|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
15-281 |
9.38e-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: 296.13 E-value: 9.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 15 YTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:pfam07651 2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 94 NELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELN 172
Cdd:pfam07651 82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 173 LFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKD 246
Cdd:pfam07651 160 LQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1907162019 247 LFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 281
Cdd:pfam07651 239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
789-987 |
3.11e-91 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 288.88 E-value: 3.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 789 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 868
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 869 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 947
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907162019 948 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 987
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
16-128 |
4.77e-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: 263.82 E-value: 4.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 16 TVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 95
Cdd:cd17013 2 TVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 81
|
90 100 110
....*....|....*....|....*....|...
gi 1907162019 96 LSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17013 82 LSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
16-128 |
5.76e-68 |
|
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: 222.54 E-value: 5.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 16 TVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNE 95
Cdd:cd17006 2 AISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSR 81
|
90 100 110
....*....|....*....|....*....|...
gi 1907162019 96 LSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17006 82 LKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
839-985 |
4.63e-59 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 198.96 E-value: 4.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 839 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 918
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 919 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 985
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
17-128 |
4.13e-55 |
|
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: 186.61 E-value: 4.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 96
Cdd:cd17014 3 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNI 82
|
90 100 110
....*....|....*....|....*....|..
gi 1907162019 97 SDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17014 83 RETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
16-128 |
5.77e-41 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 146.37 E-value: 5.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 16 TVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR- 91
Cdd:cd16986 2 EKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDa 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907162019 92 YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd16986 81 WLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
15-135 |
1.47e-36 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 133.91 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 15 YTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSLRY 92
Cdd:smart00273 3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRN 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907162019 93 KNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 135
Cdd:smart00273 83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
457-555 |
8.30e-34 |
|
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.
Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 125.12 E-value: 8.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 457 HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQ 536
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 1907162019 537 SEAKWLTQIAELEKEQGSL 555
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
17-128 |
5.90e-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: 100.46 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 96
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 1907162019 97 SDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 128
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-619 |
1.50e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAqRSLTEIERKAQAN---------EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQ 478
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 479 VDLEREKKELADSFARVSDQAQRKTQEQQDVLE---NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSL 555
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 556 ATVAAQREEELSALRDQLESTQIKLAGA--QESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-619 |
2.72e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 357 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAmddcEFLRTEL----DELKRQREDTEKAQRSLTEI 432
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELeeleLELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 433 ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQ---AQRKTQEQQDV 509
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlleAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 510 LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAtvaAQREEELsALRDQLESTQIKLAGAQESMCQ 589
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---EALAELE-EEEEEEEEALEEAAEEEAELEE 456
|
250 260 270
....*....|....*....|....*....|
gi 1907162019 590 QVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-619 |
9.31e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 429
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 430 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV 509
Cdd:TIGR02168 256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 510 ---LENLKHELATSRQELQVLHSNLE------TSAQSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:TIGR02168 329 eskLDELAEELAELEEKLEELKEELEsleaelEELEAELEELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907162019 580 LAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:TIGR02168 409 LERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-619 |
1.03e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 372 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK-AQRSLTEIERKAQANEQRYSKLKEKY 450
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 451 SELVQNHADL--LRKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQR---KTQEQQDVLENLKHELATSRQEL 524
Cdd:TIGR02168 761 AEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 525 QVLHSNLETSAQseakwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRK 604
Cdd:TIGR02168 841 EDLEEQIEELSE-------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE--LESKRS 911
|
250
....*....|....*
gi 1907162019 605 AAEREIQEALSQLEE 619
Cdd:TIGR02168 912 ELRRELEELREKLAQ 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-620 |
1.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISGLTgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK- 424
Cdd:COG1196 281 LELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAe 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 425 ---AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQR 501
Cdd:COG1196 360 laeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 502 KTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLa 581
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG- 518
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907162019 582 gaqesmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEEP 620
Cdd:COG1196 519 -------LRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
397-619 |
1.79e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 397 LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSVARQ 476
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 477 AQVDLEREKKELADSFARVsDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE----LEKEQ 552
Cdd:COG4913 683 SSDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaAALGD 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 553 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrkAAEREIQEALSQLEE 619
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL--ESLPEYLALLDRLEE 826
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-617 |
2.55e-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: 60.55 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 372 ESQRAMLQLKGRVSELEAELAEQQhlgRQAmddceflRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYS 451
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALK---KEE-------KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 452 ELvqnHADLLRKNAEVTKQVsvaRQAQVDLEREKKELADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNL 531
Cdd:COG4942 94 EL---RAELEAQKEELAELL---RALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 532 ETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQ 611
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1907162019 612 EALSQL 617
Cdd:COG4942 246 AGFAAL 251
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-619 |
3.08e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRsLTEIERKAQANEQRYSKLKEK 449
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 450 YSELVQ----NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVL----ENLKHELATSR 521
Cdd:PTZ00121 1536 ADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 522 QELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAG 601
Cdd:PTZ00121 1616 EEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250
....*....|....*...
gi 1907162019 602 IRKAAEREIQEALSQLEE 619
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEA 1712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
418-619 |
4.86e-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: 59.39 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 418 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsd 497
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 498 qaQRKTQEQQDVLENLKHELATSRQELQ----------VLHSNLETSAQSEAKWLTQIAELEKEQG-----SLATVAAQR 562
Cdd:COG4942 89 --EKEIAELRAELEAQKEELAELLRALYrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAeelraDLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 563 EEeLSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKaAEREIQEALSQLEE 619
Cdd:COG4942 167 AE-LEAERAELEALLAELEEERAAL-EALKAERQKLLARLEK-ELAELAAELAELQQ 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-617 |
6.18e-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: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 345 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 421
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 422 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvaRQAQVDLE 482
Cdd:TIGR02169 284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---DKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 483 REKKELADSFARV------SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLA 556
Cdd:TIGR02169 361 ELKEELEDLRAELeevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 557 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 617
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
17-126 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 17 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 93
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907162019 94 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 126
Cdd:cd03564 83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-619 |
1.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF--LRTELDELKRQREDTEKAQRSL 429
Cdd:COG4913 612 LAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 430 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLE-REKKELADSFARVSDQAQRKTQEQQd 508
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGDAVERE- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 509 VLENLKHELATSRQELQVLHSNLEtSAQSEAK--WLTQIAELEkeqgslATVAAqrEEELSALRDQLEstQIKLAGAQES 586
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELE-RAMRAFNreWPAETADLD------ADLES--LPEYLALLDRLE--EDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 1907162019 587 MCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG4913 836 FKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-619 |
7.83e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 353 ERLYReISGLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLGRQamddCEFLRTELDELKRQREDTEKAQRSLTE 431
Cdd:COG4717 56 DELFK-PQGRKPELNLKELKELEEELKeAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 432 IERKAQANEQ------RYSKLKEKYSELVQNHADLLRKNAEVtkqvsvaRQAQVDLEREKKELADSFARVSDQAQRKTQE 505
Cdd:COG4717 131 YQELEALEAElaelpeRLEELEERLEELRELEEELEELEAEL-------AELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 506 QQDVLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQReeELSALRDQLESTQIKLAGAQ- 584
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGVLf 280
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162019 585 ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG4717 281 lvlGLLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
375-616 |
1.19e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 375 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 450
Cdd:pfam07888 28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 451 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSN 530
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 531 LETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRK 604
Cdd:pfam07888 176 LQAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERK 252
|
250
....*....|....
gi 1907162019 605 AA--EREIQEALSQ 616
Cdd:pfam07888 253 VEglGEELSSMAAQ 266
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-581 |
1.91e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 350 HLIERLYREISGLTGQldnmkIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELK-----------R 417
Cdd:TIGR02168 747 ERIAQLSKELTELEAE-----IEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaaN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 418 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD 497
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 498 QAQ---RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwltQIAELEK-EQGSLATVAAQREEELSALRDQL 573
Cdd:TIGR02168 902 ELReleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-------RLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
....*...
gi 1907162019 574 ESTQIKLA 581
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
337-582 |
2.49e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 337 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 407
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 484
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 485 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 564
Cdd:PHA02562 308 LKELQHSL--------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250
....*....|....*...
gi 1907162019 565 ELSALRDQLESTQIKLAG 582
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSE 397
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
339-612 |
2.79e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 339 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 415
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 416 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdLEREKkeladsfarv 495
Cdd:pfam17380 351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKI-LEEER---------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 496 sdqaQRKTQEQQDVLENLKHELATSRQ-ELQVLHsnletsaQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:pfam17380 412 ----QRKIQQQKVEMEQIRAEQEEARQrEVRRLE-------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907162019 575 STQIKLAGAQES----MCQQVKDQRKTLL--AGIRKAAEREIQE 612
Cdd:pfam17380 481 KEKRDRKRAEEQrrkiLEKELEERKQAMIeeERKRKLLEKEMEE 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-575 |
3.67e-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: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 388 EAELAEQQ--HLG--RQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLL 461
Cdd:COG4913 243 ALEDAREQieLLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 462 RKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQRktqeQQDVLENLKHELATSRQELQVLHSNLETSAQSEAK 540
Cdd:COG4913 323 EELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRAR----LEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1907162019 541 WLTQIAELEKEQGSLATVAAQREEELSALRDQLES 575
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-602 |
3.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 345 KDEKDHLIERLYREISGLTGQLD---------NMKIES-QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDE 414
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEelrlevselEEEIEElQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 415 LKRQREDTEKA------------------QRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR- 475
Cdd:TIGR02168 328 LESKLDELAEElaeleekleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEa 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 476 ---QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAELEKEq 552
Cdd:TIGR02168 408 rleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE---EALEELREELEEAEQALDAAERE- 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907162019 553 gslatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGI 602
Cdd:TIGR02168 484 ----------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSG--LSGI 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-619 |
4.81e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 458
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 459 DLLRKNAEVTKQVSvarqaqvDLErEKKELADSFARVSdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQ 536
Cdd:PRK03918 270 ELKKEIEELEEKVK-------ELK-ELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 537 SEAKWLT-QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALS 615
Cdd:PRK03918 338 ERLEELKkKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEIS 408
|
....
gi 1907162019 616 QLEE 619
Cdd:PRK03918 409 KITA 412
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
386-547 |
8.43e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 386 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 465
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 466 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENLKH------ELATSRQ 522
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsgeefedSQDVTEYMQQLLEREREltverdELAARKQ 655
|
170 180
....*....|....*....|....*
gi 1907162019 523 ELQVLHSNLETSAQSEAKWLTQIAE 547
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-619 |
8.87e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 399 RQAMDDCEFLRTELDELKRQREDTEKAQR---SLTEIERKAQaneqRYSKLKEKYSELVQnhadllrknaevtkqvsVAR 475
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAELEY-----------------LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 476 QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLetSAQSEAKWLTQIAELEKEQGSL 555
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 556 ATVAAQREEELSALRDQLESTQIKLAGAQESmCQQVKDQRKTLLAGIRKA---AEREIQEALSQLEE 619
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAE-AAALLEALEEELEALEEAlaeAEAALRDLRRELRE 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-604 |
8.99e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISGLTGQLDNMKIEsqraMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKA 425
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 426 QRSLTEI------------ERKAQANEQRYSKLKEKYSelVQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSF 492
Cdd:TIGR02168 847 IEELSEDieslaaeieeleELIEELESELEALLNERAS--LEEALALLRSELEeLSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 493 ARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETsaqSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 572
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED---DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
250 260 270
....*....|....*....|....*....|....
gi 1907162019 573 LE--STQIKlagaqesmcqQVKDQRKTLLAGIRK 604
Cdd:TIGR02168 1002 YDflTAQKE----------DLTEAKETLEEAIEE 1025
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
338-621 |
9.12e-07 |
|
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: 52.65 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 338 NNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKR 417
Cdd:COG5185 140 VEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 418 QREDTEKAQRSLTEIERKAQANEQRYSKLK---EKYSELVQNHADL----LRKNAEVTKQVSVARQAQVDL-EREKKELA 489
Cdd:COG5185 220 TLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQfENTKEKIA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 490 DSFARVSD-------QAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAElEKEQGSLATVAAQR 562
Cdd:COG5185 300 EYTKSIDIkkateslEEQLAAAEAEQELEESKRETETGIQNLT---AEIEQGQESLTENLEAIKE-EIENIVGEVELSKS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 563 EEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEEPT 621
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
374-530 |
1.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 374 QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREdtEKAQRSLTEIERKAQANEQRYSKLKEKYSEL 453
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 454 vQNHADLLRKNAEVTKQVSVARQAQVdlerekKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSN 530
Cdd:COG4913 365 -EALLAALGLPLPASAEEFAALRAEA------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-619 |
1.32e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 431
Cdd:PRK02224 178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 432 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQRKTQEQQD 508
Cdd:PRK02224 239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 509 VLEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQ 577
Cdd:PRK02224 318 ELEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162019 578 IKLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 619
Cdd:PRK02224 398 ERFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
344-619 |
1.72e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 344 NKDEKDHLIER---LYREISGLTGQLDNMK---IESQRAMLQLKGRVSELEAEL-AEQQHLGR-----QAMDDCEFLRTE 411
Cdd:COG3096 276 HANERRELSERaleLRRELFGARRQLAEEQyrlVEMARELEELSARESDLEQDYqAASDHLNLvqtalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 412 LDEL----KRQREDTEKAQRSLTEIERKAQANEQRYSKLK---------------------------EKYSELVQNhADL 460
Cdd:COG3096 356 LEELterlEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqqaldvqqtraiqyqqavqalEKARALCGL-PDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 461 LRKNAEVTKQVSVARQAQVD---LEREKK-ELADSFARVSDQA-------------QRKTQEQQDVLE---NLKHeLATS 520
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATeevLELEQKlSVADAARRQFEKAyelvckiageverSQAWQTARELLRryrSQQA-LAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 521 RQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQE--SMCQQVKDQRKTL 598
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrSELRQQLEQLRAR 593
|
330 340
....*....|....*....|...
gi 1907162019 599 LAGIRKAAE--REIQEALSQLEE 619
Cdd:COG3096 594 IKELAARAPawLAAQDALERLRE 616
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-619 |
1.79e-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: 52.10 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 449
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 450 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVlENLKHELATSR 521
Cdd:pfam01576 336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS-EHKRKKLEGQL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 522 QELQVLHSNLETSAQSEAKWLTQI-AELEKEQGSLATVAAQR---EEELSALRDQL--------ESTQIKLAGAqeSMCQ 589
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLqSELESVSSLLNEAEGKNiklSKDVSSLESQLqdtqellqEETRQKLNLS--TRLR 492
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162019 590 QVKDQRKTLLAGI------RKAAEREIQEALSQLEE 619
Cdd:pfam01576 493 QLEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSD 528
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-619 |
1.98e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 448
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 449 KYSElvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKElADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLH 528
Cdd:PTZ00121 1465 KAEE--AKKADEAKKKAEEAKK---ADEAKKKAEEAKKK-ADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 529 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAA 606
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKAE 1616
|
250
....*....|....
gi 1907162019 607 EREIQ-EALSQLEE 619
Cdd:PTZ00121 1617 EAKIKaEELKKAEE 1630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
346-619 |
2.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISGLTGQLDNMkiESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 401
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNA--EDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 402 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 472
Cdd:PRK02224 465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 473 VARQAQVDLEREKKELADSFARVSDQAQrKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAkwltQIAELEKEQ 552
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAELKERIESLERIRTLLAAIADAED----EIERLREKR 615
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 553 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 619
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
406-616 |
2.73e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 406 EFLRTELDELKRQREDTE------KAQRSLTEIERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSV 473
Cdd:COG3206 178 EFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEAraelaeAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 474 ARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLEnLKHELATSRQELQVLHSNLETSAQSEAKwltqiaelekeqg 553
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILASLEAELE------------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 554 slatVAAQREEELSALRDQLESTQIKLAGAQ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 616
Cdd:COG3206 324 ----ALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-556 |
3.60e-06 |
|
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: 50.53 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 351 LIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQamddceflrTELDELKRQrEDTEKAQRSLT 430
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ---------PPLALLLSP-EDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 431 EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQdvl 510
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--- 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162019 511 enlkhELATSRQELQVLHSNLETSAQSEAKwLTQIAELEKEQGSLA 556
Cdd:COG4942 217 -----ELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLP 256
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
356-574 |
5.37e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.53 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 356 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 432
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 433 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSFARVSD 497
Cdd:pfam00038 132 -------ELAF--LKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaAKNREEAEEWYQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 498 QAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 572
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQETRQE 278
|
..
gi 1907162019 573 LE 574
Cdd:pfam00038 279 MA 280
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-619 |
6.34e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTE----LDELKRQREDTEKAQRSLTEIERKA-----QANE 440
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEaeaaADEAEAAEEKAEAAEKKKEEAKKKAdaakkKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 441 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSfARVSDQAQRKTQEQQDVlENLKHELA 518
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEE-AKKADEAKKKAEEAKKA-EEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 519 TSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTL 598
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260
....*....|....*....|.
gi 1907162019 599 LAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEE 1568
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
348-618 |
8.95e-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: 49.73 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 348 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 414
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 415 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 472
Cdd:pfam15921 563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 473 VARQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAEL 548
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 549 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAA 606
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQ 798
|
330
....*....|..
gi 1907162019 607 EREIQEALSQLE 618
Cdd:pfam15921 799 ERRLKEKVANME 810
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
423-611 |
9.10e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 423 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR----QAQVDLEREKKELADSFARVsDQ 498
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReeleQLEEELEQARSELEQLEEEL-EE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 499 AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 578
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1907162019 579 KLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQ 611
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
338-619 |
1.12e-05 |
|
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: 49.25 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 338 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 407
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 483
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 484 EKKELADSFarvsDQAQRKTQEQQDVL--ENLKHELATSRQELQVLHSNLE--TSAQSEAKWL-----TQIAELEKEQGS 554
Cdd:TIGR04523 532 EKKEKESKI----SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKslKKKQEEKQELidqkeKEKKDLIKEIEE 607
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 555 LATVAAQREEELSALRDQ---LESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 619
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEiiKKIKESKTKIDD 677
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
386-547 |
1.38e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 386 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 465
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 466 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENL------KHELATSRQ 522
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAarapawlaaqDALERLREQsgealadSQEVTAAMQQLLEREreatveRDELAARKQ 654
|
170 180
....*....|....*....|....*
gi 1907162019 523 ELQVLHSNLETSAQSEAKWLTQIAE 547
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAE 679
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-619 |
1.51e-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: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 407 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 475
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 476 QAQVDLEREKKELADSFARVSDQaQRKTQEQQDVLENLKHELATSR-QELQVLHSNLETSAQseaKWLTQIAELEKEQGS 554
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEEL-EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVS---RIEARLREIEQKLNR 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162019 555 LATVAAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 619
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL-EEELEELEAALRDLES 882
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
374-619 |
1.67e-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: 49.20 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 374 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 453
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 454 VQNHADLLRKNAEVTKQVSVARQAQvdleREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSNLET 533
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHAL----LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSI 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 534 SAQSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREI 610
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
....*....
gi 1907162019 611 QEALSQLEE 619
Cdd:TIGR00618 746 KELMHQART 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
367-619 |
2.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 367 DNMKIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRtELDELKRQREDTEKAQRSLTEIER-------KAQAN 439
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEakkadeaKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 440 EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQ-----------RKTQEQQD 508
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKkaeekkkadelKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 509 VLENLKHELATSRQELQVLHS-NLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESM 587
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162019 588 CQQVKDQRKTllAGIRKAAE----REIQEALSQLEE 619
Cdd:PTZ00121 1640 KKEAEEKKKA--EELKKAEEenkiKAAEEAKKAEED 1673
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-619 |
2.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAMLQLKGRvselEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSlteieRKAQANEQRYSKLKEK 449
Cdd:PTZ00121 1571 KAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 450 YSELVQNhADLLRKnAEVTKQVSVARQAQVDLEREKKeladsfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHS 529
Cdd:PTZ00121 1642 EAEEKKK-AEELKK-AEEENKIKAAEEAKKAEEDKKK---------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 530 NLETSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAERE 609
Cdd:PTZ00121 1711 EAEEKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
250
....*....|
gi 1907162019 610 IQEALSQLEE 619
Cdd:PTZ00121 1781 IEEELDEEDE 1790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-619 |
3.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 406 EFLRTEL-DELKRQREDTEKAQrslteiERKAQANEQRYSKLKEKYSELVQNHADLlrknAEVTKQVSVARQAQVDLERE 484
Cdd:COG4717 41 AFIRAMLlERLEKEADELFKPQ------GRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 485 KKELADSFARVSDQAQRKTQEQQdvLENLKHELATSRQELQVLHSNLETSAQseakWLTQIAELEKEQGSLATVAAQREE 564
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 565 ELS-ALRDQLESTQIKLAGAQesmcqqvkdQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG4717 185 QLSlATEEELQDLAEELEELQ---------QRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
383-545 |
4.60e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.40 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 383 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 462
Cdd:PRK12705 37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 463 KNAEvtkqvsvarqaqvdLEREKKELADSFARVSDQAQRktQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWL 542
Cdd:PRK12705 117 RELE--------------LEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERK 177
|
...
gi 1907162019 543 TQI 545
Cdd:PRK12705 178 AQN 180
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
346-614 |
6.70e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 390
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 391 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 454
Cdd:pfam10174 442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 455 QNHADLLRKNAEVTKQVSVARQAQ--VDLEREKKELADSFARVSDQAQRKTQE----QQDV---------LENLKH---- 515
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerllgilreVENEKNdkdk 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 516 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 582
Cdd:pfam10174 601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907162019 583 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 614
Cdd:pfam10174 681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-619 |
7.22e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 414 ELKRQREDTEKaqrsltEIERkAQANEQRyskLKEKYSELvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKELADSFA 493
Cdd:COG1196 169 KYKERKEEAER------KLEA-TEENLER---LEDILGEL-ERQLEPLERQAEKAER---YRELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 494 RVSDQAQRKTQEQQDVLEN-----------LKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 562
Cdd:COG1196 235 RELEAELEELEAELEELEAeleeleaelaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 563 EEELSALRDQLESTQIKLAGAQESmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
355-592 |
9.88e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 355 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 428
Cdd:PRK04863 849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 429 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 477
Cdd:PRK04863 918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 478 QVDLEREKKELADSFARVSDQAQRKTQEQQ--DVLENLKHELATSRQELQV-LHSNLETSAQSEAKWL--------TQIA 546
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSsyDAKRQMLQELKQELQDLGVpADSGAEERARARRDELharlsanrSRRN 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907162019 547 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 592
Cdd:PRK04863 1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
362-574 |
9.97e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 362 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 433
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 434 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFARVS---------DQAQRKT 503
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQET 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 504 QEQQDvlENLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 574
Cdd:pfam12128 805 WLQRR--PRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
379-618 |
1.08e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 379 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQAN---------------EQRY 443
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkdlqreleearasrDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 444 SKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdlerEKKELADsfaRVSDQAQRKTQeQQDVLENLKHELATSRQE 523
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQ----ERDELAD---EIASGASGKSA-LQDEKRRLEARIAQLEEE 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 524 LQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREeelsALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgir 603
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFKSSIA--- 970
|
250
....*....|....*
gi 1907162019 604 kAAEREIQEALSQLE 618
Cdd:pfam01576 971 -ALEAKIAQLEEQLE 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-619 |
1.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 351 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 429
Cdd:PRK03918 315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 430 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFARVSDQAQR 501
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 502 KTQEQQDVLENLKHELATSRQELqvlhsNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLA 581
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLK 538
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162019 582 GAQESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PRK03918 539 GEIKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
421-579 |
1.26e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 421 DTEKAQRSLTEIERKAQANEQRYSKLKEkyseLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArvsdqaq 500
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEA----ELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAV------- 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 501 rkTQEQqdvLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEqgslatvAAQREEELSALRDQLESTQIK 579
Cdd:COG1566 146 --SQQE---LDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQ-------VAQAEAALAQAELNLARTTIR 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
437-602 |
1.30e-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: 44.53 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 437 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV-----LE 511
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 512 NLKHELATSRQELQVLhsnletsAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQEsmcqQV 591
Cdd:COG1579 93 ALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE----EL 161
|
170
....*....|.
gi 1907162019 592 KDQRKTLLAGI 602
Cdd:COG1579 162 EAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
362-580 |
1.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 362 LTGQLDNMKIESQRAMLQLKG-RVSELEAELAEQQHLGRQAMDDcefLRTELDELKRQREDTE------KAQRSLTEIER 434
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSE---LESQLAEARAELAEAEarlaalRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 435 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarqaqVDLEREKKELAdsfARVSDQAQRKTQEQQDVLENLK 514
Cdd:COG3206 257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALR---AQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 515 HELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEelSALRDQLESTQIKL 580
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALTVGNVRV 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
352-453 |
1.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNmkiESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 431
Cdd:COG3206 293 VIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREAS--------------LQAQLAQLEARLAELPELEAELRR 355
|
90 100
....*....|....*....|..
gi 1907162019 432 IERKAQANEQRYSKLKEKYSEL 453
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-533 |
1.89e-04 |
|
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: 45.44 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 343 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 417
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 418 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtKQVSVARQAQVDLEREKKELADSFA 493
Cdd:TIGR02169 890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIR 968
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162019 494 RVSDQAQRKTQEQQDVLENL-----KHE-LATSRQELQVLHSNLET 533
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLdelkeKRAkLEEERKAILERIEEYEK 1014
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
375-580 |
1.96e-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: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 375 RAMLQLKGRVSEleAELAEQQHlgRQAMddcEFLRTELDELkrQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELV 454
Cdd:COG3096 455 EEVLELEQKLSV--ADAARRQF--EKAY---ELVCKIAGEV--ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 455 Q---NHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdQAQRKTQEQQdvLENLKHELATSRQELQVLHSNL 531
Cdd:COG3096 526 QrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL---------EAQLEELEEQ--AAEAVEQRSELRQQLEQLRARI 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162019 532 ETSAQSEAKWLTQIAELEK--EQG--SLATVAA---------QREEELSALRDQLESTQIKL 580
Cdd:COG3096 595 KELAARAPAWLAAQDALERlrEQSgeALADSQEvtaamqqllEREREATVERDELAARKQAL 656
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
400-586 |
2.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 400 QAMDDCEFLRTELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQVSVAR 475
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 476 QAQVDLEREKKEL--------ADSFA----------RVSDQ----------AQRKTQEQQDVLENLKHELATSRQELQVL 527
Cdd:COG3883 90 ERARALYRSGGSVsyldvllgSESFSdfldrlsalsKIADAdadlleelkaDKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 528 HSNLEtSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQES 586
Cdd:COG3883 170 KAELE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
352-575 |
3.13e-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: 44.94 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNMKIES--QRAMLQLKGRVSELEAELA-----EQQHlgRQAMD-------------------DC 405
Cdd:COG3096 811 LQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAqhraqEQQL--RQQLDqlkeqlqllnkllpqanllAD 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 406 EFLRTELDELKRQREDTEKAQRS-------LTEIERKA---QANEQRYSKLKEKY-----------------SELVQN-- 456
Cdd:COG3096 889 ETLADRLEELREELDAAQEAQAFiqqhgkaLAQLEPLVavlQSDPEQFEQLQADYlqakeqqrrlkqqifalSEVVQRrp 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 457 H------ADLLRKNAEVTKQV-SVARQAQVDLEREKKELADSFARVSDQAQRKT------QEQQDVLENLKHEL------ 517
Cdd:COG3096 969 HfsyedaVGLLGENSDLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLAslkssrDAKQQTLQELEQELeelgvq 1048
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162019 518 ------ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 575
Cdd:COG3096 1049 adaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
369-585 |
3.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 369 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 445
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 446 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKELADsfARVSDQ-----AQRKTQEQQDVLENLKHE 516
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEE--AKKDEEekkkiAHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 517 LATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAT--VAAQREEELSALRDQLESTQIKLAGAQE 585
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-580 |
3.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 371 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIER---KAQANEQRYSKL 446
Cdd:PRK02224 532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllaAIADAEDEIERL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 447 KEKYSELvqnhadllrknAEVTKQvsvaRQAQVDLERE-KKELADSF--ARVsDQAQRKTQEQQDVLENLKHELATSRQE 523
Cdd:PRK02224 612 REKREAL-----------AELNDE----RRERLAEKRErKRELEAEFdeARI-EEAREDKERAEEYLEQVEEKLDELREE 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 524 lqvlhsnlETSAQSEAKWLT-QIAELEKEQGSLATVAAqREEELSALRD---QLESTQIKL 580
Cdd:PRK02224 676 --------RDDLQAEIGAVEnELEELEELRERREALEN-RVEALEALYDeaeELESMYGDL 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-559 |
3.72e-04 |
|
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: 44.67 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 426
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 427 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdqaqRKTQE 505
Cdd:TIGR02169 409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------------YDLKE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162019 506 QQDVLENlkhELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 559
Cdd:TIGR02169 477 EYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
423-619 |
4.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 423 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQR- 501
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERARAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 502 -KTQEQQDVLENLKheLATSRQEL--QVlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 578
Cdd:COG3883 96 yRSGGSVSYLDVLL--GSESFSDFldRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162019 579 KLAGAQESmcqqvKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG3883 172 ELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
380-551 |
4.29e-04 |
|
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: 44.35 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 380 LKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL-DELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 458
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALkRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 459 DLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKhELATSRQELQVLHSNLETSAQSE 538
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLEKQQSSL 165
|
170
....*....|...
gi 1907162019 539 AKWLTQIAELEKE 551
Cdd:pfam05557 166 AEAEQRIKELEFE 178
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
408-533 |
4.40e-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: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREkke 487
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE--- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907162019 488 lADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQ----VLHSNLET 533
Cdd:pfam07926 80 -AESAKAELEESEESWEEQKKELEKELSELEKRIEDLNeqnkLLHDQLES 128
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
344-577 |
8.70e-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: 43.57 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 344 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 409
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 410 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSKlkEKYSELVQNHADLLRKN-AEVTKqvsvaRQAQVDLEREK-K 486
Cdd:pfam15921 331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTER--DQFSQESGNLDDQLQKLlADLHK-----REKELSLEKEQnK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 487 ELADSFARVS---DQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE 563
Cdd:pfam15921 402 RLWDRDTGNSitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV 481
|
250
....*....|....
gi 1907162019 564 EELSALRDQLESTQ 577
Cdd:pfam15921 482 EELTAKKMTLESSE 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
414-619 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 414 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFA 493
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 494 RVSDQAQRKTQEQQDVLENLKHELATSRQElqvlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQL 573
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162019 574 ESTQIKLAgaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121 1439 KAEEAKKA---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
414-619 |
1.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 414 ELKRQREDTEKAQRSLTEIERKA----QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAqvdlEREKKELA 489
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 490 DSFARVSDQAQRKTQEQQDVLENL--KHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELS 567
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907162019 568 ALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
400-619 |
1.30e-03 |
|
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: 42.80 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 400 QAMDDCEFLRTELDELKRQREDTEKAQRslteiERKAQANEQRYSKLKEKYSELVQNHADLlrKNAEVTKQVSVARQAQV 479
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKL--EEAEKARQAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 480 DLEREKKELadsfarvsdqaQRKTQEQQDVLENLKHELATSRQElqvlhsnletsaqSEAKWLTQIAELEKEQgslatva 559
Cdd:pfam17380 336 YAEQERMAM-----------ERERELERIRQEERKRELERIRQE-------------EIAMEISRMRELERLQ------- 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 560 AQREEELSALRDQLEST-QIKLagaQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:pfam17380 385 MERQQKNERVRQELEAArKVKI---LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
417-612 |
1.51e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 417 RQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDlEREKKELADSFARVS 496
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-ERQRQEEEERKQRLQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 497 DQ-AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAElekEQGSLATVAaqREEELSALRDQLES 575
Cdd:pfam15709 414 LQaAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE--MQLAE---EQKRLMEMA--EEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907162019 576 TQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQE 612
Cdd:pfam15709 487 EEKARLEAEERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
399-578 |
1.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 399 RQAMDDCEFLRTELDELKRQREDTE----KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVA 474
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEeeleQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 475 RQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAELEKEQGS 554
Cdd:COG4372 121 QKERQDLEQQRKQLEAQ----IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE--QALDELLKEANR 194
|
170 180
....*....|....*....|....
gi 1907162019 555 LATVAAQREEELSALRDQLESTQI 578
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAE 218
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
383-616 |
1.74e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 383 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 462
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 463 KNAEVTKQVSVARQ---AQVDLEREKKELADSFARVsDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEA 539
Cdd:pfam02463 251 EEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEE-ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 540 KWLTQ--IAELEKEqgsLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 616
Cdd:pfam02463 330 LKKEKeeIEELEKE---LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
379-579 |
2.08e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 379 QLKGRVSELEAELAEQQHLgrqamddceflrteldelkrqredtekaqrslteiERKAQANEQRYSKLKEKYSELVQNHA 458
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQ-----------------------------------VARLQAELDRLQALESELAISRQDYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 459 DLLRKNAEVTKQVSVArQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQse 538
Cdd:pfam00529 100 GATAQLRAAQAAVKAA-QAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162019 539 akwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 579
Cdd:pfam00529 177 ----ENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
410-570 |
2.26e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 410 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQaq 478
Cdd:PRK09039 53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 479 vdlerekkeladsfarVSDQAQRKtqeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATV 558
Cdd:PRK09039 131 ----------------VSARALAQ-------VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNV 183
|
170
....*....|...
gi 1907162019 559 A-AQREEELSALR 570
Cdd:PRK09039 184 AlAQRVQELNRYR 196
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
353-617 |
2.29e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 353 ERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLG-RQAMDDCEFLRTELDELKRQ-------REDTEK 424
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGELKLRlnqatatPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 425 AQRSLTEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSVARQAQVD--------------------LERE 484
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 485 KKELADSFARVSDQAQ--RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 562
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 563 EEELSALRDQLESTQIKLAGAQESM------CQQVKDQRKTLLAGIRKAAEREIQEALSQL 617
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALknarldLRRLFDEKQSEKDKKNKALAERKDSANERL 684
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-618 |
2.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 401
Cdd:PRK03918 448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 402 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsvarqaqvDL 481
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 482 EREKKELA---DSFARVSDqAQRKTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatv 558
Cdd:PRK03918 591 EERLKELEpfyNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS----- 657
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162019 559 aaqrEEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 618
Cdd:PRK03918 658 ----EEEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
487-619 |
2.53e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 487 ELADSFarVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLE--------TSAQSEAKWLT-QIAELEKEQGSLAT 557
Cdd:COG3206 156 ALAEAY--LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqQLSELESQLAEARA 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 558 VAAQREEELSALRDQLESTQIKLAGAQES-MCQQVKDQRKTL---LAGIR----------KAAEREIQEALSQLEE 619
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpVIQQLRAQLAELeaeLAELSarytpnhpdvIALRAQIAALRAQLQQ 309
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
357-612 |
2.57e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 357 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQqhLGRQAMDDCEFLRTElDELKRQREDTEKAQRSLTEIERKA 436
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKE-KEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 437 QANEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------VARQAQVDLER----------EKKELADSFARVSDQ 498
Cdd:TIGR00606 768 EEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqekqEKQHELDTVVSKIEL 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 499 AQRKTQEQQDVLENLKHELatsrQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQ- 577
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQq 923
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907162019 578 -----IKLAGAQESMCQ-QVKDQRKTL--LAGIRKAAEREIQE 612
Cdd:TIGR00606 924 ekeelISSKETSNKKAQdKVNDIKEKVknIHGYMKDIENKIQD 966
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
420-593 |
2.75e-03 |
|
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: 40.04 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 420 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHAD------LLRKNAEVTKQVSVARQAQV---------DLERE 484
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEfektiaQMIEEKQKQKELEHAEIQKVleekdqalaDLNSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 485 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQRE 563
Cdd:pfam05010 88 EKSFSDLF--------KRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAK 159
|
170 180 190
....*....|....*....|....*....|
gi 1907162019 564 EELSALRDQLESTQIKLAGAQESMCQQVKD 593
Cdd:pfam05010 160 AETAALQASLRKEQMKVQSLERQLEQKTKE 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-575 |
2.94e-03 |
|
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: 41.54 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 328 SSLSSDPFNFNNQNGVNKDEKDhlieRLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF 407
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKN----KLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLK---EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE 484
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKN---IDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 485 KKE-------LADSFARVSDQAQRKTQE-----------------------------QQDVLENLKHELATSRQELQVLH 528
Cdd:TIGR04523 248 ISNtqtqlnqLKDEQNKIKKQLSEKQKEleqnnkkikelekqlnqlkseisdlnnqkEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907162019 529 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 575
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
411-619 |
3.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 411 ELDELKRQREDTEKA---QRSLTEIERKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 487
Cdd:PTZ00121 1303 KADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 488 LADSFA---RVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 564
Cdd:PTZ00121 1382 AAKKKAeekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162019 565 ELSALRDQLESTQIKLAGAQESMCQQVK---DQRKTLLAGIRKAAE-REIQEALSQLEE 619
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEaKKKADEAKKAEE 1520
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
370-573 |
3.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 370 KIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEK 449
Cdd:COG1579 14 ELDSELD--RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----------IKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 450 YSElVQNHADLlrknAEVTKQVSVARQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQvlhs 529
Cdd:COG1579 82 LGN-VRNNKEY----EALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELD---- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907162019 530 nletsaqseakwlTQIAELEKEqgsLATVAAQREEELSALRDQL 573
Cdd:COG1579 149 -------------EELAELEAE---LEELEAEREELAAKIPPEL 176
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
411-590 |
3.58e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 411 ELDELKRQREDTEKAQR-SLTEIERKA-------QANEQRYSKLKEKY-SELVQNHADLLRKNAEVTKQVSVARQAQVDL 481
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQeRQKKLEQQAeeaekqrAAEQARQKELEQRAaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 482 EREKKELADSFARVSDQAQRKTQEqqdvlENLKHELATSRQELQVLHSNLETSAQSEA-------------KWLTQIAEL 548
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEE-----EAKAKAAAEAKKKAEEAKKKAEAEAKAKAeaeakakaeeakaKAEAAKAKA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907162019 549 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQ 590
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
443-577 |
3.90e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 443 YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADsfarvsdQAQRKTQEQQDVLENLKHELATSRQ 522
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD-------RAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162019 523 ELQVLHSNLETSAQSEAKWLTQIAELEKeqgSLATVAAQREEELSALRDQLESTQ 577
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
362-553 |
3.90e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 362 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 434
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 435 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--ARVSDQAQRKTQEQQD 508
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLkeANVSKFSSYKVELLQQ 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907162019 509 VLENLKHELATSRQElqvLHSNLETSAQSEAKWLTQIAELEKEQG 553
Cdd:PLN02939 359 KLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
377-607 |
3.92e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 377 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 456
Cdd:PRK10929 111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 457 hADLLRKNAEvtkqvSVARQAQVDlerekkELadsfarvsDQAQRKTQEQQDvLENLKHELATSRQE-----LQVLHSNL 531
Cdd:PRK10929 173 -AQLTALQAE-----SAALKALVD------EL--------ELAQLSANNRQE-LARLRSELAKKRSQqldayLQALRNQL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 532 ETSAQSEA-KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 607
Cdd:PRK10929 232 NSQRQREAeRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
392-619 |
4.23e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 392 AEQQHLGRQAMDDCEFLRTELDELKR--QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK 469
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAERIRtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESA 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 470 QvSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwlTQIAELE 549
Cdd:NF041483 680 D-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASAR------KRVEEAQ 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162019 550 KEQGSLATVAAQREEEL-SALRDQLESTQIKLAGAQESMCQQVkdqrktllAGIRKAAEREIQEALSQLEE 619
Cdd:NF041483 753 AEAQRLVEEADRRATELvSAAEQTAQQVRDSVAGLQEQAEEEI--------AGLRSAAEHAAERTRTEAQE 815
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
480-585 |
4.38e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 480 DLEREKKELADSFArvsdQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 559
Cdd:PRK09039 57 RLNSQIAELADLLS----LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100
....*....|....*....|....*.
gi 1907162019 560 AQREEELSALRDQLESTQIKLAGAQE 585
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEA 158
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
408-594 |
5.15e-03 |
|
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: 40.77 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 408 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSelvqnhadllrknaevtkqvsvarqaqvDLEREKK 486
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYN----------------------------DLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 487 ELADSFARVSDQAQRKtqeqQDVLENLKHELAtsrqELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 566
Cdd:TIGR04523 170 ELENELNLLEKEKLNI----QKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
170 180
....*....|....*....|....*...
gi 1907162019 567 SALRDQLESTQIKLAGAQESMcQQVKDQ 594
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQ-NKIKKQ 268
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
352-619 |
5.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 352 IERLYREISGLTGQLDNMKIESQRAMlqlkgrvSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTE 431
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLE-------EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 432 IERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLE 511
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK---ELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 512 NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI-KLAGAQESMCQQ 590
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIlKEIEELELAILV 269
|
250 260
....*....|....*....|....*....
gi 1907162019 591 VKDQRKTLLAGIRKAAEREIQEALSQLEE 619
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLL 298
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
344-597 |
6.54e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 40.04 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 344 NKDEKDHLIERLYREISGLTGQLDNMK--IESQRAMLQ-LKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELK 416
Cdd:smart00806 72 NVEELDEVKKHIDDEIDTLQNELDEVKqaLESQREAIQrLKERQQNSAANIARpaasPSPVLASSSSAISLANNPDKLNK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 417 RQREDTEKAQRSLTEIeRKAQANEQrySKLKEKYSELVQNHADLLRKNAEVTKQVSVAR--QAQVDLEREKKELADSFAR 494
Cdd:smart00806 152 EQRAELKSLQRELAVL-RQTHNSFF--TEIKESIKDILEKIDKFKSSSLSASGSSNRAYveSSKKKLSEDSDSLLTKVDD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 495 VSDQ--------AQRKTQEQQDVLENLKHELATSRQELQvlhsNLETSAQSEAKWLTQI--AELEK---EQGSLATvaaq 561
Cdd:smart00806 229 LQDIiealrkdvAQRGVRPSKKQLETVQKELETARKELK----KMEEYIDIEKPIWKKIweAELDKvceEQQFLTL---- 300
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162019 562 REEELSALRDQLESTQIKLAGAQESMCQQVKDQRKT 597
Cdd:smart00806 301 QEDLIADLKEDLEKAEETFDLVEQCCEEQEKGPSKN 336
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
406-587 |
7.21e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.01 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 406 EFLRTELDELKrqrEDTEKAQRSLTEIERK----AQANEQRYSKLKEkysELVQNHADLLRKNaevtKQVSVARQAQVDL 481
Cdd:pfam05701 183 EELTIELIATK---ESLESAHAAHLEAEEHrigaALAREQDKLNWEK---ELKQAEEELQRLN----QQLLSAKDLKSKL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 482 EREKKELADSFARVSDQAQRKTQEQQDVLENLKHE-------LATSRQELQVLHSNLEtSAQSEAKWLTQIA-----ELE 549
Cdd:pfam05701 253 ETASALLLDLKAELAAYMESKLKEEADGEGNEKKTstsiqaaLASAKKELEEVKANIE-KAKDEVNCLRVAAaslrsELE 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907162019 550 KEQGSLATV----------AAQREEELSALRDQLESTQIKLAGAQESM 587
Cdd:pfam05701 332 KEKAELASLrqregmasiaVSSLEAELNRTKSEIALVQAKEKEAREKM 379
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
353-619 |
8.32e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 353 ERLYREISGltgQLDNMKIESQRAMLQLKGR----VSELEAELAEQQHLGRQAMDDCEFLRTE-LDELKRQRedTEKAQR 427
Cdd:NF041483 396 ERIRREAEA---EADRLRGEAADQAEQLKGAakddTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIR--GEARRE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 428 SLTEIERKAQANEQRYSKLKEKYSELVQN-HADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQE 505
Cdd:NF041483 471 AVQQIEEAARTAEELLTKAKADADELRSTaTAESERVRTEaIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAA 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 506 QQDVLENLKHEL--------ATSRQELQVLHSNLE----------TSAQSEAKWLTQIAELEKEQ------GSLATVAAQ 561
Cdd:NF041483 551 AERAARELREETeraiaarqAEAAEELTRLHTEAEerltaaeealADARAEAERIRREAAEETERlrteaaERIRTLQAQ 630
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162019 562 REEELSALRDQL-----------ESTQIKL----AGAQESMCQQVKDQRKTLLAGIRKAAER---EIQEALSQLEE 619
Cdd:NF041483 631 AEQEAERLRTEAaadasaaraegENVAVRLrseaAAEAERLKSEAQESADRVRAEAAAAAERvgtEAAEALAAAQE 706
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-453 |
9.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 346 DEKDHLIERLYREISGLTGQLDNMKIESQR-AMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK 424
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELReEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907162019 425 AQRSLTEIER--------KAQANEQRYSKLKEKYSEL 453
Cdd:PRK03918 716 LEKALERVEElrekvkkyKALLKERALSKVGEIASEI 752
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
347-619 |
9.16e-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: 39.72 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 347 EKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAelAEQQHlgrqamddcEFLRTELDELKRQREDTEKAQ 426
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE--LQERL---------DLLKAKASEAEQLRQNLEKQQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 427 RSLTEIERKAQANEQRYSkLKEKYSELVQNhadllrknaevtkqvSVARQAQV-DLEREKKELADSFARVsdqaqRKTQE 505
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQ-SQEQDSEIVKN---------------SKSELARIpELEKELERLREHNKHL-----NENIE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 506 QQDVLENLKHELAT--SRQE--------LQVLHSNLETSAQSEAKwLTQIAELEkeqgslatvaAQREEELSALRDQLES 575
Cdd:pfam05557 222 NKLLLKEEVEDLKRklEREEkyreeaatLELEKEKLEQELQSWVK-LAQDTGLN----------LRSPEDLSRRIEQLQQ 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907162019 576 TQIKLAGAQESMCQQVKDQRKTllagiRKAAEREIQEALSQLEE 619
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKA-----RRELEQELAQYLKKIED 329
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
436-575 |
9.32e-03 |
|
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: 37.23 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 436 AQANEQRYSKLKEKYSELVQNHADllrknaEVTKQVSVARQAQVDLERE---KKELADSFARVSDQAQRktqeqqdvlen 512
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE------DLEKQAEIAREAQQNYERElvlHAEDIKALQALREELNE----------- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162019 513 LKHELATSRQELQVLHSNLEtsaQSEAKWLTQIAELEKEqgslATVAAQREEELSA----LRDQLES 575
Cdd:pfam07926 69 LKAEIAELKAEAESAKAELE---ESEESWEEQKKELEKE----LSELEKRIEDLNEqnklLHDQLES 128
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
436-533 |
9.38e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 39.32 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 436 AQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLErekKELADSFARVSDQAQRKTQEQQDVLENLKH 515
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQ---KELANAQAQALQTAQNNLATAQAALANAEA 332
|
90
....*....|....*...
gi 1907162019 516 ELATSRQELQVLHSNLET 533
Cdd:TIGR04320 333 RLAKAKEALANLNADLAK 350
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
379-608 |
9.94e-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: 39.89 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 379 QLKGRVSELEAELAEQQHLGRQAMDdceflrTELDELKRQREDTEKAQRSL--------TEIERKAQANEQRYSKLKEKY 450
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKE------ALRKEMKKEREELGATMLALsqnvaqleAQVEKVTREKNSLVSQLEEAQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 451 SELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSN 530
Cdd:pfam15964 438 KQLASQEMDVTKVCGEMRYQLN---QTKMKKDEAEKEHREYRTKTGRQLEIKDQE----IEKLGLELSESKQRLEQAQQD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162019 531 lETSAQSEAKWLTQ----------IAELEKEQ---------GSLATVAAQREEELS-------ALRDQLESTQIKLAGAQ 584
Cdd:pfam15964 511 -AARAREECLKLTEllgesehqlhLTRLEKESiqqsfsneaKAQALQAQQREQELTqkmqqmeAQHDKTVNEQYSLLTSQ 589
|
250 260
....*....|....*....|....
gi 1907162019 585 ESMCQQVKDQRKTLLAGIRKAAER 608
Cdd:pfam15964 590 NTFIAKLKEECCTLAKKLEEITQK 613
|
|
| |
