00273 81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
482-580 |
3.25e-34 |
|
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.
Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 126.28 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 482 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 561
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 206729937 562 SEANWAAEFAELEKERDSL 580
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
42-153 |
2.26e-27 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 107.39 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNEL 121
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 206729937 122 SDMSRMW-GHLSEGYGQLCSIYLKLLRTKMEYH 153
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-644 |
9.39e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 448
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 449 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 528
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 529 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 608
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 206729937 609 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 644
Cdd:COG1196 455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-644 |
2.75e-13 |
|
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: 74.71 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAeqqhlrqqaADDCEFLRAELDELRRQREDT----EKA 450
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALL---------VLRLEELREELEELQEELKEAeeelEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLErisdQGQRKTQE 530
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----ELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 531 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 610
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270
....*....|....*....|....*....|....
gi 206729937 611 SMCQLAKDQRKMLlvgsRKAAEQVIQDALNQLEE 644
Cdd:TIGR02168 415 RRERLQQEIEELL----KKLEEAELKELQAELEE 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-610 |
3.86e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 450
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 530
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 531 QLEVLESLKQELATSQRELQvlqgSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 610
Cdd:COG1196 423 LEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-622 |
1.28e-12 |
|
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: 72.40 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 369 NKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDte 448
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 449 kAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK-------ELEDSLERIS 521
Cdd:TIGR02168 335 -LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneieRLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 522 DQGQRKTQEQLEVLESL--------KQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSlvsgAAHREEELSA 593
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA----AERELAQLQA 489
|
250 260
....*....|....*....|....*....
gi 206729937 594 LRKELQDTQLKLASTEESMCQLAKDQRKM 622
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-644 |
1.58e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQR----VVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQR 452
Cdd:COG1196 188 LERLEDILGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEE----LEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 453 S----LSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgqrkT 528
Cdd:COG1196 264 EleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----L 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 529 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 608
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270
....*....|....*....|....*....|....*.
gi 206729937 609 EESmcQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 644
Cdd:COG1196 420 EEE--LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
377-590 |
5.00e-12 |
|
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: 69.02 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 456
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVD-LEREKKELEDSLERISDQGQRKtQEQLEVL 535
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERAEL-EALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 206729937 536 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEE 590
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-644 |
7.40e-12 |
|
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: 69.70 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 382 REISGLKAQLEnmktesqrvvlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEK-AQRSLSEIERK 460
Cdd:TIGR02168 677 REIEELEEKIE-----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 461 AQANEQRYSKLKEKYSELVQNHADL--LRKNAEVTKQVSMARQAQVD-LEREKKELE---DSLERISDQGQRKTQEQLEV 534
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALRealDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 535 LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-------REEELSALRKELQDTQLKLAS 607
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRE 905
|
250 260 270
....*....|....*....|....*....|....*...
gi 206729937 608 TEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQLEE 644
Cdd:TIGR02168 906 LESKRSELRRElEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-607 |
2.45e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLkAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 450
Cdd:COG1196 281 LELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 530
Cdd:COG1196 360 ---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 206729937 531 QLEVLESLKQELATSQRELQVLQGSLETSAQSEanwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 607
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-588 |
5.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 456
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLE 536
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 206729937 537 SLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHRE 588
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-688 |
6.59e-11 |
|
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: 66.63 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA---- 450
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAQANEQRYSKLKEKYSEL--------VQNHADLLRK-NAEVTKQVSMARQAQVDLER---EKKELEDSLE 518
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKlEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 519 RISDQgQRKTQEQLEvleSLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKEL 598
Cdd:TIGR02169 837 ELQEQ-RIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-------EAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 599 QDTQLKLasteesmcqlakdQRKMLLVGSRKAAEQVIQDALNQLEEPPliscagsadhllSTVTSISSCIEQLEKSWSQY 678
Cdd:TIGR02169 906 EELEAQI-------------EKKRKRLSELKAKLEALEEELSEIEDPK------------GEDEEIPEEELSLEDVQAEL 960
|
330
....*....|
gi 206729937 679 LACPEDISGL 688
Cdd:TIGR02169 961 QRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-644 |
3.99e-10 |
|
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: 64.31 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 369 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQlkghVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdte 448
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 449 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK----------------- 511
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieele 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 512 ----ELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRElqvlqgsletsaqseanWAAEFAELEKERDSLvsgaahr 587
Cdd:TIGR02168 866 elieELESELEALLNE-RASLEEALALLRSELEELSEELRE-----------------LESKRSELRRELEEL------- 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729937 588 EEELSALRKELQDTQLKLASTEEsmcQLAKDQRKML-----LVGSRKAAEQVIQDALNQLEE 644
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLeeaeaLENKIEDDEEEARRRLKRLEN 979
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
410-631 |
1.32e-09 |
|
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: 61.32 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 410 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL 485
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 486 LRKnaevtkQVSMARQAQVDLEREKKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE 563
Cdd:COG4942 110 LRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206729937 564 ANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAA 631
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
434-644 |
1.65e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 434 RAELDELRRQredTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLERE 509
Cdd:TIGR02168 676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 510 KKELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLET--SAQSEANwaAEFAELEKERDSLVSGAAHR 587
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKAlrEALDELR--AELTLLNEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 206729937 588 EEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEE 644
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL------EELIEELESELEALLN 880
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
435-620 |
1.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 435 AELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaEVTKQVSMARQAQVDLEREKKELE 514
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 515 DSLERIsdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLETS-AQSEANWAAEFAELEKERDSLVSGAAHREEELSA 593
Cdd:COG4717 146 ERLEEL--------EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*..
gi 206729937 594 LRKELQDTQLKLASTEESMCQLAKDQR 620
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-807 |
2.35e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLENMK------TESQRVVLQLKGHVSELEADLAEQQHLRQQaaddcefLRAELDELRRQR 444
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 445 EDTEKAQ------RSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLE 518
Cdd:PRK03918 283 KELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 519 RISDQGQRKTQeqlevLESLKQELATS-----QRELQVLQGSLETSAQSEANWAAEFAELEKERDSL------------- 580
Cdd:PRK03918 363 LYEEAKAKKEE-----LERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 581 --VSGAA----HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkaaEQVIqdalnqLEEPPLISCAGSA 654
Cdd:PRK03918 438 cpVCGRElteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------EKVL------KKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 655 DHLLSTVTSISSC-IEQLEKSWSQYLACPE-------DISGLLHSITLLAHLTSDAIAhgattCLRAPPEPADSLTEACK 726
Cdd:PRK03918 503 EQLKELEEKLKKYnLEELEKKAEEYEKLKEkliklkgEIKSLKKELEKLEELKKKLAE-----LEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 727 QYGRETLAYLASLEEE-GSLENADSTAMRncLSKIKAIGEELLPRgLDIKQEELgDLVDKEMAATSAAIETATARIEEML 805
Cdd:PRK03918 578 ELEELGFESVEELEERlKELEPFYNEYLE--LKDAEKELEREEKE-LKKLEEEL-DKAFEELAETEKRLEELRKELEELE 653
|
..
gi 206729937 806 SK 807
Cdd:PRK03918 654 KK 655
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
362-623 |
2.64e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 61.18 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 362 FNSQNGVNKDekdhLIERLYREISGLKAQLENMKtesQRVVLQLKgHVSELEA----DLAEQQHLRQQAADDCEFLRAEL 437
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQ---QQIKTYNK-NIEEQRKkngeNIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 438 DELRRQREDTEKAQRSLSEIERKAQaneQRYSKLKEKYsELVQNHADLLRKNAEV---TKQVSMARQAQVDLEREKKELE 514
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLN---TAAAKIKSKI-EQFQKVIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 515 DSLERISDQgqrktQEQLEVLESlkqELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL 594
Cdd:PHA02562 313 HSLEKLDTA-----IDELEEIMD---EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|....*....
gi 206729937 595 RKELQDTQLKLASTEESmcqlaKDQRKML 623
Cdd:PHA02562 385 QDELDKIVKTKSELVKE-----KYHRGIV 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
387-577 |
2.82e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 387 LKAQLENMKTESQRVVLQLKGHVSELEADLAE---QQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLsEIERKAQA 463
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 464 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELA 543
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|....
gi 206729937 544 TSQRELQVLQGSLETSAQSEANWAAEFAELEKER 577
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
42-126 |
5.84e-09 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 54.97 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYR 118
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
....*...
gi 206729937 119 NELSDMSR 126
Cdd:cd03564 83 GHIFNLSN 90
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
383-644 |
7.42e-09 |
|
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: 60.19 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 383 EISGLKAQLE---NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIER 459
Cdd:pfam01576 244 ELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 460 KaqaNEQRYSKLKEKYSELVQNH----ADLLRKNA----EVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQ 531
Cdd:pfam01576 324 K---REQEVTELKKALEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL--------QAE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 532 LEVLESLKQELATSQR----ELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 607
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKklegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
250 260 270
....*....|....*....|....*....|....*...
gi 206729937 608 TEEsmcQLAKDQRKMLLVGSRKAAEQVIQDAL-NQLEE 644
Cdd:pfam01576 473 TQE---LLQEETRQKLNLSTRLRQLEDERNSLqEQLEE 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
431-612 |
8.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 431 EFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREK 510
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 511 KELEDSLERISDQGQRKTQEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAElekERDSLVSGAAHREEE 590
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVEREL 767
|
170 180
....*....|....*....|..
gi 206729937 591 LSALRKELQDTQLKLASTEESM 612
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-605 |
2.67e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 361 NFNSQNGV---NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEadlaEQQHLRQQAADDCEFLRAEL 437
Cdd:TIGR04523 222 ELKKQNNQlkdNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 438 DELRRQRE---------DTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLER 508
Cdd:TIGR04523 298 SDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 509 EKKELEDSLE----RISD-----QGQRKTQEQLEV-LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 578
Cdd:TIGR04523 378 ENQSYKQEIKnlesQINDleskiQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
250 260
....*....|....*....|....*..
gi 206729937 579 SLVSGAAHREEELSALRKELQDTQLKL 605
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
381-599 |
4.69e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 381 YREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtekaqrslSEI 457
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR----------VDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 458 ERKAQANEQRYSKLKEKYSELVqnhADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQG--------QRKTQ 529
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNreeaeewyQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 530 E-QLEV------LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELE----KERDSLVSGAAHREEELSALRKEL 598
Cdd:pfam00038 200 ElQQAAarngdaLRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEM 279
|
.
gi 206729937 599 Q 599
Cdd:pfam00038 280 A 280
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-552 |
4.90e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHL--IERLYREISGLKAQ---LENMKT-----ESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDE 439
Cdd:COG4913 248 REQIELLepIRELAERYAAARERlaeLEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 440 LRRQR------------EDTEKAQRSLSEIERKAQANEQRYSKLK-------EKYSELVQNHADLL----RKNAEVTKQV 496
Cdd:COG4913 328 LEAQIrgnggdrleqleREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLealeEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 206729937 497 SMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVL 552
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
411-594 |
4.98e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 411 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 491 EVTKQVSMARQAQVDLEREKKELE----------DSLERISDQ-GQrkTQEQLEVLESLKQELATSQRELQVLQGSLETS 559
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsGE--EFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
170 180 190
....*....|....*....|....*....|....*
gi 206729937 560 AQSeanwaaefaeLEKERDSLVSGAAHREEELSAL 594
Cdd:PRK04863 654 KQA----------LDEEIERLSQPGGSEDPRLNAL 678
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
425-643 |
8.88e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 425 QAADDCEFLRAELDELRRQREDTEKAQR---SLSEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAEVTKQVSMARQ 501
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 502 AQVDLEREKKELEDSLERISDQGQRKTQEQlEVLESLKQELATSQ-RELQVLQGSLETSAQSEANWAAEFAELEKERDSL 580
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206729937 581 VSGAAHREEELSALRKELQDTQLKLASTEESmCQLAKDQRKMLLVGSRKAAEQvIQDALNQLE 643
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEA-LEEALAEAEAALRDLRRELRE-LEAEIASLE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
363-602 |
1.77e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 363 NSQNGVNKDEkdhlIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCE----------F 432
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 433 LRAELDELRRQREDTEKAQRSLS-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSMARQAQVDLER 508
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 509 EKKELEDSLERISDQ----GQRKTQEQLE-VLESLKQELAtsqrELQVLQGSLEtSAQSEANwaAEFAELEKERDSLVSG 583
Cdd:TIGR04523 532 EKKEKESKISDLEDElnkdDFELKKENLEkEIDEKNKEIE----ELKQTQKSLK-KKQEEKQ--ELIDQKEKEKKDLIKE 604
|
250
....*....|....*....
gi 206729937 584 AAHREEELSALRKELQDTQ 602
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAK 623
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
410-632 |
1.90e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 410 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEkaqRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN 489
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 490 AEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELAT---SQRELQVLQGSLETSAQSEANW 566
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 567 AAEFAELEK---ERDSLVS-------------GAAHREE-ELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRK 629
Cdd:pfam07888 191 SKEFQELRNslaQRDTQVLqlqdtittltqklTTAHRKEaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
...
gi 206729937 630 AAE 632
Cdd:pfam07888 271 QAE 273
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
377-608 |
3.33e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQrvVLQLKGHVSELEADLAEqqhLRQQAADdcefLRAELDELRRQREDTEKAQRSLSE 456
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSE---LESQLAE----ARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 IERKAQANEQrYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqVDLEREKKELEDSLERISDQGQRKTQEQLEVLE 536
Cdd:COG3206 255 ALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729937 537 SLKQELatsQRELQVLQGSLETSAQSEAnwaaEFAELEKERDSLvsgaahrEEELSALRKELQDTQLKLAST 608
Cdd:COG3206 327 AREASL---QAQLAQLEARLAELPELEA----ELRRLEREVEVA-------RELYESLLQRLEEARLAEALT 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
433-617 |
4.00e-07 |
|
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: 54.30 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 433 LRAELDELRRQREDTEKAQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK 511
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 512 ELEDSLERISDQGQRKTQEQLEVLES-----------LKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL 580
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGELEAeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190
....*....|....*....|....*....|....*..
gi 206729937 581 VSGAAHREEELSALRKELQDTQLKLASTEESMCQLAK 617
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
376-621 |
4.69e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 376 LIERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQ-AADDCEFLRAELDELRRQREDTEKAQ 451
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLrqqLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 452 RSLSEIERKA---QANEQRYSKLKEKYSELVQNHaDLLRKNAEVTKQVsMARQAQ------VDLEREKKELEDSLERISD 522
Cdd:COG3096 917 KALAQLEPLVavlQSDPEQFEQLQADYLQAKEQQ-RRLKQQIFALSEV-VQRRPHfsyedaVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 523 QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-----REEELSALRKE 597
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARirrdeLHEELSQNRSR 1074
|
250 260
....*....|....*....|....
gi 206729937 598 LQDTQLKLASTEESMCQLAKDQRK 621
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-578 |
6.37e-07 |
|
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: 53.53 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 383 EISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 462
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 463 ANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEqlevLESLKQEL 542
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDRVEKEL 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 206729937 543 ATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 578
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-644 |
7.36e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 443 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD 522
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 523 QGQRKTQEQLEVLESL--------------KQELATSQRELQVLQGSLETSAQSEANWAAEFAEL-------EKERDSLV 581
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalraelEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206729937 582 SGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEE 644
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL------QQEAEELEALIARLEA 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
389-644 |
8.18e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 389 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADdCEFLRAELDELRRQREDTEKA---------QRSLSEIER 459
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahIKAVTQIEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 460 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLevLESLK 539
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH--IHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 540 QELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVsgAAHREEELSALRKELQdtqlKLASTEESMCQLAKDQ 619
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA--HAKKQQELQQRYAELC----AAAITCTAQCEKLEKI 459
|
250 260
....*....|....*....|....*
gi 206729937 620 RKMLLVGSRKAAEQVIQDALNQLEE 644
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQ 484
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
370-561 |
8.43e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHvsELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEK 449
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRslseieRKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQ 529
Cdd:pfam17380 482 EKR------DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190
....*....|....*....|....*....|..
gi 206729937 530 EQLEVLESLKQELATSQRELQVLQGSLETSAQ 561
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-603 |
1.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 411 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQRE------DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQN 481
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 482 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLE--------------VLESLKQELATSQR 547
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavereLRENLEERIDALRA 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 548 ELQVLQGSLEtSAQSEAN--WAAEFAEL----------EKERDSLV-SGAAHREEELSALRKELQDTQL 603
Cdd:COG4913 781 RLNRAEEELE-RAMRAFNreWPAETADLdadleslpeyLALLDRLEeDGLPEYEERFKELLNENSIEFV 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-644 |
1.20e-06 |
|
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: 52.76 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 432 FLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSelvqnhaDLLRKNAEVTKQVSMARQaqvDLEREKK 511
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQ---EEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 512 ELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLETSAQSEANwaAEFAELEKERDSLVSGAAHREEEL 591
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 206729937 592 SALRKELQDTQLKLASTEESMCQLakdQRKMLLVGSRKAAEQVIQDALN-QLEE 644
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIEKEIENLNgKKEE 865
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-651 |
1.36e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKGHVSELEAdlAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQR 467
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 468 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERISDQGQRKTQEQLEVLESLK-QELATSQ 546
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 547 RELQVLQGSLETSAQSEANWAAEFA-ELEKERDSLVSGAAHREEELSA--LRKElQDTQLKLASTEEsmcqlAKDQRKML 623
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAeeAKKA-EEAKIKAEELKK-----AEEEKKKV 1635
|
250 260
....*....|....*....|....*....
gi 206729937 624 LVGSRKAAEQVIQ-DALNQLEEPPLISCA 651
Cdd:PTZ00121 1636 EQLKKKEAEEKKKaEELKKAEEENKIKAA 1664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
374-643 |
1.66e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 374 DHLIERL---YREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 450
Cdd:pfam15921 415 DHLRRELddrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QR-------SLSEIERKAQANEQRYSKLKE----KYSEL--VQNHADLLRkNAEV---TKQVSMARQAQVdLEREKKELE 514
Cdd:pfam15921 495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhLKNEGDHLR-NVQTeceALKLQMAEKDKV-IEILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 515 DSLERISDQGQ-------RKTQEQLEV---------LESLKQELATSQRELQVLQGSLETSAQSEANWAAE----FAELE 574
Cdd:pfam15921 573 NMTQLVGQHGRtagamqvEKAQLEKEIndrrlelqeFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIK 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 575 KERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMcQLAKDQRKMLLVGSRKAAEQViQDALNQLE 643
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQT-RNTLKSME 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-601 |
1.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 382 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAAD---DCEFLRAELDELRRQREDTEKAQRSLSEIe 458
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNE- 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 459 rKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELE---DSL-ERISDQGQRKTQEQLEV 534
Cdd:TIGR02168 882 -RASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLqERLSEEYSLTLEEAEAL 959
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 535 LESLKQELATSQRELQVLQGSLEtsAQSEANWAA--EFAELEKERDSLvsgaAHREEELSALRKELQDT 601
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIK--ELGPVNLAAieEYEELKERYDFL----TAQKEDLTEAKETLEEA 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
376-644 |
1.71e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 376 LIERLYREISGLKA-------QLENMKTESQ-RVVLQLKGH-------VSELEADLAEQQHLRQQAADDCEFLRAELDEL 440
Cdd:pfam15921 225 ILRELDTEISYLKGrifpvedQLEALKSESQnKIELLLQQHqdrieqlISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 441 RRQ-REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQN-HADLLRKNAEVTKqvsmARQAQVDLEREKKELEDSLE 518
Cdd:pfam15921 305 QEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 519 R-ISDQGQRKTQEQLE----------------VLESLKQELATSQRELQVLQGSLET-SAQSEANWAAEFAELEKERDSL 580
Cdd:pfam15921 381 KlLADLHKREKELSLEkeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 206729937 581 vsgaahreEELSALRKELQDTQLKLASTEESMCqlakdQRKMLLvgsrKAAEQVIQDALNQLEE 644
Cdd:pfam15921 461 --------EKVSSLTAQLESTKEMLRKVVEELT-----AKKMTL----ESSERTVSDLTASLQE 507
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
393-635 |
1.71e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 393 NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDEL------RRQREDTEKAQRslSEIERKAQ--AN 464
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKareverRRKLEEAEKARQ--AEMDRQAAiyAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 465 EQRYSKLKEKYSELVQNHadllrknaEVTKQVSMARQAQVDLEREKKEledSLERISDQGQRKTQEQLEVLESL-KQELA 543
Cdd:pfam17380 339 QERMAMERERELERIRQE--------ERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAArKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 544 TSQRELQVLQGSLETS---AQSEANWAAEFAELEKER----DSLVSGAAHREEELSALRKELQDTQLK--LASTEESMCQ 614
Cdd:pfam17380 408 EEERQRKIQQQKVEMEqirAEQEEARQREVRRLEEERaremERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRK 487
|
250 260
....*....|....*....|.
gi 206729937 615 LAKDQRKMLLVGSRKAAEQVI 635
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAM 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-644 |
1.86e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKGHVSEL-EADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRsLSEIERKAQ 462
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 463 ANEQRYSKLKEKYSELVQ----NHADLLRKNAEVTK--QVSMARQAQVDLER--------------EKKELEDSLERISD 522
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKaeekKKADELKKAEELKKaeEKKKAEEAKKAEEDknmalrkaeeakkaEEARIEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 523 QGQRKTQE-QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 601
Cdd:PTZ00121 1604 EKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 206729937 602 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 644
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
440-644 |
2.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 440 LRRQREDTEKAQRSLSE----IERKAQANEQRYSKLKEKYS--ELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKEL 513
Cdd:COG3206 166 LELRREEARKALEFLEEqlpeLRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 514 EDSLERISDQGQRKTQEQleVLESLKQELATSQRELQVLQGSL-----------ETSAQSEANWAAEFAELEKERDSLVS 582
Cdd:COG3206 246 RAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729937 583 GAAHREEELsalRKELQDTQLKLASTEESMCQLAKDQRKmllvgsRKAAEQVIQDALNQLEE 644
Cdd:COG3206 324 ALQAREASL---QAQLAQLEARLAELPELEAELRRLERE------VEVARELYESLLQRLEE 376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-644 |
2.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRSLSEIERKAQA 463
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 464 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQA-QVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQ-- 540
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKad 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 541 EL--ATSQRELQVLQGSLETSAQSEANWAAEF---------AELEKERDSLVSGAAHREEE--LSALRKELQDTQLKLAS 607
Cdd:PTZ00121 1514 EAkkAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEAR 1593
|
250 260 270
....*....|....*....|....*....|....*...
gi 206729937 608 TEESMcQLAKDQRKMLLVGSRKAAEQVIQ-DALNQLEE 644
Cdd:PTZ00121 1594 IEEVM-KLYEEEKKMKAEEAKKAEEAKIKaEELKKAEE 1630
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
411-594 |
3.43e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 411 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 491 EVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL-ESLKQELATSQRELQVLQGSLE---TSAQSEANW 566
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPA-----WLAAQDALERLrEQSGEALADSQEVTAAMQQLLErerEATVERDEL 649
|
170 180
....*....|....*....|....*...
gi 206729937 567 AAEFAELEKERDSLVSGAAHREEELSAL 594
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-554 |
3.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQ--AADDCEFLRAElDELRRQREDTEKAQ--RSLSEIERKAQA 463
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAA-EEAKKAEEDKKKAEeaKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 464 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ----VSMARQAQVDLEREKKELEdslERISDQGQRKTQEQLEVLESLK 539
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKK 1769
|
170
....*....|....*
gi 206729937 540 QELATSQRELQVLQG 554
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEE 1784
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
417-565 |
4.98e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.48 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 417 AEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEvtkqv 496
Cdd:PRK12705 46 AEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELE----- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 497 smarqaqvdLEREKKELEDSLERISdqGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAN 565
Cdd:PRK12705 121 ---------LEELEKQLDNELYRVA--GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-604 |
7.76e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELE------ADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQ 451
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAE----LPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 452 RSLSEIERKAQANEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRktQE 530
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 531 QLEVLESLKQEL--ATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSLVSGAAHREEELSALRKELQDTQ 602
Cdd:COG4717 241 LEERLKEARLLLliAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEE 320
|
..
gi 206729937 603 LK 604
Cdd:COG4717 321 LE 322
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
431-642 |
8.58e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 431 EFLRAELDELRRQR-EDTEKAQRSLSEIERKAQAnEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvdleRE 509
Cdd:TIGR00618 545 EDVYHQLTSERKQRaSLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL----LR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 510 KKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRElQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaaHREE 589
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSIRVLPKELLASRQLALQKMQ--------SEKE 690
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 206729937 590 ELSALRKELQDTQLKLASTEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 642
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREfNEIENASSSLGSDLAAREDALNQS 744
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
380-610 |
8.62e-06 |
|
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: 50.17 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 380 LYREISGLKAQLENMKTESQRVVLQLKGHVSELE----ADLAEQQHLRQQAADDCEFLRAEldELRRQREDTEK--AQRS 453
Cdd:pfam01576 55 LCAEAEEMRARLAARKQELEEILHELESRLEEEEersqQLQNEKKKMQQHIQDLEEQLDEE--EAARQKLQLEKvtTEAK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 454 LSEIERKAQANEQRYSKL-------KEKYSELVQNHADLLRKNAEVT----KQVSMARQAQVDLEREKK---ELED---S 516
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLskerkllEERISEFTSNLAEEEEKAKSLSklknKHEAMISDLEERLKKEEKgrqELEKakrK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 517 LERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWA----------AEFAE-LEKERDSLVSGAA 585
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireleaqiSELQEdLESERAARNKAEK 292
|
250 260
....*....|....*....|....*...
gi 206729937 586 HR---EEELSALRKELQDTQLKLASTEE 610
Cdd:pfam01576 293 QRrdlGEELEALKTELEDTLDTTAAQQE 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-605 |
8.82e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 414 ADLAEQQHLRQ-QAADdceflrAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK 488
Cdd:COG1579 1 AMPEDLRALLDlQELD------SELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 489 NAEVTKQVSMAR--------QAQVD-LEREKKELEDSLerisdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLEts 559
Cdd:COG1579 75 IKKYEEQLGNVRnnkeyealQKEIEsLKRRISDLEDEI-----------LELMERIEELEEELAELEAELAELEAELE-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 206729937 560 aQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKELQDTQLKL 605
Cdd:COG1579 142 -EKKAELDEELAELEAELEEL-------EAEREELAAKIPPELLAL 179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
383-611 |
8.93e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 383 EISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 462
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 463 ANEQRYSKLKEKYSELV--QNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSlerisdqgQRKTQEQLEVLESLKQ 540
Cdd:COG3883 93 RALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAK--------KAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729937 541 ELATSQRELQvlqgsletSAQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 611
Cdd:COG3883 165 ELEAAKAELE--------AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-611 |
9.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 425 QAADDCEFLRAELDELRRQREDtekAQRSLSEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQV---- 496
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERReelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 497 SMARQAQVDLER--------EKKELED------SLERISDQGQRKTQEQ---LEVLESLKQELATSQRELQVLQGSLEtS 559
Cdd:COG3883 90 ERARALYRSGGSvsyldvllGSESFSDfldrlsALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELE-A 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 206729937 560 AQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 611
Cdd:COG3883 169 AKAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
377-648 |
9.28e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVvlqlkghVSELEADLAEQQHLRQQaaddceflraeldeLRRQREDTEKAQRSLSE 456
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQL-------EEELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQLEVLE 536
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL--------QEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 537 SLKQELATSQRELQVLQgsLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLA 616
Cdd:COG4372 171 QELQALSEAEAEQALDE--LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270
....*....|....*....|....*....|..
gi 206729937 617 KDQRKMLLVGSRKAAEQVIQDALNQLEEPPLI 648
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
362-672 |
9.63e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 362 FNSQNGVNKDEKDHLIER---LYREISGLKAQLENMK---TESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRA 435
Cdd:PRK02224 340 HNEEAESLREDADDLEERaeeLREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 436 ELDELRRQREDTEKAQRSLSEIERKAQA-------------------------NEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 491 EVTKQVSMARQaqvdLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAA 568
Cdd:PRK02224 500 RAEDLVEAEDR----IERLEERREDLEELIAERRETieEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 569 EF----AELEKERDSL------VSGAAHREEELSALRKELQDTQL-------KLASTEESMCQLA---KDQRKMLLVGSR 628
Cdd:PRK02224 576 ELnsklAELKERIESLerirtlLAAIADAEDEIERLREKREALAElnderreRLAEKRERKRELEaefDEARIEEAREDK 655
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 206729937 629 KAAEQVIQDALNQLEEpplisCAGSADHLLSTVTSISSCIEQLE 672
Cdd:PRK02224 656 ERAEEYLEQVEEKLDE-----LREERDDLQAEIGAVENELEELE 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
499-657 |
1.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 499 ARQAQVDLEREKKELEDSLERISDQgqrktqeqlevLESLKQELATSQRELQVLQGsLETSAQSEANWAA---EFAELEK 575
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEER-----------LEALEAELDALQERREALQR-LAEYSWDEIDVASaerEIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 576 ERDSLVSGAAhreeELSALRKELQDTQLKLASTEESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 655
Cdd:COG4913 676 ELERLDASSD----DLAALEEQLEELEAELEELEEELDELKGEIGR--LEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
..
gi 206729937 656 HL 657
Cdd:COG4913 750 LL 751
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
382-618 |
1.62e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.27 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 382 REISGLKAQLENMKTESQRVV---LQLKGHVSELEADLAE----QQHLRQQAADD-----CEFLRAELDELRRQREDTEK 449
Cdd:pfam15905 94 KRLQALEEELEKVEAKLNAAVrekTSLSASVASLEKQLLEltrvNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEAKMK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqvdlerekKELEDSLERISDQGQRKT 528
Cdd:pfam15905 174 EVMAKQEgMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET--------------EKLLEYITELSCVSEQVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 529 QEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAE----LEKERDSLVSGAAHREEELSAlrkELQDTQLK 604
Cdd:pfam15905 240 KYKLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEkcklLESEKEELLREYEEKEQTLNA---ELEELKEK 315
|
250
....*....|....
gi 206729937 605 LASTEESMCQLAKD 618
Cdd:pfam15905 316 LTLEEQEHQKLQQK 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
371-612 |
1.68e-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: 49.05 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEAD--------------LAEQ----QHLRQQAADDCEF 432
Cdd:pfam10174 390 DVKERKINVLQKKIENLQEQLR----DKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKeriiERLKEQREREDRE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 433 LRAELDELRRQRED---------TEKAQRSLSEIERKAQANEQRYSKLKeKYSELVQNHADLLRKNAEVTKQVSMARQAQ 503
Cdd:pfam10174 466 RLEELESLKKENKDlkekvsalqPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 504 --VDLEREKKELEDSLERISDQGQRKTQE----QLEV---LESLKQ----------------ELATSQRELQVLQGSLET 558
Cdd:pfam10174 545 naEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerlLGILREvenekndkdkkiaeleSLTLRQMKEQNKKVANIK 624
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729937 559 SAQSE--ANWAAEFAELEKERDSLVSGAAHR--EEELSAL---RKELQDTQLKLASTEESM 612
Cdd:pfam10174 625 HGQQEmkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSSTQQSL 685
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
409-644 |
2.11e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 409 VSELEADLAEQQHLRQQAADDCEFLRA-------ELDELRRQREDTekaQRSLSEIERKAQANEQRYSKLkEKYSELVQN 481
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEArleaaeeEVDSLKSQLADY---QQALDVQQTRAIQYQQAVQAL-EKARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 482 hADLLRKNAEVTKQVSMARQAQVDleREKKELEDSLeRISDQGQRKTQEQLEVLESLKQELATSQ-----RELQVLQGSL 556
Cdd:COG3096 432 -PDLTPENAEDYLAAFRAKEQQAT--EEVLELEQKL-SVADAARRQFEKAYELVCKIAGEVERSQawqtaRELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 557 ETSAQSEANWAAEFAELEKERDSL-----------------VSGAAHREEELSALRKELQDTQLKLASTEESMCQL---- 615
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQqnaerlleefcqrigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELrqql 587
|
250 260 270
....*....|....*....|....*....|.
gi 206729937 616 --AKDQRKMLlvGSRKAAEQVIQDALNQLEE 644
Cdd:COG3096 588 eqLRARIKEL--AARAPAWLAAQDALERLRE 616
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
372-625 |
2.19e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 372 EKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEaDLAEQQHLRQQAADDCEFLRAELDelRRQREDTEKAQ 451
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 452 RsLSEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQR--- 526
Cdd:pfam05557 171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaat 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 527 ------KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQD 600
Cdd:pfam05557 250 lelekeKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
250 260
....*....|....*....|....*
gi 206729937 601 TQLKLASTEESMCQLakdQRKMLLV 625
Cdd:pfam05557 330 LNKKLKRHKALVRRL---QRRVLLL 351
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-633 |
2.48e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELeadlaeQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRS 453
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQrsqLEQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 454 -------LSEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVsm 498
Cdd:PRK04863 913 vqqhgnaLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKL-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 499 aRQAQVDLEREKKELEDSLERISDQGQRKTQeqleVLESLKQELATSQRELQVLQGSL-ETSAQSEANwAAEFAELEKER 577
Cdd:PRK04863 991 -RQRLEQAEQERTRAREQLRQAQAQLAQYNQ----VLASLKSSYDAKRQMLQELKQELqDLGVPADSG-AEERARARRDE 1064
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 206729937 578 dslvsgaahREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM--LLVGSRKAAEQ 633
Cdd:PRK04863 1065 ---------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerDYHEMREQVVN 1113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-607 |
2.94e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 382 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAadDCEFLRAELDEL-RRQREDTEKAQRSLSEIERK 460
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALlAEAGVEDEEELRAALEQAEE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 461 AQANEQRYSKLKEKyselVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKELEDSLERISDQgQRKTQEQLEVLESlKQ 540
Cdd:COG4717 397 YQELKEELEELEEQ----LEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELREE-LAELEAELEQLEE-DG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 206729937 541 ELATSQRELQVLqgsletsaqseanwAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 607
Cdd:COG4717 470 ELAELLQELEEL--------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
377-527 |
3.03e-05 |
|
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: 47.45 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAEQ------------QHLRQQAADDCEFLRAELDELRR 442
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 443 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVqnhadllrknAEVTKQVSMARQAQVDLEREKKELEDSLERISD 522
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLL----------ARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*
gi 206729937 523 QGQRK 527
Cdd:COG4942 235 EAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
379-598 |
3.36e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 379 RLYREISGLKAQLENMKTESQR-VVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrslseI 457
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----L 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 458 ERKAQANEQRYSKLKEKYSEL-VQNHADLLRKNAEvtkqvsmaRQAQVDLEREKKELEDSLERISDQGQRKT------QE 530
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALeTWYKRDLASLGVD--------PDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyQE 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 531 Q-LEVLESLKQELATSQRELQVLQGSLetsAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKEL 598
Cdd:pfam12128 804 TwLQRRPRLATQLSNIERAISELQQQL---ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
412-622 |
4.14e-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: 47.86 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 412 LEADLAEqqhLRQQAADdcefLRAELDELRRQREDTEKA-QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:pfam01576 213 LEGESTD---LQEQIAE----LQAQIAELRAQLAKKEEElQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 491 EVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEsLKQELATSQR--ELQV-------------LQGS 555
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE-LKKALEEETRshEAQLqemrqkhtqaleeLTEQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 206729937 556 LETSAQSEANW-------AAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM 622
Cdd:pfam01576 365 LEQAKRNKANLekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
388-692 |
4.25e-05 |
|
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: 47.73 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELD----ELRRQREDTEKAQRSLSEIERKAQA 463
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 464 NEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------MARQAQVDLER-------EKKELEDSLERISDQG---Q 525
Cdd:TIGR00606 770 QETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqEKQEKQHELDTVVSKIelnR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 526 RKTQEQLEVLESLKQELatsqRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL---RKELQDTQ 602
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetfLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 603 LKLASTEESMCQLAKDQRKML------LVGSRKAAEQVIQDalnqleeppliscaGSADHLLSTVTSISSCIEQLEKSWS 676
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIkekvknIHGYMKDIENKIQD--------------GKDDYLKQKETELNTVNAQLEECEK 991
|
330
....*....|....*.
gi 206729937 677 QYLACPEDISGLLHSI 692
Cdd:TIGR00606 992 HQEKINEDMRLMRQDI 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
378-621 |
4.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEI 457
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 458 ERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS------DQGQ 525
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELeerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkrlsrlEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 526 RKTQEQLEVLES-------LKQELATSQRELQVLQGSLETSAQSEANwAAEFAELEKERDSLVSGAAHRE-EELSALRKE 597
Cdd:PRK03918 324 NGIEERIKELEEkeerleeLKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKElEELEKAKEE 402
|
250 260
....*....|....*....|....
gi 206729937 598 LQDTQLKLASTEESMCQLAKDQRK 621
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKK 426
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
378-644 |
5.01e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREisgLKAQLENMKTESQRVVLQLKghVSELE-------ADLAEQQHLRQQAADDCEFLRAELDELRRQREDtekA 450
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMS--TDALEqeilqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE---A 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAQANEQRYSKLKEkyselvqnhADLLRKNAEVTkqvsmARQAQVDlerekkELEdsLERIS-DQGQRKTQ 529
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQ---------AQLTALQAESA-----ALKALVD------ELE--LAQLSaNNRQELAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 530 EQLEVLESLKQELatsQRELQVLQGSLETSAQSEANWAAEFAE-LEKERDSL---VSGAAHREEELSALrkelqdtqlkl 605
Cdd:PRK10929 208 LRSELAKKRSQQL---DAYLQALRNQLNSQRQREAERALESTElLAEQSGDLpksIVAQFKINRELSQA----------- 273
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 206729937 606 asteesmcqLAKDQRKMLLVGS--RKAAEQVIQ--DALNQLEE 644
Cdd:PRK10929 274 ---------LNQQAQRMDLIASqqRQAASQTLQvrQALNTLRE 307
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
370-643 |
6.46e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHLIErlyrEISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHL---RQQAADDCEFLRAELDELRRQRED 446
Cdd:COG1340 28 KEKRDELNE----ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 447 TEKAQRSLSEIERKAQANEQRY-----SKLKEKysELVQNHADlLRKNAEvtkqvsmARQAQVDLEREKKELEDSLERIS 521
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK--ELVEKIKE-LEKELE-------KAKKALEKNEKLKELRAELKELR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 522 DQgqrktqeqlevLESLKQELATSQRELQVLQGSLeTSAQSEANwaaefaELEKERDSLVSGAAHREEELSALRKELQDT 601
Cdd:COG1340 174 KE-----------AEEIHKKIKELAEEAQELHEEM-IELYKEAD------ELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 206729937 602 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLE 643
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
387-580 |
6.56e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 387 LKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQR-------SLSEIER 459
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 460 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL 535
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKE-----ANVSKFSSYKV 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 206729937 536 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSL 580
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTlsklkeESKKRSL 404
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-590 |
1.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHLIERLYREISGLKAQLENMKTESqrvVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEK 449
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQ--RK 527
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEerEK 708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 206729937 528 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE-ANWAAE-FAELEKERdslVSGAAHREEE 590
Cdd:PRK03918 709 AKKELEKLEKALERVEELREKVKKYKALLKERALSKvGEIASEiFEELTEGK---YSGVRVKAEE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
368-541 |
1.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 368 VNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAeqqhlRQQAADDCEFLRaELDELR-----R 442
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKkaeekK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 443 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERiSD 522
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEK-AE 1367
|
170
....*....|....*....
gi 206729937 523 QGQRKTQEQLEVLESLKQE 541
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKK 1386
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-644 |
1.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQLKghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSlseieRKAQANEQR 467
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 468 YSKLKEKYSELVQNhADLLRKNAEVT--KQVSMARQAqvdlEREKKELEDSleRISDQGQRKTQEQlevlesLKQELATS 545
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEENkiKAAEEAKKA----EEDKKKAEEA--KKAEEDEKKAAEA------LKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 546 QRELQVLQGSLEtsaqsEANWAAEFAELEKERDSLVSGAAHREEElsalrKELQDTQLKLASTEESMCQLAKDQRKMLLV 625
Cdd:PTZ00121 1702 KKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*....
gi 206729937 626 GSRKAAEQVIQDALNQLEE 644
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-644 |
1.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 361 NFNSQNGVNKDEKDHLIERLYREISGLKAQlENMKTESQRVVLQLKGHvseleadlAEQQHLRQQAADDCEFLRAELDEL 440
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKK--------AEEAKKADEAKKKAEEAKKKADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 441 RRQREDTEKAQRSlSEIERKAQANEQRYSKLKEKYSEL----VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDS 516
Cdd:PTZ00121 1335 KKKAEEAKKAAEA-AKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 517 LE--RISDQGQRKTQEQLEVLESLKQelATSQRELQVLQGSLETSAQSE-----------ANWAAEFAELEKERDSLVSG 583
Cdd:PTZ00121 1414 AAakKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEeakkkaeeakkADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 206729937 584 AAHREEELSALRKELQDT----QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 644
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
380-535 |
1.94e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 380 LYREISGLKAQLENmktesqrvVLQLKGHVSELEADLAEQQHLRQQAADDC----------EFLRAELDELRRQREDTEK 449
Cdd:COG3096 500 LLRRYRSQQALAQR--------LQQLRAQLAELEQRLRQQQNAERLLEEFCqrigqqldaaEELEELLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSE----IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEV------TKQVSMARQAQVDLEREKKELEDSLEr 519
Cdd:COG3096 572 QAAEAVEqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadSQEVTAAMQQLLEREREATVERDELA- 650
|
170
....*....|....*.
gi 206729937 520 isdQGQRKTQEQLEVL 535
Cdd:COG3096 651 ---ARKQALESQIERL 663
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
388-565 |
2.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 388 KAQLENMKTESQRVVLQlkghvSELEADLAEQQHLRQQaaddceflRAELDELRRQREDTEKAQRSlsEIERKAQANEQR 467
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-----AKKEAEAIKKEALLEA--------KEEIHKLRNEFEKELRERRN--ELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 468 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqRKTQEQL--EVLESLKQELats 545
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS----GLTAEEAkeILLEKVEEEA--- 167
|
170 180
....*....|....*....|
gi 206729937 546 QRELQVLQGSLETSAQSEAN 565
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEAD 187
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
370-608 |
2.18e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 370 KDEKDHLIERLYREISGL---KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELdelRRQRED 446
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLeleKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSEE 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 447 TEKAQRSLSEIERKAQAN-EQRYSKLKEKysELVQNHAdlLRKNAEVTKQVSmARQAQVD-LEREKKELEDSLERISDQG 524
Cdd:pfam15921 690 METTTNKLKMQLKSAQSElEQTRNTLKSM--EGSDGHA--MKVAMGMQKQIT-AKRGQIDaLQSKIQFLEEAMTNANKEK 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 525 QRKTQEQlevlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSalRKELQDTQLK 604
Cdd:pfam15921 765 HFLKEEK----NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ--RQEQESVRLK 838
|
....
gi 206729937 605 LAST 608
Cdd:pfam15921 839 LQHT 842
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
448-639 |
2.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 448 EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrK 527
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----S 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 528 TQEQLEVLEslkQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQdtQLKLAS 607
Cdd:COG4372 106 LQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAE 180
|
170 180 190
....*....|....*....|....*....|..
gi 206729937 608 TEESMCQLAKDQRKMLLVGSRKAAEQVIQDAL 639
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
446-609 |
2.37e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 446 DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLEREKKELED--S 516
Cdd:pfam00529 52 DPTDYQAALDSAEaqlAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQaavkAAQAQLAQAQIDLARrrV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 517 LERISDQGQRKTQEQLEVLESLKQELATSQRELqvlqgsletsAQSEANWAAEFAELEKERDSLVSGAahrEEELSALRK 596
Cdd:pfam00529 132 LAPIGGISRESLVTAGALVAQAQANLLATVAQL----------DQIYVQITQSAAENQAEVRSELSGA---QLQIAEAEA 198
|
170
....*....|...
gi 206729937 597 ELQDTQLKLASTE 609
Cdd:pfam00529 199 ELKLAKLDLERTE 211
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-607 |
2.38e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 414 ADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQAneqRYSKLKEKYSELVQNHADLLRKNAEVT 493
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR---RAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 494 KQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL 573
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
170 180 190
....*....|....*....|....*....|....
gi 206729937 574 EKERDSLVSGAAHREEELSALRKELQDTQLKLAS 607
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-540 |
2.38e-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: 45.43 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtEKAQRS 453
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRREL---EELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 454 LSEIERKAQANEQRYSKLKEKYSELVQ-NHADLLRKNAEVTKQVSMARQAQVDLEREKKEL----EDSLERISDQGQRK- 527
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYd 1003
|
170
....*....|....*
gi 206729937 528 --TQEQLEVLESLKQ 540
Cdd:TIGR02168 1004 flTAQKEDLTEAKET 1018
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
389-655 |
2.71e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 389 AQLENMKTESQRVVLQLkghvSELEADLAEQQHLRQQA------------ADDCEflrAELDELRRQREDtekAQRSLSE 456
Cdd:PRK04863 786 KRIEQLRAEREELAERY----ATLSFDVQKLQRLHQAFsrfigshlavafEADPE---AELRQLNRRRVE---LERALAD 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 IERKAQANEQRYSKLKEKYSEL--VQNHADLLRKN------AEVTKQVSMARQAQVDLEREKKELEdSLERIsdqgQRKT 528
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSALnrLLPRLNLLADEtladrvEEIREQLDEAEEAKRFVQQHGNALA-QLEPI----VSVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 529 QEQLEVLESLKQELATSQRELQVLQG---SLETSAQSEANWA-AEFAELEKERDSLVSGAAHREEELSALRKElQDTQLK 604
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTR-AREQLR 1009
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 206729937 605 lasteESMCQLAK-DQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 655
Cdd:PRK04863 1010 -----QAQAQLAQyNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
|
|
| F-BAR_FCHO1 |
cd07674 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ... |
450-612 |
2.94e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153358 [Multi-domain] Cd Length: 261 Bit Score: 43.78 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSEIERKAQANEQRYSKLKEKYSELVQN--HADLLRKNAEVTKqVSMARQAQVDLEREKKeLEDSLERISdqgqRK 527
Cdd:cd07674 20 STKELADFVRERAAIEETYSKSMSKLSKMASNgsPLGTFAPMWEVFR-VSSDKLALCHLELMRK-LNDLIKDIN----RY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 528 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaahREeelSALRKELQDTQLKLAS 607
Cdd:cd07674 94 GDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR---------RE---GVPQKELEKAELKTKK 161
|
....*
gi 206729937 608 TEESM 612
Cdd:cd07674 162 AAESL 166
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
377-602 |
2.96e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQ----QAADDCEFLRAELDELRRQREDTEKAQR 452
Cdd:pfam19220 74 LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEalerQLAAETEQNRALEEENKALREEAQAAEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 453 SLSEIERKAQANEQRYS-------KLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgq 525
Cdd:pfam19220 154 ALQRAEGELATARERLAlleqenrRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 526 rktqeQLEVLESLKQELATSQRELQVLQGSLETSAQ------------SEANWAAE--FAELEKERDSLVSGAAHREEEL 591
Cdd:pfam19220 232 -----LEEAVEAHRAERASLRMKLEALTARAAATEQllaearnqlrdrDEAIRAAErrLKEASIERDTLERRLAGLEADL 306
|
250
....*....|.
gi 206729937 592 SALRKELQDTQ 602
Cdd:pfam19220 307 ERRTQQFQEMQ 317
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
371-542 |
3.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLENMKTEsqrvVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdteka 450
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSmarQAQVDLEREKKELEDSLERISDQGQRKTQE 530
Cdd:COG1579 91 ---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|..
gi 206729937 531 QLEVLESLKQEL 542
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
511-672 |
3.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 511 KELEDSLERISDQGQRKTQ---EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL--VSGAA 585
Cdd:COG4717 49 ERLEKEADELFKPQGRKPElnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 586 HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSIS 665
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEEL------EELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
....*..
gi 206729937 666 SCIEQLE 672
Cdd:COG4717 203 ELQQRLA 209
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
377-632 |
3.59e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLA-----------EQQHLRQQAA-DDCEFLRAELDELR 441
Cdd:pfam05701 72 LESTKRLIEELKLNLERAQTEEAQAKQDSelaKLRVEEMEQGIAdeasvaakaqlEVAKARHAAAvAELKSVKEELESLR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 442 RQRED--------TEKAQRSLS---EIERKAQANEQRYSKLKEkysELVQNHADLLrkNAEVTK-QVSMAR-QAQVDLER 508
Cdd:pfam05701 152 KEYASlvserdiaIKRAEEAVSaskEIEKTVEELTIELIATKE---SLESAHAAHL--EAEEHRiGAALAReQDKLNWEK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 509 EKKELEDSLERISDQ------GQRKTQEQLEVLESLKQEL-----------------------------ATSQRELQVLQ 553
Cdd:pfam05701 227 ELKQAEEELQRLNQQllsakdLKSKLETASALLLDLKAELaaymesklkeeadgegnekktstsiqaalASAKKELEEVK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 554 GSLEtSAQSEANW---AAEF--AELEKERDSLVS----------GAAHREEELSALRKELQDTQLKLASTEESMCQLAkd 618
Cdd:pfam05701 307 ANIE-KAKDEVNClrvAAASlrSELEKEKAELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELP-- 383
|
330
....*....|....
gi 206729937 619 qrKMLLVGSRKAAE 632
Cdd:pfam05701 384 --KQLQQAAQEAEE 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
416-644 |
3.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 416 LAEQQHLRQQAADDCEfLRAELDELRRQREDTEKAQRSLSEIERKAQANEqryskLKEKYSELVQNHADLLRKNAEVTKQ 495
Cdd:COG4717 293 LAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDLSPEELLE-----LLDRIEELQELLREAEELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 496 VSMARQAQVdLEREKKELEDSLERISDQGQRKtQEQLEVLESLKQELATSQRELQVLQgsletSAQSEANWAAEFAELEk 575
Cdd:COG4717 367 ELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELE- 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 576 erdslvsgaahreEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkAAEQVIQDALNQLEE 644
Cdd:COG4717 439 -------------EELEELEEELEELREELAELEAELEQLEEDGELA-------ELLQELEELKAELRE 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
378-644 |
3.69e-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: 44.43 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREISGLKAQLENMKT--ESQRvvlQLKGHVSELEADLAEQQHLRQQAADDCEflraELDELRRQredTEKAQRSLS 455
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELriETQK---QTLGARDESIKKLLEMLQSKGLPKKSGE----EDWERTRR---IAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 456 EIERKAQANEQRYSKLKEKYSELVQNHADllRKNAEVTKQVSMARQAQV-DLEREKKELEDSLERISDQGQRKTQE---- 530
Cdd:pfam10174 196 HLEVLLDQKEKENIHLREELHRRNQLQPD--PAKTKALQTVIEMKDTKIsSLERNIRDLEDEVQMLKTNGLLHTEDreee 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 531 --QLEV-----------LESLKQELATSQRELQVLQGSLET--SAQSEANWAAEF------------AELEKERDSLVSG 583
Cdd:pfam10174 274 ikQMEVykshskfmknkIDQLKQELSKKESELLALQTKLETltNQNSDCKQHIEVlkesltakeqraAILQTEVDALRLR 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206729937 584 AAHREEELSALRKELQDTqlklasTEESMCQLA--KDQRKMLLVGSRKAaeQVIQDALNQLEE 644
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDL------TEEKSTLAGeiRDLKDMLDVKERKI--NVLQKKIENLQE 408
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
397-576 |
3.85e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 397 ESQRVVLQLKGHVSELEADLAeqqHLRQQAADDCEFLRAELDELRRQ-----------REDTEKAQRSLSEIERKAQANE 465
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsGEESQRGERILAYFGYLNQARQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 466 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLE-----REK--KELEDSLERisDQGQRKTQEQLEVleSL 538
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEqarneRKKtlTGLESSLQK--DQQQLSELRANES--RL 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 206729937 539 KQELATSQRELQvlqgsleTSAQSEANWAAEFAELEKE 576
Cdd:PRK11637 246 RDSIARAEREAK-------ARAEREAREAARVRDKQKQ 276
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
471-642 |
4.92e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 471 LKEKYSELVQNHADLLRKNAEVTKQVSMARQ----AQVDLEREKKELEDSLERISDQGQRKTQEQlevleslkQELATSQ 546
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKErykrDREQWERQRRELESRVAELKEELRQSREKH--------EELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 547 RELQVLQGSL--ETSAQSEANWA--AEFAELEKERDSLVSGAAHREEELS----------ALRKELQ----DTQLKLAST 608
Cdd:pfam07888 104 KELSASSEELseEKDALLAQRAAheARIRELEEDIKTLTQRVLERETELErmkerakkagAQRKEEEaerkQLQAKLQQT 183
|
170 180 190
....*....|....*....|....*....|....*
gi 206729937 609 EESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 642
Cdd:pfam07888 184 EEELRSLSKEfQELRNSLAQRDTQVLQLQDTITTL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-644 |
6.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 385 SGLKAQLEnmKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKA 461
Cdd:PRK02224 190 DQLKAQIE--EKEEKDLHERLNGLeseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 462 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESL 538
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 539 KQELATsqrelqvlqgsLETSAQsEANWAAefAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAkD 618
Cdd:PRK02224 348 REDADD-----------LEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-D 412
|
250 260 270
....*....|....*....|....*....|..
gi 206729937 619 QRKML------LVGSRKAAEQVIQDALNQLEE 644
Cdd:PRK02224 413 FLEELreerdeLREREAELEATLRTARERVEE 444
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
535-673 |
7.19e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 535 LESLKQELAT-SQRELQVLQ-----------GSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQ 602
Cdd:pfam09787 2 LESAKQELADyKQKAARILQskekliaslkeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729937 603 LKLASTEESMCQLAKDQRKMLLvgSRKAAEQVIQDALNQLEEppliSCAGSADHLLSTVTSISSCIEQLEK 673
Cdd:pfam09787 82 AQQQEEAESSREQLQELEEQLA--TERSARREAEAELERLQE----ELRYLEEELRRSKATLQSRIKDREA 146
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
372-644 |
7.24e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 372 EKDHLIERLYREISGLKAQLENMKTESQRVvLQLKGHVSELEADLAEQQHLRQqaaddcEFLRAELDELRRQREDTEKAQ 451
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALL------RKLQPEQDLQDVRLHLQQCSQ 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 452 R-SLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN-AEVTKQVSMARQAQVDLE--REKKELEDSLERISDQGQRK 527
Cdd:TIGR00618 640 ElALKLTALHALQLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 528 TQEQLEVLESLKQELATSQRELQVLQGSLetsaQSEANWAAEFAELEKERDSLVSGA--------AHREEELSALRKELQ 599
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKEL----MHQARTVLKARTEAHFNNNEEVTAalqtgaelSHLAAEIQFFNRLRE 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 206729937 600 DTQLKLASTEESMCQLAKDQRKMLLVGSRKAAeQVIQDALNQLEE 644
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEE 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-611 |
8.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 372 EKDHLIERLYREISGLKaQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQ 451
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 452 RSLSEIERkaqaNEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDqgQRKTQEQ 531
Cdd:PRK03918 221 EELEKLEK----EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 532 LEVLESLKQELATSQRELQVLQGSLEtsaqseanwaAEFAELEKERDSLVSgaahREEELSALRKELQDTQLKLASTEES 611
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEER 360
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
418-633 |
1.08e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 418 EQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK--- 494
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQ--LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskq 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 495 --QVSMARQAQVDLEREKKELEDSL-ERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFA 571
Cdd:pfam02463 259 eiEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729937 572 ELEKERDSLVSGAAHREEELSALRKElqdtQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQ 633
Cdd:pfam02463 339 ELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
376-539 |
1.08e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 376 LIERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAelDELRRQREDTEKAQRsls 455
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDP--TELDRAKEKLKKLLQ--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 456 EIERKaqaneqrysklkekyselVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERI---SDQGQRKTQEQL 532
Cdd:smart00787 219 EIMIK------------------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQL 280
|
....*..
gi 206729937 533 EVLESLK 539
Cdd:smart00787 281 KLLQSLT 287
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
438-644 |
1.12e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.22 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 438 DELRRQREDTEKAQRSLS----EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKEL 513
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREhlekEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQ-NLKGIKREL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 514 EDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSeANWAAEFAELEKERDSLVSGAAHREEELSA 593
Cdd:pfam18971 689 SDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQ 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 206729937 594 LRKELQDT------QLKLASTEESMCQLAKDQRKMllvGSRKAAEQVIQDALNQLEE 644
Cdd:pfam18971 768 AKSDLENSvkdviiNQKVTDKVDNLNQAVSVAKAM---GDFSRVEQVLADLKNFSKE 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-601 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 363 NSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRR 442
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 443 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD 522
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 523 QGQRKTQEQLEV----------LESLKQELATSQRELQVLqGSLetsaqseaNWAA--EFAELEKERDSLVSgaahREEE 590
Cdd:COG1196 740 ELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL-GPV--------NLLAieEYEELEERYDFLSE----QRED 806
|
250
....*....|.
gi 206729937 591 LSALRKELQDT 601
Cdd:COG1196 807 LEEARETLEEA 817
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
371-612 |
1.32e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLENMKTEsqrvvlqlkghVSELEADLAEQQHLRQQAADDCEFlrAELDEL-RRQREDTEK 449
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEK-----------IAEYTKSIDIKKATESLEEQLAAA--EAEQELeESKRETETG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHAdlLRKNAEvtkqvsmarqaqvDLEREKKELEDSLERISDQGQRKTQ 529
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE--LSKSSE-------------ELDSFKDTIESTKESLDEIPQNQRG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 530 EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKE-----RDSLVSGAAHREEELSALRKELQDTQLK 604
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvmREADEESQSRLEEAYDEINRSVRSKKED 482
|
....*...
gi 206729937 605 LASTEESM 612
Cdd:COG5185 483 LNEELTQI 490
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
373-551 |
1.34e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 373 KDHLIERLYREISGLKAQLENM--KTESQRVvlqlkghvsELEADLAEQQHLRQQAaddceflraeldelRRQREDTEKA 450
Cdd:PRK00409 500 PENIIEEAKKLIGEDKEKLNELiaSLEELER---------ELEQKAEEAEALLKEA--------------EKLKEELEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAqaneqrYSKLKEKYSELVQNhadlLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrktqE 530
Cdd:PRK00409 557 KEKLQEEEDKL------LEEAEKEAQQAIKE----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLN--------K 618
|
170 180
....*....|....*....|.
gi 206729937 531 QLEVLESLKQELATSQRELQV 551
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKV 639
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
397-562 |
1.37e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 397 ESQRVVLQLkghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLK 472
Cdd:COG1579 4 EDLRALLDL----QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAktelEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 473 EKYSElVQNH---ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQREL 549
Cdd:COG1579 80 EQLGN-VRNNkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 206729937 550 QVLQGSLETSAQS 562
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-622 |
1.49e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 372 EKDHLIERLyreisglKAQLENMktesqrvvLQLKG-HVSELEADLAEQQHLRQQAADDceflRAELDELRRQREdteKA 450
Cdd:pfam15921 559 EKDKVIEIL-------RQQIENM--------TQLVGqHGRTAGAMQVEKAQLEKEINDR----RLELQEFKILKD---KK 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 451 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 530
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 531 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKE---LQDTQLKLAs 607
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLS- 775
|
250
....*....|....*
gi 206729937 608 teESMCQLAKDQRKM 622
Cdd:pfam15921 776 --QELSTVATEKNKM 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
399-499 |
1.60e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 399 QRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEK 474
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|....*
gi 206729937 475 YSELVQNHADLLRKNAEVTKQVSMA 499
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-644 |
1.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 371 DEKDHLIERLYREISGLKAQLENMKTESQrvvlQLKGHVSELEADLAEQQHLR------------------------QQA 426
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIklkelaeqlkeleeklkkynleelEKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 427 ADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsmarqaqvDL 506
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 507 EREKKELEDSLER---ISDQGQRKtQEQLEVLESLKQELATSQRELQVLQGSLEtSAQSEANWAA------EFAELEKER 577
Cdd:PRK03918 591 EERLKELEPFYNEyleLKDAEKEL-EREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEkkyseeEYEELREEY 668
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 578 DSLvsgaahrEEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsRKAAEQV--IQDALNQLEE 644
Cdd:PRK03918 669 LEL-------SRELAGLRAELEELEKRREEIKKTLEKLKEELEER-----EKAKKELekLEKALERVEE 725
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
411-644 |
1.71e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 411 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLkEKYSElvqnhaDLLRKNA 490
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQA------DLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 491 EVTKQvSMARQaqvdlerEKKELEDSLERisdqgqRKTQEQLEVLEsLKQELATSQRELQVLQgsLETSAQSEANWAAEF 570
Cdd:PRK04863 363 RLEEQ-NEVVE-------EADEQQEENEA------RAEAAEEEVDE-LKSQLADYQQALDVQQ--TRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 571 AELEKERDSL-VSGAAHREEELSALRKELQDTQLKLAsTEESMCQLAKDQ--RKMLLVG------SRKAAEQVIQDALNQ 641
Cdd:PRK04863 426 AKQLCGLPDLtADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQfeQAYQLVRkiagevSRSEAWDVARELLRR 504
|
...
gi 206729937 642 LEE 644
Cdd:PRK04863 505 LRE 507
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
378-643 |
2.02e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 378 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEF--------LRAELDELRRQREDTEK 449
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSMARQAQVD--------------------LERE 509
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 510 KKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHR 587
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 206729937 588 EEELSALRKELQDTQLKLA-------STEESMCQLAKDQR--KMLLVGSRKAAEQVIQDALNQLE 643
Cdd:pfam12128 624 EEQLVQANGELEKASREETfartalkNARLDLRRLFDEKQseKDKKNKALAERKDSANERLNSLE 688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
461-643 |
2.17e-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: 42.35 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 461 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKTQEQLEVLESLKQ 540
Cdd:TIGR02168 632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRK 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 541 ELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEEsmcQLAKDQR 620
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE---ELAEAEA 782
|
170 180
....*....|....*....|...
gi 206729937 621 KmllvgsRKAAEQVIQDALNQLE 643
Cdd:TIGR02168 783 E------IEELEAQIEQLKEELK 799
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
366-552 |
2.35e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 366 NGVNKDEKDHLIER--LYREISGLKAQLENMKTESQRVVLQLKGHVSEleadlaEQQHLRQQAADDCEFLRAeLDELRRQ 443
Cdd:pfam00038 106 VGLRKDLDEATLARvdLEAKIESLKEELAFLKKNHEEEVRELQAQVSD------TQVNVEMDAARKLDLTSA-LAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 444 REdtEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNH----ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLER 519
Cdd:pfam00038 179 YE--EIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAkeeiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
|
170 180 190
....*....|....*....|....*....|...
gi 206729937 520 ISDQGQRKTQEQLEVLESLKQELATSQRELQVL 552
Cdd:pfam00038 257 QLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
435-604 |
2.39e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 435 AELDElRRQREDTEKAQRSLSEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtkqvsmaRQAQVDLEREKKELE 514
Cdd:COG1566 74 ARLDP-TDLQAALAQAEAQLAA----AEAQLARLEAELGAEAEIAAAEAQLAAAQAQL-------DLAQRELERYQALYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 515 DSLerISDQgqrktqeqleVLESLKQELATSQRELQVLQGSLEtSAQSEANWAAEFAELEKERDSLvsgaahrEEELSAL 594
Cdd:COG1566 142 KGA--VSQQ----------ELDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQVAQA-------EAALAQA 201
|
170
....*....|
gi 206729937 595 RKELQDTQLK 604
Cdd:COG1566 202 ELNLARTTIR 211
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
432-599 |
2.43e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 432 FLRAELDELRRQREDTEKAQ-RSLSEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNaEVTKQVSMarQAQVDLEREK 510
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQEL-QKRIRLLEKR-EAEAEEAL--REQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 511 KELEDSLERISDQGQRKTQEQLEVLESLKQELA--------------TSQRELQVLQGSLETSAQSEANWAAEFAELEKE 576
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSelrrqiqraelelqSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180
....*....|....*....|...
gi 206729937 577 RDSLvsgaAHREEELSALRKELQ 599
Cdd:pfam05557 162 QSSL----AEAEQRIKELEFEIQ 180
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-589 |
2.45e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKtesQRV-----VLQLKGHVSELEA--DLAEQQHLRQQaaddcefLRAELDELRRQREdteK 449
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRDAK---QQAfalteVVQRRAHFSYEDAaeMLAKNSDLNEK-------LRQRLEQAEQERT---R 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 450 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV--SMARQAQVDLEREKKELEDSLERISDQGQRK 527
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdsGAEERARARRDELHARLSANRSRRNQLEKQL 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729937 528 TQEQLEvLESLKQELATSQRELQVLQgslETSAQSEANWaaeFAELEKERDSLVSGAAHREE 589
Cdd:PRK04863 1084 TFCEAE-MDNLTKKLRKLERDYHEMR---EQVVNAKAGW---CAVLRLVKDNGVERRLHRRE 1138
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
434-549 |
3.69e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 434 RAELDE-LRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKE 512
Cdd:pfam20492 8 KQELEErLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 206729937 513 LEDSLERISDQGQRKTQEQlevlESLKQELATSQREL 549
Cdd:pfam20492 88 AQEEIARLEEEVERKEEEA----RRLQEELEEAREEE 120
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
376-644 |
4.52e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 376 LIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQ---QHLRQQAADD-----------CEFLRAELDEL- 440
Cdd:pfam07111 307 LLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQsqeQAILQRALQDkaaevevermsAKGLQMELSRAq 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 441 ---RRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS-----MARQ---AQVDLE-- 507
Cdd:pfam07111 387 earRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglMARKvalAQLRQEsc 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 508 ---------------------REKKELEDSLE-----------RISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGS 555
Cdd:pfam07111 467 pppppappvdadlsleleqlrEERNRLDAELQlsahliqqevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQ 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 556 LETSAQSEANWAAEFAELEKE--RDSLVSGAAHRE---EELSALRKELQDTQLKLastEESMCQLAKDQRKMLLVGSRKA 630
Cdd:pfam07111 547 LEVARQGQQESTEEAASLRQEltQQQEIYGQALQEkvaEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAT 623
|
330
....*....|....
gi 206729937 631 AEQVIQDALNQLEE 644
Cdd:pfam07111 624 QEKERNQELRRLQD 637
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
365-644 |
4.89e-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: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 365 QNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQR 444
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 445 EDTEK------------------AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDL 506
Cdd:pfam01576 450 NEAEGkniklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 507 EREKKELEDSLERIsDQGQRKTQEQLEVL------------------ESLKQEL------ATSQRE----LQVLQGSLET 558
Cdd:pfam01576 530 KKKLEEDAGTLEAL-EEGKKRLQRELEALtqqleekaaaydklektkNRLQQELddllvdLDHQRQlvsnLEKKQKKFDQ 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 559 SAQSEANWAAEFAElekERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKML------------LVG 626
Cdd:pfam01576 609 MLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgknvheLER 685
|
330
....*....|....*...
gi 206729937 627 SRKAAEQVIQDALNQLEE 644
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEE 703
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
372-557 |
4.89e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 372 EKDHLIERLYREISGLKAQLENMKTESQrvvlqlkghvseleadLAEQQHLRQQAA-DDCEFLRAEL--------DELRR 442
Cdd:pfam15619 8 ARLHKIKELQNELAELQSKLEELRKENR----------------LLKRLQKRQEKAlGKYEGTESELpqliarhnEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 443 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL-LRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS 521
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELEN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 206729937 522 DQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE 557
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
377-628 |
6.16e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 377 IERLYREISGLKAQLENMKTESQRvvLQ-LKGHVSELEAdlaeqQHLRQQAADDCEflrAELDELRRQREDtekAQRSLS 455
Cdd:COG3096 787 LEELRAERDELAEQYAKASFDVQK--LQrLHQAFSQFVG-----GHLAVAFAPDPE---AELAALRQRRSE---LERELA 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 456 EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNA------EVTKQVSMARQAQVDLEREKKELEdSLERI------- 520
Cdd:COG3096 854 QHRAQEQQLRQQLDQLKEQLQLLnkLLPQANLLADETladrleELREELDAAQEAQAFIQQHGKALA-QLEPLvavlqsd 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 521 -------------SDQGQRKTQEQLEVLESLKQ-----------ELATSQREL-QVLQGSLE--TSAQSEANWA-----A 568
Cdd:COG3096 933 peqfeqlqadylqAKEQQRRLKQQIFALSEVVQrrphfsyedavGLLGENSDLnEKLRARLEqaEEARREAREQlrqaqA 1012
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 569 EFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSR 628
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNR 1072
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
436-597 |
6.50e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 436 ELDELRRQ-----------REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqv 504
Cdd:PRK09039 54 ALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 505 dlerekkeleDSLERISDQGQRktqeQLEVLeslKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKErdsLVSGA 584
Cdd:PRK09039 126 ----------DSEKQVSARALA----QVELL---NQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR---LNVAL 185
|
170
....*....|...
gi 206729937 585 AHREEELSALRKE 597
Cdd:PRK09039 186 AQRVQELNRYRSE 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
369-605 |
6.89e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 369 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFlraeldELRRQREDTE 448
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE------EQKLEKLAEE 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 449 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK-NAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRK 527
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKeKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 528 TQ------EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 601
Cdd:pfam02463 935 EEpeelllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
....
gi 206729937 602 QLKL 605
Cdd:pfam02463 1015 TCQR 1018
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
389-601 |
7.64e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.24 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 389 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE------------ 456
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEaekaadesergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 457 --IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMarqAQVDLEREKKELEDSLERISD--QGQRKTQEQL 532
Cdd:pfam00261 81 kvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVV---VEGDLERAEERAELAESKIVEleEELKVVGNNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 533 EVLESlkQELATSQRE------LQVLQGSLEtsaqsEANWAAEFAE-----LEKERDSLVSGAAHREEELSALRKELQDT 601
Cdd:pfam00261 158 KSLEA--SEEKASEREdkyeeqIRFLTEKLK-----EAETRAEFAErsvqkLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
409-564 |
7.94e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 38.15 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 409 VSELEADLAEQQHLRQQAAddceflraeldeLRRQREDTEKAQRSLSEIERKAQANEQRYsklkekYSELvQNHADLLRK 488
Cdd:pfam07321 7 VKHLREDRAEKAVKRQEQA------------LAAARAAHQQAQASLQDYRAWRPQEEQRL------YAEI-QGKLVLLKE 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206729937 489 NAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEA 564
Cdd:pfam07321 68 LEKVKQQVALLRENEADLEKQVAEARQQLEAEREalrQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELEEF 146
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
435-647 |
8.84e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 435 AELDELRRQREDTEKAQRSLsEIERKAQANEQRYSKLKEKYselvqnhaDLLRK----NAEVTKQVSMARQAQVDLEREK 510
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENL-ELDEAEEALEEIEERIDQLY--------DLLEKevdaKKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 511 KELEDSLERIsDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE--TSAQSE-----ANWAAEFAELEKERDSLVSG 583
Cdd:pfam06160 308 KELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEekEVAYSElqeelEEILEQLEEIEEEQEEFKES 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729937 584 AAH-REEELSAlRKELQDTQLKLASTEESMCQ-----LAKDQRKMLLVGSRKaaeqvIQDALNQLEEPPL 647
Cdd:pfam06160 387 LQSlRKDELEA-REKLDEFKLELREIKRLVEKsnlpgLPESYLDYFFDVSDE-----IEDLADELNEVPL 450
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|
| |
