|
Name |
Accession |
Description |
Interval |
E-value |
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
785-983 |
3.70e-95 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 299.28 E-value: 3.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 785 GVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLV 864
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 865 VQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQ-IEETDNMDFSSMT 943
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838745027 944 LTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELA 983
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
12-277 |
6.01e-94 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 299.21 E-value: 6.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 12 TVSINKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:pfam07651 3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 91 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 169
Cdd:pfam07651 83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 170 FQTVFNSLDMSRSVSVTaAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 243
Cdd:pfam07651 161 QKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
|
250 260 270
....*....|....*....|....*....|....
gi 1838745027 244 FYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 277
Cdd:pfam07651 240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
11-124 |
2.76e-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: 264.21 E-value: 2.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 11 ETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1838745027 91 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
12-124 |
7.92e-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: 224.85 E-value: 7.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 12 TVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNE 91
Cdd:cd17006 2 AISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSR 81
|
90 100 110
....*....|....*....|....*....|...
gi 1838745027 92 LSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17006 82 LKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
835-981 |
6.51e-60 |
|
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: 201.27 E-value: 6.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 835 KNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVN 914
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 915 QATAGVVASTISGKSQIEE--TDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYE 981
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
11-124 |
2.97e-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: 2.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 11 ETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRN 90
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 1838745027 91 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
12-124 |
1.10e-40 |
|
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: 145.60 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 12 TVSINKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAVLCWKFCHVFHKLLRDGHP--NVLKDSLR- 87
Cdd:cd16986 2 EKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDa 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1838745027 88 YRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd16986 81 WLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
9-131 |
8.04e-38 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 137.76 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 9 PPETVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVLKDSL 86
Cdd:smart00273 1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1838745027 87 RYRNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTKMEYHTKNPRFP 131
Cdd:smart00273 81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
453-551 |
1.56e-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: 127.05 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 1838745027 533 SEANWAAEFAELEKERDSL 551
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
13-124 |
2.32e-27 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 107.39 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 13 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNEL 92
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 1838745027 93 SDMSRMW-GHLSEGYGQLCSIYLKLLRTKMEYH 124
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-615 |
5.61e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHL-IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTE 419
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKT 499
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----EAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 1838745027 580 EESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196 455 EEEEEALLELLAE--LLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-615 |
1.84e-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: 75.09 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAeqqhlrqqaADDCEFLRAELDELRRQREDTE----KA 421
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALL---------VLRLEELREELEELQEELKEAEeeleEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLErisdQGQRKTQE 501
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----ELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270
....*....|....*....|....*....|....
gi 1838745027 582 SMCQLAKDQRKMLlvgsRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168 415 RRERLQQEIEELL----KKLEEAELKELQAELEE 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-581 |
2.82e-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: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 QLEVLESLKQELATSQRELQvlqgSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:COG1196 423 LEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-593 |
8.73e-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: 72.78 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 340 NKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDte 419
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 420 kAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK-------ELEDSLERIS 492
Cdd:TIGR02168 335 -LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneieRLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 493 DQGQRKTQEQLEVLESL--------KQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSlvsgAAHREEELSA 564
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA----AERELAQLQA 489
|
250 260
....*....|....*....|....*....
gi 1838745027 565 LRKELQDTQLKLASTEESMCQLAKDQRKM 593
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-615 |
1.05e-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: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQR----VVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQR 423
Cdd:COG1196 188 LERLEDILGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEE----LEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 424 S----LSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgqrkT 499
Cdd:COG1196 264 EleaeLEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----L 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 500 QEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAST 579
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270
....*....|....*....|....*....|....*.
gi 1838745027 580 EESmcQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG1196 420 EEE--LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-561 |
2.84e-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: 69.41 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE 427
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 428 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVD-LEREKKELEDSLERISDQGQRKtQEQLEVL 506
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERAEL-EALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838745027 507 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEE 561
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-615 |
5.11e-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: 70.47 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 353 REISGLKAQLEnmktesqrvvlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEK-AQRSLSEIERK 431
Cdd:TIGR02168 677 REIEELEEKIE-----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 432 AQANEQRYSKLKEKYSELVQNHADL--LRKNAEVTKQVSMARQAQVD-LEREKKELE---DSLERISDQGQRKTQEQLEV 505
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALRealDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 506 LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-------REEELSALRKELQDTQLKLAS 578
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRE 905
|
250 260 270
....*....|....*....|....*....|....*...
gi 1838745027 579 TEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168 906 LESKRSELRRElEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-610 |
1.59e-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: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLkAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:COG1196 281 LELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1196 360 ---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEanwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEE 581
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELL----EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
250 260 270
....*....|....*....|....*....|....
gi 1838745027 582 SmcQLAKDQRKMLLVGSR-----KAAEQVIQDAL 610
Cdd:COG1196 513 A--LLLAGLRGLAGAVAVligveAAYEAALEAAL 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-659 |
4.15e-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: 67.40 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA---- 421
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIenrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAQANEQRYSKLKEKYSEL--------VQNHADLLRK-NAEVTKQVSMARQAQVDLER---EKKELEDSLE 489
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKlEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 490 RISDQgQRKTQEQLEvleSLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKEL 569
Cdd:TIGR02169 837 ELQEQ-RIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-------EAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 570 QDTQLKLasteesmcqlakdQRKMLLVGSRKAAEQVIQDALNQLEEPPliscagsadhllSTVTSISSCIEQLEKSWSQY 649
Cdd:TIGR02169 906 EELEAQI-------------EKKRKRLSELKAKLEALEEELSEIEDPK------------GEDEEIPEEELSLEDVQAEL 960
|
330
....*....|
gi 1838745027 650 LACPEDISGL 659
Cdd:TIGR02169 961 QRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-615 |
2.43e-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: 64.69 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 340 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQlkghVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdte 419
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK----------------- 482
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieele 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 483 ----ELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRElqvlqgsletsaqseanWAAEFAELEKERDSLvsgaahr 558
Cdd:TIGR02168 866 elieELESELEALLNE-RASLEEALALLRSELEELSEELRE-----------------LESKRSELRRELEEL------- 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 559 EEELSALRKELQDTQLKLASTEEsmcQLAKDQRKML-----LVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLeeaeaLENKIEDDEEEARRRLKRLEN 979
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
381-602 |
7.76e-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: 62.09 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 381 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL 456
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 457 LRKnaevtkQVSMARQAQVDLEREKKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE 534
Cdd:COG4942 110 LRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838745027 535 ANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAA 602
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-591 |
1.13e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 406 AELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaEVTKQVSMARQAQVDLEREKKELE 485
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 486 DSLERIsdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLETS-AQSEANWAAEFAELEKERDSLVSGAAHREEELSA 564
Cdd:COG4717 146 ERLEEL--------EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*..
gi 1838745027 565 LRKELQDTQLKLASTEESMCQLAKDQR 591
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
405-615 |
1.17e-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: 62.77 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 405 RAELDELRRQredTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLERE 480
Cdd:TIGR02168 676 RREIEELEEK---IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaeveQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 481 KKELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLET--SAQSEANwaAEFAELEKERDSLVSGAAHR 558
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKAlrEALDELR--AELTLLNEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838745027 559 EEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEE 615
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL------EELIEELESELEALLN 880
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-778 |
1.71e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLENMK------TESQRVVLQLKGHVSELEADLAEQQHLRQQaaddcefLRAELDELRRQR 415
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEEKIRELEERIEE-------LKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 416 EDTEKAQ------RSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLE 489
Cdd:PRK03918 283 KELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 490 RISDQGQRKTQeqlevLESLKQELATS-----QRELQVLQGSLETSAQSEANWAAEFAELEKERDSL------------- 551
Cdd:PRK03918 363 LYEEAKAKKEE-----LERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaieelkkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 552 --VSGAA----HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkaaEQVIqdalnqLEEPPLISCAGSA 625
Cdd:PRK03918 438 cpVCGRElteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL---------EKVL------KKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 626 DHLLSTVTSISSC-IEQLEKSWSQYLACPE-------DISGLLHSITLLAHLTSDAIAhgattCLRAPPEPADSLTEACK 697
Cdd:PRK03918 503 EQLKELEEKLKKYnLEELEKKAEEYEKLKEkliklkgEIKSLKKELEKLEELKKKLAE-----LEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 698 QYGRETLAYLASLEEE-GSLENADSTAMRncLSKIKAIGEELLPRgLDIKQEELgDLVDKEMAATSAAIETATARIEEML 776
Cdd:PRK03918 578 ELEELGFESVEELEERlKELEPFYNEYLE--LKDAEKELEREEKE-LKKLEEEL-DKAFEELAETEKRLEELRKELEELE 653
|
..
gi 1838745027 777 SK 778
Cdd:PRK03918 654 KK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-548 |
2.15e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 358 LKAQLENMKTESQRVVLQLKGHVSELEADLAE---QQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLsEIERKAQA 434
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELA 514
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|....
gi 1838745027 515 TSQRELQVLQGSLETSAQSEANWAAEFAELEKER 548
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
333-594 |
2.50e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 61.18 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 333 FNSQNGVNKDekdhLIERLYREISGLKAQLENMKtesQRVVLQLKgHVSELEA----DLAEQQHLRQQAADDCEFLRAEL 408
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQ---QQIKTYNK-NIEEQRKkngeNIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 409 DELRRQREDTEKAQRSLSEIERKAQaneQRYSKLKEKYsELVQNHADLLRKNAEV---TKQVSMARQAQVDLEREKKELE 485
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLN---TAAAKIKSKI-EQFQKVIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 486 DSLERISDQgqrktQEQLEVLESlkqELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL 565
Cdd:PHA02562 313 HSLEKLDTA-----IDELEEIMD---EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|....*....
gi 1838745027 566 RKELQDTQLKLASTEESmcqlaKDQRKML 594
Cdd:PHA02562 385 QDELDKIVKTKSELVKE-----KYHRGIV 408
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
354-615 |
5.00e-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: 60.57 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 354 EISGLKAQLE---NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIER 430
Cdd:pfam01576 244 ELQAALARLEeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 431 KaqaNEQRYSKLKEKYSELVQNH----ADLLRKNA----EVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQ 502
Cdd:pfam01576 324 K---REQEVTELKKALEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL--------QAE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 503 LEVLESLKQELATSQR----ELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKklegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
250 260 270
....*....|....*....|....*....|....*...
gi 1838745027 579 TEEsmcQLAKDQRKMLLVGSRKAAEQVIQDAL-NQLEE 615
Cdd:pfam01576 473 TQE---LLQEETRQKLNLSTRLRQLEDERNSLqEQLEE 507
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
13-97 |
5.14e-09 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 54.97 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 13 VSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYR 89
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
....*...
gi 1838745027 90 NELSDMSR 97
Cdd:cd03564 83 GHIFNLSN 90
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-583 |
6.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 402 EFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREK 481
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 482 KELEDSLERISDQGQRKTQEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAElekERDSLVSGAAHREEE 561
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVEREL 767
|
170 180
....*....|....*....|..
gi 1838745027 562 LSALRKELQDTQLKLASTEESM 583
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
332-576 |
2.88e-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: 57.72 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 332 NFNSQNGV---NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEadlaEQQHLRQQAADDCEFLRAEL 408
Cdd:TIGR04523 222 ELKKQNNQlkdNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 409 DELRRQRE---------DTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLER 479
Cdd:TIGR04523 298 SDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 480 EKKELEDSLE----RISD-----QGQRKTQEQLEV-LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 549
Cdd:TIGR04523 378 ENQSYKQEIKnlesQINDleskiQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
250 260
....*....|....*....|....*..
gi 1838745027 550 SLVSGAAHREEELSALRKELQDTQLKL 576
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
341-523 |
3.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHL--IERLYREISGLKAQ---LENMKT-----ESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDE 410
Cdd:COG4913 248 REQIELLepIRELAERYAAARERlaeLEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 411 LRRQR------------EDTEKAQRSLSEIERKAQANEQRYSKLK-------EKYSELVQNHADLL----RKNAEVTKQV 467
Cdd:COG4913 328 LEAQIrgnggdrleqleREIERLERELEERERRRARLEALLAALGlplpasaEEFAALRAEAAALLealeEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838745027 468 SMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVL 523
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
382-565 |
3.51e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 382 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 462 EVTKQVSMARQAQVDLEREKKELE----------DSLERISDQ-GQrkTQEQLEVLESLKQELATSQRELQVLQGSLETS 530
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsGE--EFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
170 180 190
....*....|....*....|....*....|....*
gi 1838745027 531 AQSeanwaaefaeLEKERDSLVSGAAHREEELSAL 565
Cdd:PRK04863 654 KQA----------LDEEIERLSQPGGSEDPRLNAL 678
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
352-570 |
3.68e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 352 YREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtekaqrslSEI 428
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR----------VDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 429 ERKAQANEQRYSKLKEKYSELVqnhADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQG--------QRKTQ 500
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNreeaeewyQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 501 E-QLEV------LESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELE----KERDSLVSGAAHREEELSALRKEL 569
Cdd:pfam00038 200 ElQQAAarngdaLRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEM 279
|
.
gi 1838745027 570 Q 570
Cdd:pfam00038 280 A 280
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-614 |
5.99e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 396 QAADDCEFLRAELDELRRQREDTEKAQR---SLSEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAEVTKQVSMARQ 472
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 473 AQVDLEREKKELEDSLERISDQGQRKTQEQlEVLESLKQELATSQ-RELQVLQGSLETSAQSEANWAAEFAELEKERDSL 551
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALR-EELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838745027 552 VSGAAHREEELSALRKELQDTQLKLASTEESmCQLAKDQRKMLLVGSRKAAEQvIQDALNQLE 614
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEA-LEEALAEAEAALRDLRRELRE-LEAEIASLE 432
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
381-603 |
1.26e-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: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 381 SELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEkaqRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN 460
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 461 AEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELAT---SQRELQVLQGSLETSAQSEANW 537
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 538 AAEFAELEK---ERDSLVS-------------GAAHREE-ELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRK 600
Cdd:pfam07888 191 SKEFQELRNslaQRDTQVLqlqdtittltqklTTAHRKEaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
...
gi 1838745027 601 AAE 603
Cdd:pfam07888 271 QAE 273
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
334-579 |
1.77e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 334 NSQNGVNKDEKDHLIERLYREISGLKAQLEnmktESQRVVLQLK---GHVS-ELEADLAEQQ--HLRQQAADdcefLRAE 407
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRqknGLVDlSEEAKLLLQQlsELESQLAE----ARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 408 LDELRRQREDTEKAQRSLSEIERKAQANEQrYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqVDLEREKKELEDS 487
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 488 LERISDQGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAnwaaEFAELEKERDSLvsgaahrEEELSALRK 567
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASL---QAQLAQLEARLAELPELEA----ELRRLEREVEVA-------RELYESLLQ 372
|
250
....*....|..
gi 1838745027 568 ELQDTQLKLAST 579
Cdd:COG3206 373 RLEEARLAEALT 384
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-573 |
2.08e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 334 NSQNGVNKDEkdhlIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCE----------F 403
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 404 LRAELDELRRQREDTEKAQRSLS-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSMARQAQVDLER 479
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 480 EKKELEDSLERISDQ----GQRKTQEQLE-VLESLKQELAtsqrELQVLQGSLEtSAQSEANwaAEFAELEKERDSLVSG 554
Cdd:TIGR04523 532 EKKEKESKISDLEDElnkdDFELKKENLEkEIDEKNKEIE----ELKQTQKSLK-KKQEEKQ--ELIDQKEKEKKDLIKE 604
|
250
....*....|....*....
gi 1838745027 555 AAHREEELSALRKELQDTQ 573
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAK 623
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
404-588 |
3.07e-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: 54.69 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 404 LRAELDELRRQREDTEKAQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKK 482
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 483 ELEDSLERISDQGQRKTQEQLEVLES-----------LKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL 551
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGELEAeiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838745027 552 VSGAAHREEELSALRKELQDTQLKLASTEESMCQLAK 588
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
347-592 |
3.48e-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: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 347 LIERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELEADLAEQQHLRQQ-AADDCEFLRAELDELRRQREDTEKAQ 422
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLrqqLDQLKEQLQLLNKLLPQANLLADEtLADRLEELREELDAAQEAQAFIQQHG 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 423 RSLSEIERKA---QANEQRYSKLKEKYSELVQNHaDLLRKNAEVTKQVsMARQAQ------VDLEREKKELEDSLERISD 493
Cdd:COG3096 917 KALAQLEPLVavlQSDPEQFEQLQADYLQAKEQQ-RRLKQQIFALSEV-VQRRPHfsyedaVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 494 QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAH-----REEELSALRKE 568
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARirrdeLHEELSQNRSR 1074
|
250 260
....*....|....*....|....
gi 1838745027 569 LQDTQLKLASTEESMCQLAKDQRK 592
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-549 |
5.15e-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: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 354 EISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 433
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 434 ANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEqlevLESLKQEL 513
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDRVEKEL 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838745027 514 ATSQRELQVLQGSLETSAQSEANWAAEFAELEKERD 549
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
341-532 |
6.92e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHvsELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEK 420
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRslseieRKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQ 500
Cdd:pfam17380 482 EKR------DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190
....*....|....*....|....*....|..
gi 1838745027 501 EQLEVLESLKQELATSQRELQVLQGSLETSAQ 532
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
360-615 |
7.01e-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: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 360 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADdCEFLRAELDELRRQREDTEKA---------QRSLSEIER 430
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-IEELRAQEAVLEETQERINRArkaaplaahIKAVTQIEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 431 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLevLESLK 510
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH--IHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 511 QELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVsgAAHREEELSALRKELQdtqlKLASTEESMCQLAKDQ 590
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA--HAKKQQELQQRYAELC----AAAITCTAQCEKLEKI 459
|
250 260
....*....|....*....|....*
gi 1838745027 591 RKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQ 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-574 |
7.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 382 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQRE------DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQN 452
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 453 HADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLE--------------VLESLKQELATSQR 518
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavereLRENLEERIDALRA 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 519 ELQVLQGSLEtSAQSEAN--WAAEFAEL----------EKERDSLV-SGAAHREEELSALRKELQDTQL 574
Cdd:COG4913 781 RLNRAEEELE-RAMRAFNreWPAETADLdadleslpeyLALLDRLEeDGLPEYEERFKELLNENSIEFV 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
403-615 |
8.56e-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: 53.15 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 403 FLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSelvqnhaDLLRKNAEVTKQVSMARQaqvDLEREKK 482
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQ---EEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 483 ELEDSLERISDQGQRKTQEQLEvLESLKQELATSQRELQVLQGSLETSAQSEANwaAEFAELEKERDSLVSGAAHREEEL 562
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838745027 563 SALRKELQDTQLKLASTEESMCQLakdQRKMLLVGSRKAAEQVIQDALN-QLEE 615
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIEKEIENLNgKKEE 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
345-614 |
1.08e-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: 52.81 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 345 DHLIERL---YREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA 421
Cdd:pfam15921 415 DHLRRELddrNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QR-------SLSEIERKAQANEQRYSKLKE----KYSEL--VQNHADLLRkNAEV---TKQVSMARQAQVdLEREKKELE 485
Cdd:pfam15921 495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhLKNEGDHLR-NVQTeceALKLQMAEKDKV-IEILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 486 DSLERISDQGQ-------RKTQEQLEV---------LESLKQELATSQRELQVLQGSLETSAQSEANWAAE----FAELE 545
Cdd:pfam15921 573 NMTQLVGQHGRtagamqvEKAQLEKEIndrrlelqeFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIK 652
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 546 KERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMcQLAKDQRKMLLVGSRKAAEQViQDALNQLE 614
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQT-RNTLKSME 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-572 |
1.10e-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: 52.75 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 353 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAAD---DCEFLRAELDELRRQREDTEKAQRSLSEIe 429
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNE- 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 430 rKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELE---DSL-ERISDQGQRKTQEQLEV 505
Cdd:TIGR02168 882 -RASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLqERLSEEYSLTLEEAEAL 959
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 506 LESLKQELATSQRELQVLQGSLEtsAQSEANWAA--EFAELEKERDSLvsgaAHREEELSALRKELQDT 572
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIK--ELGPVNLAAieEYEELKERYDFL----TAQKEDLTEAKETLEEA 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
347-615 |
1.13e-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: 52.81 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 347 LIERLYREISGLKA-------QLENMKTESQ-RVVLQLKGH-------VSELEADLAEQQHLRQQAADDCEFLRAELDEL 411
Cdd:pfam15921 225 ILRELDTEISYLKGrifpvedQLEALKSESQnKIELLLQQHqdrieqlISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 412 RRQ-REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQN-HADLLRKNAEVTKqvsmARQAQVDLEREKKELEDSLE 489
Cdd:pfam15921 305 QEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSELTE----ARTERDQFSQESGNLDDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 490 R-ISDQGQRKTQEQLE----------------VLESLKQELATSQRELQVLQGSLET-SAQSEANWAAEFAELEKERDSL 551
Cdd:pfam15921 381 KlLADLHKREKELSLEkeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838745027 552 vsgaahreEELSALRKELQDTQLKLASTEESMCqlakdQRKMLLvgsrKAAEQVIQDALNQLEE 615
Cdd:pfam15921 461 --------EKVSSLTAQLESTKEMLRKVVEELT-----AKKMTL----ESSERTVSDLTASLQE 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
411-615 |
1.22e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 411 LRRQREDTEKAQRSLSE----IERKAQANEQRYSKLKEKYS--ELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKEL 484
Cdd:COG3206 166 LELRREEARKALEFLEEqlpeLRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 485 EDSLERISDQGQRKTQEQleVLESLKQELATSQRELQVLQGSLETS-----------AQSEANWAAEFAELEKERDSLVS 553
Cdd:COG3206 246 RAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYTPNhpdvialraqiAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 554 GAAHREEELsalRKELQDTQLKLASTEESMCQLAKDQRKmllvgsRKAAEQVIQDALNQLEE 615
Cdd:COG3206 324 ALQAREASL---QAQLAQLEARLAELPELEAELRRLERE------VEVARELYESLLQRLEE 376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-622 |
1.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKGHVSELEAdlAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQR 438
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 439 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERISDQGQRKTQEQLEVLESLK-QELATSQ 517
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADELKKaEELKKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 518 RELQVLQGSLETSAQSEANWAAEFA-ELEKERDSLVSGAAHREEELSA--LRKElQDTQLKLASTEEsmcqlAKDQRKML 594
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAeeAKKA-EEAKIKAEELKK-----AEEEKKKV 1635
|
250 260
....*....|....*....|....*....
gi 1838745027 595 LVGSRKAAEQVIQ-DALNQLEEPPLISCA 622
Cdd:PTZ00121 1636 EQLKKKEAEEKKKaEELKKAEEENKIKAA 1664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
364-606 |
1.44e-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: 52.43 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 364 NMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDEL------RRQREDTEKAQRslSEIERKAQ--AN 435
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKareverRRKLEEAEKARQ--AEMDRQAAiyAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 436 EQRYSKLKEKYSELVQNHadllrknaEVTKQVSMARQAQVDLEREKKEledSLERISDQGQRKTQEQLEVLESL-KQELA 514
Cdd:pfam17380 339 QERMAMERERELERIRQE--------ERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAArKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 515 TSQRELQVLQGSLETS---AQSEANWAAEFAELEKER----DSLVSGAAHREEELSALRKELQDTQLK--LASTEESMCQ 585
Cdd:pfam17380 408 EEERQRKIQQQKVEMEqirAEQEEARQREVRRLEEERaremERVRLEEQERQQQVERLRQQEEERKRKklELEKEKRDRK 487
|
250 260
....*....|....*....|.
gi 1838745027 586 LAKDQRKMLLVGSRKAAEQVI 606
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAM 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-615 |
1.70e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKGHVSEL-EADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRsLSEIERKAQ 433
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEakkkAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 434 ANEQRYSKLKEKYSELVQ----NHADLLRKNAEVTK--QVSMARQAQVDLER--------------EKKELEDSLERISD 493
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKaeekKKADELKKAEELKKaeEKKKAEEAKKAEEDknmalrkaeeakkaEEARIEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 494 QGQRKTQE-QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:PTZ00121 1604 EKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1838745027 573 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
382-565 |
2.52e-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: 51.88 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 382 ELEADLAEQQHLRQQAaddcEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 462 EVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL-ESLKQELATSQRELQVLQGSLE---TSAQSEANW 537
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPA-----WLAAQDALERLrEQSGEALADSQEVTAAMQQLLErerEATVERDEL 649
|
170 180
....*....|....*....|....*...
gi 1838745027 538 AAEFAELEKERDSLVSGAAHREEELSAL 565
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-615 |
2.60e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADD----CEFLRAELDELRRQREDTEKAQRSLSEIERKAQA 434
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQA-QVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQ-- 511
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKad 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 512 EL--ATSQRELQVLQGSLETSAQSEANWAAEF---------AELEKERDSLVSGAAHREEE--LSALRKELQDTQLKLAS 578
Cdd:PTZ00121 1514 EAkkAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEAR 1593
|
250 260 270
....*....|....*....|....*....|....*...
gi 1838745027 579 TEESMcQLAKDQRKMLLVGSRKAAEQVIQ-DALNQLEE 615
Cdd:PTZ00121 1594 IEEVM-KLYEEEKKMKAEEAKKAEEAKIKaEELKKAEE 1630
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-525 |
3.08e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQ--AADDCEFLRAElDELRRQREDTEKAQ--RSLSEIERKAQA 434
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAA-EEAKKAEEDKKKAEeaKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 435 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ----VSMARQAQVDLEREKKELEdslERISDQGQRKTQEQLEVLESLK 510
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKK 1769
|
170
....*....|....*
gi 1838745027 511 QELATSQRELQVLQG 525
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEE 1784
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
388-536 |
4.19e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.48 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 388 AEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEvtkqv 467
Cdd:PRK12705 46 AEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELE----- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 468 smarqaqvdLEREKKELEDSLERISdqGQRKTQEQLEVLESLKQELatsQRELQVLQGSLETSAQSEAN 536
Cdd:PRK12705 121 ---------LEELEKQLDNELYRVA--GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
396-582 |
4.45e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 396 QAADDCEFLRAELDELRRQREDtekAQRSLSEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQV---- 467
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERReelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 468 SMARQAQVDLER--------EKKELED------SLERISDQGQRKTQEQ---LEVLESLKQELATSQRELQVLQGSLEtS 530
Cdd:COG3883 90 ERARALYRSGGSvsyldvllGSESFSDfldrlsALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELE-A 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 531 AQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 582
Cdd:COG3883 169 AKAELE--AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
354-582 |
4.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 354 EISGLKAQLENMKTESQRVVLQLKghvsELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQ 433
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 434 ANEQRYSKLKEKYSELV--QNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSlerisdqgQRKTQEQLEVLESLKQ 511
Cdd:COG3883 93 RALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAK--------KAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838745027 512 ELATSQRELQvlqgsletSAQSEANwaAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEES 582
Cdd:COG3883 165 ELEAAKAELE--------AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
348-619 |
4.91e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVvlqlkghVSELEADLAEQQHLRQQaaddceflraeldeLRRQREDTEKAQRSLSE 427
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQL-------EEELEQARSELEQLEEE--------------LEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 428 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgqrktQEQLEVLE 507
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL--------QEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 508 SLKQELATSQRELQVLQgsLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLA 587
Cdd:COG4372 171 QELQALSEAEAEQALDE--LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270
....*....|....*....|....*....|..
gi 1838745027 588 KDQRKMLLVGSRKAAEQVIQDALNQLEEPPLI 619
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
349-575 |
5.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELE------ADLAEQQHLRQQAADdcefLRAELDELRRQREDTEKAQ 422
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAE----LPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 423 RSLSEIERKAQANEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRktQE 501
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 QLEVLESLKQEL--ATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSLVSGAAHREEELSALRKELQDTQ 573
Cdd:COG4717 241 LEERLKEARLLLliAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEE 320
|
..
gi 1838745027 574 LK 575
Cdd:COG4717 321 LE 322
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
351-581 |
5.83e-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: 50.56 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 351 LYREISGLKAQLENMKTESQRVVLQLKGHVSELE----ADLAEQQHLRQQAADDCEFLRAEldELRRQREDTEK--AQRS 424
Cdd:pfam01576 55 LCAEAEEMRARLAARKQELEEILHELESRLEEEEersqQLQNEKKKMQQHIQDLEEQLDEE--EAARQKLQLEKvtTEAK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 425 LSEIERKAQANEQRYSKL-------KEKYSELVQNHADLLRKNAEVT----KQVSMARQAQVDLEREKK---ELEDS--- 487
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLskerkllEERISEFTSNLAEEEEKAKSLSklknKHEAMISDLEERLKKEEKgrqELEKAkrk 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 488 LERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWA----------AEFAE-LEKERDSLVSGAA 556
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALkkireleaqiSELQEdLESERAARNKAEK 292
|
250 260
....*....|....*....|....*...
gi 1838745027 557 HR---EEELSALRKELQDTQLKLASTEE 581
Cdd:pfam01576 293 QRrdlGEELEALKTELEDTLDTTAAQQE 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
385-576 |
5.87e-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: 48.77 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 385 ADLAEQQHLRQ-QAADdceflrAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK 459
Cdd:COG1579 1 AMPEDLRALLDlQELD------SELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 460 NAEVTKQVSMAR--------QAQVD-LEREKKELEDSLerisdqgqrktQEQLEVLESLKQELATSQRELQVLQGSLEts 530
Cdd:COG1579 75 IKKYEEQLGNVRnnkeyealQKEIEsLKRRISDLEDEI-----------LELMERIEELEEELAELEAELAELEAELE-- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838745027 531 aQSEANWAAEFAELEKERDSLvsgaahrEEELSALRKELQDTQLKL 576
Cdd:COG1579 142 -EKKAELDEELAELEAELEEL-------EAEREELAAKIPPELLAL 179
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
333-643 |
6.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 333 FNSQNGVNKDEKDHLIER---LYREISGLKAQLENMK---TESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRA 406
Cdd:PRK02224 340 HNEEAESLREDADDLEERaeeLREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 407 ELDELRRQREDTEKAQRSLSEIERKAQA-------------------------NEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 462 EVTKQVSMARQaqvdLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAA 539
Cdd:PRK02224 500 RAEDLVEAEDR----IERLEERREDLEELIAERRETieEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 540 EF----AELEKERDSL------VSGAAHREEELSALRKELQDTQL-------KLASTEESMCQLA---KDQRKMLLVGSR 599
Cdd:PRK02224 576 ELnsklAELKERIESLerirtlLAAIADAEDEIERLREKREALAElnderreRLAEKRERKRELEaefDEARIEEAREDK 655
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1838745027 600 KAAEQVIQDALNQLEEpplisCAGSADHLLSTVTSISSCIEQLE 643
Cdd:PRK02224 656 ERAEEYLEQVEEKLDE-----LREERDDLQAEIGAVENELEELE 694
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
402-613 |
6.93e-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: 50.35 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 402 EFLRAELDELRRQR-EDTEKAQRSLSEIERKAQAnEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvdleRE 480
Cdd:TIGR00618 545 EDVYHQLTSERKQRaSLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL----LR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 481 KKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRElQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaaHREE 560
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSIRVLPKELLASRQLALQKMQ--------SEKE 690
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838745027 561 ELSALRKELQDTQLKLASTEESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 613
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREfNEIENASSSLGSDLAAREDALNQS 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
470-628 |
8.08e-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: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 470 ARQAQVDLEREKKELEDSLERISDQgqrktqeqlevLESLKQELATSQRELQVLQGsLETSAQSEANWAA---EFAELEK 546
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEER-----------LEALEAELDALQERREALQR-LAEYSWDEIDVASaerEIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 547 ERDSLVSGAAhreeELSALRKELQDTQLKLASTEESMCQLAKDQRKmlLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 626
Cdd:COG4913 676 ELERLDASSD----DLAALEEQLEELEAELEELEEELDELKGEIGR--LEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
..
gi 1838745027 627 HL 628
Cdd:COG4913 750 LL 751
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
353-589 |
1.19e-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: 48.65 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 353 REISGLKAQLENMKTESQRVV---LQLKGHVSELEADLAE----QQHLRQQAADD-----CEFLRAELDELRRQREDTEK 420
Cdd:pfam15905 94 KRLQALEEELEKVEAKLNAAVrekTSLSASVASLEKQLLEltrvNELLKAKFSEDgtqkkMSSLSMELMKLRNKLEAKMK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSE-IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqvdlerekKELEDSLERISDQGQRKT 499
Cdd:pfam15905 174 EVMAKQEgMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSET--------------EKLLEYITELSCVSEQVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 500 QEQLEVlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAE----LEKERDSLVSGAAHREEELSAlrkELQDTQLK 575
Cdd:pfam15905 240 KYKLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEkcklLESEKEELLREYEEKEQTLNA---ELEELKEK 315
|
250
....*....|....
gi 1838745027 576 LASTEESMCQLAKD 589
Cdd:pfam15905 316 LTLEEQEHQKLQQK 329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
380-615 |
1.28e-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: 49.57 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 380 VSELEADLAEQQHLRQQAADDCEFLRA-------ELDELRRQREDTekaQRSLSEIERKAQANEQRYSKLkEKYSELVQN 452
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEArleaaeeEVDSLKSQLADY---QQALDVQQTRAIQYQQAVQAL-EKARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 453 hADLLRKNAEVTKQVSMARQAQVDleREKKELEDSLeRISDQGQRKTQEQLEVLESLKQELATSQ-----RELQVLQGSL 527
Cdd:COG3096 432 -PDLTPENAEDYLAAFRAKEQQAT--EEVLELEQKL-SVADAARRQFEKAYELVCKIAGEVERSQawqtaRELLRRYRSQ 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 528 ETSAQSEANWAAEFAELEKERDSL-----------------VSGAAHREEELSALRKELQDTQLKLASTEESMCQL---- 586
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQqnaerlleefcqrigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELrqql 587
|
250 260 270
....*....|....*....|....*....|.
gi 1838745027 587 --AKDQRKMLlvGSRKAAEQVIQDALNQLEE 615
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 ... |
342-583 |
1.32e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLEnmktESQRVVLQLKGHVSELEAD--------------LAEQ----QHLRQQAADDCEF 403
Cdd:pfam10174 390 DVKERKINVLQKKIENLQEQLR----DKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKeriiERLKEQREREDRE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 404 LRAELDELRRQRED---------TEKAQRSLSEIERKAQANEQRYSKLKeKYSELVQNHADLLRKNAEVTKQVSMARQAQ 474
Cdd:pfam10174 466 RLEELESLKKENKDlkekvsalqPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 475 --VDLEREKKELEDSLERISDQGQRKTQE----QLEV---LESLKQ----------------ELATSQRELQVLQGSLET 529
Cdd:pfam10174 545 naEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerlLGILREvenekndkdkkiaeleSLTLRQMKEQNKKVANIK 624
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838745027 530 SAQSE--ANWAAEFAELEKERDSLVSGAAHR--EEELSAL---RKELQDTQLKLASTEESM 583
Cdd:pfam10174 625 HGQQEmkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSSTQQSL 685
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
348-604 |
1.54e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRV---VLQLKGHVSELeadlaeQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRS 424
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQrsqLEQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 425 -------LSEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVsm 469
Cdd:PRK04863 913 vqqhgnaLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKL-- 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 470 aRQAQVDLEREKKELEDSLERISDQGQRKTQeqleVLESLKQELATSQRELQVLQGSL-ETSAQSEANwAAEFAELEKER 548
Cdd:PRK04863 991 -RQRLEQAEQERTRAREQLRQAQAQLAQYNQ----VLASLKSSYDAKRQMLQELKQELqDLGVPADSG-AEERARARRDE 1064
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838745027 549 dslvsgaahREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM--LLVGSRKAAEQ 604
Cdd:PRK04863 1065 ---------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerDYHEMREQVVN 1113
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
343-596 |
1.58e-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: 48.97 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 343 EKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEaDLAEQQHLRQQAADDCEFLRAELDelRRQREDTEKAQ 422
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 423 RsLSEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQR--- 497
Cdd:pfam05557 171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaat 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 498 ------KTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQD 571
Cdd:pfam05557 250 lelekeKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
250 260
....*....|....*....|....*
gi 1838745027 572 TQLKLASTEESMCQLakdQRKMLLV 596
Cdd:pfam05557 330 LNKKLKRHKALVRRL---QRRVLLL 351
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-578 |
1.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 353 REISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAadDCEFLRAELDEL-RRQREDTEKAQRSLSEIERK 431
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALlAEAGVEDEEELRAALEQAEE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 432 AQANEQRYSKLKEKyselVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKELEDSLERISDQgQRKTQEQLEVLESlKQ 511
Cdd:COG4717 397 YQELKEELEELEEQ----LEELLGELEELLEALDEEELEEELE-ELEEELEELEEELEELREE-LAELEAELEQLEE-DG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838745027 512 ELATSQRELQVLqgsletsaqseanwAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:COG4717 470 ELAELLQELEEL--------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-498 |
1.93e-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: 48.22 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVV--LQLKGHVSELEADLAEQ------------QHLRQQAADDCEFLRAELDELRR 413
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVqnhadllrknAEVTKQVSMARQAQVDLEREKKELEDSLERISD 493
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLL----------ARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*
gi 1838745027 494 QGQRK 498
Cdd:COG4942 235 EAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
350-569 |
2.56e-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: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 350 RLYREISGLKAQLENMKTESQR-VVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrslseI 428
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----L 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 429 ERKAQANEQRYSKLKEKYSEL-VQNHADLLRKNAEvtkqvsmaRQAQVDLEREKKELEDSLERISDQGQRKT------QE 501
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALeTWYKRDLASLGVD--------PDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyQE 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 502 Q-LEVLESLKQELATSQRELQVLQGSLetsAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKEL 569
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 ... |
383-593 |
2.90e-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: 48.25 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 383 LEADLAEqqhLRQQAADdcefLRAELDELRRQREDTEKA-QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 461
Cdd:pfam01576 213 LEGESTD---LQEQIAE----LQAQIAELRAQLAKKEEElQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 462 EVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEsLKQELATSQR--ELQV-------------LQGS 526
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE-LKKALEEETRshEAQLqemrqkhtqaleeLTEQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838745027 527 LETSAQSEANW-------AAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKM 593
Cdd:pfam01576 365 LEQAKRNKANLekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
359-663 |
3.19e-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: 48.12 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELD----ELRRQREDTEKAQRSLSEIERKAQA 434
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 435 NEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------MARQAQVDLER-------EKKELEDSLERISDQG---Q 496
Cdd:TIGR00606 770 QETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqEKQEKQHELDTVVSKIelnR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 497 RKTQEQLEVLESLKQELatsqRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSAL---RKELQDTQ 573
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLetfLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 574 LKLASTEESMCQLAKDQRKML------LVGSRKAAEQVIQDalnqleeppliscaGSADHLLSTVTSISSCIEQLEKSWS 647
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIkekvknIHGYMKDIENKIQD--------------GKDDYLKQKETELNTVNAQLEECEK 991
|
330
....*....|....*.
gi 1838745027 648 QYLACPEDISGLLHSI 663
Cdd:TIGR00606 992 HQEKINEDMRLMRQDI 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-592 |
3.81e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEI 428
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 429 ERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKT--- 499
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELeerieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeei 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 500 ---QEQLEVLES-------LKQELATSQRELQVLQGSLETSAQSEANwAAEFAELEKERDSLVSGAAHRE-EELSALRKE 568
Cdd:PRK03918 324 ngiEERIKELEEkeerleeLKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKElEELEKAKEE 402
|
250 260
....*....|....*....|....
gi 1838745027 569 LQDTQLKLASTEESMCQLAKDQRK 592
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKK 426
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
341-614 |
4.62e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHLIErlyrEISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHL---RQQAADDCEFLRAELDELRRQRED 417
Cdd:COG1340 28 KEKRDELNE----ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 418 TEKAQRSLSEIERKAQANEQRY-----SKLKEKysELVQNHADlLRKNAEvtkqvsmARQAQVDLEREKKELEDSLERIS 492
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK--ELVEKIKE-LEKELE-------KAKKALEKNEKLKELRAELKELR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 493 DQgqrktqeqlevLESLKQELATSQRELQVLQGSLeTSAQSEANwaaefaELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:COG1340 174 KE-----------AEEIHKKIKELAEEAQELHEEM-IELYKEAD------ELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1838745027 573 QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLE 614
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
349-615 |
4.64e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREisgLKAQLENMKTESQRVVLQLKghVSELE-------ADLAEQQHLRQQAADDCEFLRAELDELRRQREDtekA 421
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMS--TDALEqeilqvsSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE---A 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAQANEQRYSKLKEkyselvqnhADLLRKNAEVTkqvsmARQAQVDlerekkELEdsLERIS-DQGQRKTQ 500
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQ---------AQLTALQAESA-----ALKALVD------ELE--LAQLSaNNRQELAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 501 EQLEVLESLKQELatsQRELQVLQGSLETSAQSEANWAAEFAE-LEKERDSL---VSGAAHREEELSALrkelqdtqlkl 576
Cdd:PRK10929 208 LRSELAKKRSQQL---DAYLQALRNQLNSQRQREAERALESTElLAEQSGDLpksIVAQFKINRELSQA----------- 273
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1838745027 577 asteesmcqLAKDQRKMLLVGS--RKAAEQVIQ--DALNQLEE 615
Cdd:PRK10929 274 ---------LNQQAQRMDLIASqqRQAASQTLQvrQALNTLRE 307
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
358-551 |
6.50e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 358 LKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQR-------SLSEIER 430
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 431 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERisdqgQRKTQEQLEVL 506
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKE-----ANVSKFSSYKV 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838745027 507 ESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL------EKERDSL 551
Cdd:PLN02939 354 ELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTlsklkeESKKRSL 404
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-561 |
9.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHLIERLYREISGLKAQLENMKTESqrvVLQLKGHVSELEADLAEQQHLRQQAADdcefLRAELDELRRQREDTEK 420
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQ--RK 498
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEerEK 708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838745027 499 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSE-ANWAAE-FAELEKERdslVSGAAHREEE 561
Cdd:PRK03918 709 AKKELEKLEKALERVEELREKVKKYKALLKERALSKvGEIASEiFEELTEGK---YSGVRVKAEE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-512 |
9.90e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 339 VNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAeqqhlRQQAADDCEFLRaELDELR-----R 413
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKkaeekK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVdlEREKKELEDSLERiSD 493
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEK-AE 1367
|
170
....*....|....*....
gi 1838745027 494 QGQRKTQEQLEVLESLKQE 512
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKK 1386
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-615 |
1.18e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQLKghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSlseieRKAQANEQR 438
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 439 YSKLKEKYSELVQNhADLLRKNAEVT--KQVSMARQAqvdlEREKKELEDSleRISDQGQRKTQEQlevlesLKQELATS 516
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEENkiKAAEEAKKA----EEDKKKAEEA--KKAEEDEKKAAEA------LKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 517 QRELQVLQGSLEtsaqsEANWAAEFAELEKERDSLVSGAAHREEElsalrKELQDTQLKLASTEESMCQLAKDQRKMLLV 596
Cdd:PTZ00121 1702 KKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
250
....*....|....*....
gi 1838745027 597 GSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDE 1790
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
419-610 |
1.35e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 419 EKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrK 498
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE-----S 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 499 TQEQLEVLEslkQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQdtQLKLAS 578
Cdd:COG4372 106 LQEEAEELQ---EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAE 180
|
170 180 190
....*....|....*....|....*....|..
gi 1838745027 579 TEESMCQLAKDQRKMLLVGSRKAAEQVIQDAL 610
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
332-615 |
1.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 332 NFNSQNGVNKDEKDHLIERLYREISGLKAQlENMKTESQRVVLQLKGHvseleadlAEQQHLRQQAADDCEFLRAELDEL 411
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKK--------AEEAKKADEAKKKAEEAKKKADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 412 RRQREDTEKAQRSlSEIERKAQANEQRYSKLKEKYSEL----VQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDS 487
Cdd:PTZ00121 1335 KKKAEEAKKAAEA-AKAEAEAAADEAEAAEEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 488 LE--RISDQGQRKTQEQLEVLESLKQelATSQRELQVLQGSLETSAQSE-----------ANWAAEFAELEKERDSLVSG 554
Cdd:PTZ00121 1414 AAakKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEeakkkaeeakkADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838745027 555 AAHREEELSALRKELQDT----QLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-506 |
1.44e-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: 46.10 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 351 LYREISGLKAQLENmktesqrvVLQLKGHVSELEADLAEQQHLRQQAADDC----------EFLRAELDELRRQREDTEK 420
Cdd:COG3096 500 LLRRYRSQQALAQR--------LQQLRAQLAELEQRLRQQQNAERLLEEFCqrigqqldaaEELEELLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSE----IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEV------TKQVSMARQAQVDLEREKKELEDSLEr 490
Cdd:COG3096 572 QAAEAVEqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSgealadSQEVTAAMQQLLEREREATVERDELA- 650
|
170
....*....|....*.
gi 1838745027 491 isdQGQRKTQEQLEVL 506
Cdd:COG3096 651 ---ARKQALESQIERL 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
341-579 |
1.51e-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: 45.88 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 341 KDEKDHLIERLYREISGL---KAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELdelRRQRED 417
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLeleKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSEE 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 418 TEKAQRSLSEIERKAQAN-EQRYSKLKEKysELVQNHAdlLRKNAEVTKQVSmARQAQVD-LEREKKELEDSLERISDQG 495
Cdd:pfam15921 690 METTTNKLKMQLKSAQSElEQTRNTLKSM--EGSDGHA--MKVAMGMQKQIT-AKRGQIDaLQSKIQFLEEAMTNANKEK 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 496 QRKTQEQlevlESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSalRKELQDTQLK 575
Cdd:pfam15921 765 HFLKEEK----NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ--RQEQESVRLK 838
|
....
gi 1838745027 576 LAST 579
Cdd:pfam15921 839 LQHT 842
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
417-580 |
1.64e-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: 45.11 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 417 DTEKAQRSLSEIE---RKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMAR----QAQVDLEREKKELED--S 487
Cdd:pfam00529 52 DPTDYQAALDSAEaqlAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQaavkAAQAQLAQAQIDLARrrV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 488 LERISDQGQRKTQEQLEVLESLKQELATSQRELqvlqgsletsAQSEANWAAEFAELEKERDSLVSGAahrEEELSALRK 567
Cdd:pfam00529 132 LAPIGGISRESLVTAGALVAQAQANLLATVAQL----------DQIYVQITQSAAENQAEVRSELSGA---QLQIAEAEA 198
|
170
....*....|...
gi 1838745027 568 ELQDTQLKLASTE 580
Cdd:pfam00529 199 ELKLAKLDLERTE 211
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
348-573 |
1.65e-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: 45.06 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQ----QAADDCEFLRAELDELRRQREDTEKAQR 423
Cdd:pfam19220 74 LTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEalerQLAAETEQNRALEEENKALREEAQAAEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 424 SLSEIERKAQANEQRYS-------KLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQgq 496
Cdd:pfam19220 154 ALQRAEGELATARERLAlleqenrRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 497 rktqeQLEVLESLKQELATSQRELQVLQGSLETSAQ------------SEANWAAE--FAELEKERDSLVSGAAHREEEL 562
Cdd:pfam19220 232 -----LEEAVEAHRAERASLRMKLEALTARAAATEQllaearnqlrdrDEAIRAAErrLKEASIERDTLERRLAGLEADL 306
|
250
....*....|.
gi 1838745027 563 SALRKELQDTQ 573
Cdd:pfam19220 307 ERRTQQFQEMQ 317
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
359-536 |
1.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 359 KAQLENMKTESQRVVLQlkghvSELEADLAEQQHLRQQaaddceflRAELDELRRQREDtEKAQRsLSEIERKAQANEQR 438
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE-----AKKEAEAIKKEALLEA--------KEEIHKLRNEFEK-ELRER-RNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 439 YSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqRKTQEQL--EVLESLKQELats 516
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS----GLTAEEAkeILLEKVEEEA--- 167
|
170 180
....*....|....*....|
gi 1838745027 517 QRELQVLQGSLETSAQSEAN 536
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEAD 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
360-626 |
1.67e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 360 AQLENMKTESQRVVLQLkghvSELEADLAEQQHLRQQA------------ADDCEflrAELDELRRQREDtekAQRSLSE 427
Cdd:PRK04863 786 KRIEQLRAEREELAERY----ATLSFDVQKLQRLHQAFsrfigshlavafEADPE---AELRQLNRRRVE---LERALAD 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 428 IERKAQANEQRYSKLKEKYSEL--VQNHADLLRKN------AEVTKQVSMARQAQVDLEREKKELEdSLERIsdqgQRKT 499
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSALnrLLPRLNLLADEtladrvEEIREQLDEAEEAKRFVQQHGNALA-QLEPI----VSVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 500 QEQLEVLESLKQELATSQRELQVLQG---SLETSAQSEANWA-AEFAELEKERDSLVSGAAHREEELSALRKElQDTQLK 575
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTR-AREQLR 1009
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 576 lasteESMCQLAK-DQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSAD 626
Cdd:PRK04863 1010 -----QAQAQLAQyNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-511 |
1.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQRedtEKAQRS 424
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRREL---EELREK 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 425 LSEIERKAQANEQRYSKLKEKYSELVQ-NHADLLRKNAEVTKQVSMARQAQVDLEREKKEL----EDSLERISDQGQRK- 498
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYd 1003
|
170
....*....|....*
gi 1838745027 499 --TQEQLEVLESLKQ 511
Cdd:TIGR02168 1004 flTAQKEDLTEAKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-578 |
1.91e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 385 ADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQAneqRYSKLKEKYSELVQNHADLLRKNAEVT 464
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR---RAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 465 KQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAEL 544
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
170 180 190
....*....|....*....|....*....|....
gi 1838745027 545 EKERDSLVSGAAHREEELSALRKELQDTQLKLAS 578
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
348-603 |
2.08e-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: 45.02 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRVVLQL---KGHVSELEADLA-----------EQQHLRQQAA-DDCEFLRAELDELR 412
Cdd:pfam05701 72 LESTKRLIEELKLNLERAQTEEAQAKQDSelaKLRVEEMEQGIAdeasvaakaqlEVAKARHAAAvAELKSVKEELESLR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 413 RQRED--------TEKAQRSLS---EIERKAQANEQRYSKLKEkysELVQNHADLLrkNAEVTK-QVSMAR-QAQVDLER 479
Cdd:pfam05701 152 KEYASlvserdiaIKRAEEAVSaskEIEKTVEELTIELIATKE---SLESAHAAHL--EAEEHRiGAALAReQDKLNWEK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 480 EKKELEDSLERISDQ------GQRKTQEQLEVLESLKQEL-----------------------------ATSQRELQVLQ 524
Cdd:pfam05701 227 ELKQAEEELQRLNQQllsakdLKSKLETASALLLDLKAELaaymesklkeeadgegnekktstsiqaalASAKKELEEVK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 525 GSLEtSAQSEANW---AAEF--AELEKERDSLVS----------GAAHREEELSALRKELQDTQLKLASTEESMCQLAkd 589
Cdd:pfam05701 307 ANIE-KAKDEVNClrvAAASlrSELEKEKAELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELP-- 383
|
330
....*....|....
gi 1838745027 590 qrKMLLVGSRKAAE 603
Cdd:pfam05701 384 --KQLQQAAQEAEE 395
|
|
| F-BAR_FCHO1 |
cd07674 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ... |
421-583 |
2.30e-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: 44.16 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQN--HADLLRKNAEVTKqVSMARQAQVDLEREKKeLEDSLERISdqgqRK 498
Cdd:cd07674 20 STKELADFVRERAAIEETYSKSMSKLSKMASNgsPLGTFAPMWEVFR-VSSDKLALCHLELMRK-LNDLIKDIN----RY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 499 TQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERdslvsgaahREeelSALRKELQDTQLKLAS 578
Cdd:cd07674 94 GDEQVKIHKKTKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR---------RE---GVPQKELEKAELKTKK 161
|
....*
gi 1838745027 579 TEESM 583
Cdd:cd07674 162 AAESL 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
387-615 |
2.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 387 LAEQQHLRQQAADDCEfLRAELDELRRQREDTEKAQRSLSEIERKAQANEqryskLKEKYSELVQNHADLLRKNAEVTKQ 466
Cdd:COG4717 293 LAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDLSPEELLE-----LLDRIEELQELLREAEELEEELQLE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 467 VSMARQAQVdLEREKKELEDSLERISDQGQRKtQEQLEVLESLKQELATSQRELQVLQgsletSAQSEANWAAEFAELEk 546
Cdd:COG4717 367 ELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELE- 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 547 erdslvsgaahreEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrkAAEQVIQDALNQLEE 615
Cdd:COG4717 439 -------------EELEELEEELEELREELAELEAELEQLEEDGELA-------ELLQELEELKAELRE 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-513 |
2.54e-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: 43.76 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLENMKTEsqrvVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREdteka 421
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 qrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSmarQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:COG1579 91 ---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|..
gi 1838745027 502 QLEVLESLKQEL 513
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
482-643 |
2.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 482 KELEDSLERISDQGQRKTQ---EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSL--VSGAA 556
Cdd:COG4717 49 ERLEKEADELFKPQGRKPElnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 557 HREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsrKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSIS 636
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEEL------EELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
....*..
gi 1838745027 637 SCIEQLE 643
Cdd:COG4717 203 ELQQRLA 209
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
349-615 |
2.62e-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: 44.81 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREISGLKAQLENMKT--ESQRvvlQLKGHVSELEADLAEQQHLRQQAADDCEflraELDELRRQredTEKAQRSLS 426
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMELriETQK---QTLGARDESIKKLLEMLQSKGLPKKSGE----EDWERTRR---IAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 427 EIERKAQANEQRYSKLKEKYSELVQNHADllRKNAEVTKQVSMARQAQV-DLEREKKELEDSLERISDQGQRKTQE---- 501
Cdd:pfam10174 196 HLEVLLDQKEKENIHLREELHRRNQLQPD--PAKTKALQTVIEMKDTKIsSLERNIRDLEDEVQMLKTNGLLHTEDreee 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 --QLEV-----------LESLKQELATSQRELQVLQGSLET--SAQSEANWAAEF------------AELEKERDSLVSG 554
Cdd:pfam10174 274 ikQMEVykshskfmknkIDQLKQELSKKESELLALQTKLETltNQNSDCKQHIEVlkesltakeqraAILQTEVDALRLR 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838745027 555 AAHREEELSALRKELQDTqlklasTEESMCQLA--KDQRKMLLVGSRKAaeQVIQDALNQLEE 615
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDL------TEEKSTLAGeiRDLKDMLDVKERKI--NVLQKKIENLQE 408
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
368-547 |
2.73e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 368 ESQRVVLQLKGHVSELEADLAeqqHLRQQAADDCEFLRAELDELRRQ-----------REDTEKAQRSLSEIERKAQANE 436
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsGEESQRGERILAYFGYLNQARQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 437 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLE-----REK--KELEDSLERisDQGQRKTQEQLEVleSL 509
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEqarneRKKtlTGLESSLQK--DQQQLSELRANES--RL 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 1838745027 510 KQELATSQRELQvlqgsleTSAQSEANWAAEFAELEKE 547
Cdd:PRK11637 246 RDSIARAEREAK-------ARAEREAREAARVRDKQKQ 276
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
442-613 |
3.40e-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: 44.50 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 442 LKEKYSELVQNHADLLRKNAEVTKQVSMARQ----AQVDLEREKKELEDSLERISDQGQRKTQEQlevleslkQELATSQ 517
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKErykrDREQWERQRRELESRVAELKEELRQSREKH--------EELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 518 RELQVLQGSL--ETSAQSEANWA--AEFAELEKERDSLVSGAAHREEELS----------ALRKELQ----DTQLKLAST 579
Cdd:pfam07888 104 KELSASSEELseEKDALLAQRAAheARIRELEEDIKTLTQRVLERETELErmkerakkagAQRKEEEaerkQLQAKLQQT 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1838745027 580 EESMCQLAKD-QRKMLLVGSRKAAEQVIQDALNQL 613
Cdd:pfam07888 184 EEELRSLSKEfQELRNSLAQRDTQVLQLQDTITTL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
356-615 |
4.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 356 SGLKAQLEnmKTESQRVVLQLKGH---VSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKA 432
Cdd:PRK02224 190 DQLKAQIE--EKEEKDLHERLNGLeseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 433 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESL 509
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 510 KQELATsqrelqvlqgsLETSAQsEANWAAefAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAkD 589
Cdd:PRK02224 348 REDADD-----------LEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-D 412
|
250 260 270
....*....|....*....|....*....|..
gi 1838745027 590 QRKML------LVGSRKAAEQVIQDALNQLEE 615
Cdd:PRK02224 413 FLEELreerdeLREREAELEATLRTARERVEE 444
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
506-644 |
5.34e-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: 43.21 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 506 LESLKQELAT-SQRELQVLQ-----------GSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQ 573
Cdd:pfam09787 2 LESAKQELADyKQKAARILQskekliaslkeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838745027 574 LKLASTEESMCQLAKDQRKMLLvgSRKAAEQVIQDALNQLEEppliSCAGSADHLLSTVTSISSCIEQLEK 644
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 ... |
343-615 |
5.43e-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: 44.19 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 343 EKDHLIERLYREISGLKAQLENMKTESQRVvLQLKGHVSELEADLAEQQHLRQqaaddcEFLRAELDELRRQREDTEKAQ 422
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALL------RKLQPEQDLQDVRLHLQQCSQ 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 423 R-SLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKN-AEVTKQVSMARQAQVDLE--REKKELEDSLERISDQGQRK 498
Cdd:TIGR00618 640 ElALKLTALHALQLTLTQERVREHALSIRVLPKELLASRqLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDRE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 499 TQEQLEVLESLKQELATSQRELQVLQGSLetsaQSEANWAAEFAELEKERDSLVSGA--------AHREEELSALRKELQ 570
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKEL----MHQARTVLKARTEAHFNNNEEVTAalqtgaelSHLAAEIQFFNRLRE 795
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1838745027 571 DTQLKLASTEESMCQLAKDQRKMLLVGSRKAAeQVIQDALNQLEE 615
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEE 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-582 |
7.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 343 EKDHLIERLYREISGLKaQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQ 422
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 423 RSLSEIERkaqaNEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDqgQRKTQEQ 502
Cdd:PRK03918 221 EELEKLEK----EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE--LKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 503 LEVLESLKQELATSQRELQVLQGSLEtsaqseanwaAEFAELEKERDSLVSgaahREEELSALRKELQDTQLKLASTEES 582
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEER 360
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
334-572 |
7.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 334 NSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRR 413
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISD 493
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 494 QGQRKTQEQLEV----------LESLKQELATSQRELQVLqGSLetsaqseaNWAA--EFAELEKERDSLVSgaahREEE 561
Cdd:COG1196 740 ELLEEEELLEEEaleelpeppdLEELERELERLEREIEAL-GPV--------NLLAieEYEELEERYDFLSE----QRED 806
|
250
....*....|.
gi 1838745027 562 LSALRKELQDT 572
Cdd:COG1196 807 LEEARETLEEA 817
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
389-604 |
8.36e-04 |
|
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: 43.42 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 389 EQQHLRQQAADDCEFLRAELDELRRQREDTEKAQrsLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK--- 465
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQ--LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskq 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 466 --QVSMARQAQVDLEREKKELEDSL-ERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFA 542
Cdd:pfam02463 259 eiEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 543 ELEKERDSLVSGAAHREEELSALRKElqdtQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQ 604
Cdd:pfam02463 339 ELEKELKELEIKREAEEEEEEELEKL----QEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-615 |
9.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 466 QVSMARQAQVDLEREKKELEDSLERISDQgQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQseanwaaEFAELE 545
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838745027 546 KERDSLVSGAAHREEELSALRKELQ----DTQLKLASTEESMCQLAKDQRKM-LLVGSRKAAEQVIQDALNQLEE 615
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAA 164
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
343-593 |
1.02e-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: 43.18 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 343 EKDHLIERLyreisglKAQLENMktesqrvvLQLKG-HVSELEADLAEQQHLRQQAADDceflRAELDELRRQREdteKA 421
Cdd:pfam15921 559 EKDKVIEIL-------RQQIENM--------TQLVGqHGRTAGAMQVEKAQLEKEINDR----RLELQEFKILKD---KK 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQE 501
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 502 QLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKE---LQDTQLKLAs 578
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLS- 775
|
250
....*....|....*
gi 1838745027 579 teESMCQLAKDQRKM 593
Cdd:pfam15921 776 --QELSTVATEKNKM 788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
368-533 |
1.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 368 ESQRVVLQLkghvSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDT----EKAQRSLSEIERKAQANEQRYSKLK 443
Cdd:COG1579 4 EDLRALLDL----QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAktelEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 444 EKYSElVQNH---ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQREL 520
Cdd:COG1579 80 EQLGN-VRNNkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 1838745027 521 QVLQGSLETSAQS 533
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
409-615 |
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 1838745027 409 DELRRQREDTEKAQRSLS----EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQvDLEREKKEL 484
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREhlekEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQ-NLKGIKREL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 485 EDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSeANWAAEFAELEKERDSLVSGAAHREEELSA 564
Cdd:pfam18971 689 SDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGIN-PEWISKVENLNAALNEFKNGKNKDFSKVTQ 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838745027 565 LRKELQDT------QLKLASTEESMCQLAKDQRKMllvGSRKAAEQVIQDALNQLEE 615
Cdd:pfam18971 768 AKSDLENSvkdviiNQKVTDKVDNLNQAVSVAKAM---GDFSRVEQVLADLKNFSKE 821
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
342-583 |
1.09e-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: 43.02 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLENMKTEsqrvvlqlkghVSELEADLAEQQHLRQQAADDCEFlrAELDEL-RRQREDTEK 420
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEK-----------IAEYTKSIDIKKATESLEEQLAAA--EAEQELeESKRETETG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHAdlLRKNAEvtkqvsmarqaqvDLEREKKELEDSLERISDQGQRKTQ 500
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE--LSKSSE-------------ELDSFKDTIESTKESLDEIPQNQRG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 501 EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKE-----RDSLVSGAAHREEELSALRKELQDTQLK 575
Cdd:COG5185 403 YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvmREADEESQSRLEEAYDEINRSVRSKKED 482
|
....*...
gi 1838745027 576 LASTEESM 583
Cdd:COG5185 483 LNEELTQI 490
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
347-510 |
1.10e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 347 LIERLYREISGLKAQLENMKTESQRVVlQLKGHVSELEADLAEQQHLRQQAADDCEFLRAelDELRRQREDTEKAQRsls 426
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEEELRQLKQLEDELEDCDP--TELDRAKEKLKKLLQ--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 427 EIERKaqaneqrysklkekyselVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERI---SDQGQRKTQEQL 503
Cdd:smart00787 219 EIMIK------------------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQL 280
|
....*..
gi 1838745027 504 EVLESLK 510
Cdd:smart00787 281 KLLQSLT 287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
344-522 |
1.17e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 344 KDHLIERLYREISGLKAQLENM--KTESQRVvlqlkghvsELEADLAEQQHLRQQAaddceflraeldelRRQREDTEKA 421
Cdd:PRK00409 500 PENIIEEAKKLIGEDKEKLNELiaSLEELER---------ELEQKAEEAEALLKEA--------------EKLKEELEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 422 QRSLSEIERKAqaneqrYSKLKEKYSELVQNhadlLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISdqgqrktqE 501
Cdd:PRK00409 557 KEKLQEEEDKL------LEEAEKEAQQAIKE----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLN--------K 618
|
170 180
....*....|....*....|.
gi 1838745027 502 QLEVLESLKQELATSQRELQV 522
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKV 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
370-470 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 370 QRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKA----QRSLSEIERKAQANEQRYSKLKEK 445
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|....*
gi 1838745027 446 YSELVQNHADLLRKNAEVTKQVSMA 470
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
382-615 |
1.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 382 ELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLkEKYSElvqnhaDLLRKNA 461
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQA------DLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 462 EVTKQvSMARQaqvdlerEKKELEDSLERisdqgqRKTQEQLEVLEsLKQELATSQRELQVLQgsLETSAQSEANWAAEF 541
Cdd:PRK04863 363 RLEEQ-NEVVE-------EADEQQEENEA------RAEAAEEEVDE-LKSQLADYQQALDVQQ--TRAIQYQQAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 542 AELEKERDSL-VSGAAHREEELSALRKELQDTQLKLAsTEESMCQLAKDQ--RKMLLVG------SRKAAEQVIQDALNQ 612
Cdd:PRK04863 426 AKQLCGLPDLtADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQfeQAYQLVRkiagevSRSEAWDVARELLRR 504
|
...
gi 1838745027 613 LEE 615
Cdd:PRK04863 505 LRE 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-615 |
1.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 342 DEKDHLIERLYREISGLKAQLENMKTESQrvvlQLKGHVSELEADLAEQQHLR------------------------QQA 397
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIklkelaeqlkeleeklkkynleelEKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 398 ADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsmarqaqvDL 477
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 478 EREKKELEDSLER---ISDQGQRKtQEQLEVLESLKQELATSQRELQVLQGSLEtSAQSEANWAA------EFAELEKER 548
Cdd:PRK03918 591 EERLKELEPFYNEyleLKDAEKEL-EREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEkkyseeEYEELREEY 668
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 549 DSLvsgaahrEEELSALRKELQDTQLKLASTEESMCQLAKDQRKMllvgsRKAAEQV--IQDALNQLEE 615
Cdd:PRK03918 669 LEL-------SRELAGLRAELEELEKRREEIKKTLEKLKEELEER-----EKAKKELekLEKALERVEE 725
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
406-575 |
1.54e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 406 AELDElRRQREDTEKAQRSLSEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtkqvsmaRQAQVDLEREKKELE 485
Cdd:COG1566 74 ARLDP-TDLQAALAQAEAQLAA----AEAQLARLEAELGAEAEIAAAEAQLAAAQAQL-------DLAQRELERYQALYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 486 DSLerISDQgqrktqeqleVLESLKQELATSQRELQVLQGSLEtSAQSEANWAAEFAELEKERDSLvsgaahrEEELSAL 565
Cdd:COG1566 142 KGA--VSQQ----------ELDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQVAQA-------EAALAQA 201
|
170
....*....|
gi 1838745027 566 RKELQDTQLK 575
Cdd:COG1566 202 ELNLARTTIR 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
432-614 |
1.59e-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: 42.74 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 432 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIsdqgQRKTQEQLEVLESLKQ 511
Cdd:TIGR02168 632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRK 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 512 ELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEEsmcQLAKDQR 591
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE---ELAEAEA 782
|
170 180
....*....|....*....|...
gi 1838745027 592 KmllvgsRKAAEQVIQDALNQLE 614
Cdd:TIGR02168 783 E------IEELEAQIEQLKEELK 799
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
349-614 |
1.65e-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: 42.52 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 349 ERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEF--------LRAELDELRRQREDTEK 420
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSMARQAQVD--------------------LERE 480
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 481 KKELEDSLERISDQGQ--RKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHR 558
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838745027 559 EEELSALRKELQDTQLKLA-------STEESMCQLAKDQR--KMLLVGSRKAAEQVIQDALNQLE 614
Cdd:pfam12128 624 EEQLVQANGELEKASREETfartalkNARLDLRRLFDEKQseKDKKNKALAERKDSANERLNSLE 688
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
348-560 |
1.70e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKtesQRV-----VLQLKGHVSELEA--DLAEQQHLRQQaaddcefLRAELDELRRQREdteK 420
Cdd:PRK04863 937 FEQLKQDYQQAQQTQRDAK---QQAfalteVVQRRAHFSYEDAaeMLAKNSDLNEK-------LRQRLEQAEQERT---R 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 421 AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV--SMARQAQVDLEREKKELEDSLERISDQGQRK 498
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdsGAEERARARRDELHARLSANRSRRNQLEKQL 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838745027 499 TQEQLEvLESLKQELATSQRELQVLQgslETSAQSEANWaaeFAELEKERDSLVSGAAHREE 560
Cdd:PRK04863 1084 TFCEAE-MDNLTKKLRKLERDYHEMR---EQVVNAKAGW---CAVLRLVKDNGVERRLHRRE 1138
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
403-570 |
1.98e-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: 42.04 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 403 FLRAELDELRRQREDTEKAQ-RSLSEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNaEVTKQVSMarQAQVDLEREK 481
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQEL-QKRIRLLEKR-EAEAEEAL--REQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 482 KELEDSLERISDQGQRKTQEQLEVLESLKQELA--------------TSQRELQVLQGSLETSAQSEANWAAEFAELEKE 547
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSelrrqiqraelelqSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180
....*....|....*....|...
gi 1838745027 548 RDSLvsgaAHREEELSALRKELQ 570
Cdd:pfam05557 162 QSSL----AEAEQRIKELEFEIQ 180
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
337-523 |
2.06e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 337 NGVNKDEKDHLIER--LYREISGLKAQLENMKTESQRVVLQLKGHVSEleadlaEQQHLRQQAADDCEFLRAeLDELRRQ 414
Cdd:pfam00038 106 VGLRKDLDEATLARvdLEAKIESLKEELAFLKKNHEEEVRELQAQVSD------TQVNVEMDAARKLDLTSA-LAEIRAQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 415 REdtEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNH----ADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLER 490
Cdd:pfam00038 179 YE--EIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAkeeiTELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
|
170 180 190
....*....|....*....|....*....|...
gi 1838745027 491 ISDQGQRKTQEQLEVLESLKQELATSQRELQVL 523
Cdd:pfam00038 257 QLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
347-615 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 347 LIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQ---QHLRQQAADD-----------CEFLRAELDEL- 411
Cdd:pfam07111 307 LLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQsqeQAILQRALQDkaaevevermsAKGLQMELSRAq 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 412 ---RRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS-----MARQ---AQVDLE-- 478
Cdd:pfam07111 387 earRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglMARKvalAQLRQEsc 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 479 ---------------------REKKELEDSLE-----------RISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGS 526
Cdd:pfam07111 467 pppppappvdadlsleleqlrEERNRLDAELQlsahliqqevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQ 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 527 LETSAQSEANWAAEFAELEKE--RDSLVSGAAHRE---EELSALRKELQDTQLKLastEESMCQLAKDQRKMLLVGSRKA 601
Cdd:pfam07111 547 LEVARQGQQESTEEAASLRQEltQQQEIYGQALQEkvaEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAT 623
|
330
....*....|....
gi 1838745027 602 AEQVIQDALNQLEE 615
Cdd:pfam07111 624 QEKERNQELRRLQD 637
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
405-520 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 405 RAELDE-LRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKE 483
Cdd:pfam20492 8 KQELEErLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 1838745027 484 LEDSLERISDQGQRKTQEQlevlESLKQELATSQREL 520
Cdd:pfam20492 88 AQEEIARLEEEVERKEEEA----RRLQEELEEAREEE 120
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
336-615 |
3.04e-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: 41.70 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 336 QNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQR 415
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 416 EDTEK------------------AQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDL 477
Cdd:pfam01576 450 NEAEGkniklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 478 EREKKELEDSLERIsDQGQRKTQEQLEVL------------------ESLKQEL------ATSQRE----LQVLQGSLET 529
Cdd:pfam01576 530 KKKLEEDAGTLEAL-EEGKKRLQRELEALtqqleekaaaydklektkNRLQQELddllvdLDHQRQlvsnLEKKQKKFDQ 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 530 SAQSEANWAAEFAElekERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKML------------LVG 597
Cdd:pfam01576 609 MLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgknvheLER 685
|
330
....*....|....*...
gi 1838745027 598 SRKAAEQVIQDALNQLEE 615
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEE 703
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
343-528 |
3.50e-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: 39.89 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 343 EKDHLIERLYREISGLKAQLENMKTESQrvvlqlkghvseleadLAEQQHLRQQAA-DDCEFLRAEL--------DELRR 413
Cdd:pfam15619 8 ARLHKIKELQNELAELQSKLEELRKENR----------------LLKRLQKRQEKAlGKYEGTESELpqliarhnEEVRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 414 QREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADL-LRKNAEVTKQVSMARQAQVDLEREKKELEDSLERIS 492
Cdd:pfam15619 72 LRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELEN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838745027 493 DQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE 528
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
348-599 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 348 IERLYREISGLKAQLENMKTESQRvvLQ-LKGHVSELEAdlaeqQHLRQQAADDCEflrAELDELRRQREDtekAQRSLS 426
Cdd:COG3096 787 LEELRAERDELAEQYAKASFDVQK--LQrLHQAFSQFVG-----GHLAVAFAPDPE---AELAALRQRRSE---LERELA 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 427 EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNA------EVTKQVSMARQAQVDLEREKKELEdSLERI------- 491
Cdd:COG3096 854 QHRAQEQQLRQQLDQLKEQLQLLnkLLPQANLLADETladrleELREELDAAQEAQAFIQQHGKALA-QLEPLvavlqsd 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 492 -------------SDQGQRKTQEQLEVLESLKQ-----------ELATSQREL-QVLQGSLE--TSAQSEANWA-----A 539
Cdd:COG3096 933 peqfeqlqadylqAKEQQRRLKQQIFALSEVVQrrphfsyedavGLLGENSDLnEKLRARLEqaEEARREAREQlrqaqA 1012
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 540 EFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSR 599
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNR 1072
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
380-535 |
4.40e-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: 38.92 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 380 VSELEADLAEQQHLRQQAAddceflraeldeLRRQREDTEKAQRSLSEIERKAQANEQRYsklkekYSELvQNHADLLRK 459
Cdd:pfam07321 7 VKHLREDRAEKAVKRQEQA------------LAAARAAHQQAQASLQDYRAWRPQEEQRL------YAEI-QGKLVLLKE 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838745027 460 NAEVTKQVSMARQAQVDLEREKKELEDSLERISD---QGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEA 535
Cdd:pfam07321 68 LEKVKQQVALLRENEADLEKQVAEARQQLEAEREalrQARQALAEARRAVEKFAELVRLVQAEELRQQERQEEQELEEF 146
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
407-568 |
4.72e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 407 ELDELRRQ-----------REDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsmarqaqv 475
Cdd:PRK09039 54 ALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL-------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 476 dlerekkeleDSLERISDQGQRktqeQLEVLeslKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKErdsLVSGA 555
Cdd:PRK09039 126 ----------DSEKQVSARALA----QVELL---NQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRR---LNVAL 185
|
170
....*....|...
gi 1838745027 556 AHREEELSALRKE 568
Cdd:PRK09039 186 AQRVQELNRYRSE 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
340-576 |
5.58e-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: 40.73 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 340 NKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFlraeldELRRQREDTE 419
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE------EQKLEKLAEE 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 420 KAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRK-NAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRK 498
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKeKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 499 TQ------EQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:pfam02463 935 EEpeelllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
....
gi 1838745027 573 QLKL 576
Cdd:pfam02463 1015 TCQR 1018
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
360-572 |
5.91e-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: 39.63 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 360 AQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSE------------ 427
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEaekaadesergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 428 --IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMarqAQVDLEREKKELEDSLERISD--QGQRKTQEQL 503
Cdd:pfam00261 81 kvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVV---VEGDLERAEERAELAESKIVEleEELKVVGNNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 504 EVLESlkQELATSQRE------LQVLQGSLEtsaqsEANWAAEFAE-----LEKERDSLVSGAAHREEELSALRKELQDT 572
Cdd:pfam00261 158 KSLEA--SEEKASEREdkyeeqIRFLTEKLK-----EAETRAEFAErsvqkLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
406-618 |
8.48e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 406 AELDELRRQREDTEKAQRSLsEIERKAQANEQRYSKLKEKYselvqnhaDLLRK----NAEVTKQVSMARQAQVDLEREK 481
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENL-ELDEAEEALEEIEERIDQLY--------DLLEKevdaKKYVEKNLPEIEDYLEHAEEQN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 482 KELEDSLERIsDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLE--TSAQSE-----ANWAAEFAELEKERDSLVSG 554
Cdd:pfam06160 308 KELKEELERV-QQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEekEVAYSElqeelEEILEQLEEIEEEQEEFKES 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 555 AAH-REEELSAlRKELQDTQLKLASTEESMCQ-----LAKDQRKMLLVGSRKaaeqvIQDALNQLEEPPL 618
Cdd:pfam06160 387 LQSlRKDELEA-REKLDEFKLELREIKRLVEKsnlpgLPESYLDYFFDVSDE-----IEDLADELNEVPL 450
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
393-521 |
8.93e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 393 LRQQAADDCEFLRAELD-ELRRQREDTEKAQRSLSEIERKAQaneqRYSKLKEKySELVQNHADLLRKNAEVTKQVS--M 469
Cdd:pfam05262 186 LREDNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQI----DADKAQQK-ADFAQDNADKQRDEVRQKQQEAknL 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 470 ARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVL--------ESLKQELATSQRELQ 521
Cdd:pfam05262 261 PKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEAlkakdhkaFDLKQESKASEKEAE 320
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
345-568 |
9.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.67 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 345 DHLIErlyreISGLKAQLENMKTESQRVVL-------QLKGHVSE-------LEADLAEQQHLRQQAADDCEFLRAELDE 410
Cdd:COG0497 123 ELLVD-----IHGQHEHQSLLDPDAQRELLdafagleELLEEYREayrawraLKKELEELRADEAERARELDLLRFQLEE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 411 LRRQR----EDTEKAQrslseiERKAQAN-EQRYSKLKEKYSELVQNH---ADLLRK-----------NAEVTKQVSMAR 471
Cdd:COG0497 198 LEAAAlqpgEEEELEE------ERRRLSNaEKLREALQEALEALSGGEggaLDLLGQalralerlaeyDPSLAELAERLE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 472 QAQVDLEREKKELEDSLERISDQGQR--KTQEQLEVLESLKQ-------ELATSQRELQVLQGSLETSAQSEANWAAEFA 542
Cdd:COG0497 272 SALIELEEAASELRRYLDSLEFDPERleEVEERLALLRRLARkygvtveELLAYAEELRAELAELENSDERLEELEAELA 351
|
250 260
....*....|....*....|....*.
gi 1838745027 543 ELEKErdslVSGAAhreEELSALRKE 568
Cdd:COG0497 352 EAEAE----LLEAA---EKLSAARKK 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
456-615 |
9.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 456 LLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLEslkQELATSQRELQVLQGSLEtsaQSEA 535
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLL---QKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838745027 536 NwaaefaeLEKERDSLvsgaAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEE 615
Cdd:PRK12704 97 N-------LDRKLELL----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE 165
|
|
| |
