|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
39-306 |
2.77e-93 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 297.67 E-value: 2.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 39 TQTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRY 117
Cdd:pfam07651 1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 118 KNELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECEL 196
Cdd:pfam07651 81 RRRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 197 NLFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLK 270
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLK 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 755514337 271 DLFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
806-1004 |
1.50e-90 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 287.34 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 806 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 885
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 886 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 964
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755514337 965 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 1004
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
1.12e-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: 265.75 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 755514337 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
6.83e-69 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 225.24 E-value: 6.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 755514337 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
856-1002 |
1.37e-58 |
|
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: 197.81 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 856 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 935
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755514337 936 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 1002
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
6.78e-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: 188.92 E-value: 6.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 755514337 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
40-153 |
2.58e-41 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 147.14 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 40 QTVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR 116
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 755514337 117 -YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
38-160 |
4.75e-37 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 135.45 E-value: 4.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 38 RTQTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSL 115
Cdd:smart00273 1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755514337 116 RYKNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 160
Cdd:smart00273 81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
482-572 |
1.05e-27 |
|
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: 107.79 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 482 HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFAR--------TQEQQDVLENLKHELATSRQELQVLHSNLETSAQ 553
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERakeeaqmkLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 755514337 554 SEAKWLTQIAELEKEQGSL 572
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
42-153 |
4.58e-25 |
|
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: 100.84 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 42 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 121
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 755514337 122 SDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-636 |
2.58e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 382 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAmddcEFLRTEL----DELKRQREDTEKAQRSLTEI 457
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELeeleLELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 458 ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATS 537
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 538 RQELQVLHSNLETSAQSEAKwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLA 617
Cdd:COG1196 381 LEELAEELLEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|....*....
gi 755514337 618 giRKAAEREIQEALSQLEE 636
Cdd:COG1196 458 --EEALLELLAELLEEAAL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-631 |
1.28e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 369 NKDEKDHLIERLYREISGLTGQLDNMKIESQramlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREdte 448
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--- 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 449 KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarqaqvDLEREKKELADSFARTQEQqdvLE 528
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-------ATERRLEDLEEQIEELSED---IE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 529 NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQV 608
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL-EGL 934
|
250 260
....*....|....*....|...
gi 755514337 609 KDQRKTLLAGIRKAAEREIQEAL 631
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAE 957
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-636 |
3.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAqRSLTEIERKAQAN---------EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQ 503
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 504 VDLEREKKELADSFARTQEQqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 583
Cdd:COG1196 277 EELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755514337 584 SALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgiRKAAEREIQEALSQLEE 636
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEE 404
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-637 |
3.27e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISGLTgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK- 449
Cdd:COG1196 281 LELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAe 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 450 ---AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV 526
Cdd:COG1196 360 laeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 527 LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQ 606
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
250 260 270
....*....|....*....|....*....|.
gi 755514337 607 QVKDQRKTLLAGIRKAAEREIQEALSQLEEP 637
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-636 |
1.49e-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: 65.46 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 402 MLQLKGRVSELEAELAEQQhlgrqamDDCEFLRTELDELKRQRED----TEKAQRSLTEIERKAQANEQRYSKLKEKYSE 477
Cdd:TIGR02168 672 ILERRREIEELEEKIEELE-------EKIAELEKALAELRKELEEleeeLEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 478 LVQNHADLLRKNAEVTKQVSV-------ARQAQVDLEREKKELADSFARTQEQ-----------QDVLENLKHELATSRQ 539
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEEleerleeAEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 540 ELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGI 619
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL-ALLRSELEELSEEL 903
|
250
....*....|....*..
gi 755514337 620 RKaAEREIQEALSQLEE 636
Cdd:TIGR02168 904 RE-LESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-664 |
2.65e-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: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 454
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 455 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENlkhEL 534
Cdd:TIGR02168 256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---QL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 535 ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQ-----QVK 609
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneiERL 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755514337 610 DQRKTLLAGIRKAAEREIQEALSQLEEPTLISCAGSTDHLLSKVSSVSSCLEQLE 664
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-634 |
2.68e-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: 63.63 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 397 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLKEKYS 476
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 477 ELVQNHADLLRKnaevtkQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 556
Cdd:COG4942 101 AQKEELAELLRA------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 557 KWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQL 634
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-636 |
2.74e-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: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNMKIESQRamlqLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK----AQR 452
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 453 SLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKH 532
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 533 ELATSRQELQvlhsnlETSAQSEAkwltQIAELEKEQGSLATVAAQREEEL---SALRDQLESTQIKLAGAQESMCQQVK 609
Cdd:TIGR02168 835 ATERRLEDLE------EQIEELSE----DIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELR 904
|
250 260
....*....|....*....|....*..
gi 755514337 610 DQRKTllagiRKAAEREIQEALSQLEE 636
Cdd:TIGR02168 905 ELESK-----RSELRRELEELREKLAQ 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-636 |
1.42e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 443 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQE 522
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 523 QqdvLENLKHELATSRQELQ----------VLHSNLETSAQSEAKWLTQIAELEKEQG-----SLATVAAQReEELSALR 587
Cdd:COG4942 98 E---LEAQKEELAELLRALYrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAeelraDLAELAALR-AELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755514337 588 DQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKaAEREIQEALSQLEE 636
Cdd:COG4942 174 AELEALLAELEEERAAL-EALKAERQKLLARLEK-ELAELAAELAELQQ 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-634 |
8.08e-09 |
|
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: 60.08 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 370 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 446
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 447 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQV----------- 496
Cdd:TIGR02169 284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdklteeyaelk 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 497 SVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 576
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 577 AQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 634
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
42-151 |
1.14e-08 |
|
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: 54.20 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 42 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 118
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 755514337 119 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 151
Cdd:cd03564 83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
362-599 |
1.31e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 58.87 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 362 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 432
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 509
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 510 KKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 589
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|
gi 755514337 590 LESTQIKLAG 599
Cdd:PHA02562 388 LDKIVKTKSE 397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-573 |
5.34e-08 |
|
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: 56.31 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQ------- 443
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 444 ---------------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER 508
Cdd:COG4942 113 lyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755514337 509 EKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwLTQIAELEKEQGSLA 573
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLP 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-636 |
6.21e-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: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 424 RQAMDDCEFLRTELDELKRQREDTEKAQR---SLTEIERKAQaneqRYSKLKEKYSELvqnhaDLLRKNAevtkQVSVAR 500
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAEL-----EYLRAAL----RLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 501 QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSaqseakwltQIAELEKEQGSLATVAAQRE 580
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD---------RLEQLEREIERLERELEERE 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 581 EELSALRDQLESTQIKLAGAQESMCQQVK--DQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAeaAALLEALEEELEALEEALAEAEAALRD 416
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-636 |
8.27e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 448 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVL 527
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 528 E----NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ-- 601
Cdd:TIGR02168 746 EeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRer 825
|
170 180 190
....*....|....*....|....*....|....*...
gi 755514337 602 -ESMCQQVKDQRKTL--LAGIRKAAEREIQEALSQLEE 636
Cdd:TIGR02168 826 lESLERRIAATERRLedLEEQIEELSEDIESLAAEIEE 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
395-592 |
9.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAmdDCEFLRTELDELKRQREDTEKAQRSLteiERKAQANEQRYSKLKEK 474
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARL---EAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 475 YSELVQNHADLLRKNAEvtkqvsvarQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQS 554
Cdd:COG4913 325 LDELEAQIRGNGGDRLE---------QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 755514337 555 EAKWLtqiAELEKEQGSLATVAAQREEELSALRDQLES 592
Cdd:COG4913 396 LEEEL---EALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-636 |
1.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF--LRTELDELKRQREDTEKAQRSL 454
Cdd:COG4913 612 LAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 455 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKK-----ELADSFARTQE---QQDV 526
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGdavEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 527 LENLKHELATSRQELQVLHSNLEtSAQSEAK--WLTQIAELEkeqgslATVAAqrEEELSALRDQLEstQIKLAGAQESM 604
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELE-RAMRAFNreWPAETADLD------ADLES--LPEYLALLDRLE--EDGLPEYEERF 836
|
250 260 270
....*....|....*....|....*....|..
gi 755514337 605 CQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:COG4913 837 KELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
400-612 |
1.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 400 RAMLqlkgrVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKy 475
Cdd:COG4717 44 RAML-----LERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 476 selvqnhadllRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETS-AQS 554
Cdd:COG4717 118 -----------LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 555 EAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQR 612
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-635 |
2.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 422 LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVqnhaDLLrknaevtkqvSVARQ 501
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI----DVA----------SAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 502 AQvDLEREKKELADSfartqeqQDVLENLKHELATSRQELQVLHSnletsaqseakwltQIAELEKEQGSLATVAAQREE 581
Cdd:COG4913 670 IA-ELEAELERLDAS-------SDDLAALEEQLEELEAELEELEE--------------ELDELKGEIGRLEKELEQAEE 727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755514337 582 ELSALRDQLESTQIKLAGAQESMCQQVKDQ--RKTLLAGIRKAAEREIQEALSQLE 635
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAalGDAVERELRENLEERIDALRARLN 783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-547 |
3.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 370 KDEKDHL--IERLYREISGLTGQLDnmKIESQRAMLQLKG---RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR 444
Cdd:COG4913 248 REQIELLepIRELAERYAAARERLA--ELEYLRAALRLWFaqrRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 445 EDTEKAQRS-----LTEIERKAQANEQRYSKLKEK---YSELVQN-HADLLRKNAEVTKQVSVARQAQVDLEREKKELAD 515
Cdd:COG4913 326 DELEAQIRGnggdrLEQLEREIERLERELEERERRrarLEALLAAlGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190
....*....|....*....|....*....|..
gi 755514337 516 SFARTQEQqdvLENLKHELATSRQELQVLHSN 547
Cdd:COG4913 406 ALAEAEAA---LRDLRRELRELEAEIASLERR 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-636 |
4.14e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 404 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 483
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 484 DLLRKNAEVTKQVSVARQaqvdLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQSEAKWLT- 560
Cdd:PRK03918 270 ELKKEIEELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERLEELKk 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755514337 561 QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALSQLEE 636
Cdd:PRK03918 346 KLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEISKITA 412
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
400-623 |
1.96e-06 |
|
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: 51.43 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 400 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 475
Cdd:pfam07888 28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 476 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA----RTQEQQDVLENLKHE---LATSRQELQVLHSNL 548
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtltqRVLERETELERMKERakkAGAQRKEEEAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 549 ETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRKA 622
Cdd:pfam07888 177 QAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERKV 253
|
.
gi 755514337 623 A 623
Cdd:pfam07888 254 E 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-636 |
2.56e-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: 51.66 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 369 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 434
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 435 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSklKEKYSELVQNHADLLRK-NAEVTKqvsvaRQAQVDLEREK-K 511
Cdd:pfam15921 331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTE--RDQFSQESGNLDDQLQKlLADLHK-----REKELSLEKEQnK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 512 ELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLET-SAQSEAKWLTQIAELEKEQGSLatvaaqreEELSALRDQL 590
Cdd:pfam15921 402 RLWD---RDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESL--------EKVSSLTAQL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755514337 591 ESTQIKLagaqESMCQQVKDQRKTLlagirKAAEREIQEALSQLEE 636
Cdd:pfam15921 471 ESTKEML----RKVVEELTAKKMTL-----ESSERTVSDLTASLQE 507
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
363-638 |
5.53e-06 |
|
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: 50.34 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 363 NNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKR 442
Cdd:COG5185 140 VEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 443 QREDTEKAQRSLTEIERKAQANEQRYSKLK---EKYSELVQNHADL----LRKNAEVTKQVSVARQAQVDLEREKKELAD 515
Cdd:COG5185 220 TLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQFENTKEKIA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 516 SFARTQEQQDVLENLKHELATSRQELQVLHSNLETsaqsEAKWLTQIAELEKEQGSLATV----------------AAQR 579
Cdd:COG5185 300 EYTKSIDIKKATESLEEQLAAAEAEQELEESKRET----ETGIQNLTAEIEQGQESLTENleaikeeienivgeveLSKS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755514337 580 EEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEEPT 638
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
404-594 |
6.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 404 QLKGRVSELEAELAE--QQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEKYSELVQN 481
Cdd:COG3206 186 ELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQ----------LAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 482 HADLLRknaevTKQVSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWL-T 560
Cdd:COG3206 256 LPELLQ-----SPVIQQLRAQLAELEAELAELS---ARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALqA 327
|
170 180 190
....*....|....*....|....*....|....*..
gi 755514337 561 QIAELEKEQGSL---ATVAAQREEELSALRDQLESTQ 594
Cdd:COG3206 328 REASLQAQLAQLearLAELPELEAELRRLEREVEVAR 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-593 |
7.71e-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: 50.06 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISGLTGQLDNMKIE--SQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDT 447
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEElkALREALDeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 448 EKAQRSLT-EIERKAQANEQRYSKLKEKYSEL--VQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSFARTQEQ 523
Cdd:TIGR02168 851 SEDIESLAaEIEELEELIEELESELEALLNERasLEEALALLRSELEeLSEELRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 524 QDVLEN--------LKHELATSRQELQVLHSNLETS---AQSEAKWLTQ------------IAELEKEQGSLATVAAQRE 580
Cdd:TIGR02168 931 LEGLEVridnlqerLSEEYSLTLEEAEALENKIEDDeeeARRRLKRLENkikelgpvnlaaIEEYEELKERYDFLTAQKE 1010
|
250
....*....|...
gi 755514337 581 EELSAlRDQLEST 593
Cdd:TIGR02168 1011 DLTEA-KETLEEA 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-635 |
7.97e-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: 50.12 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 373 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 439
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 440 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 497
Cdd:pfam15921 563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 498 VARQAQVDLEREKKELADSFARTQEQQDVL----ENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAELEKEQ 569
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLsedyEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSMEGSD 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 570 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAAEREI 627
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQERRL 802
|
....*...
gi 755514337 628 QEALSQLE 635
Cdd:pfam15921 803 KEKVANME 810
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
363-636 |
8.28e-06 |
|
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: 50.02 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 363 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 432
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 508
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 509 EKKELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLETSaqseaKWLTQIAELEKEQGSLATVAAQREEELSALRD 588
Cdd:TIGR04523 532 EKKEKES---KISDLEDELNKDDFELKKENLEKEIDEKNKEIE-----ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755514337 589 QLEsTQIKLAGAQESMCQQVKDQRKTLLAGIRKaaereIQEALSQLEE 636
Cdd:TIGR04523 604 EIE-EKEKKISSLEKELEKAKKENEKLSSIIKN-----IKSKKNKLKQ 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
404-635 |
8.76e-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: 49.79 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 404 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQAN---------------EQRY 468
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkdlqreleearasrDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 469 SKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNL 548
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 549 ETSAQSEAKWLTQIAELEKEQGSLATVAAQREeelsALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkAAEREIQ 628
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFKSSIA----ALEAKIA 977
|
....*..
gi 755514337 629 EALSQLE 635
Cdd:pfam01576 978 QLEEQLE 984
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
411-590 |
9.84e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 411 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 491 EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKH----ELATSR---QELQVLHSNLETSAQSEAKWLTQIA 563
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQdvtEYMQQLLERERELTVERDELAARKQ 655
|
170 180
....*....|....*....|....*..
gi 755514337 564 ELEKEQGSLATVAAQREEELSALRDQL 590
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-636 |
1.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 456
Cdd:PRK02224 178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 457 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART-------QEQQDV 526
Cdd:PRK02224 239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 527 LEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 595
Cdd:PRK02224 319 LEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755514337 596 KLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 636
Cdd:PRK02224 399 RFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
411-590 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 411 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 491 EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELA---TSRQEL----QVLHSNLETSAQSEAKWLTQIA 563
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGealADSQEVtaamQQLLEREREATVERDELAARKQ 654
|
170 180
....*....|....*....|....*..
gi 755514337 564 ELEKEQGSLATVAAQREEELSALRDQL 590
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
387-564 |
1.48e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 387 LTGQLDNMKIESQRAMlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL---DELKRQREDTEKAQRSLTeiERKAQA 463
Cdd:PRK04863 501 LLRRLREQRHLAEQLQ-QLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLddeDELEQLQEELEARLESLS--ESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 464 NEQRysklkekySELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKK----ELADSFARTQEQQDVLENLKH------E 533
Cdd:PRK04863 578 RERR--------MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeEFEDSQDVTEYMQQLLEREREltverdE 649
|
170 180 190
....*....|....*....|....*....|.
gi 755514337 534 LATSRQELQVLHSNLETSAQSEAKWLTQIAE 564
Cdd:PRK04863 650 LAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-550 |
1.58e-05 |
|
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: 49.30 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 368 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 442
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 443 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA---DLLRKNAEVTKQVSVARQAQVDLEREKKELA- 514
Cdd:TIGR02169 890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRa 969
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755514337 515 ---------DSFARTQEQQDVLENLKHELATSRQELQVLHSNLET 550
Cdd:TIGR02169 970 lepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
395-636 |
1.66e-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: 49.02 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 474
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 475 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSR----QELQ 542
Cdd:pfam01576 336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRkkleGQLQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 543 VLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE-------EELSALRDQL--------ESTQIKLAGAqeSMCQQ 607
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniklsKDVSSLESQLqdtqellqEETRQKLNLS--TRLRQ 493
|
250 260 270
....*....|....*....|....*....|....*
gi 755514337 608 VKDQRKTLLAGI------RKAAEREIQEALSQLEE 636
Cdd:pfam01576 494 LEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSD 528
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
408-562 |
1.69e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.55 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 408 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 487
Cdd:PRK12705 37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755514337 488 KNAEVTkqvsvARQAQVDLEREKKEladSFARTQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWLTQI 562
Cdd:PRK12705 117 RELELE-----ELEKQLDNELYRVA---GLTPEQARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
438-636 |
1.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 438 DELKRQREDTEKAQrsltEIERKAQANEQRYSKLKEKYSElvQNHADLLRKNAEVTKQVSVARQaqvdlEREKKELADSF 517
Cdd:PTZ00121 1381 DAAKKKAEEKKKAD----EAKKKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKK-----KAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 518 ARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKL 597
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190
....*....|....*....|....*....|....*....
gi 755514337 598 AGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
446-596 |
1.79e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 446 DTEKAQRSLTEIERKAQANEQRYSKLKEkyseLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArTQEQqd 525
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEA----ELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAV-SQQE-- 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755514337 526 vLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEqgslatvAAQREEELSALRDQLESTQIK 596
Cdd:COG1566 150 -LDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQ-------VAQAEAALAQAELNLARTTIR 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-636 |
1.89e-05 |
|
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: 48.91 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 432 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 500
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 501 QAQVDLEREKKELADSFARTQEQQDVLENLKHELAT-----SRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATV 575
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755514337 576 AAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 636
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL-EEELEELEAALRDLES 882
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
364-636 |
1.94e-05 |
|
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: 48.58 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 364 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 440
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 441 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--- 517
Cdd:pfam17380 351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKvem 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 518 ---------ARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR----EEELS 584
Cdd:pfam17380 423 eqiraeqeeARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkilEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755514337 585 A--------------LRDQLESTQIKLA-------GAQESMCQQVKDQRKTLLAGIRKAA-EREIQEALSQLEE 636
Cdd:pfam17380 503 ErkqamieeerkrklLEKEMEERQKAIYeeerrreAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMERERE 576
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
454-639 |
2.53e-05 |
|
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: 46.84 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 454 LTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKhe 533
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 534 latsrqELQVLhsnletsaqseakwLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRK 613
Cdd:COG1579 90 ------EYEAL--------------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL-EEKKAELD 148
|
170 180
....*....|....*....|....*....
gi 755514337 614 TLLAGIRKAAER---EIQEALSQLEEPTL 639
Cdd:COG1579 149 EELAELEAELEEleaEREELAAKIPPELL 177
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
445-610 |
2.74e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 46.21 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 445 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHAD------LLRKNAEVTKQVSVARQAQV---------DLERE 509
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEfektiaQMIEEKQKQKELEHAEIQKVleekdqalaDLNSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 510 KKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQREEELSALRD 588
Cdd:pfam05010 88 EKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAKAETAALQA 167
|
170 180
....*....|....*....|..
gi 755514337 589 QLESTQIKLAGAQESMCQQVKD 610
Cdd:pfam05010 168 SLRKEQMKVQSLERQLEQKTKE 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-636 |
4.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISGLTGQLDNmkIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 426
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGN--AEDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 427 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 497
Cdd:PRK02224 465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 498 VARQAQVDLE---REKKELADSFA-RTQEQQDVLENLKHELATSRQELQVLhSNLETSAQSEAKWLTQIAELEKEQGSLA 573
Cdd:PRK02224 541 ELRERAAELEaeaEEKREAAAEAEeEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALA 619
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755514337 574 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 636
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
399-636 |
4.41e-05 |
|
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: 47.66 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 399 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 478
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 479 VQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFARTQEQQDVLENLKHELATSRQELQVL------HSNLETSA 552
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHAL---LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRV 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 553 QSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQE 629
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
....*..
gi 755514337 630 ALSQLEE 636
Cdd:TIGR00618 748 LMHQART 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-636 |
4.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 473
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 474 KYSElvQNHADLLRKNAEVTKQVSVARQAQVDLER---------EKKELADSFARTQEQQDVLENLKHELATSRQELQvl 544
Cdd:PTZ00121 1465 KAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-- 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 545 hsnlETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKA 622
Cdd:PTZ00121 1541 ----KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKA 1615
|
250
....*....|....*
gi 755514337 623 AEREIQ-EALSQLEE 636
Cdd:PTZ00121 1616 EEAKIKaEELKKAEE 1630
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
380-609 |
5.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 380 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 453
Cdd:PRK04863 849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 454 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 502
Cdd:PRK04863 918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 503 QVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLH-----------SNLETSAQSEAKWL--------TQIA 563
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKqelqdlgvpadSGAEERARARRDELharlsanrSRRN 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755514337 564 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 609
Cdd:PRK04863 1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
404-603 |
5.18e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 404 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKE--------- 473
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaEIAEAEAEIEERREELGEraralyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 474 ---KYSELV---QNHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfartqEQQDVLENLKHELATSRQELQVLHSN 547
Cdd:COG3883 100 gsvSYLDVLlgsESFSDFLDRLSALSKIADADADLLEELKADKAELE-------AKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755514337 548 LEtSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQES 603
Cdd:COG3883 173 LE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
431-633 |
6.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 431 EFLRTELDELKRQREDTE------KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQ--------- 495
Cdd:COG3206 178 EFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpdalp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 496 -------VSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwltqiaeleke 568
Cdd:COG3206 258 ellqspvIQQLRAQLAELEAELAELS---ARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE----------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 569 qgslatVAAQREEELSALRDQLESTQIKLAGAQ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 633
Cdd:COG3206 324 ------ALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-576 |
6.03e-05 |
|
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: 47.37 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 451
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 452 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsFARTQEQQDVLEnl 530
Cdd:TIGR02169 409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL---YDLKEEYDRVEK-- 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755514337 531 khELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 576
Cdd:TIGR02169 484 --ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
376-636 |
6.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 376 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 454
Cdd:PRK03918 315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 455 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFarTQEQQDV 526
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEY--TAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 527 LENLKhELATSRQELQVLHSNLETSAQSEAKWLT------QIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLAGA 600
Cdd:PRK03918 465 EKELK-EIEEKERKLRKELRELEKVLKKESELIKlkelaeQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLKGE 540
|
250 260 270
....*....|....*....|....*....|....*.
gi 755514337 601 QESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:PRK03918 541 IKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
398-564 |
6.62e-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: 47.25 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 398 SQRAMLQ----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL---DELKRQREDTEKAQRSLTEierkaQANEQRysk 470
Cdd:COG3096 506 SQQALAQrlqqLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLdaaEELEELLAELEAQLEELEE-----QAAEAV--- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 471 lkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE----LADSFARTQEQQDVLENL------KHELATSRQE 540
Cdd:COG3096 578 --EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAMQQLLEREreatveRDELAARKQA 655
|
170 180
....*....|....*....|....
gi 755514337 541 LQVLHSNLETSAQSEAKWLTQIAE 564
Cdd:COG3096 656 LESQIERLSQPGGAEDPRLLALAE 679
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
441-628 |
6.95e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 441 KRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART 520
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 521 QEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGA 600
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180
....*....|....*....|....*...
gi 755514337 601 QESMCQQVKDQRKTLLAGIRKAAEREIQ 628
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-636 |
1.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 425 QAMDDCEFLRTELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEKYSELvQNHADLLRKNAEVTKQVSVARQAQV 504
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 505 dlerekKELADSFARTQEQQDVLENLKheLATSRQEL--QVlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE 582
Cdd:COG3883 89 ------GERARALYRSGGSVSYLDVLL--GSESFSDFldRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755514337 583 LSALRDQLESTQIKLAGAQESmcqqvKDQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
499-636 |
1.68e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 499 ARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLET-----SAQSE-AKWLTQIAELEKEQGSL 572
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREiAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755514337 573 ATVAAQREE---ELSALRDQLESTQIKLAGAQESmcqqvkdqrktllagiRKAAEREIQEALSQLEE 636
Cdd:COG4913 688 AALEEQLEEleaELEELEEELDELKGEIGRLEKE----------------LEQAEEELDELQDRLEA 738
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
437-633 |
1.89e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 437 LDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNH------ADLLRKNAEVTKQVSvarQAQVDL---- 506
Cdd:PRK11281 72 LDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQ---NAQNDLaeyn 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 507 ----------EREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHsNLETSA--------QSEAKWLTQIAELEKE 568
Cdd:PRK11281 149 sqlvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL-QAEQALlnaqndlqRKSLEGNTQLQDLLQK 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755514337 569 QGSLATVAAQR-EEELSALRD-----QLESTQIKLAGAQESMcQQVKDQRKTLLagirkAAEREIQEALSQ 633
Cdd:PRK11281 228 QRDYLTARIQRlEHQLQLLQEainskRLTLSEKTVQEAQSQD-EAARIQANPLV-----AQELEINLQLSQ 292
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-597 |
1.90e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 400 RAMLQLKGRVSEleAELAEQQHlgRQAMddcEFLRTELDELkrQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELV 479
Cdd:COG3096 455 EEVLELEQKLSV--ADAARRQF--EKAY---ELVCKIAGEV--ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 480 Q---NHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 556
Cdd:COG3096 526 QrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755514337 557 KWLTQIAELEK--EQG--SLATVAA---------QREEELSALRDQLESTQIKL 597
Cdd:COG3096 603 AWLAAQDALERlrEQSgeALADSQEvtaamqqllEREREATVERDELAARKQAL 656
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
387-591 |
2.11e-04 |
|
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: 45.60 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 387 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 458
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 459 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFAR-TQEQQDVLE-------- 528
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERiAVRRQEVLRyfdwyqet 804
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755514337 529 ------NLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 591
Cdd:pfam12128 805 wlqrrpRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
377-478 |
2.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNmkiESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 456
Cdd:COG3206 293 VIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREAS--------------LQAQLAQLEARLAELPELEAELRR 355
|
90 100
....*....|....*....|..
gi 755514337 457 IERKAQANEQRYSKLKEKYSEL 478
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-517 |
2.22e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 368 VNKDEKDHLIERLYREISGLTGQLD-------NMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMD--DCEFLRTELD 438
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELE 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755514337 439 ELKRQREDTEKAQRSLTEiERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF 517
Cdd:COG4717 436 ELEEELEELEEELEELRE-ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
517-625 |
2.34e-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: 44.75 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 517 FARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 596
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100
....*....|....*....|....*....
gi 755514337 597 LAGAQESmcqqvKDQRKTLLAGIRKAAER 625
Cdd:COG4942 92 IAELRAE-----LEAQKEELAELLRALYR 115
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
381-591 |
2.93e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 381 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 457
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 458 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSF-ARTQ 521
Cdd:pfam00038 132 -------ELAF--LKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaAKNREEAEEWYqSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 522 EQQ-------DVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 589
Cdd:pfam00038 200 ELQqaaarngDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQETRQE 278
|
..
gi 755514337 590 LE 591
Cdd:pfam00038 279 MA 280
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-635 |
2.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 426
Cdd:PRK03918 448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 427 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKQVSVARQAQVDL 506
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVEELEERLKELEPF 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 507 EREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatvaaqrEEELSAL 586
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS---------EEEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755514337 587 RDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 635
Cdd:PRK03918 665 REEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
433-635 |
3.02e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRY-----SKLKEKyselvqnhaDLLRKNAEVTKQVSVARQAqvdlE 507
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlSPEEEK---------ELVEKIKELEKELEKAKKA----L 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 508 REKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLetsaqseAKWLTQIAELEKEQGSLATVAAQREEELSALR 587
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM-------IELYKEADELRKEADELHKEIVEAQEKADELH 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755514337 588 DQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLE 635
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
384-620 |
3.32e-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: 44.72 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 384 ISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQA 463
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 464 NEQRYSKLKekySELVQNHADLLRKNAEVTKQvsvarQAQVDLE-REKKELADSFARTQEQQDVLENLKHELATSRQELQ 542
Cdd:pfam15921 494 SERTVSDLT---ASLQEKERAIEATNAEITKL-----RSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 543 VLHSNLETSAQ-------SEAKWLTQIAELEKEQGS----------LATVAAQREEELSALRDQLESTQIKLAGAQESMC 605
Cdd:pfam15921 566 ILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDrrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAGSERL 645
|
250
....*....|....*...
gi 755514337 606 QQVKD---QRKTLLAGIR 620
Cdd:pfam15921 646 RAVKDikqERDQLLNEVK 663
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
433-550 |
4.48e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE--- 509
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEaes 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755514337 510 -KKELADSFARTQEQQDVLENLKHELATSRQELQ----VLHSNLET 550
Cdd:pfam07926 83 aKAELEESEESWEEQKKELEKELSELEKRIEDLNeqnkLLHDQLES 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-636 |
5.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAMLQLKgRVSELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYS-KLKE 473
Cdd:PTZ00121 1559 KAEEKKKAEEAK-KAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 474 KYSELVQNHADLLRKNAEVTK--QVSVARQAQV--DLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLE 549
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKaeEENKIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 550 TSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQE 629
Cdd:PTZ00121 1714 EKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
....*..
gi 755514337 630 ALSQLEE 636
Cdd:PTZ00121 1784 ELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
394-542 |
7.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 394 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 470
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755514337 471 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKElADSFARTQEQQDVLENLKHELATSRQELQ 542
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKK-AEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
402-624 |
7.80e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 402 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 481
Cdd:PRK10929 111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 482 hADLLRKNAEvtkqvSVARQAQVDlEREKKELadSFARTQEqqdvLENLKHELATSRQE-----LQVLHSNLETSAQSEA 556
Cdd:PRK10929 173 -AQLTALQAE-----SAALKALVD-ELELAQL--SANNRQE----LARLRSELAKKRSQqldayLQALRNQLNSQRQREA 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755514337 557 -KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 624
Cdd:PRK10929 240 eRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-590 |
8.13e-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: 42.22 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEK 474
Cdd:COG1579 14 ELDSELD--RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----------IKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 475 YSElVQNHADLlrknAEVTKQVSVARQAQVDLEREKKELADsfaRTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqs 554
Cdd:COG1579 82 LGN-VRNNKEY----EALQKEIESLKRRISDLEDEILELME---RIEELEEELAELEAELAELEAELEEKKAELD----- 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 755514337 555 eakwlTQIAELEKEqgsLATVAAQREEELSALRDQL 590
Cdd:COG1579 149 -----EELAELEAE---LEELEAEREELAAKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
433-611 |
8.43e-04 |
|
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: 43.47 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSELvqnhadllrknaevTKQVSvarqaqvDLEREKK 511
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYNDL--------------KKQKE-------ELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 512 ELADSfartqeqqdvLENLKHELATSRQELQVLH---SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRD 588
Cdd:TIGR04523 177 LLEKE----------KLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
170 180
....*....|....*....|...
gi 755514337 589 QLESTQIKLAGAQESMcQQVKDQ 611
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQ-NKIKKQ 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
439-636 |
8.74e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 439 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA 518
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 519 RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 598
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
170 180 190
....*....|....*....|....*....|....*...
gi 755514337 599 gaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:PTZ00121 1447 ---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-636 |
9.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 370 KDEKDHLIERLYREISGLTGQLDnmKIESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEK 449
Cdd:COG4717 97 LEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAE--------------LPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 450 AQRSLTEIERKAQANEQRYSKLKEKYS--------ELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQ 521
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 522 EQQDVLENL-----------------------------------------------KHELATSRQELQVLHSNLETSAQS 554
Cdd:COG4717 241 LEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 555 EAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAgaqesmCQQVKDQRKTLLAGIRKAAEREIQEALSQL 634
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ------LEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
..
gi 755514337 635 EE 636
Cdd:COG4717 395 EE 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
406-636 |
1.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 406 KGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDT-----------EKAQRSLTEIERKAQANEQRYSKLKEK 474
Cdd:PTZ00121 1301 KKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 475 YSELvQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSA 552
Cdd:PTZ00121 1380 ADAA-KKKAEEKKKADEAKKKAEEDKKKADELKKaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 553 QSEAKWLTQIA----ELEK--EQGSLATVAAQREEELSALRDQLESTQIKLAGAQESmcQQVKDQRKTllAGIRKAAERE 626
Cdd:PTZ00121 1459 AEEAKKKAEEAkkadEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA--KKAEEAKKA--DEAKKAEEAK 1534
|
250
....*....|
gi 755514337 627 IQEALSQLEE 636
Cdd:PTZ00121 1535 KADEAKKAEE 1544
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-632 |
1.19e-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: 42.90 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 386 GLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDtekAQRSLteieRKAQAN 464
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASEEeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTAL----KNARLD 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 465 EQRYSklkekyselVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELAdsfartQEQQDVLENLKHELATSRQELQvl 544
Cdd:pfam12128 655 LRRLF---------DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD------KKHQAWLEEQKEQKREARTEKQ-- 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 545 hsnletsaqseAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES---TQIKLAGAQESMCQQVKDQRKTLLAGIRK 621
Cdd:pfam12128 718 -----------AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwykRDLASLGVDPDVIAKLKREIRTLERKIER 786
|
250
....*....|.
gi 755514337 622 AAEREiQEALS 632
Cdd:pfam12128 787 IAVRR-QEVLR 796
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
433-633 |
1.43e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 433 LRTELDELKRQRE----------DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR---KNAEVTKQ---- 495
Cdd:PRK11281 41 VQAQLDALNKQKLleaedklvqqDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkdDNDEETREtlst 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 496 VSVAR------QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNL-ETSAQSEAKWLTQIAELEKE 568
Cdd:PRK11281 121 LSLRQlesrlaQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLkGGKVGGKALRPSQRVLLQAE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 569 QGSLATVAAQREEEL---SALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 633
Cdd:PRK11281 201 QALLNAQNDLQRKSLegnTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
374-592 |
1.54e-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: 42.63 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 374 DHLIERlyreISGLTGQLDNMKiESQRAMLQLKGRVSELEAELA-----EQQHlgrqamddcEFLRTELDELKRQREDTE 448
Cdd:COG3096 889 ETLADR----LEELREELDAAQ-EAQAFIQQHGKALAQLEPLVAvlqsdPEQF---------EQLQADYLQAKEQQRRLK 954
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 449 KAQRSLTE-IERKAQANEQRYSKLKEKYSELV-QNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV 526
Cdd:COG3096 955 QQIFALSEvVQRRPHFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755514337 527 LENLKHEL------------ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 592
Cdd:COG3096 1035 LQELEQELeelgvqadaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
461-636 |
1.93e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 461 AQANEQRySKLKEKYSeLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQE 540
Cdd:TIGR02168 632 DNALELA-KKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 541 LQVLHSNLETSAQSEAKWLT----QIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLL 616
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-AEAEAEIEELE 788
|
170 180
....*....|....*....|..
gi 755514337 617 AGIRKAAER--EIQEALSQLEE 636
Cdd:TIGR02168 789 AQIEQLKEElkALREALDELRA 810
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
441-569 |
2.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 441 KRQREDTEKAQRSLTEIERKAQA-NEQRYSKLKEKYSELVQNH-ADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfa 518
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAiKKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLDRKLELL----- 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 755514337 519 rtQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQ 569
Cdd:PRK12704 106 --EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
505-602 |
2.11e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 505 DLEREKKELADSFA----RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE 580
Cdd:PRK09039 57 RLNSQIAELADLLSlerqGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100
....*....|....*....|..
gi 755514337 581 EELSALRDQLESTQIKLAGAQE 602
Cdd:PRK09039 137 AQVELLNQQIAALRRQLAALEA 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-550 |
2.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 396 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIE---------------- 458
Cdd:PRK02224 532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtllaaiadaedeierl 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 459 ---RKAQA--NEQRYSKLKEK---YSELVQNHADLLRKNAEVTKQVSVARQAQVD-----LEREKKELADSFARTQEQQD 525
Cdd:PRK02224 612 rekREALAelNDERRERLAEKrerKRELEAEFDEARIEEAREDKERAEEYLEQVEekldeLREERDDLQAEIGAVENELE 691
|
170 180
....*....|....*....|....*...
gi 755514337 526 VLENLKHE---LATSRQELQVLHSNLET 550
Cdd:PRK02224 692 ELEELRERreaLENRVEALEALYDEAEE 719
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
446-636 |
2.30e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 446 DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLlrknaevtkqVSVARQAQVDLErekkELADSFARTQEQQD 525
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEA----------TSGASRSAQDLA----ELLSSFSGSSTTDT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 526 VLenLKHELATSRQELQvlhsnLETSAQSEAKWLTQIAELEKEqgslatVAAQREEELSALRDQLESTQIKLagaqesmc 605
Cdd:pfam05667 293 GL--TKGSRFTHTEKLQ-----FTNEAPAATSSPPTKVETEEE------LQQQREEELEELQEQLEDLESSI-------- 351
|
170 180 190
....*....|....*....|....*....|...
gi 755514337 606 QQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 636
Cdd:pfam05667 352 QELEKEIKKLESSIKQVEEelEELKEQNEELEK 384
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
384-636 |
2.69e-03 |
|
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: 41.88 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 384 ISGLTGqLDNMKIESQRAMLQLKGRVSELEAELAEQQHLgrqaMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQA 463
Cdd:TIGR00618 169 LMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL----TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 464 NEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarqAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQV 543
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 544 LHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEelsaLRDQLEstqiklagaQESMCQQVKDQRKTLLAGIRKAA 623
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH----IRDAHE---------VATSIREISCQQHTLTQHIHTLQ 385
|
250
....*....|...
gi 755514337 624 erEIQEALSQLEE 636
Cdd:TIGR00618 386 --QQKTTLTQKLQ 396
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
371-631 |
3.01e-03 |
|
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: 41.73 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 371 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 415
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 416 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 479
Cdd:pfam10174 442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 480 QNHADLLRKNAEVTKQVSVARQAQ------------VD----LEREKKELADSFARTQEQQDVL-------ENLKH---- 532
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHnaeeavrtnpeiNDrirlLEQEVARYKEESGKAQAEVERLlgilrevENEKNdkdk 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 533 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 599
Cdd:pfam10174 601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
|
330 340 350
....*....|....*....|....*....|....*.
gi 755514337 600 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 631
Cdd:pfam10174 681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
377-640 |
3.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 377 IERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAelAEQQhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 456
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ--LEEE------------LEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 457 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELAT 536
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 537 SRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLL 616
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|....
gi 755514337 617 AGIRKAAEREIQEALSQLEEPTLI 640
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALE 289
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
436-597 |
4.04e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 436 ELDELKRQREDTEKAQRSLtEIERKAQANEQRYSKLKEKYSEL---VQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 512
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL-DLDEAEEKNEEIQERIDQLYDILereVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 513 LADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQ--SE-----AKWLTQIAELEKEQGSLA-TVAAQREEELS 584
Cdd:PRK04778 336 VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIaySElqeelEEILKQLEEIEKEQEKLSeMLQGLRKDELE 415
|
170
....*....|...
gi 755514337 585 AlRDQLESTQIKL 597
Cdd:PRK04778 416 A-REKLERYRNKL 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-630 |
4.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 395 KIESQRAMLQLKGRVSEL----EAELAEQQHLGRQAMDDCEFLRTE----LDELKRQrEDTEKAQRsLTEIERKAQANEQ 466
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEAKKAEekkkADELKKA-EELKKAEE-KKKAEEAKKAEED 1575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 467 RYSKLKEkyselvqnhadllrknAEVTKQVSVARQAQVD--LEREKKELADSFARTQEQQDVLENLKHElatsrQELQVL 544
Cdd:PTZ00121 1576 KNMALRK----------------AEEAKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 545 HSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTllAGIRKAAE 624
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA--EELKKKEA 1712
|
....*.
gi 755514337 625 REIQEA 630
Cdd:PTZ00121 1713 EEKKKA 1718
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
372-597 |
6.70e-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: 40.49 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 372 EKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEaELAEQQHLGRQAMDDCEFLRTELDelKRQREDTEKAQ 451
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLE--KQQSSLAEAEQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 452 RsLTEIERKAQANEQRYSKLKEKYSELVQ--NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLEN 529
Cdd:pfam05557 171 R-IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAAT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 530 LKHELATSRQELQ-----------------VLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 592
Cdd:pfam05557 250 LELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
....*
gi 755514337 593 TQIKL 597
Cdd:pfam05557 330 LNKKL 334
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
514-632 |
6.98e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 514 ADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQgslatvaAQREEELSALRDQLEST 593
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQ-------QELEAQLEQLQEKAAET 210
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755514337 594 QiklagaqesmcQQVKDQRKTLlagIRKAAER-EIQEALS 632
Cdd:PRK11448 211 S-----------QERKQKRKEI---TDQAAKRlELSEEET 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
501-637 |
7.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 501 QAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETsaqseakwltQIAELEkeqgslatvaaqrE 580
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE----------KKEKLQ-------------E 562
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 755514337 581 EELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEEP 637
Cdd:PRK00409 563 EEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKA 619
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
437-636 |
7.22e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.21 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 437 LDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarQAQVDLEREKKELADS 516
Cdd:pfam12795 29 LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLL----QTSAQLQELQNQLAQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 517 FARTQEQQDVLENLKHELATSRQELQVLHSNLE-TSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSA--LRDQLEST 593
Cdd:pfam12795 105 NSQLIELQTRPERAQQQLSEARQRLQQIRNRLNgPAPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSnnNRQDLLKA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 755514337 594 QIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 636
Cdd:pfam12795 185 RRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
404-625 |
8.06e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 40.27 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 404 QLKGRVSELEAELAEQQHLGRQAMDdceflrTELDELKRQREDTEKAQRSL--------TEIERKAQANEQRYSKLKEKY 475
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKE------ALRKEMKKEREELGATMLALsqnvaqleAQVEKVTREKNSLVSQLEEAQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 476 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDV-LENLKHELATSRQELQVLHSNlETSAQS 554
Cdd:pfam15964 438 KQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQeIEKLGLELSESKQRLEQAQQD-AARARE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 555 EAKWLTQ----------IAELEK---------EQGSLATVAAQREEELS-------ALRDQLESTQIKLAGAQESMCQQV 608
Cdd:pfam15964 517 ECLKLTEllgesehqlhLTRLEKesiqqsfsnEAKAQALQAQQREQELTqkmqqmeAQHDKTVNEQYSLLTSQNTFIAKL 596
|
250
....*....|....*..
gi 755514337 609 KDQRKTLLAGIRKAAER 625
Cdd:pfam15964 597 KEECCTLAKKLEEITQK 613
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-636 |
8.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 439 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFA 518
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 519 RTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIaELEKEQGSLATVAAQREEELSALRDQLESTQIKLA 598
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*...
gi 755514337 599 GAqESMCQQVKDQRKTllagirkaaEREIQEALSQLEE 636
Cdd:PRK03918 332 EL-EEKEERLEELKKK---------LKELEKRLEELEE 359
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
435-587 |
8.51e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 435 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQvsvarqaq 503
Cdd:PRK09039 53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE-------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 504 vdLEREKKELADsfARTQeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATVA-AQREEE 582
Cdd:PRK09039 125 --LDSEKQVSAR--ALAQ-----VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNVAlAQRVQE 191
|
....*
gi 755514337 583 LSALR 587
Cdd:PRK09039 192 LNRYR 196
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
387-570 |
8.54e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 387 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 459
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 460 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFART---QEQQDVLENLKH 532
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAnvsKFSSYKVELLQQ 358
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 755514337 533 ELATSRQELQV----LHSNLETSAQSEAKWLTQIAELEKEQG 570
Cdd:PLN02939 359 KLKLLEERLQAsdheIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
401-526 |
9.91e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755514337 401 AMLQLKGRVSELEAELAEQ------QHLGRQAmddcefLRTELDELKRQREDTEKAQRSLTEIERK-AQANEQRYSKLKE 473
Cdd:COG3206 264 VIQQLRAQLAELEAELAELsarytpNHPDVIA------LRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQAQLA 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755514337 474 KYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKEladsfARTQEQQDV 526
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE-----ARLAEALTV 385
|
|
| |
