|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
39-306 |
3.10e-93 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 297.67 E-value: 3.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 39 TQTVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRY 117
Cdd:pfam07651 1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 118 KNELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECEL 196
Cdd:pfam07651 81 RRRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 197 NLFQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLK 270
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLK 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162011 271 DLFQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
814-1012 |
3.03e-90 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 286.96 E-value: 3.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 814 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 893
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 894 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 972
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907162011 973 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 1012
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
1.23e-83 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 265.75 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1907162011 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
7.19e-69 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 225.24 E-value: 7.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 1907162011 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
864-1010 |
2.22e-58 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 197.04 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 864 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 943
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 944 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 1010
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
6.92e-56 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 188.92 E-value: 6.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 40 QTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 119
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 1907162011 120 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
40-153 |
2.78e-41 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 147.14 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 40 QTVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR 116
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907162011 117 -YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
38-160 |
4.84e-37 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 135.45 E-value: 4.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 38 RTQTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSL 115
Cdd:smart00273 1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907162011 116 RYKNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 160
Cdd:smart00273 81 RNRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
482-580 |
2.43e-33 |
|
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: 123.97 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 482 HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQ 561
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 1907162011 562 SEAKWLTQIAELEKEQGSL 580
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
42-153 |
4.66e-25 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 100.84 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 42 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 121
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 1907162011 122 SDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 153
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-644 |
2.89e-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: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAqRSLTEIERKAQAN---------EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQ 503
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 504 VDLEREKKELADSFARVSDQAQRKTQEQQDVLE---NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSL 580
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162011 581 ATVAAQREEELSALRDQLESTQIKLAGA--QESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
382-644 |
5.24e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 382 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAmddcEFLRTEL----DELKRQREDTEKAQRSLTEI 457
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELeeleLELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 458 ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQ---AQRKTQEQQDV 534
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlleAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 535 LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAtvaAQREEELsALRDQLESTQIKLAGAQESMCQ 614
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---EALAELE-EEEEEEEEALEEAAEEEAELEE 456
|
250 260 270
....*....|....*....|....*....|
gi 1907162011 615 QVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-644 |
1.64e-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: 68.54 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 397 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK-AQRSLTEIERKAQANEQRYSKLKEKY 475
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 476 SELVQNHADL--LRKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQR---KTQEQQDVLENLKHELATSRQEL 549
Cdd:TIGR02168 761 AEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 550 QVLHSNLETSAQseakwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRK 629
Cdd:TIGR02168 841 EDLEEQIEELSE-------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE--LESKRS 911
|
250
....*....|....*
gi 1907162011 630 AAEREIQEALSQLEE 644
Cdd:TIGR02168 912 ELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-644 |
1.70e-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: 68.54 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 454
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 455 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV 534
Cdd:TIGR02168 256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 535 ---LENLKHELATSRQELQVLHSNLE------TSAQSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 604
Cdd:TIGR02168 329 eskLDELAEELAELEEKLEELKEELEsleaelEELEAELEELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907162011 605 LAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:TIGR02168 409 LERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
371-645 |
1.92e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 371 DEKDHLIERLYREISGLTgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK- 449
Cdd:COG1196 281 LELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAe 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 450 ---AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQR 526
Cdd:COG1196 360 laeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 527 KTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLa 606
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG- 518
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907162011 607 gaqesmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEEP 645
Cdd:COG1196 519 -------LRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
422-644 |
2.43e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 422 LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSVARQ 501
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 502 AQVDLEREKKELADSFARVsDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE----LEKEQ 577
Cdd:COG4913 683 SSDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaAALGD 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 578 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrkAAEREIQEALSQLEE 644
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL--ESLPEYLALLDRLEE 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-644 |
3.67e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRsLTEIERKAQANEQRYSKLKEK 474
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 475 YSELVQ----NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVL----ENLKHELATSR 546
Cdd:PTZ00121 1536 ADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 547 QELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAG 626
Cdd:PTZ00121 1616 EEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250
....*....|....*...
gi 1907162011 627 IRKAAEREIQEALSQLEE 644
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEA 1712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-642 |
4.27e-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: 59.78 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 397 ESQRAMLQLKGRVSELEAELAEQQhlgrqamddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYS 476
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALK----------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 477 ELvqnHADLLRKNAEVTKQVsvaRQAQVDLEREKKELADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNL 556
Cdd:COG4942 94 EL---RAELEAQKEELAELL---RALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 557 ETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQ 636
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1907162011 637 EALSQL 642
Cdd:COG4942 246 AGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
443-644 |
8.20e-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: 59.01 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 443 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsd 522
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 523 qaQRKTQEQQDVLENLKHELATSRQELQ----------VLHSNLETSAQSEAKWLTQIAELEKEQG-----SLATVAAQR 587
Cdd:COG4942 89 --EKEIAELRAELEAQKEELAELLRALYrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAeelraDLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 588 EEeLSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKaAEREIQEALSQLEE 644
Cdd:COG4942 167 AE-LEAERAELEALLAELEEERAAL-EALKAERQKLLARLEK-ELAELAAELAELQQ 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-642 |
1.04e-08 |
|
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: 59.70 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 370 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 446
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 447 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvaRQAQVDLE 507
Cdd:TIGR02169 284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---DKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 508 REKKELADSFARV------SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLA 581
Cdd:TIGR02169 361 ELKEELEDLRAELeevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 582 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 642
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
42-151 |
1.14e-08 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 54.20 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 42 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 118
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907162011 119 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 151
Cdd:cd03564 83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-644 |
1.76e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF--LRTELDELKRQREDTEKAQRSL 454
Cdd:COG4913 612 LAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 455 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLE-REKKELADSFARVSDQAQRKTQEQQd 533
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGDAVERE- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 534 VLENLKHELATSRQELQVLHSNLEtSAQSEAK--WLTQIAELEkeqgslATVAAqrEEELSALRDQLEstQIKLAGAQES 611
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELE-RAMRAFNreWPAETADLD------ADLES--LPEYLALLDRLE--EDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 1907162011 612 MCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG4913 836 FKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-644 |
1.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 378 ERLYReISGLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLGRQamddCEFLRTELDELKRQREDTEKAQRSLTE 456
Cdd:COG4717 56 DELFK-PQGRKPELNLKELKELEEELKeAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 457 IERKAQANEQ------RYSKLKEKYSELVQNHADLLRKNAEVtkqvsvaRQAQVDLEREKKELADSFARVSDQAQRKTQE 530
Cdd:COG4717 131 YQELEALEAElaelpeRLEELEERLEELRELEEELEELEAEL-------AELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 531 QQDVLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQReeELSALRDQLESTQIKLAGAQ- 609
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGVLf 280
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162011 610 ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG4717 281 lvlGLLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
400-631 |
2.38e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.52 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 400 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 475
Cdd:pfam07888 28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 476 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSN 555
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 556 LETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRK 629
Cdd:pfam07888 176 LQAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERK 252
|
..
gi 1907162011 630 AA 631
Cdd:pfam07888 253 VE 254
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
362-607 |
2.59e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.64 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 362 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 432
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 509
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 510 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 589
Cdd:PHA02562 308 LKELQHSL--------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250
....*....|....*...
gi 1907162011 590 ELSALRDQLESTQIKLAG 607
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
375-606 |
3.08e-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: 54.68 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 375 HLIERLYREISGLTGQldnmkIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELK-----------R 442
Cdd:TIGR02168 747 ERIAQLSKELTELEAE-----IEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaaN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 443 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD 522
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 523 QAQ---RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwltQIAELEK-EQGSLATVAAQREEELSALRDQL 598
Cdd:TIGR02168 902 ELReleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-------RLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
....*...
gi 1907162011 599 ESTQIKLA 606
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-600 |
5.41e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 413 EAELAEQQ--HLG--RQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLL 486
Cdd:COG4913 243 ALEDAREQieLLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 487 RKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQRktqeQQDVLENLKHELATSRQELQVLHSNLETSAQSEAK 565
Cdd:COG4913 323 EELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRAR----LEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1907162011 566 WLTQIAELEKEQGSLATVAAQREEELSALRDQLES 600
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-627 |
5.97e-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: 53.91 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 370 KDEKDHLIERLYREISGLTGQLD---------NMKIES-QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDE 439
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEelrlevselEEEIEElQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 440 LKRQREDTEKA------------------QRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR- 500
Cdd:TIGR02168 328 LESKLDELAEElaeleekleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEa 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 501 ---QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAELEKEq 577
Cdd:TIGR02168 408 rleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE---EALEELREELEEAEQALDAAERE- 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907162011 578 gslatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGI 627
Cdd:TIGR02168 484 ----------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSG--LSGI 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
364-637 |
6.53e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 364 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 440
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 441 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdLEREKkeladsfarv 520
Cdd:pfam17380 351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKI-LEEER---------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 521 sdqaQRKTQEQQDVLENLKHELATSRQ-ELQVLHsnletsaQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 599
Cdd:pfam17380 412 ----QRKIQQQKVEMEQIRAEQEEARQrEVRRLE-------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907162011 600 STQIKLAGAQES----MCQQVKDQRKTLL--AGIRKAAEREIQE 637
Cdd:pfam17380 481 KEKRDRKRAEEQrrkiLEKELEERKQAMIeeERKRKLLEKEMEE 524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-644 |
6.85e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 404 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 483
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 484 DLLRKNAEVTKQVSvarqaqvDLErEKKELADSFARVSdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQ 561
Cdd:PRK03918 270 ELKKEIEELEEKVK-------ELK-ELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 562 SEAKWLT-QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALS 640
Cdd:PRK03918 338 ERLEELKkKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEIS 408
|
....
gi 1907162011 641 QLEE 644
Cdd:PRK03918 409 KITA 412
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
411-572 |
1.12e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 411 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 491 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENLKH------ELATSRQ 547
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsgeefedSQDVTEYMQQLLEREREltverdELAARKQ 655
|
170 180
....*....|....*....|....*
gi 1907162011 548 ELQVLHSNLETSAQSEAKWLTQIAE 572
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
363-646 |
1.29e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 363 NNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKR 442
Cdd:COG5185 140 VEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 443 QREDTEKAQRSLTEIERKAQANEQRYSKLK---EKYSELVQNHADL----LRKNAEVTKQVSVARQAQVDL-EREKKELA 514
Cdd:COG5185 220 TLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQfENTKEKIA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 515 DSFARVSD-------QAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAElEKEQGSLATVAAQR 587
Cdd:COG5185 300 EYTKSIDIkkateslEEQLAAAEAEQELEESKRETETGIQNLT---AEIEQGQESLTENLEAIKE-EIENIVGEVELSKS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 588 EEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEEPT 646
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-644 |
1.33e-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: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 424 RQAMDDCEFLRTELDELKRQREDTEKAQR---SLTEIERKAQaneqRYSKLKEKYSELVQnhadllrknaevtkqvsVAR 500
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAELEY-----------------LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 501 QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLetSAQSEAKWLTQIAELEKEQGSL 580
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 581 ATVAAQREEELSALRDQLESTQIKLAGAQESmCQQVKDQRKTLLAGIRKA---AEREIQEALSQLEE 644
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAE-AAALLEALEEELEALEEAlaeAEAALRDLRRELRE 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-629 |
1.50e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 371 DEKDHLIERLYREISGLTGQLDNMKIEsqraMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKA 450
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 451 QRSLTEI------------ERKAQANEQRYSKLKEKYSelVQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSF 517
Cdd:TIGR02168 847 IEELSEDieslaaeieeleELIEELESELEALLNERAS--LEEALALLRSELEeLSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 518 ARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETsaqSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 597
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED---DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
250 260 270
....*....|....*....|....*....|....
gi 1907162011 598 LE--STQIKlagaqesmcqQVKDQRKTLLAGIRK 629
Cdd:TIGR02168 1002 YDflTAQKE----------DLTEAKETLEEAIEE 1025
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-555 |
1.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 399 QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREdtEKAQRSLTEIERKAQANEQRYSKLKEKYSEL 478
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 479 vQNHADLLRKNAEVTKQVSVARQAQVdlerekKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSN 555
Cdd:COG4913 365 -EALLAALGLPLPASAEEFAALRAEA------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-644 |
2.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 473
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 474 KYSElvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKElADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLH 553
Cdd:PTZ00121 1465 KAEE--AKKADEAKKKAEEAKK---ADEAKKKAEEAKKK-ADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 554 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAA 631
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKAE 1616
|
250
....*....|....
gi 1907162011 632 EREIQ-EALSQLEE 644
Cdd:PTZ00121 1617 EAKIKaEELKKAEE 1630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-644 |
2.43e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 456
Cdd:PRK02224 178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 457 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQRKTQEQQD 533
Cdd:PRK02224 239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 534 VLEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQ 602
Cdd:PRK02224 318 ELEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162011 603 IKLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 644
Cdd:PRK02224 398 ERFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
369-644 |
2.99e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 369 NKDEKDHLIER---LYREISGLTGQLDNMK---IESQRAMLQLKGRVSELEAEL-AEQQHLGR-----QAMDDCEFLRTE 436
Cdd:COG3096 276 HANERRELSERaleLRRELFGARRQLAEEQyrlVEMARELEELSARESDLEQDYqAASDHLNLvqtalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 437 LDEL----KRQREDTEKAQRSLTEIERKAQANEQRYSKLK---------------------------EKYSELVQNhADL 485
Cdd:COG3096 356 LEELterlEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqqaldvqqtraiqyqqavqalEKARALCGL-PDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 486 LRKNAEVTKQVSVARQAQVD---LEREKK-ELADSFARVSDQA-------------QRKTQEQQDVLE---NLKHeLATS 545
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATeevLELEQKlSVADAARRQFEKAyelvckiageverSQAWQTARELLRryrSQQA-LAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 546 RQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQE--SMCQQVKDQRKTL 623
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrSELRQQLEQLRAR 593
|
330 340
....*....|....*....|...
gi 1907162011 624 LAGIRKAAE--REIQEALSQLEE 644
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 ... |
395-644 |
3.45e-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: 51.33 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 474
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 475 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVlENLKHELATSR 546
Cdd:pfam01576 336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS-EHKRKKLEGQL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 547 QELQVLHSNLETSAQSEAKWLTQI-AELEKEQGSLATVAAQR---EEELSALRDQL--------ESTQIKLAGAqeSMCQ 614
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLqSELESVSSLLNEAEGKNiklSKDVSSLESQLqdtqellqEETRQKLNLS--TRLR 492
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162011 615 QVKDQRKTLLAGI------RKAAEREIQEALSQLEE 644
Cdd:pfam01576 493 QLEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSD 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-644 |
3.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 371 DEKDHLIERLYREISGLTGQLDNmkIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 426
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGN--AEDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 427 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 497
Cdd:PRK02224 465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 498 VARQAQVDLEREKKELADSFARVSDQAQrKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAkwltQIAELEKEQ 577
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAELKERIESLERIRTLLAAIADAED----EIERLREKR 615
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 578 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 644
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
431-641 |
4.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 431 EFLRTELDELKRQREDTE------KAQRSLTEIERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSV 498
Cdd:COG3206 178 EFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEAraelaeAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 499 ARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLEnLKHELATSRQELQVLHSNLETSAQSEAKwltqiaelekeqg 578
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILASLEAELE------------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162011 579 slatVAAQREEELSALRDQLESTQIKLAGAQ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 641
Cdd:COG3206 324 ----ALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
376-581 |
5.74e-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: 49.76 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 376 LIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQamddceflrTELDELKRQrEDTEKAQRSLT 455
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ---------PPLALLLSP-EDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 456 EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQdvl 535
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--- 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162011 536 enlkhELATSRQELQVLHSNLETSAQSEAKwLTQIAELEKEQGSLA 581
Cdd:COG4942 217 -----ELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLP 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-644 |
6.21e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTE----LDELKRQREDTEKAQRSLTEIERKA-----QANE 465
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEaeaaADEAEAAEEKAEAAEKKKEEAKKKAdaakkKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 466 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSfARVSDQAQRKTQEQQDVlENLKHELA 543
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEE-AKKADEAKKKAEEAKKA-EEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 544 TSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTL 623
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260
....*....|....*....|.
gi 1907162011 624 LAGIRKAAEREIQEALSQLEE 644
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEE 1568
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
381-599 |
8.85e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 381 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 457
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 458 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSFARVSD 522
Cdd:pfam00038 132 -------ELAF--LKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaAKNREEAEEWYQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 523 QAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 597
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQETRQE 278
|
..
gi 1907162011 598 LE 599
Cdd:pfam00038 279 MA 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
363-644 |
9.18e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 363 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 432
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 508
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 509 EKKELADSFarvsDQAQRKTQEQQDVL--ENLKHELATSRQELQVLHSNLE--TSAQSEAKWL-----TQIAELEKEQGS 579
Cdd:TIGR04523 532 EKKEKESKI----SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKslKKKQEEKQELidqkeKEKKDLIKEIEE 607
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 580 LATVAAQREEELSALRDQ---LESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 644
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEiiKKIKESKTKIDD 677
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-643 |
1.48e-05 |
|
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: 49.35 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 373 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 439
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 440 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 497
Cdd:pfam15921 563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 498 VARQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAEL 573
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 574 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAA 631
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQ 798
|
330
....*....|..
gi 1907162011 632 EREIQEALSQLE 643
Cdd:pfam15921 799 ERRLKEKVANME 810
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
411-572 |
1.89e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 411 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 490
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 491 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENL------KHELATSRQ 547
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAarapawlaaqDALERLREQsgealadSQEVTAAMQQLLEREreatveRDELAARKQ 654
|
170 180
....*....|....*....|....*
gi 1907162011 548 ELQVLHSNLETSAQSEAKWLTQIAE 572
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAE 679
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
448-636 |
1.92e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 448 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR----QAQVDLEREKKELADSFARVsDQ 523
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReeleQLEEELEQARSELEQLEEEL-EE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 524 AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 603
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1907162011 604 KLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQ 636
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-644 |
2.17e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 392 DNMKIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRtELDELKRQREDTEKAQRSLTEIER-------KAQAN 464
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEakkadeaKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 465 EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQ-----------RKTQEQQD 533
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKkaeekkkadelKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 534 VLENLKHELATSRQELQVLHS-NLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESM 612
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162011 613 CQQVKDQRKTllAGIRKAAE----REIQEALSQLEE 644
Cdd:PTZ00121 1640 KKEAEEKKKA--EELKKAEEenkiKAAEEAKKAEED 1673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-644 |
2.20e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 432 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 500
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 501 QAQVDLEREKKELADSFARVSDQaQRKTQEQQDVLENLKHELATSR-QELQVLHSNLETSAQseaKWLTQIAELEKEQGS 579
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEEL-EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVS---RIEARLREIEQKLNR 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162011 580 LATVAAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 644
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 ... |
399-644 |
2.24e-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: 48.81 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 399 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 478
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 479 VQNHADLLRKNAEVTKQVSVARQAQvdleREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSNLET 558
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHAL----LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSI 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 559 SAQSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREI 635
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
....*....
gi 1907162011 636 QEALSQLEE 644
Cdd:TIGR00618 746 KELMHQART 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-644 |
2.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAMLQLKGRvselEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSlteieRKAQANEQRYSKLKEK 474
Cdd:PTZ00121 1571 KAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 475 YSELVQNhADLLRKnAEVTKQVSVARQAQVDLEREKKeladsfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHS 554
Cdd:PTZ00121 1642 EAEEKKK-AEELKK-AEEENKIKAAEEAKKAEEDKKK---------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 555 NLETSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAERE 634
Cdd:PTZ00121 1711 EAEEKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
250
....*....|
gi 1907162011 635 IQEALSQLEE 644
Cdd:PTZ00121 1781 IEEELDEEDE 1790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
431-644 |
5.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 431 EFLRTEL-DELKRQREDTEKAQrslteiERKAQANEQRYSKLKEKYSELVQNHADLlrknAEVTKQVSVARQAQVDLERE 509
Cdd:COG4717 41 AFIRAMLlERLEKEADELFKPQ------GRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 510 KKELADSFARVSDQAQRKTQEQQdvLENLKHELATSRQELQVLHSNLETSAQseakWLTQIAELEKEQGSLATVAAQREE 589
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162011 590 ELS-ALRDQLESTQIKLAGAQesmcqqvkdQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG4717 185 QLSlATEEELQDLAEELEELQ---------QRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
408-570 |
5.44e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 408 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 487
Cdd:PRK12705 37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 488 KNAEvtkqvsvarqaqvdLEREKKELADSFARVSDQAQRktQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWL 567
Cdd:PRK12705 117 RELE--------------LEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERK 177
|
...
gi 1907162011 568 TQI 570
Cdd:PRK12705 178 AQN 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-644 |
1.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 439 ELKRQREDTEKaqrsltEIERkAQANEQRyskLKEKYSELvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKELADSFA 518
Cdd:COG1196 169 KYKERKEEAER------KLEA-TEENLER---LEDILGEL-ERQLEPLERQAEKAER---YRELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 519 RVSDQAQRKTQEQQDVLEN-----------LKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 587
Cdd:COG1196 235 RELEAELEELEAELEELEAeleeleaelaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162011 588 EEELSALRDQLESTQIKLAGAQESmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
371-639 |
1.51e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 371 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 415
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 416 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 479
Cdd:pfam10174 442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 480 QNHADLLRKNAEVTKQVSVARQAQ--VDLEREKKELADSFARVSDQAQRKTQE----QQDV---------LENLKH---- 540
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerllgilreVENEKNdkdk 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 541 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 607
Cdd:pfam10174 601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907162011 608 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 639
Cdd:pfam10174 681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
376-644 |
1.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 376 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 454
Cdd:PRK03918 315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 455 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFARVSDQAQR 526
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 527 KTQEQQDVLENLKHELATSRQELqvlhsNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLA 606
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLK 538
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162011 607 GAQESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:PRK03918 539 GEIKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
387-599 |
1.57e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 387 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 458
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 459 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFARVS---------DQAQRKT 528
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQET 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 529 QEQQDvlENLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 599
Cdd:pfam12128 805 WLQRR--PRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
380-617 |
1.76e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 380 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 453
Cdd:PRK04863 849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 454 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 502
Cdd:PRK04863 918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 503 QVDLEREKKELADSFARVSDQAQRKTQEQQ--DVLENLKHELATSRQELQV-LHSNLETSAQSEAKWL--------TQIA 571
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSsyDAKRQMLQELKQELQDLGVpADSGAEERARARRDELharlsanrSRRN 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907162011 572 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 617
Cdd:PRK04863 1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-627 |
1.81e-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: 44.15 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 462 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV-----LE 536
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 537 NLKHELATSRQELQVLhsnletsAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQEsmcqQV 616
Cdd:COG1579 93 ALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE----EL 161
|
170
....*....|.
gi 1907162011 617 KDQRKTLLAGI 627
Cdd:COG1579 162 EAEREELAAKI 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
404-643 |
1.99e-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: 45.55 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 404 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQAN---------------EQRY 468
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkdlqreleearasrDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 469 SKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdlerEKKELADsfaRVSDQAQRKTQeQQDVLENLKHELATSRQE 548
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQ----ERDELAD---EIASGASGKSA-LQDEKRRLEARIAQLEEE 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 549 LQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREeelsALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgir 628
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFKSSIA--- 970
|
250
....*....|....*
gi 1907162011 629 kAAEREIQEALSQLE 643
Cdd:pfam01576 971 -ALEAKIAQLEEQLE 984
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
446-604 |
2.06e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.65 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 446 DTEKAQRSLTEIERKAQANEQRYSKLKEkyseLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArvsdqaq 525
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEA----ELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAV------- 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 526 rkTQEQqdvLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEqgslatvAAQREEELSALRDQLESTQIK 604
Cdd:COG1566 146 --SQQE---LDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQ-------VAQAEAALAQAELNLARTTIR 211
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
387-589 |
2.24e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 387 LTGQLDNMKIESQRAMLQLKG-RVSELEAELAEQQHLGRQAMDDcefLRTELDELKRQREDTE------KAQRSLTEIER 459
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSE---LESQLAEARAELAEAEarlaalRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 460 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarqaqVDLEREKKELAdsfARVSDQAQRKTQEQQDVLENLK 539
Cdd:COG3206 257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALR---AQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907162011 540 HELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 589
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
377-478 |
2.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDNmkiESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 456
Cdd:COG3206 293 VIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREAS--------------LQAQLAQLEARLAELPELEAELRR 355
|
90 100
....*....|....*....|..
gi 1907162011 457 IERKAQANEQRYSKLKEKYSEL 478
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-558 |
2.53e-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: 45.06 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 368 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 442
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 443 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtKQVSVARQAQVDLEREKKELADSFA 518
Cdd:TIGR02169 890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIR 968
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162011 519 RVSDQAQRKTQEQQDVLENL-----KHE-LATSRQELQVLHSNLET 558
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLdelkeKRAkLEEERKAILERIEEYEK 1014
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
400-605 |
2.79e-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: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 400 RAMLQLKGRVSEleAELAEQQHlgRQAMddcEFLRTELDELkrQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELV 479
Cdd:COG3096 455 EEVLELEQKLSV--ADAARRQF--EKAY---ELVCKIAGEV--ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 480 Q---NHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdQAQRKTQEQQdvLENLKHELATSRQELQVLHSNL 556
Cdd:COG3096 526 QrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL---------EAQLEELEEQ--AAEAVEQRSELRQQLEQLRARI 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162011 557 ETSAQSEAKWLTQIAELEK--EQG--SLATVAA---------QREEELSALRDQLESTQIKL 605
Cdd:COG3096 595 KELAARAPAWLAAQDALERlrEQSgeALADSQEvtaamqqllEREREATVERDELAARKQAL 656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
394-610 |
3.58e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 394 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 470
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 471 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKELADsfARVSDQ-----AQRKTQEQQDVLENLKHE 541
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEE--AKKDEEekkkiAHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 542 LATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAT--VAAQREEELSALRDQLESTQIKLAGAQE 610
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
377-600 |
5.49e-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: 44.17 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDNMKIES--QRAMLQLKGRVSELEAELA-----EQQHlgRQAMD-------------------DC 430
Cdd:COG3096 811 LQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAqhraqEQQL--RQQLDqlkeqlqllnkllpqanllAD 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 431 EFLRTELDELKRQREDTEKAQRS-------LTEIERKA---QANEQRYSKLKEKY-----------------SELVQN-- 481
Cdd:COG3096 889 ETLADRLEELREELDAAQEAQAFiqqhgkaLAQLEPLVavlQSDPEQFEQLQADYlqakeqqrrlkqqifalSEVVQRrp 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 482 H------ADLLRKNAEVTKQV-SVARQAQVDLEREKKELADSFARVSDQAQRKT------QEQQDVLENLKHEL------ 542
Cdd:COG3096 969 HfsyedaVGLLGENSDLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLAslkssrDAKQQTLQELEQELeelgvq 1048
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162011 543 ------ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 600
Cdd:COG3096 1049 adaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
405-576 |
5.56e-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: 43.96 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 405 LKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL-DELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 483
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALkRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 484 DLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKhELATSRQELQVLHSNLETSAQSE 563
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLEKQQSSL 165
|
170
....*....|...
gi 1907162011 564 AKWLTQIAELEKE 576
Cdd:pfam05557 166 AEAEQRIKELEFE 178
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-584 |
5.65e-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: 43.90 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 377 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 451
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 452 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdqaqRKTQE 530
Cdd:TIGR02169 409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------------YDLKE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162011 531 QQDVLENlkhELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 584
Cdd:TIGR02169 477 EYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
433-558 |
6.03e-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: 40.70 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREkke 512
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE--- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907162011 513 lADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQ----VLHSNLET 558
Cdd:pfam07926 80 -AESAKAELEESEESWEEQKKELEKELSELEKRIEDLNeqnkLLHDQLES 128
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-605 |
6.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 396 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIER---KAQANEQRYSKL 471
Cdd:PRK02224 532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllaAIADAEDEIERL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 472 KEKYSELvqnhadllrknAEVTKQvsvaRQAQVDLERE-KKELADSF--ARVsDQAQRKTQEQQDVLENLKHELATSRQE 548
Cdd:PRK02224 612 REKREAL-----------AELNDE----RRERLAEKRErKRELEAEFdeARI-EEAREDKERAEEYLEQVEEKLDELREE 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 549 lqvlhsnlETSAQSEAKWLT-QIAELEKEQGSLATVAAqREEELSALRD---QLESTQIKL 605
Cdd:PRK02224 676 --------RDDLQAEIGAVEnELEELEELRERREALEN-RVEALEALYDeaeELESMYGDL 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
425-611 |
6.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 425 QAMDDCEFLRTELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQVSVAR 500
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 501 QAQVDLEREKKEL--------ADSFA----------RVSDQ----------AQRKTQEQQDVLENLKHELATSRQELQVL 552
Cdd:COG3883 90 ERARALYRSGGSVsyldvllgSESFSdfldrlsalsKIADAdadlleelkaDKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 553 HSNLEtSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQES 611
Cdd:COG3883 170 KAELE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
448-644 |
9.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 448 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQR- 526
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERARAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 527 -KTQEQQDVLENLKheLATSRQEL--QVlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 603
Cdd:COG3883 96 yRSGGSVSYLDVLL--GSESFSDFldRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162011 604 KLAGAQESmcqqvKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:COG3883 172 ELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
439-644 |
1.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 439 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFA 518
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 519 RVSDQAQRKTQEQQDVLENLKHELATSRQElqvlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQL 598
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162011 599 ESTQIKLAgaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:PTZ00121 1439 KAEEAKKA---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-602 |
1.28e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 369 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 434
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 435 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSKlkEKYSELVQNHADLLRKN-AEVTKqvsvaRQAQVDLEREK-K 511
Cdd:pfam15921 331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTER--DQFSQESGNLDDQLQKLlADLHK-----REKELSLEKEQnK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 512 ELADSFARVS---DQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE 588
Cdd:pfam15921 402 RLWDRDTGNSitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV 481
|
250
....*....|....
gi 1907162011 589 EELSALRDQLESTQ 602
Cdd:pfam15921 482 EELTAKKMTLESSE 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
439-644 |
1.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 439 ELKRQREDTEKAQRSLTEIERKA----QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAqvdlEREKKELA 514
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 515 DSFARVSDQAQRKTQEQQDVLENL--KHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELS 592
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907162011 593 ALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
425-644 |
2.33e-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: 42.03 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 425 QAMDDCEFLRTELDELKRQREDTEKAQRslteiERKAQANEQRYSKLKEKYSELVQNHADLlrKNAEVTKQVSVARQAQV 504
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKL--EEAEKARQAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 505 DLEREKKELadsfarvsdqaQRKTQEQQDVLENLKHELATSRQElqvlhsnletsaqSEAKWLTQIAELEKEQgslatva 584
Cdd:pfam17380 336 YAEQERMAM-----------ERERELERIRQEERKRELERIRQE-------------EIAMEISRMRELERLQ------- 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 585 AQREEELSALRDQLEST-QIKLagaQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 644
Cdd:pfam17380 385 MERQQKNERVRQELEAArKVKI---LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
408-641 |
2.41e-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: 41.88 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 408 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 487
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 488 KNAEVTKQVSVARQ---AQVDLEREKKELADSFARV-SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSE 563
Cdd:pfam02463 251 EEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162011 564 AKWLTQIAELEKEqgsLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 641
Cdd:pfam02463 331 KKEKEEIEELEKE---LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
353-600 |
2.60e-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: 41.93 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 353 SSLSSDPFNFNNQNGVNKDEKDhlieRLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF 432
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKN----KLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLK---EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE 509
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKN---IDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 510 KKE-------LADSFARVSDQAQRKTQE-----------------------------QQDVLENLKHELATSRQELQVLH 553
Cdd:TIGR04523 248 ISNtqtqlnqLKDEQNKIKKQLSEKQKEleqnnkkikelekqlnqlkseisdlnnqkEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907162011 554 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 600
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
424-603 |
2.95e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 424 RQAMDDCEFLRTELDELKRQREDTE----KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVA 499
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEeeleQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 500 RQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAELEKEQGS 579
Cdd:COG4372 121 QKERQDLEQQRKQLEAQ----IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE--QALDELLKEANR 194
|
170 180
....*....|....*....|....
gi 1907162011 580 LATVAAQREEELSALRDQLESTQI 603
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAE 218
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
442-637 |
3.04e-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: 41.48 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 442 RQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDlEREKKELADSFARVS 521
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-ERQRQEEEERKQRLQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 522 DQ-AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAElekEQGSLATVAaqREEELSALRDQLES 600
Cdd:pfam15709 414 LQaAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE--MQLAE---EQKRLMEMA--EEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907162011 601 TQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQE 637
Cdd:pfam15709 487 EEKARLEAEERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
378-642 |
3.12e-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: 41.75 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 378 ERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLG-RQAMDDCEFLRTELDELKRQ-------REDTEK 449
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGELKLRlnqatatPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 450 AQRSLTEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSVARQAQVD--------------------LERE 509
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 510 KKELADSFARVSDQAQ--RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 587
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 588 EEELSALRDQLESTQIKLAGAQESM------CQQVKDQRKTLLAGIRKAAEREIQEALSQL 642
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALknarldLRRLFDEKQSEKDKKNKALAERKDSANERL 684
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-644 |
3.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 436 ELDELKRQREDTEKA---QRSLTEIERKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 512
Cdd:PTZ00121 1303 KADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 513 LADSFA---RVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 589
Cdd:PTZ00121 1382 AAKKKAeekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 590 ELSALRDQLESTQIKLAGAQESMCQQVK---DQRKTLLAGIRKAAE-REIQEALSQLEE 644
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEaKKKADEAKKAEE 1520
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-637 |
3.38e-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: 41.57 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 382 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQqhLGRQAMDDCEFLRTElDELKRQREDTEKAQRSLTEIERKA 461
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKE-KEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 462 QANEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------VARQAQVDLER----------EKKELADSFARVSDQ 523
Cdd:TIGR00606 768 EEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqekqEKQHELDTVVSKIEL 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 524 AQRKTQEQQDVLENLKHELatsrQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQ- 602
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQq 923
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907162011 603 -----IKLAGAQESMCQ-QVKDQRKTL--LAGIRKAAEREIQE 637
Cdd:TIGR00606 924 ekeelISSKETSNKKAQdKVNDIKEKVknIHGYMKDIENKIQD 966
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
445-618 |
3.46e-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: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 445 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHAD------LLRKNAEVTKQVSVARQAQV---------DLERE 509
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEfektiaQMIEEKQKQKELEHAEIQKVleekdqalaDLNSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 510 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQRE 588
Cdd:pfam05010 88 EKSFSDLF--------KRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAK 159
|
170 180 190
....*....|....*....|....*....|
gi 1907162011 589 EELSALRDQLESTQIKLAGAQESMCQQVKD 618
Cdd:pfam05010 160 AETAALQASLRKEQMKVQSLERQLEQKTKE 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-643 |
3.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 371 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 426
Cdd:PRK03918 448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 427 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsvarqaqvDL 506
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 507 EREKKELA---DSFARVSDqAQRKTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatv 583
Cdd:PRK03918 591 EERLKELEpfyNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS----- 657
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162011 584 aaqrEEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 643
Cdd:PRK03918 658 ----EEEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
435-595 |
3.56e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 435 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQaq 503
Cdd:PRK09039 53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 504 vdlerekkeladsfarVSDQAQRKtqeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATV 583
Cdd:PRK09039 131 ----------------VSARALAQ-------VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNV 183
|
170
....*....|...
gi 1907162011 584 A-AQREEELSALR 595
Cdd:PRK09039 184 AlAQRVQELNRYR 196
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
404-604 |
3.79e-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: 40.48 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 404 QLKGRVSELEAELAEQQHLgrqamddceflrteldelkrqredtekaqrslteiERKAQANEQRYSKLKEKYSELVQNHA 483
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQ-----------------------------------VARLQAELDRLQALESELAISRQDYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 484 DLLRKNAEVTKQVSVArQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQse 563
Cdd:pfam00529 100 GATAQLRAAQAAVKAA-QAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162011 564 akwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 604
Cdd:pfam00529 177 ----ENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
468-602 |
3.87e-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: 40.77 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 468 YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADsfarvsdQAQRKTQEQQDVLENLKHELATSRQ 547
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD-------RAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162011 548 ELQVLHSNLETSAQSEAKWLTQIAELEKeqgSLATVAAQREEELSALRDQLESTQ 602
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
387-578 |
3.98e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 387 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 459
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 460 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--ARVSDQAQRKTQEQQD 533
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLkeANVSKFSSYKVELLQQ 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907162011 534 VLENLKHELATSRQElqvLHSNLETSAQSEAKWLTQIAELEKEQG 578
Cdd:PLN02939 359 KLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
512-644 |
4.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 512 ELADSFarVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLE--------TSAQSEAKWLT-QIAELEKEQGSLAT 582
Cdd:COG3206 156 ALAEAY--LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqQLSELESQLAEARA 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162011 583 VAAQREEELSALRDQLESTQIKLAGAQES-MCQQVKDQRKTLLAGIRKAAER------EIQEALSQLEE 644
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpVIQQLRAQLAELEAELAELSARytpnhpDVIALRAQIAA 302
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
402-632 |
4.82e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 402 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 481
Cdd:PRK10929 111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 482 hADLLRKNAEvtkqvSVARQAQVDlerekkELadsfarvsDQAQRKTQEQQDvLENLKHELATSRQE-----LQVLHSNL 556
Cdd:PRK10929 173 -AQLTALQAE-----SAALKALVD------EL--------ELAQLSANNRQE-LARLRSELAKKRSQqldayLQALRNQL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 557 ETSAQSEA-KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 632
Cdd:PRK10929 232 NSQRQREAeRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
433-619 |
5.13e-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: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 433 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSelvqnhadllrknaevtkqvsvarqaqvDLEREKK 511
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYN----------------------------DLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 512 ELADSFARVSDQAQRKtqeqQDVLENLKHELAtsrqELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 591
Cdd:TIGR04523 170 ELENELNLLEKEKLNI----QKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
170 180
....*....|....*....|....*...
gi 1907162011 592 SALRDQLESTQIKLAGAQESMcQQVKDQ 619
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQ-NKIKKQ 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
395-598 |
5.61e-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: 39.52 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 395 KIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEK 474
Cdd:COG1579 14 ELDSELD--RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----------IKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 475 YSElVQNHADLlrknAEVTKQVSVARQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQvlhs 554
Cdd:COG1579 82 LGN-VRNNKEY----EALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELD---- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907162011 555 nletsaqseakwlTQIAELEKEqgsLATVAAQREEELSALRDQL 598
Cdd:COG1579 149 -------------EELAELEAE---LEELEAEREELAAKIPPEL 176
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
505-610 |
5.85e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 505 DLEREKKELADSFArvsdQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 584
Cdd:PRK09039 57 RLNSQIAELADLLS----LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100
....*....|....*....|....*.
gi 1907162011 585 AQREEELSALRDQLESTQIKLAGAQE 610
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEA 158
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
436-615 |
7.01e-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: 39.83 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 436 ELDELKRQREDTEKAQR-SLTEIERKA-------QANEQRYSKLKEKY-SELVQNHADLLRKNAEVTKQVSVARQAQVDL 506
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQeRQKKLEQQAeeaekqrAAEQARQKELEQRAaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 507 EREKKELADSFARVSDQAQRKTQEQQDVLENlkhELATSRQELQVLHSNLETSAQSEA-----------KWLTQIAELEK 575
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAA---AEAKKKAEEAKKKAEAEAKAKAEAeakakaeeakaKAEAAKAKAAA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907162011 576 EQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQ 615
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
417-644 |
7.80e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 417 AEQQHLGRQAMDDCEFLRTELDELKR--QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK 494
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAERIRtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESA 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 495 QvSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwlTQIAELE 574
Cdd:NF041483 680 D-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASAR------KRVEEAQ 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162011 575 KEQGSLATVAAQREEEL-SALRDQLESTQIKLAGAQESMCQQVkdqrktllAGIRKAAEREIQEALSQLEE 644
Cdd:NF041483 753 AEAQRLVEEADRRATELvSAAEQTAQQVRDSVAGLQEQAEEEI--------AGLRSAAEHAAERTRTEAQE 815
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
369-622 |
8.78e-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: 39.65 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 369 NKDEKDHLIERLYREISGLTGQLDNMK--IESQRAMLQ-LKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELK 441
Cdd:smart00806 72 NVEELDEVKKHIDDEIDTLQNELDEVKqaLESQREAIQrLKERQQNSAANIARpaasPSPVLASSSSAISLANNPDKLNK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 442 RQREDTEKAQRSLTEIeRKAQANEQrySKLKEKYSELVQNHADLLRKNAEVTKQVSVAR--QAQVDLEREKKELADSFAR 519
Cdd:smart00806 152 EQRAELKSLQRELAVL-RQTHNSFF--TEIKESIKDILEKIDKFKSSSLSASGSSNRAYveSSKKKLSEDSDSLLTKVDD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 520 VSDQ--------AQRKTQEQQDVLENLKHELATSRQELQvlhsNLETSAQSEAKWLTQI--AELEK---EQGSLATvaaq 586
Cdd:smart00806 229 LQDIiealrkdvAQRGVRPSKKQLETVQKELETARKELK----KMEEYIDIEKPIWKKIweAELDKvceEQQFLTL---- 300
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162011 587 REEELSALRDQLESTQIKLAGAQESMCQQVKDQRKT 622
Cdd:smart00806 301 QEDLIADLKEDLEKAEETFDLVEQCCEEQEKGPSKN 336
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
461-558 |
9.65e-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: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162011 461 AQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLErekKELADSFARVSDQAQRKTQEQQDVLENLKH 540
Cdd:TIGR04320 256 LAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQ---KELANAQAQALQTAQNNLATAQAALANAEA 332
|
90
....*....|....*...
gi 1907162011 541 ELATSRQELQVLHSNLET 558
Cdd:TIGR04320 333 RLAKAKEALANLNADLAK 350
|
|
| |
