|
Name |
Accession |
Description |
Interval |
E-value |
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
780-978 |
1.87e-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: 1.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 780 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 859
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 860 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 938
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462613986 939 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 978
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
7-272 |
1.23e-93 |
|
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: 298.06 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 7 TVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 85
Cdd:pfam07651 3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 86 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 164
Cdd:pfam07651 83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 165 FQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 238
Cdd:pfam07651 161 QKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
|
250 260 270
....*....|....*....|....*....|....
gi 2462613986 239 FYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 272
Cdd:pfam07651 240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
1.38e-83 |
|
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: 264.98 E-value: 1.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 6 MTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 85
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 2462613986 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 119
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
3.82e-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: 225.62 E-value: 3.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 6 MTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 85
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 2462613986 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 119
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 ... |
830-976 |
1.76e-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: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 830 KNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVN 909
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 910 QATAGVVASTISGKSQIEE--TDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYE 976
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
8-119 |
3.36e-56 |
|
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: 189.69 E-value: 3.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 8 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNEL 87
Cdd:cd17014 3 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNI 82
|
90 100 110
....*....|....*....|....*....|..
gi 2462613986 88 SDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 119
Cdd:cd17014 83 RETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
6-119 |
2.68e-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: 147.14 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 6 MTVSINKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAVLCWKFCHVFHKLLRDGHP--NVLKDSLR 82
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462613986 83 -YRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 119
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
4-126 |
3.31e-38 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 138.92 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 4 SKMTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVLKDSL 81
Cdd:smart00273 1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462613986 82 RYRNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTKMEYHTKNPRFP 126
Cdd:smart00273 81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
448-546 |
3.02e-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: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 448 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 527
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 2462613986 528 SEANWAAEFAELEKERDSL 546
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
6-119 |
1.83e-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: 107.78 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 6 MTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 85
Cdd:cd17007 1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2462613986 86 ELSDMSRMW-GHLSEGYGQLCSIYLKLLRTKMEYH 119
Cdd:cd17007 81 WLESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
336-610 |
7.57e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 414
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 415 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 494
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 495 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 574
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462613986 575 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 610
Cdd:COG1196 455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-610 |
2.49e-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: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAeqqhlrqqaADDCEFLRAELDELRRQREDT----EKA 416
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALL---------VLRLEELREELEELQEELKEAeeelEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLErisdQGQRKTQE 496
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----ELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 497 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 576
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270
....*....|....*....|....*....|....
gi 2462613986 577 SMCQLAKDQRKMLlvgsRKAAEQVIQDALNQLEE 610
Cdd:TIGR02168 415 RRERLQQEIEELL----KKLEEAELKELQAELEE 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-576 |
3.21e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 416
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 496
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 497 QLEVLESLKQELATSQRELQvlqgSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 576
Cdd:COG1196 423 LEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-588 |
1.20e-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: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 335 NKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDte 414
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 415 kAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK-------ELEDSLERIS 487
Cdd:TIGR02168 335 -LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneieRLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 488 DQGQRKTQEQLEVLESL--------KQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSlvsgAAHREEELSA 559
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA----AERELAQLQA 489
|
250 260
....*....|....*....|....*....
gi 2462613986 560 LRKELQDTQLKLASTEESMCQLAKDQRKM 588
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-610 |
1.28e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQR----VVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQR 418
Cdd:COG1196 188 LERLEDILGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEE----LEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 419 S----LSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgqrkT 494
Cdd:COG1196 264 EleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----L 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 495 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 574
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462613986 575 EESmcQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 610
Cdd:COG1196 420 EEE--LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-556 |
3.79e-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: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 422
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 423 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVD-LEREKKELEDSLERISDQGQRKtQEQLEVL 501
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERAEL-EALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462613986 502 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEE 556
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-610 |
6.71e-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: 70.09 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 348 REISGLKAQLEnmktesqrvvlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEK-AQRSLSEIERK 426
Cdd:TIGR02168 677 REIEELEEKIE-----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 427 AQANEQRYSKLKEKYSELVQNHADL--LRKNAEVTKQVSMARQAQVD-LEREKKELE---DSLERISDQGQRKTQEQLEV 500
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALRealDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 501 LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-------REEELSALRKELQDTQLKLAS 573
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRE 905
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462613986 574 TEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQLEE 610
Cdd:TIGR02168 906 LESKRSELRRElEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-573 |
2.03e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLkAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 416
Cdd:COG1196 281 LELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 496
Cdd:COG1196 360 ---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613986 497 QLEVLESLKQELATSQRELQVLQGSLETSAQSEanwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 573
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-554 |
4.95e-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: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 422
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 423 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLE 502
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 503 SLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHRE 554
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-654 |
5.59e-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: 67.02 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA---- 416
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAQANEQRYSKLKEKYSEL--------VQNHADLLRK-NAEVTKQVSMARQAQVDLER---EKKELEDSLE 484
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKlEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 485 RISDQgQRKTQEQLEvleSLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKEL 564
Cdd:TIGR02169 837 ELQEQ-RIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-------EAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 565 QDTQLKLasteesmcqlakdQRKMLLVGSRKAAEQVIQDALNQLEEPPliscagsadhllSTVTSISSCIEQLEKSWSQY 644
Cdd:TIGR02169 906 EELEAQI-------------EKKRKRLSELKAKLEALEEELSEIEDPK------------GEDEEIPEEELSLEDVQAEL 960
|
330
....*....|
gi 2462613986 645 LACPEDISGL 654
Cdd:TIGR02169 961 QRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-610 |
3.69e-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: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 335 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQlkghVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdte 414
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 415 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK----------------- 477
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieele 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 478 ----ELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRElqvlqgsletsaqseanWAAEFAELEKERDSLvsgaahr 553
Cdd:TIGR02168 866 elieELESELEALLNE-RASLEEALALLRSELEELSEELRE-----------------LESKRSELRRELEEL------- 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 554 EEELSALRKELQDTQLKLASTEEsmcQLAKDQRKML-----LVGSRKAAEQVIQDALNQLEE 610
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLeeaeaLENKIEDDEEEARRRLKRLEN 979
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
376-597 |
9.62e-10 |
|
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: 61.70 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 376 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL 451
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 452 LRKnaevtkQVSMARQAQVDLEREKKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE 529
Cdd:COG4942 110 LRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462613986 530 ANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAA 597
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-610 |
1.46e-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: 62.38 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 400 RAELDELRRQredTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLERE 475
Cdd:TIGR02168 676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 476 KKELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLET--SAQSEANwaAEFAELEKERDSLVSGAAHR 553
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKAlrEALDELR--AELTLLNEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613986 554 EEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEE 610
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL------EELIEELESELEALLN 880
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
401-586 |
1.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 401 AELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaEVTKQVSMARQAQVDLEREKKELE 480
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 481 DSLERIsdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLETS-AQSEANWAAEFAELEKERDSLVSGAAHREEELSA 559
Cdd:COG4717 146 ERLEEL--------EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*..
gi 2462613986 560 LRKELQDTQLKLASTEESMCQLAKDQR 586
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-773 |
2.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLENMK------TESQRVVLQLKGHVSELEADLAEQQHLRQQaaddcefLRAELDELRRQR 410
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 411 EDTEKAQ------RSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLE 484
Cdd:PRK03918 283 KELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 485 RISDQGQRKTQeqlevLESLKQELATS-----QRELQVLQGSLETSAQSEANWAAEFAELEKERDSL------------- 546
Cdd:PRK03918 363 LYEEAKAKKEE-----LERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 547 --VSGAA----HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkaaEQVIqdalnqLEEPPLISCAGSA 620
Cdd:PRK03918 438 cpVCGRElteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------EKVL------KKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 621 DHLLSTVTSISSC-IEQLEKSWSQYLACPE-------DISGLLHSITLLAHLTSDAIAhgattCLRAPPEPADSLTEACK 692
Cdd:PRK03918 503 EQLKELEEKLKKYnLEELEKKAEEYEKLKEkliklkgEIKSLKKELEKLEELKKKLAE-----LEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 693 QYGRETLAYLASLEEE-GSLENADSTAMRncLSKIKAIGEELLPRgLDIKQEELgDLVDKEMAATSAAIETATARIEEML 771
Cdd:PRK03918 578 ELEELGFESVEELEERlKELEPFYNEYLE--LKDAEKELEREEKE-LKKLEEEL-DKAFEELAETEKRLEELRKELEELE 653
|
..
gi 2462613986 772 SK 773
Cdd:PRK03918 654 KK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-543 |
2.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 353 LKAQLENMKTESQRVVLQLKGHVSELEADLAE---QQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLsEIERKAQA 429
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 430 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELA 509
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|....
gi 2462613986 510 TSQRELQVLQGSLETSAQSEANWAAEFAELEKER 543
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-589 |
3.08e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 60.80 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 328 FNSQNGVNKDekdhLIERLYREISGLKAQLENMKtesQRVVLQLKgHVSELEA----DLAEQQHLRQQAADDCEFLRAEL 403
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQ---QQIKTYNK-NIEEQRKkngeNIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 404 DELRRQREDTEKAQRSLSEIERKAQaneQRYSKLKEKYsELVQNHADLLRKNAEV---TKQVSMARQAQVDLEREKKELE 480
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLN---TAAAKIKSKI-EQFQKVIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 481 DSLERISDQgqrktQEQLEVLESlkqELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL 560
Cdd:PHA02562 313 HSLEKLDTA-----IDELEEIMD---EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|....*....
gi 2462613986 561 RKELQDTQLKLASTEESmcqlaKDQRKML 589
Cdd:PHA02562 385 QDELDKIVKTKSELVKE-----KYHRGIV 408
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
8-92 |
6.27e-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: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 8 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYR 84
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
....*...
gi 2462613986 85 NELSDMSR 92
Cdd:cd03564 83 GHIFNLSN 90
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
397-578 |
6.89e-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: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 397 EFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREK 476
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 477 KELEDSLERISDQGQRKTQEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAElekERDSLVSGAAHREEE 556
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVEREL 767
|
170 180
....*....|....*....|..
gi 2462613986 557 LSALRKELQDTQLKLASTEESM 578
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL 789
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
349-610 |
7.04e-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: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 349 EISGLKAQLE---NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIER 425
Cdd:pfam01576 244 ELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 426 KaqaNEQRYSKLKEKYSELVQNH----ADLLRKNA----EVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQ 497
Cdd:pfam01576 324 K---REQEVTELKKALEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL--------QAE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 498 LEVLESLKQELATSQR----ELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 573
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKklegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462613986 574 TEEsmcQLAKDQRKMLLVGSRKAAEQVIQDAL-NQLEE 610
Cdd:pfam01576 473 TQE---LLQEETRQKLNLSTRLRQLEDERNSLqEQLEE 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-518 |
3.96e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHL--IERLYREISGLKAQ---LENMKT-----ESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDE 405
Cdd:COG4913 248 REQIELLepIRELAERYAAARERlaeLEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 406 LRRQR------------EDTEKAQRSLSEIERKAQANEQRYSKLK-------EKYSELVQNHADLL----RKNAEVTKQV 462
Cdd:COG4913 328 LEAQIrgnggdrleqleREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLealeEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462613986 463 SMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVL 518
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-571 |
4.06e-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: 57.34 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 327 NFNSQNGV---NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEadlaEQQHLRQQAADDCEFLRAEL 403
Cdd:TIGR04523 222 ELKKQNNQlkdNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 404 DELRRQRE---------DTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLER 474
Cdd:TIGR04523 298 SDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 475 EKKELEDSLE----RISD-----QGQRKTQEQLEV-LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 544
Cdd:TIGR04523 378 ENQSYKQEIKnlesQINDleskiQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
250 260
....*....|....*....|....*..
gi 2462613986 545 SLVSGAAHREEELSALRKELQDTQLKL 571
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-560 |
4.53e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 377 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 457 EVTKQVSMARQAQVDLEREKKELE----------DSLERISDQ-GQrkTQEQLEVLESLKQELATSQRELQVLQGSLETS 525
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsGE--EFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
170 180 190
....*....|....*....|....*....|....*
gi 2462613986 526 AQSeanwaaefaeLEKERDSLVSGAAHREEELSAL 560
Cdd:PRK04863 654 KQA----------LDEEIERLSQPGGSEDPRLNAL 678
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
347-565 |
4.54e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 347 YREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtekaqrslSEI 423
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR----------VDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 424 ERKAQANEQRYSKLKEKYSELVqnhADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQG--------QRKTQ 495
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNreeaeewyQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 496 E-QLEV------LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELE----KERDSLVSGAAHREEELSALRKEL 564
Cdd:pfam00038 200 ElQQAAarngdaLRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEM 279
|
.
gi 2462613986 565 Q 565
Cdd:pfam00038 280 A 280
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-609 |
7.49e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 391 QAADDCEFLRAELDELRRQREDTEKAQR---SLSEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAEVTKQVSMARQ 467
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 468 AQVDLEREKKELEDSLERISDQGQRKTQEQlEVLESLKQELATSQ-RELQVLQGSLETSAQSEANWAAEFAELEKERDSL 546
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462613986 547 VSGAAHREEELSALRKELQDTQLKLASTEESmCQLAKDQRKMLLVGSRKAAEQvIQDALNQLE 609
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEA-LEEALAEAEAALRDLRRELRE-LEAEIASLE 432
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
376-598 |
1.52e-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: 55.29 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 376 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEkaqRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN 455
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 456 AEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELAT---SQRELQVLQGSLETSAQSEANW 532
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 533 AAEFAELEK---ERDSLVS-------------GAAHREE-ELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRK 595
Cdd:pfam07888 191 SKEFQELRNslaQRDTQVLqlqdtittltqklTTAHRKEaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
...
gi 2462613986 596 AAE 598
Cdd:pfam07888 271 QAE 273
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
329-574 |
2.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 329 NSQNGVNKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLK---GHVS-ELEADLAEQQ--HLRQQAADdcefLRAE 402
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRqknGLVDlSEEAKLLLQQlsELESQLAE----ARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 403 LDELRRQREDTEKAQRSLSEIERKAQANEQrYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqVDLEREKKELEDS 482
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 483 LERISDQGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAnwaaEFAELEKERDSLvsgaahrEEELSALRK 562
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASL---QAQLAQLEARLAELPELEA----ELRRLEREVEVA-------RELYESLLQ 372
|
250
....*....|..
gi 2462613986 563 ELQDTQLKLAST 574
Cdd:COG3206 373 RLEEARLAEALT 384
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
336-568 |
3.31e-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: 54.26 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCE----------FLRAELDE 405
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsVKELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 406 LRRQREDTEKAQRSLS-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELED 481
Cdd:TIGR04523 459 LDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 482 SLERISDQ----GQRKTQEQLE-VLESLKQELAtsqrELQVLQGSLEtSAQSEANwaAEFAELEKERDSLVSGAAHREEE 556
Cdd:TIGR04523 539 KISDLEDElnkdDFELKKENLEkEIDEKNKEIE----ELKQTQKSLK-KKQEEKQ--ELIDQKEKEKKDLIKEIEEKEKK 611
|
250
....*....|..
gi 2462613986 557 LSALRKELQDTQ 568
Cdd:TIGR04523 612 ISSLEKELEKAK 623
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-583 |
3.70e-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: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 399 LRAELDELRRQREDTEKAQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK 477
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 478 ELEDSLERISDQGQRKTQEQLEVLES-----------LKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL 546
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGELEAeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462613986 547 VSGAAHREEELSALRKELQDTQLKLASTEESMCQLAK 583
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
342-587 |
3.90e-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: 54.57 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 342 LIERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQ-AADDCEFLRAELDELRRQREDTEKAQ 417
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLrqqLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 418 RSLSEIERKA---QANEQRYSKLKEKYSELVQNHaDLLRKNAEVTKQVsMARQAQ------VDLEREKKELEDSLERISD 488
Cdd:COG3096 917 KALAQLEPLVavlQSDPEQFEQLQADYLQAKEQQ-RRLKQQIFALSEV-VQRRPHfsyedaVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 489 QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-----REEELSALRKE 563
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARirrdeLHEELSQNRSR 1074
|
250 260
....*....|....*....|....
gi 2462613986 564 LQDTQLKLASTEESMCQLAKDQRK 587
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
336-527 |
5.75e-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: 53.59 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHvsELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEK 415
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRslseieRKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQ 495
Cdd:pfam17380 482 EKR------DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190
....*....|....*....|....*....|..
gi 2462613986 496 EQLEVLESLKQELATSQRELQVLQGSLETSAQ 527
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-544 |
6.06e-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: 53.92 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 349 EISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 428
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 429 ANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEqlevLESLKQEL 508
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDRVEKEL 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462613986 509 ATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 544
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
355-610 |
7.91e-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: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 355 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADdCEFLRAELDELRRQREDTEKA---------QRSLSEIER 425
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahIKAVTQIEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 426 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLevLESLK 505
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH--IHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 506 QELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVsgAAHREEELSALRKELQdtqlKLASTEESMCQLAKDQ 585
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA--HAKKQQELQQRYAELC----AAAITCTAQCEKLEKI 459
|
250 260
....*....|....*....|....*
gi 2462613986 586 RKMLLVGSRKAAEQVIQDALNQLEE 610
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQ 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-569 |
9.07e-07 |
|
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: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 377 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQRE------DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQN 447
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 448 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLE--------------VLESLKQELATSQR 513
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavereLRENLEERIDALRA 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 514 ELQVLQGSLEtSAQSEAN--WAAEFAEL----------EKERDSLV-SGAAHREEELSALRKELQDTQL 569
Cdd:COG4913 781 RLNRAEEELE-RAMRAFNreWPAETADLdadleslpeyLALLDRLEeDGLPEYEERFKELLNENSIEFV 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-610 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 398 FLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSelvqnhaDLLRKNAEVTKQVSMARQaqvDLEREKK 477
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQ---EEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 478 ELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLETSAQSEANwaAEFAELEKERDSLVSGAAHREEEL 557
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462613986 558 SALRKELQDTQLKLASTEESMCQLakdQRKMLLVGSRKAAEQVIQDALN-QLEE 610
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIEKEIENLNgKKEE 865
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
359-601 |
1.14e-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: 52.82 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 359 NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDEL------RRQREDTEKAQRslSEIERKAQ--AN 430
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKareverRRKLEEAEKARQ--AEMDRQAAiyAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 431 EQRYSKLKEKYSELVQNHadllrknaEVTKQVSMARQAQVDLEREKKEledSLERISDQGQRKTQEQLEVLESL-KQELA 509
Cdd:pfam17380 339 QERMAMERERELERIRQE--------ERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAArKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 510 TSQRELQVLQGSLETS---AQSEANWAAEFAELEKER----DSLVSGAAHREEELSALRKELQDTQLK--LASTEESMCQ 580
Cdd:pfam17380 408 EEERQRKIQQQKVEMEqirAEQEEARQREVRRLEEERaremERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRK 487
|
250 260
....*....|....*....|.
gi 2462613986 581 LAKDQRKMLLVGSRKAAEQVI 601
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAM 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-617 |
1.30e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKGHVSELEAdlAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQR 433
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 434 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERISDQGQRKTQEQLEVLESLK-QELATSQ 512
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 513 RELQVLQGSLETSAQSEANWAAEFA-ELEKERDSLVSGAAHREEELSA--LRKElQDTQLKLASTEEsmcqlAKDQRKML 589
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAeeAKKA-EEAKIKAEELKK-----AEEEKKKV 1635
|
250 260
....*....|....*....|....*....
gi 2462613986 590 LVGSRKAAEQVIQ-DALNQLEEPPLISCA 617
Cdd:PTZ00121 1636 EQLKKKEAEEKKKaEELKKAEEENKIKAA 1664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-567 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 348 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAAD---DCEFLRAELDELRRQREDTEKAQRSLSEIe 424
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNE- 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 425 rKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELE---DSL-ERISDQGQRKTQEQLEV 500
Cdd:TIGR02168 882 -RASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLqERLSEEYSLTLEEAEAL 959
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 501 LESLKQELATSQRELQVLQGSLEtsAQSEANWAA--EFAELEKERDSLvsgaAHREEELSALRKELQDT 567
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIK--ELGPVNLAAieEYEELKERYDFL----TAQKEDLTEAKETLEEA 1022
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
406-610 |
1.51e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 406 LRRQREDTEKAQRSLSE----IERKAQANEQRYSKLKEKYS--ELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKEL 479
Cdd:COG3206 166 LELRREEARKALEFLEEqlpeLRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 480 EDSLERISDQGQRKTQEQleVLESLKQELATSQRELQVLQGSL-----------ETSAQSEANWAAEFAELEKERDSLVS 548
Cdd:COG3206 246 RAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 549 GAAHREEELsalRKELQDTQLKLASTEESMCQLAKDQRKmllvgsRKAAEQVIQDALNQLEE 610
Cdd:COG3206 324 ALQAREASL---QAQLAQLEARLAELPELEAELRRLERE------VEVARELYESLLQRLEE 376
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
340-609 |
1.61e-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: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 340 DHLIERL---YREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 416
Cdd:pfam15921 415 DHLRRELddrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QR-------SLSEIERKAQANEQRYSKLKE----KYSEL--VQNHADLLRkNAEV---TKQVSMARQAQVdLEREKKELE 480
Cdd:pfam15921 495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhLKNEGDHLR-NVQTeceALKLQMAEKDKV-IEILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 481 DSLERISDQGQ-------RKTQEQLEV---------LESLKQELATSQRELQVLQGSLETSAQSEANWAAE----FAELE 540
Cdd:pfam15921 573 NMTQLVGQHGRtagamqvEKAQLEKEIndrrlelqeFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIK 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 541 KERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMcQLAKDQRKMLLVGSRKAAEQViQDALNQLE 609
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQT-RNTLKSME 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
342-610 |
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 2462613986 342 LIERLYREISGLKA-------QLENMKTESQ-RVVLQLKGH-------VSELEADLAEQQHLRQQAADDCEFLRAELDEL 406
Cdd:pfam15921 225 ILRELDTEISYLKGrifpvedQLEALKSESQnKIELLLQQHqdrieqlISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 407 RRQ-REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQN-HADLLRKNAEVTKqvsmARQAQVDLEREKKELEDSLE 484
Cdd:pfam15921 305 QEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 485 R-ISDQGQRKTQEQLE----------------VLESLKQELATSQRELQVLQGSLET-SAQSEANWAAEFAELEKERDSL 546
Cdd:pfam15921 381 KlLADLHKREKELSLEkeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462613986 547 vsgaahreEELSALRKELQDTQLKLASTEESMCqlakdQRKMLLvgsrKAAEQVIQDALNQLEE 610
Cdd:pfam15921 461 --------EKVSSLTAQLESTKEMLRKVVEELT-----AKKMTL----ESSERTVSDLTASLQE 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-610 |
1.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKGHVSEL-EADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRsLSEIERKAQ 428
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 429 ANEQRYSKLKEKYSELVQ----NHADLLRKNAEVTK--QVSMARQAQVDLER--------------EKKELEDSLERISD 488
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKaeekKKADELKKAEELKKaeEKKKAEEAKKAEEDknmalrkaeeakkaEEARIEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 489 QGQRKTQE-QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 567
Cdd:PTZ00121 1604 EKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462613986 568 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 610
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-610 |
2.72e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRSLSEIERKAQA 429
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 430 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQA-QVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQ-- 506
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKad 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 507 EL--ATSQRELQVLQGSLETSAQSEANWAAEF---------AELEKERDSLVSGAAHREEE--LSALRKELQDTQLKLAS 573
Cdd:PTZ00121 1514 EAkkAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEAR 1593
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462613986 574 TEESMcQLAKDQRKMLLVGSRKAAEQVIQ-DALNQLEE 610
Cdd:PTZ00121 1594 IEEVM-KLYEEEKKMKAEEAKKAEEAKIKaEELKKAEE 1630
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
377-560 |
3.00e-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: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 377 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 457 EVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL-ESLKQELATSQRELQVLQGSLE---TSAQSEANW 532
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPA-----WLAAQDALERLrEQSGEALADSQEVTAAMQQLLErerEATVERDEL 649
|
170 180
....*....|....*....|....*...
gi 2462613986 533 AAEFAELEKERDSLVSGAAHREEELSAL 560
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-520 |
3.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQ--AADDCEFLRAElDELRRQREDTEKAQ--RSLSEIERKAQA 429
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAA-EEAKKAEEDKKKAEeaKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 430 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ----VSMARQAQVDLEREKKELEdslERISDQGQRKTQEQLEVLESLK 505
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKK 1769
|
170
....*....|....*
gi 2462613986 506 QELATSQRELQVLQG 520
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEE 1784
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
383-531 |
4.83e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.48 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 383 AEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEvtkqv 462
Cdd:PRK12705 46 AEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELE----- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 463 smarqaqvdLEREKKELEDSLERISdqGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAN 531
Cdd:PRK12705 121 ---------LEELEKQLDNELYRVA--GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-570 |
7.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELE------ADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQ 417
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAE----LPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 418 RSLSEIERKAQANEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRktQE 496
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 497 QLEVLESLKQEL--ATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSLVSGAAHREEELSALRKELQDTQ 568
Cdd:COG4717 241 LEERLKEARLLLliAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEE 320
|
..
gi 2462613986 569 LK 570
Cdd:COG4717 321 LE 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
349-577 |
7.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 349 EISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 428
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 429 ANEQRYSKLKEKYSELV--QNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSlerisdqgQRKTQEQLEVLESLKQ 506
Cdd:COG3883 93 RALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAK--------KAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613986 507 ELATSQRELQvlqgsletSAQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 577
Cdd:COG3883 165 ELEAAKAELE--------AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-577 |
7.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 391 QAADDCEFLRAELDELRRQREDtekAQRSLSEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQV---- 462
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERReelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 463 SMARQAQVDLER--------EKKELED------SLERISDQGQRKTQEQ---LEVLESLKQELATSQRELQVLQGSLEtS 525
Cdd:COG3883 90 ERARALYRSGGSvsyldvllGSESFSDfldrlsALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELE-A 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 526 AQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 577
Cdd:COG3883 169 AKAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
328-638 |
7.93e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 328 FNSQNGVNKDEKDHLIER---LYREISGLKAQLENMK---TESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRA 401
Cdd:PRK02224 340 HNEEAESLREDADDLEERaeeLREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 402 ELDELRRQREDTEKAQRSLSEIERKAQA-------------------------NEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 457 EVTKQVSMARQaqvdLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAA 534
Cdd:PRK02224 500 RAEDLVEAEDR----IERLEERREDLEELIAERRETieEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 535 EF----AELEKERDSL------VSGAAHREEELSALRKELQDTQL-------KLASTEESMCQLA---KDQRKMLLVGSR 594
Cdd:PRK02224 576 ELnsklAELKERIESLerirtlLAAIADAEDEIERLREKREALAElnderreRLAEKRERKRELEaefDEARIEEAREDK 655
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462613986 595 KAAEQVIQDALNQLEEpplisCAGSADHLLSTVTSISSCIEQLE 638
Cdd:PRK02224 656 ERAEEYLEQVEEKLDE-----LREERDDLQAEIGAVENELEELE 694
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
346-576 |
8.28e-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: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 346 LYREISGLKAQLENMKTESQRVVLQLKGHVSELE----ADLAEQQHLRQQAADDCEFLRAEldELRRQREDTEK--AQRS 419
Cdd:pfam01576 55 LCAEAEEMRARLAARKQELEEILHELESRLEEEEersqQLQNEKKKMQQHIQDLEEQLDEE--EAARQKLQLEKvtTEAK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 420 LSEIERKAQANEQRYSKL-------KEKYSELVQNHADLLRKNAEVT----KQVSMARQAQVDLEREKK---ELED---S 482
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLskerkllEERISEFTSNLAEEEEKAKSLSklknKHEAMISDLEERLKKEEKgrqELEKakrK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 483 LERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWA----------AEFAE-LEKERDSLVSGAA 551
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireleaqiSELQEdLESERAARNKAEK 292
|
250 260
....*....|....*....|....*...
gi 2462613986 552 HR---EEELSALRKELQDTQLKLASTEE 576
Cdd:pfam01576 293 QRrdlGEELEALKTELEDTLDTTAAQQE 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
380-571 |
8.49e-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: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 380 ADLAEQQHLRQ-QAADdceflrAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK 454
Cdd:COG1579 1 AMPEDLRALLDlQELD------SELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 455 NAEVTKQVSMAR--------QAQVD-LEREKKELEDSLerisdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLEts 525
Cdd:COG1579 75 IKKYEEQLGNVRnnkeyealQKEIEsLKRRISDLEDEI-----------LELMERIEELEEELAELEAELAELEAELE-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462613986 526 aQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKELQDTQLKL 571
Cdd:COG1579 142 -EKKAELDEELAELEAELEEL-------EAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
397-608 |
8.66e-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: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 397 EFLRAELDELRRQR-EDTEKAQRSLSEIERKAQAnEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvdleRE 475
Cdd:TIGR00618 545 EDVYHQLTSERKQRaSLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL----LR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 476 KKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRElQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaaHREE 555
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSIRVLPKELLASRQLALQKMQ--------SEKE 690
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462613986 556 ELSALRKELQDTQLKLASTEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 608
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREfNEIENASSSLGSDLAAREDALNQS 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
343-614 |
8.92e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVvlqlkghVSELEADLAEQQHLRQQaaddceflraeldeLRRQREDTEKAQRSLSE 422
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQL-------EEELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 423 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQLEVLE 502
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL--------QEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 503 SLKQELATSQRELQVLQgsLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLA 582
Cdd:COG4372 171 QELQALSEAEAEQALDE--LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270
....*....|....*....|....*....|..
gi 2462613986 583 KDQRKMLLVGSRKAAEQVIQDALNQLEEPPLI 614
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-623 |
9.27e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 465 ARQAQVDLEREKKELEDSLERISDQgqrktqeqlevLESLKQELATSQRELQVLQGsLETSAQSEANWAA---EFAELEK 541
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEER-----------LEALEAELDALQERREALQR-LAEYSWDEIDVASaerEIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 542 ERDSLVSGAAhreeELSALRKELQDTQLKLASTEESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 621
Cdd:COG4913 676 ELERLDASSD----DLAALEEQLEELEAELEELEEELDELKGEIGR--LEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
..
gi 2462613986 622 HL 623
Cdd:COG4913 750 LL 751
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
348-584 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 348 REISGLKAQLENMKTESQRVV---LQLKGHVSELEADLAE----QQHLRQQAADD-----CEFLRAELDELRRQREDTEK 415
Cdd:pfam15905 94 KRLQALEEELEKVEAKLNAAVrekTSLSASVASLEKQLLEltrvNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEAKMK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqvdlerekKELEDSLERISDQGQRKT 494
Cdd:pfam15905 174 EVMAKQEgMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET--------------EKLLEYITELSCVSEQVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 495 QEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAE----LEKERDSLVSGAAHREEELSAlrkELQDTQLK 570
Cdd:pfam15905 240 KYKLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEkcklLESEKEELLREYEEKEQTLNA---ELEELKEK 315
|
250
....*....|....
gi 2462613986 571 LASTEESMCQLAKD 584
Cdd:pfam15905 316 LTLEEQEHQKLQQK 329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
375-610 |
1.67e-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: 49.18 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 375 VSELEADLAEQQHLRQQAADDCEFLRA-------ELDELRRQREDTekaQRSLSEIERKAQANEQRYSKLkEKYSELVQN 447
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEArleaaeeEVDSLKSQLADY---QQALDVQQTRAIQYQQAVQAL-EKARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 448 hADLLRKNAEVTKQVSMARQAQVDleREKKELEDSLeRISDQGQRKTQEQLEVLESLKQELATSQ-----RELQVLQGSL 522
Cdd:COG3096 432 -PDLTPENAEDYLAAFRAKEQQAT--EEVLELEQKL-SVADAARRQFEKAYELVCKIAGEVERSQawqtaRELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 523 ETSAQSEANWAAEFAELEKERDSL-----------------VSGAAHREEELSALRKELQDTQLKLASTEESMCQL---- 581
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQqnaerlleefcqrigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELrqql 587
|
250 260 270
....*....|....*....|....*....|.
gi 2462613986 582 --AKDQRKMLlvGSRKAAEQVIQDALNQLEE 610
Cdd:COG3096 588 eqLRARIKEL--AARAPAWLAAQDALERLRE 616
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
337-578 |
1.77e-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: 48.66 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEAD--------------LAEQ----QHLRQQAADDCEF 398
Cdd:pfam10174 390 DVKERKINVLQKKIENLQEQLR----DKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKeriiERLKEQREREDRE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 399 LRAELDELRRQRED---------TEKAQRSLSEIERKAQANEQRYSKLKeKYSELVQNHADLLRKNAEVTKQVSMARQAQ 469
Cdd:pfam10174 466 RLEELESLKKENKDlkekvsalqPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 470 --VDLEREKKELEDSLERISDQGQRKTQE----QLEV---LESLKQ----------------ELATSQRELQVLQGSLET 524
Cdd:pfam10174 545 naEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerlLGILREvenekndkdkkiaeleSLTLRQMKEQNKKVANIK 624
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613986 525 SAQSE--ANWAAEFAELEKERDSLVSGAAHR--EEELSAL---RKELQDTQLKLASTEESM 578
Cdd:pfam10174 625 HGQQEmkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSSTQQSL 685
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
338-591 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 338 EKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEaDLAEQQHLRQQAADDCEFLRAELDelRRQREDTEKAQ 417
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 418 RsLSEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQR--- 492
Cdd:pfam05557 171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaat 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 493 ------KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQD 566
Cdd:pfam05557 250 lelekeKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
250 260
....*....|....*....|....*
gi 2462613986 567 TQLKLASTEESMCQLakdQRKMLLV 591
Cdd:pfam05557 330 LNKKLKRHKALVRRL---QRRVLLL 351
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
343-599 |
2.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELeadlaeQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRS 419
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQrsqLEQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 420 -------LSEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVsm 464
Cdd:PRK04863 913 vqqhgnaLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKL-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 465 aRQAQVDLEREKKELEDSLERISDQGQRKTQeqleVLESLKQELATSQRELQVLQGSL-ETSAQSEANwAAEFAELEKER 543
Cdd:PRK04863 991 -RQRLEQAEQERTRAREQLRQAQAQLAQYNQ----VLASLKSSYDAKRQMLQELKQELqDLGVPADSG-AEERARARRDE 1064
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462613986 544 dslvsgaahREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM--LLVGSRKAAEQ 599
Cdd:PRK04863 1065 ---------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerDYHEMREQVVN 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-493 |
2.54e-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: 47.84 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAEQ------------QHLRQQAADDCEFLRAELDELRR 408
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 409 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVqnhadllrknAEVTKQVSMARQAQVDLEREKKELEDSLERISD 488
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLL----------ARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*
gi 2462613986 489 QGQRK 493
Cdd:COG4942 235 EAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
348-573 |
2.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 348 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAadDCEFLRAELDEL-RRQREDTEKAQRSLSEIERK 426
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALlAEAGVEDEEELRAALEQAEE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 427 AQANEQRYSKLKEKyselVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKELEDSLERISDQgQRKTQEQLEVLESlKQ 506
Cdd:COG4717 397 YQELKEELEELEEQ----LEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELREE-LAELEAELEQLEE-DG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613986 507 ELATSQRELQVLqgsletsaqseanwAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 573
Cdd:COG4717 470 ELAELLQELEEL--------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAS 522
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
345-564 |
3.04e-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: 48.30 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 345 RLYREISGLKAQLENMKTESQR-VVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrslseI 423
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----L 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 424 ERKAQANEQRYSKLKEKYSEL-VQNHADLLRKNAEvtkqvsmaRQAQVDLEREKKELEDSLERISDQGQRKT------QE 496
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALeTWYKRDLASLGVD--------PDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyQE 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 497 Q-LEVLESLKQELATSQRELQVLQGSLetsAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKEL 564
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 ... |
378-588 |
4.04e-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: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 378 LEADLAEqqhLRQQAADdcefLRAELDELRRQREDTEKA-QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:pfam01576 213 LEGESTD---LQEQIAE----LQAQIAELRAQLAKKEEElQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 457 EVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEsLKQELATSQR--ELQV-------------LQGS 521
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE-LKKALEEETRshEAQLqemrqkhtqaleeLTEQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462613986 522 LETSAQSEANW-------AAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM 588
Cdd:pfam01576 365 LEQAKRNKANLekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
344-587 |
4.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEI 423
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 424 ERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS------DQGQ 491
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELeerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkrlsrlEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 492 RKTQEQLEVLES-------LKQELATSQRELQVLQGSLETSAQSEANwAAEFAELEKERDSLVSGAAHRE-EELSALRKE 563
Cdd:PRK03918 324 NGIEERIKELEEkeerleeLKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKElEELEKAKEE 402
|
250 260
....*....|....*....|....
gi 2462613986 564 LQDTQLKLASTEESMCQLAKDQRK 587
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKK 426
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
354-658 |
4.56e-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: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELD----ELRRQREDTEKAQRSLSEIERKAQA 429
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 430 NEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------MARQAQVDLER-------EKKELEDSLERISDQG---Q 491
Cdd:TIGR00606 770 QETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqEKQEKQHELDTVVSKIelnR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 492 RKTQEQLEVLESLKQELatsqRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL---RKELQDTQ 568
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetfLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 569 LKLASTEESMCQLAKDQRKML------LVGSRKAAEQVIQDalnqleeppliscaGSADHLLSTVTSISSCIEQLEKSWS 642
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIkekvknIHGYMKDIENKIQD--------------GKDDYLKQKETELNTVNAQLEECEK 991
|
330
....*....|....*.
gi 2462613986 643 QYLACPEDISGLLHSI 658
Cdd:TIGR00606 992 HQEKINEDMRLMRQDI 1007
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
344-610 |
4.89e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREisgLKAQLENMKTESQRVVLQLKghVSELE-------ADLAEQQHLRQQAADDCEFLRAELDELRRQREDtekA 416
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMS--TDALEqeilqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE---A 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAQANEQRYSKLKEkyselvqnhADLLRKNAEVTkqvsmARQAQVDlerekkELEdsLERIS-DQGQRKTQ 495
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQ---------AQLTALQAESA-----ALKALVD------ELE--LAQLSaNNRQELAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 496 EQLEVLESLKQELatsQRELQVLQGSLETSAQSEANWAAEFAE-LEKERDSL---VSGAAHREEELSALrkelqdtqlkl 571
Cdd:PRK10929 208 LRSELAKKRSQQL---DAYLQALRNQLNSQRQREAERALESTElLAEQSGDLpksIVAQFKINRELSQA----------- 273
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462613986 572 asteesmcqLAKDQRKMLLVGS--RKAAEQVIQ--DALNQLEE 610
Cdd:PRK10929 274 ---------LNQQAQRMDLIASqqRQAASQTLQvrQALNTLRE 307
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
353-546 |
6.41e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 353 LKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQR-------SLSEIER 425
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 426 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL 501
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKE-----ANVSKFSSYKV 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462613986 502 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSL 546
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTlsklkeESKKRSL 404
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
336-609 |
7.23e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHLIErlyrEISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHL---RQQAADDCEFLRAELDELRRQRED 412
Cdd:COG1340 28 KEKRDELNE----ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 413 TEKAQRSLSEIERKAQANEQRY-----SKLKEKysELVQNHADlLRKNAEvtkqvsmARQAQVDLEREKKELEDSLERIS 487
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK--ELVEKIKE-LEKELE-------KAKKALEKNEKLKELRAELKELR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 488 DQgqrktqeqlevLESLKQELATSQRELQVLQGSLeTSAQSEANwaaefaELEKERDSLVSGAAHREEELSALRKELQDT 567
Cdd:COG1340 174 KE-----------AEEIHKKIKELAEEAQELHEEM-IELYKEAD------ELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462613986 568 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLE 609
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
334-507 |
1.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 334 VNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAeqqhlRQQAADDCEFLRaELDELR-----R 408
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKkaeekK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 409 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERiSD 488
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEK-AE 1367
|
170
....*....|....*....
gi 2462613986 489 QGQRKTQEQLEVLESLKQE 507
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKK 1386
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
336-556 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHLIERLYREISGLKAQLENMKTESqrvVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEK 415
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQ--RK 493
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEerEK 708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613986 494 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE-ANWAAE-FAELEKERdslVSGAAHREEE 556
Cdd:PRK03918 709 AKKELEKLEKALERVEELREKVKKYKALLKERALSKvGEIASEiFEELTEGK---YSGVRVKAEE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
354-610 |
1.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQLKghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSlseieRKAQANEQR 433
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 434 YSKLKEKYSELVQNhADLLRKNAEVT--KQVSMARQAqvdlEREKKELEDSleRISDQGQRKTQEQlevlesLKQELATS 511
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEENkiKAAEEAKKA----EEDKKKAEEA--KKAEEDEKKAAEA------LKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 512 QRELQVLQGSLEtsaqsEANWAAEFAELEKERDSLVSGAAHREEElsalrKELQDTQLKLASTEESMCQLAKDQRKMLLV 591
Cdd:PTZ00121 1702 KKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*....
gi 2462613986 592 GSRKAAEQVIQDALNQLEE 610
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-610 |
1.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 327 NFNSQNGVNKDEKDHLIERLYREISGLKAQlENMKTESQRVVLQLKGHvseleadlAEQQHLRQQAADDCEFLRAELDEL 406
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKK--------AEEAKKADEAKKKAEEAKKKADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 407 RRQREDTEKAQRSlSEIERKAQANEQRYSKLKEKYSEL----VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDS 482
Cdd:PTZ00121 1335 KKKAEEAKKAAEA-AKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 483 LE--RISDQGQRKTQEQLEVLESLKQelATSQRELQVLQGSLETSAQSE-----------ANWAAEFAELEKERDSLVSG 549
Cdd:PTZ00121 1414 AAakKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEeakkkaeeakkADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613986 550 AAHREEELSALRKELQDT----QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 610
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
346-501 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 346 LYREISGLKAQLENmktesqrvVLQLKGHVSELEADLAEQQHLRQQA-------------ADDCEFLRAELDELRRQRED 412
Cdd:COG3096 500 LLRRYRSQQALAQR--------LQQLRAQLAELEQRLRQQQNAERLLeefcqrigqqldaAEELEELLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 413 T-EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEV------TKQVSMARQAQVDLEREKKELEDSLEr 485
Cdd:COG3096 572 QaAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadSQEVTAAMQQLLEREREATVERDELA- 650
|
170
....*....|....*.
gi 2462613986 486 isdQGQRKTQEQLEVL 501
Cdd:COG3096 651 ---ARKQALESQIERL 663
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
412-575 |
1.88e-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: 44.72 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 412 DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLEREKKELED--S 482
Cdd:pfam00529 52 DPTDYQAALDSAEaqlAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQaavkAAQAQLAQAQIDLARrrV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 483 LERISDQGQRKTQEQLEVLESLKQELATSQRELqvlqgsletsAQSEANWAAEFAELEKERDSLVSGAahrEEELSALRK 562
Cdd:pfam00529 132 LAPIGGISRESLVTAGALVAQAQANLLATVAQL----------DQIYVQITQSAAENQAEVRSELSGA---QLQIAEAEA 198
|
170
....*....|...
gi 2462613986 563 ELQDTQLKLASTE 575
Cdd:pfam00529 199 ELKLAKLDLERTE 211
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
354-531 |
1.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 354 KAQLENMKTESQRVVLQlkghvSELEADLAEQQHLRQQaaddceflRAELDELRRQREDTEKAQRSlsEIERKAQANEQR 433
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-----AKKEAEAIKKEALLEA--------KEEIHKLRNEFEKELRERRN--ELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 434 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqRKTQEQL--EVLESLKQELats 511
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS----GLTAEEAkeILLEKVEEEA--- 167
|
170 180
....*....|....*....|
gi 2462613986 512 QRELQVLQGSLETSAQSEAN 531
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEAD 187
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
336-574 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 336 KDEKDHLIERLYREISGL---KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELdelRRQRED 412
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLeleKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSEE 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 413 TEKAQRSLSEIERKAQAN-EQRYSKLKEKysELVQNHAdlLRKNAEVTKQVSmARQAQVD-LEREKKELEDSLERISDQG 490
Cdd:pfam15921 690 METTTNKLKMQLKSAQSElEQTRNTLKSM--EGSDGHA--MKVAMGMQKQIT-AKRGQIDaLQSKIQFLEEAMTNANKEK 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 491 QRKTQEQlevlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSalRKELQDTQLK 570
Cdd:pfam15921 765 HFLKEEK----NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ--RQEQESVRLK 838
|
....
gi 2462613986 571 LAST 574
Cdd:pfam15921 839 LQHT 842
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
414-605 |
2.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 414 EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrK 493
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----S 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 494 TQEQLEVLEslkQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQdtQLKLAS 573
Cdd:COG4372 106 LQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAE 180
|
170 180 190
....*....|....*....|....*....|..
gi 2462613986 574 TEESMCQLAKDQRKMLLVGSRKAAEQVIQDAL 605
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
380-573 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 380 ADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQAneqRYSKLKEKYSELVQNHADLLRKNAEVT 459
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR---RAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 460 KQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL 539
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
170 180 190
....*....|....*....|....*....|....
gi 2462613986 540 EKERDSLVSGAAHREEELSALRKELQDTQLKLAS 573
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-506 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtEKAQRS 419
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRREL---EELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 420 LSEIERKAQANEQRYSKLKEKYSELVQ-NHADLLRKNAEVTKQVSMARQAQVDLEREKKEL----EDSLERISDQGQRK- 493
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYd 1003
|
170
....*....|....*
gi 2462613986 494 --TQEQLEVLESLKQ 506
Cdd:TIGR02168 1004 flTAQKEDLTEAKET 1018
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
355-621 |
2.24e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 355 AQLENMKTESQRVVLQLkghvSELEADLAEQQHLRQQA------------ADDCEflrAELDELRRQREDtekAQRSLSE 422
Cdd:PRK04863 786 KRIEQLRAEREELAERY----ATLSFDVQKLQRLHQAFsrfigshlavafEADPE---AELRQLNRRRVE---LERALAD 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 423 IERKAQANEQRYSKLKEKYSEL--VQNHADLLRKN------AEVTKQVSMARQAQVDLEREKKELEdSLERIsdqgQRKT 494
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSALnrLLPRLNLLADEtladrvEEIREQLDEAEEAKRFVQQHGNALA-QLEPI----VSVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 495 QEQLEVLESLKQELATSQRELQVLQG---SLETSAQSEANWA-AEFAELEKERDSLVSGAAHREEELSALRKElQDTQLK 570
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTR-AREQLR 1009
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 571 lasteESMCQLAK-DQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 621
Cdd:PRK04863 1010 -----QAQAQLAQyNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
343-568 |
2.29e-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: 44.67 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQ----QAADDCEFLRAELDELRRQREDTEKAQR 418
Cdd:pfam19220 74 LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEalerQLAAETEQNRALEEENKALREEAQAAEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 419 SLSEIERKAQANEQRYS-------KLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgq 491
Cdd:pfam19220 154 ALQRAEGELATARERLAlleqenrRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 492 rktqeQLEVLESLKQELATSQRELQVLQGSLETSAQ------------SEANWAAE--FAELEKERDSLVSGAAHREEEL 557
Cdd:pfam19220 232 -----LEEAVEAHRAERASLRMKLEALTARAAATEQllaearnqlrdrDEAIRAAErrLKEASIERDTLERRLAGLEADL 306
|
250
....*....|.
gi 2462613986 558 SALRKELQDTQ 568
Cdd:pfam19220 307 ERRTQQFQEMQ 317
|
|
| F-BAR_FCHO1 |
cd07674 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ... |
416-578 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSEIERKAQANEQRYSKLKEKYSELVQN--HADLLRKNAEVTKqVSMARQAQVDLEREKKeLEDSLERISdqgqRK 493
Cdd:cd07674 20 STKELADFVRERAAIEETYSKSMSKLSKMASNgsPLGTFAPMWEVFR-VSSDKLALCHLELMRK-LNDLIKDIN----RY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 494 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaahREeelSALRKELQDTQLKLAS 573
Cdd:cd07674 94 GDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR---------RE---GVPQKELEKAELKTKK 161
|
....*
gi 2462613986 574 TEESM 578
Cdd:cd07674 162 AAESL 166
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
343-598 |
2.98e-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: 44.63 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLA-----------EQQHLRQQAA-DDCEFLRAELDELR 407
Cdd:pfam05701 72 LESTKRLIEELKLNLERAQTEEAQAKQDSelaKLRVEEMEQGIAdeasvaakaqlEVAKARHAAAvAELKSVKEELESLR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 408 RQRED--------TEKAQRSLS---EIERKAQANEQRYSKLKEkysELVQNHADLLrkNAEVTK-QVSMAR-QAQVDLER 474
Cdd:pfam05701 152 KEYASlvserdiaIKRAEEAVSaskEIEKTVEELTIELIATKE---SLESAHAAHL--EAEEHRiGAALAReQDKLNWEK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 475 EKKELEDSLERISDQ------GQRKTQEQLEVLESLKQEL-----------------------------ATSQRELQVLQ 519
Cdd:pfam05701 227 ELKQAEEELQRLNQQllsakdLKSKLETASALLLDLKAELaaymesklkeeadgegnekktstsiqaalASAKKELEEVK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 520 GSLEtSAQSEANW---AAEF--AELEKERDSLVS----------GAAHREEELSALRKELQDTQLKLASTEESMCQLAkd 584
Cdd:pfam05701 307 ANIE-KAKDEVNClrvAAASlrSELEKEKAELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELP-- 383
|
330
....*....|....
gi 2462613986 585 qrKMLLVGSRKAAE 598
Cdd:pfam05701 384 --KQLQQAAQEAEE 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
477-638 |
3.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 477 KELEDSLERISDQGQRKTQ---EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL--VSGAA 551
Cdd:COG4717 49 ERLEKEADELFKPQGRKPElnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 552 HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSIS 631
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEEL------EELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
....*..
gi 2462613986 632 SCIEQLE 638
Cdd:COG4717 203 ELQQRLA 209
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
363-542 |
3.14e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 363 ESQRVVLQLKGHVSELEADLAeqqHLRQQAADDCEFLRAELDELRRQ-----------REDTEKAQRSLSEIERKAQANE 431
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsGEESQRGERILAYFGYLNQARQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 432 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLE-----REK--KELEDSLERisDQGQRKTQEQLEVleSL 504
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEqarneRKKtlTGLESSLQK--DQQQLSELRANES--RL 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462613986 505 KQELATSQRELQvlqgsleTSAQSEANWAAEFAELEKE 542
Cdd:PRK11637 246 RDSIARAEREAK-------ARAEREAREAARVRDKQKQ 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
337-508 |
3.16e-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: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLENMKTEsqrvVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdteka 416
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSmarQAQVDLEREKKELEDSLERISDQGQRKTQE 496
Cdd:COG1579 91 ---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|..
gi 2462613986 497 QLEVLESLKQEL 508
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-610 |
3.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 382 LAEQQHLRQQAADDCEfLRAELDELRRQREDTEKAQRSLSEIERKAQANEqryskLKEKYSELVQNHADLLRKNAEVTKQ 461
Cdd:COG4717 293 LAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDLSPEELLE-----LLDRIEELQELLREAEELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 462 VSMARQAQVdLEREKKELEDSLERISDQGQRKtQEQLEVLESLKQELATSQRELQVLQgsletSAQSEANWAAEFAELEk 541
Cdd:COG4717 367 ELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELE- 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 542 erdslvsgaahreEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkAAEQVIQDALNQLEE 610
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 ... |
344-610 |
3.76e-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: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREISGLKAQLENMKT--ESQRvvlQLKGHVSELEADLAEQQHLRQQAADDCEflraELDELRRQredTEKAQRSLS 421
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELriETQK---QTLGARDESIKKLLEMLQSKGLPKKSGE----EDWERTRR---IAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 422 EIERKAQANEQRYSKLKEKYSELVQNHADllRKNAEVTKQVSMARQAQV-DLEREKKELEDSLERISDQGQRKTQE---- 496
Cdd:pfam10174 196 HLEVLLDQKEKENIHLREELHRRNQLQPD--PAKTKALQTVIEMKDTKIsSLERNIRDLEDEVQMLKTNGLLHTEDreee 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 497 --QLEV-----------LESLKQELATSQRELQVLQGSLET--SAQSEANWAAEF------------AELEKERDSLVSG 549
Cdd:pfam10174 274 ikQMEVykshskfmknkIDQLKQELSKKESELLALQTKLETltNQNSDCKQHIEVlkesltakeqraAILQTEVDALRLR 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462613986 550 AAHREEELSALRKELQDTqlklasTEESMCQLA--KDQRKMLLVGSRKAaeQVIQDALNQLEE 610
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDL------TEEKSTLAGeiRDLKDMLDVKERKI--NVLQKKIENLQE 408
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
437-608 |
3.95e-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: 44.12 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 437 LKEKYSELVQNHADLLRKNAEVTKQVSMARQ----AQVDLEREKKELEDSLERISDQGQRKTQEQlevleslkQELATSQ 512
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKErykrDREQWERQRRELESRVAELKEELRQSREKH--------EELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 513 RELQVLQGSL--ETSAQSEANWA--AEFAELEKERDSLVSGAAHREEELS----------ALRKELQ----DTQLKLAST 574
Cdd:pfam07888 104 KELSASSEELseEKDALLAQRAAheARIRELEEDIKTLTQRVLERETELErmkerakkagAQRKEEEaerkQLQAKLQQT 183
|
170 180 190
....*....|....*....|....*....|....*
gi 2462613986 575 EESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 608
Cdd:pfam07888 184 EEELRSLSKEfQELRNSLAQRDTQVLQLQDTITTL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-610 |
5.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 351 SGLKAQLEnmKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKA 427
Cdd:PRK02224 190 DQLKAQIE--EKEEKDLHERLNGLeseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 428 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESL 504
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 505 KQELATsqrelqvlqgsLETSAQsEANWAAefAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAkD 584
Cdd:PRK02224 348 REDADD-----------LEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-D 412
|
250 260 270
....*....|....*....|....*....|..
gi 2462613986 585 QRKML------LVGSRKAAEQVIQDALNQLEE 610
Cdd:PRK02224 413 FLEELreerdeLREREAELEATLRTARERVEE 444
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
501-639 |
6.68e-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: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 501 LESLKQELAT-SQRELQVLQ-----------GSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQ 568
Cdd:pfam09787 2 LESAKQELADyKQKAARILQskekliaslkeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462613986 569 LKLASTEESMCQLAKDQRKMLLvgSRKAAEQVIQDALNQLEEppliSCAGSADHLLSTVTSISSCIEQLEK 639
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 ... |
338-610 |
7.14e-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: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 338 EKDHLIERLYREISGLKAQLENMKTESQRVvLQLKGHVSELEADLAEQQHLRQqaaddcEFLRAELDELRRQREDTEKAQ 417
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALL------RKLQPEQDLQDVRLHLQQCSQ 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 418 R-SLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN-AEVTKQVSMARQAQVDLE--REKKELEDSLERISDQGQRK 493
Cdd:TIGR00618 640 ElALKLTALHALQLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 494 TQEQLEVLESLKQELATSQRELQVLQGSLetsaQSEANWAAEFAELEKERDSLVSGA--------AHREEELSALRKELQ 565
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKEL----MHQARTVLKARTEAHFNNNEEVTAalqtgaelSHLAAEIQFFNRLRE 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462613986 566 DTQLKLASTEESMCQLAKDQRKMLLVGSRKAAeQVIQDALNQLEE 610
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEE 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
338-577 |
8.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 338 EKDHLIERLYREISGLKaQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQ 417
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 418 RSLSEIERkaqaNEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDqgQRKTQEQ 497
Cdd:PRK03918 221 EELEKLEK----EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 498 LEVLESLKQELATSQRELQVLQGSLEtsaqseanwaAEFAELEKERDSLVSgaahREEELSALRKELQDTQLKLASTEES 577
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEER 360
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-567 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 329 NSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRR 408
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 409 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD 488
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 489 QGQRKTQEQLEV----------LESLKQELATSQRELQVLqGSLetsaqseaNWAA--EFAELEKERDSLVSgaahREEE 556
Cdd:COG1196 740 ELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL-GPV--------NLLAieEYEELEERYDFLSE----QRED 806
|
250
....*....|.
gi 2462613986 557 LSALRKELQDT 567
Cdd:COG1196 807 LEEARETLEEA 817
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
404-610 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 404 DELRRQREDTEKAQRSLS----EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKEL 479
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREhlekEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQ-NLKGIKREL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 480 EDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSeANWAAEFAELEKERDSLVSGAAHREEELSA 559
Cdd:pfam18971 689 SDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQ 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613986 560 LRKELQDT------QLKLASTEESMCQLAKDQRKMllvGSRKAAEQVIQDALNQLEE 610
Cdd:pfam18971 768 AKSDLENSvkdviiNQKVTDKVDNLNQAVSVAKAM---GDFSRVEQVLADLKNFSKE 821
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
461-610 |
1.13e-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: 42.44 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 461 QVSMARQAQVDLEREKKELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQseanwaaEFAELE 540
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613986 541 KERDSLVSGAAHREEELSALRKELQ----DTQLKLASTEESMCQLAKDQRKM-LLVGSRKAAEQVIQDALNQLEE 610
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAA 164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
384-599 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 384 EQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK--- 460
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQ--LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskq 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 461 --QVSMARQAQVDLEREKKELEDSL-ERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFA 537
Cdd:pfam02463 259 eiEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 538 ELEKERDSLVSGAAHREEELSALRKElqdtQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQ 599
Cdd:pfam02463 339 ELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
342-505 |
1.31e-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: 41.93 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 342 LIERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAelDELRRQREDTEKAQRsls 421
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDP--TELDRAKEKLKKLLQ--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 422 EIERKaqaneqrysklkekyselVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERI---SDQGQRKTQEQL 498
Cdd:smart00787 219 EIMIK------------------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQL 280
|
....*..
gi 2462613986 499 EVLESLK 505
Cdd:smart00787 281 KLLQSLT 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
363-528 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 363 ESQRVVLQLkghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLK 438
Cdd:COG1579 4 EDLRALLDL----QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAktelEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 439 EKYSElVQNH---ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQREL 515
Cdd:COG1579 80 EQLGN-VRNNkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 2462613986 516 QVLQGSLETSAQS 528
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
339-517 |
1.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 339 KDHLIERLYREISGLKAQLENM--KTESQRVvlqlkghvsELEADLAEQQHLRQQAaddceflraeldelRRQREDTEKA 416
Cdd:PRK00409 500 PENIIEEAKKLIGEDKEKLNELiaSLEELER---------ELEQKAEEAEALLKEA--------------EKLKEELEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAqaneqrYSKLKEKYSELVQNhadlLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrktqE 496
Cdd:PRK00409 557 KEKLQEEEDKL------LEEAEKEAQQAIKE----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLN--------K 618
|
170 180
....*....|....*....|.
gi 2462613986 497 QLEVLESLKQELATSQRELQV 517
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKV 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
365-465 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 365 QRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEK 440
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|....*
gi 2462613986 441 YSELVQNHADLLRKNAEVTKQVSMA 465
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-588 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 338 EKDHLIERLyreisglKAQLENMktesqrvvLQLKG-HVSELEADLAEQQHLRQQAADDceflRAELDELRRQREdteKA 416
Cdd:pfam15921 559 EKDKVIEIL-------RQQIENM--------TQLVGqHGRTAGAMQVEKAQLEKEINDR----RLELQEFKILKD---KK 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 417 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 496
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 497 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKE---LQDTQLKLAs 573
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLS- 775
|
250
....*....|....*
gi 2462613986 574 teESMCQLAKDQRKM 588
Cdd:pfam15921 776 --QELSTVATEKNKM 788
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-610 |
1.49e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 377 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLkEKYSElvqnhaDLLRKNA 456
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQA------DLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 457 EVTKQvSMARQaqvdlerEKKELEDSLERisdqgqRKTQEQLEVLEsLKQELATSQRELQVLQgsLETSAQSEANWAAEF 536
Cdd:PRK04863 363 RLEEQ-NEVVE-------EADEQQEENEA------RAEAAEEEVDE-LKSQLADYQQALDVQQ--TRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 537 AELEKERDSL-VSGAAHREEELSALRKELQDTQLKLAsTEESMCQLAKDQ--RKMLLVG------SRKAAEQVIQDALNQ 607
Cdd:PRK04863 426 AKQLCGLPDLtADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQfeQAYQLVRkiagevSRSEAWDVARELLRR 504
|
...
gi 2462613986 608 LEE 610
Cdd:PRK04863 505 LRE 507
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
337-578 |
1.53e-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: 42.25 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLENMKTEsqrvvlqlkghVSELEADLAEQQHLRQQAADDCEFlrAELDEL-RRQREDTEK 415
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEK-----------IAEYTKSIDIKKATESLEEQLAAA--EAEQELeESKRETETG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHAdlLRKNAEvtkqvsmarqaqvDLEREKKELEDSLERISDQGQRKTQ 495
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE--LSKSSE-------------ELDSFKDTIESTKESLDEIPQNQRG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 496 EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKE-----RDSLVSGAAHREEELSALRKELQDTQLK 570
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvmREADEESQSRLEEAYDEINRSVRSKKED 482
|
....*...
gi 2462613986 571 LASTEESM 578
Cdd:COG5185 483 LNEELTQI 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-610 |
1.54e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 337 DEKDHLIERLYREISGLKAQLENMKTESQrvvlQLKGHVSELEADLAEQQHLR------------------------QQA 392
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIklkelaeqlkeleeklkkynleelEKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 393 ADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsmarqaqvDL 472
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 473 EREKKELEDSLER---ISDQGQRKtQEQLEVLESLKQELATSQRELQVLQGSLEtSAQSEANWAA------EFAELEKER 543
Cdd:PRK03918 591 EERLKELEPFYNEyleLKDAEKEL-EREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEkkyseeEYEELREEY 668
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 544 DSLvsgaahrEEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsRKAAEQV--IQDALNQLEE 610
Cdd:PRK03918 669 LEL-------SRELAGLRAELEELEKRREEIKKTLEKLKEELEER-----EKAKKELekLEKALERVEE 725
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
344-609 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 344 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEF--------LRAELDELRRQREDTEK 415
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSMARQAQVD--------------------LERE 475
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 476 KKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHR 553
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462613986 554 EEELSALRKELQDTQLKLA-------STEESMCQLAKDQR--KMLLVGSRKAAEQVIQDALNQLE 609
Cdd:pfam12128 624 EEQLVQANGELEKASREETfartalkNARLDLRRLFDEKQseKDKKNKALAERKDSANERLNSLE 688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-609 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 427 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKTQEQLEVLESLKQ 506
Cdd:TIGR02168 632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRK 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 507 ELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEEsmcQLAKDQR 586
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE---ELAEAEA 782
|
170 180
....*....|....*....|...
gi 2462613986 587 KmllvgsRKAAEQVIQDALNQLE 609
Cdd:TIGR02168 783 E------IEELEAQIEQLKEELK 799
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
401-570 |
2.03e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 401 AELDElRRQREDTEKAQRSLSEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtkqvsmaRQAQVDLEREKKELE 480
Cdd:COG1566 74 ARLDP-TDLQAALAQAEAQLAA----AEAQLARLEAELGAEAEIAAAEAQLAAAQAQL-------DLAQRELERYQALYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 481 DSLerISDQgqrktqeqleVLESLKQELATSQRELQVLQGSLEtSAQSEANWAAEFAELEKERDSLvsgaahrEEELSAL 560
Cdd:COG1566 142 KGA--VSQQ----------ELDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQVAQA-------EAALAQA 201
|
170
....*....|
gi 2462613986 561 RKELQDTQLK 570
Cdd:COG1566 202 ELNLARTTIR 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
343-555 |
2.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKtesQRV-----VLQLKGHVSELEA--DLAEQQHLRQQaaddcefLRAELDELRRQREdteK 415
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRDAK---QQAfalteVVQRRAHFSYEDAaeMLAKNSDLNEK-------LRQRLEQAEQERT---R 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 416 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV--SMARQAQVDLEREKKELEDSLERISDQGQRK 493
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdsGAEERARARRDELHARLSANRSRRNQLEKQL 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613986 494 TQEQLEvLESLKQELATSQRELQVLQgslETSAQSEANWaaeFAELEKERDSLVSGAAHREE 555
Cdd:PRK04863 1084 TFCEAE-MDNLTKKLRKLERDYHEMR---EQVVNAKAGW---CAVLRLVKDNGVERRLHRRE 1138
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
332-518 |
2.28e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 332 NGVNKDEKDHLIER--LYREISGLKAQLENMKTESQRVVLQLKGHVSEleadlaEQQHLRQQAADDCEFLRAeLDELRRQ 409
Cdd:pfam00038 106 VGLRKDLDEATLARvdLEAKIESLKEELAFLKKNHEEEVRELQAQVSD------TQVNVEMDAARKLDLTSA-LAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 410 REdtEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNH----ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLER 485
Cdd:pfam00038 179 YE--EIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAkeeiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
|
170 180 190
....*....|....*....|....*....|...
gi 2462613986 486 ISDQGQRKTQEQLEVLESLKQELATSQRELQVL 518
Cdd:pfam00038 257 QLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
398-565 |
2.40e-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: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 398 FLRAELDELRRQREDTEKAQ-RSLSEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNaEVTKQVSMarQAQVDLEREK 476
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQEL-QKRIRLLEKR-EAEAEEAL--REQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 477 KELEDSLERISDQGQRKTQEQLEVLESLKQELA--------------TSQRELQVLQGSLETSAQSEANWAAEFAELEKE 542
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSelrrqiqraelelqSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180
....*....|....*....|...
gi 2462613986 543 RDSLvsgaAHREEELSALRKELQ 565
Cdd:pfam05557 162 QSSL----AEAEQRIKELEFEIQ 180
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
400-515 |
3.08e-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: 38.75 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 400 RAELDE-LRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKE 478
Cdd:pfam20492 8 KQELEErLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462613986 479 LEDSLERISDQGQRKTQEQlevlESLKQELATSQREL 515
Cdd:pfam20492 88 AQEEIARLEEEVERKEEEA----RRLQEELEEAREEE 120
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
342-610 |
3.10e-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: 41.66 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 342 LIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQ---QHLRQQAADD-----------CEFLRAELDEL- 406
Cdd:pfam07111 307 LLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQsqeQAILQRALQDkaaevevermsAKGLQMELSRAq 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 407 ---RRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS-----MARQ---AQVDLE-- 473
Cdd:pfam07111 387 earRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglMARKvalAQLRQEsc 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 474 ---------------------REKKELEDSLE-----------RISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGS 521
Cdd:pfam07111 467 pppppappvdadlsleleqlrEERNRLDAELQlsahliqqevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQ 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 522 LETSAQSEANWAAEFAELEKE--RDSLVSGAAHRE---EELSALRKELQDTQLKLastEESMCQLAKDQRKMLLVGSRKA 596
Cdd:pfam07111 547 LEVARQGQQESTEEAASLRQEltQQQEIYGQALQEkvaEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAT 623
|
330
....*....|....
gi 2462613986 597 AEQVIQDALNQLEE 610
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 ... |
331-610 |
4.66e-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: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 331 QNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQR 410
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 411 EDTEK------------------AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDL 472
Cdd:pfam01576 450 NEAEGkniklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 473 EREKKELEDSLERIsDQGQRKTQEQLEVL------------------ESLKQEL------ATSQRE----LQVLQGSLET 524
Cdd:pfam01576 530 KKKLEEDAGTLEAL-EEGKKRLQRELEALtqqleekaaaydklektkNRLQQELddllvdLDHQRQlvsnLEKKQKKFDQ 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 525 SAQSEANWAAEFAElekERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKML------------LVG 592
Cdd:pfam01576 609 MLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgknvheLER 685
|
330
....*....|....*...
gi 2462613986 593 SRKAAEQVIQDALNQLEE 610
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEE 703
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
338-523 |
4.94e-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: 39.12 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 338 EKDHLIERLYREISGLKAQLENMKTESQrvvlqlkghvseleadLAEQQHLRQQAA-DDCEFLRAEL--------DELRR 408
Cdd:pfam15619 8 ARLHKIKELQNELAELQSKLEELRKENR----------------LLKRLQKRQEKAlGKYEGTESELpqliarhnEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 409 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL-LRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS 487
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELEN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462613986 488 DQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE 523
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
343-594 |
5.04e-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: 41.09 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 343 IERLYREISGLKAQLENMKTESQRvvLQ-LKGHVSELEAdlaeqQHLRQQAADDCEflrAELDELRRQREDtekAQRSLS 421
Cdd:COG3096 787 LEELRAERDELAEQYAKASFDVQK--LQrLHQAFSQFVG-----GHLAVAFAPDPE---AELAALRQRRSE---LERELA 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 422 EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNA------EVTKQVSMARQAQVDLEREKKELEdSLERI------- 486
Cdd:COG3096 854 QHRAQEQQLRQQLDQLKEQLQLLnkLLPQANLLADETladrleELREELDAAQEAQAFIQQHGKALA-QLEPLvavlqsd 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 487 -------------SDQGQRKTQEQLEVLESLKQ-----------ELATSQREL-QVLQGSLE--TSAQSEANWA-----A 534
Cdd:COG3096 933 peqfeqlqadylqAKEQQRRLKQQIFALSEVVQrrphfsyedavGLLGENSDLnEKLRARLEqaEEARREAREQlrqaqA 1012
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 535 EFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSR 594
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNR 1072
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
402-563 |
5.39e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 402 ELDELRRQ-----------REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqv 470
Cdd:PRK09039 54 ALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 471 dlerekkeleDSLERISDQGQRktqeQLEVLeslKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKErdsLVSGA 550
Cdd:PRK09039 126 ----------DSEKQVSARALA----QVELL---NQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR---LNVAL 185
|
170
....*....|...
gi 2462613986 551 AHREEELSALRKE 563
Cdd:PRK09039 186 AQRVQELNRYRSE 198
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
375-530 |
5.99e-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: 38.53 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 375 VSELEADLAEQQHLRQQAAddceflraeldeLRRQREDTEKAQRSLSEIERKAQANEQRYsklkekYSELvQNHADLLRK 454
Cdd:pfam07321 7 VKHLREDRAEKAVKRQEQA------------LAAARAAHQQAQASLQDYRAWRPQEEQRL------YAEI-QGKLVLLKE 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613986 455 NAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEA 530
Cdd:pfam07321 68 LEKVKQQVALLRENEADLEKQVAEARQQLEAEREalrQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELEEF 146
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
355-567 |
7.42e-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: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 355 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE------------ 422
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEaekaadesergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 423 --IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMarqAQVDLEREKKELEDSLERISD--QGQRKTQEQL 498
Cdd:pfam00261 81 kvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVV---VEGDLERAEERAELAESKIVEleEELKVVGNNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 499 EVLESlkQELATSQRE------LQVLQGSLEtsaqsEANWAAEFAE-----LEKERDSLVSGAAHREEELSALRKELQDT 567
Cdd:pfam00261 158 KSLEA--SEEKASEREdkyeeqIRFLTEKLK-----EAETRAEFAErsvqkLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
335-571 |
7.46e-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: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 335 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFlraeldELRRQREDTE 414
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE------EQKLEKLAEE 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 415 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK-NAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRK 493
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKeKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 494 TQ------EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 567
Cdd:pfam02463 935 EEpeelllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
....
gi 2462613986 568 QLKL 571
Cdd:pfam02463 1015 TCQR 1018
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
401-613 |
9.92e-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: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 401 AELDELRRQREDTEKAQRSLsEIERKAQANEQRYSKLKEKYselvqnhaDLLRK----NAEVTKQVSMARQAQVDLEREK 476
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENL-ELDEAEEALEEIEERIDQLY--------DLLEKevdaKKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 477 KELEDSLERIsDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE--TSAQSE-----ANWAAEFAELEKERDSLVSG 549
Cdd:pfam06160 308 KELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEekEVAYSElqeelEEILEQLEEIEEEQEEFKES 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613986 550 AAH-REEELSAlRKELQDTQLKLASTEESMCQ-----LAKDQRKMLLVGSRKaaeqvIQDALNQLEEPPL 613
Cdd:pfam06160 387 LQSlRKDELEA-REKLDEFKLELREIKRLVEKsnlpgLPESYLDYFFDVSDE-----IEDLADELNEVPL 450
|
|
| |
