|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
7-272 |
2.62e-92 |
|
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: 294.59 E-value: 2.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 7 TVSVNKAINTQEVAVKEKHARTCILGTHH-EKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:pfam07651 3 EVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 86 ELSDMSRMWGH-LSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFfqLTVEMFDYLECELNL 164
Cdd:pfam07651 83 RISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 165 FQTVFNSLDMSRSVSVTTaGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFMEQFTKLKDL 238
Cdd:pfam07651 161 QKLLFRLLKCRPTGNALS-NECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKEF 239
|
250 260 270
....*....|....*....|....*....|....
gi 1907162022 239 FQRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 272
Cdd:pfam07651 240 YEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
780-978 |
1.28e-90 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 287.34 E-value: 1.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 780 GVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLV 859
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 860 VQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQ-IEETDSMDFSSMT 938
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907162022 939 LTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELA 978
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
1.71e-83 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 264.59 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1907162022 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
6-119 |
1.95e-68 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 223.70 E-value: 1.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 1907162022 86 ELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
830-976 |
1.26e-58 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 197.81 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 830 KNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVN 909
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 910 QATAAVVASTISGKSQIEE--TDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYE 976
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
8-119 |
4.03e-55 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 186.61 E-value: 4.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 8 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNEL 87
Cdd:cd17014 3 ISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNI 82
|
90 100 110
....*....|....*....|....*....|..
gi 1907162022 88 SDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17014 83 RETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
6-119 |
1.18e-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: 148.30 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 6 MTVSVNKAINTQEVAVKEKHARTCILGT-HHEKGAQTFWSVVNRLpLSSNAMLCWKFCHVFHKLLRDGHP--NVLKDSLR 82
Cdd:cd16986 1 FEKAVNKATNKTDSPPKPKHVRTIIVKSwTHQKGPQFYEELSKRL-LLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLD 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907162022 83 -YKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd16986 80 aWLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
6-126 |
3.34e-36 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 133.14 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAM--LCWKFCHVFHKLLRDGHPNVLKDSLRY 83
Cdd:smart00273 3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRN 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907162022 84 KNELSDMSRMWGHLSEG--YGQLCSIYLKLLRTRMEYHTKNPRFP 126
Cdd:smart00273 83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
448-546 |
1.80e-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: 124.35 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 448 HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQ 527
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 1907162022 528 SEAKWLTQIAELEKEQGSL 546
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
6-119 |
3.36e-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: 101.23 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 6 MTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 85
Cdd:cd17007 1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1907162022 86 ELSDMSRMW-GHLSEGYGQLCSIYLKLLRTRMEYH 119
Cdd:cd17007 81 WLESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
399-610 |
2.28e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAqRSLTEIERKAQAN---------EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQ 469
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 470 VDLEREKKELADSFARVSDQAQRKTQEQQDVLE---NLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSL 546
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162022 547 ATVAAQREEELSALRDQLESTQIKLAGA--QESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-610 |
4.04e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 348 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAmddcEFLRTEL----DELKRQREDTEKAQRSLTEI 423
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELeeleLELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 424 ERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQ---AQRKTQEQQDV 500
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlleAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 501 LENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAtvaAQREEELsALRDQLESTQIKLAGAQESMCQ 580
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE---EALAELE-EEEEEEEEALEEAAEEEAELEE 456
|
250 260 270
....*....|....*....|....*....|
gi 1907162022 581 QVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
363-610 |
1.45e-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: 68.93 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 363 ESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK-AQRSLTEIERKAQANEQRYSKLKEKY 441
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 442 SELVQNHADL--LRKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQR---KTQEQQDVLENLKHELATSRQEL 515
Cdd:TIGR02168 761 AEIEELEERLeeAEEELAEAEAEIEELEAQIEqLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 516 QVLHSNLETSAQseakwltQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRK 595
Cdd:TIGR02168 841 EDLEEQIEELSE-------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE--LESKRS 911
|
250
....*....|....*
gi 1907162022 596 AAEREIQEALSQLEE 610
Cdd:TIGR02168 912 ELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-610 |
1.52e-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: 68.93 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDNMKIESQRA--MLQLKGRVSELEAELAeqqhlgrqaMDDCEFLRTELDELKRQREdteKAQRSL 420
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAerYKELKAELRELELALL---------VLRLEELREELEELQEELK---EAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 421 TEIERKAQANEqrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV 500
Cdd:TIGR02168 256 EELTAELQELE-------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 501 ---LENLKHELATSRQELQVLHSNLE------TSAQSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 570
Cdd:TIGR02168 329 eskLDELAEELAELEEKLEELKEELEsleaelEELEAELEELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907162022 571 LAGAQESMcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:TIGR02168 409 LERLEDRR-ERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-611 |
1.39e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 337 DEKDHLIERLYREISGLTgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEK- 415
Cdd:COG1196 281 LELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAe 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 416 ---AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQR 492
Cdd:COG1196 360 laeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 493 KTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLa 572
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG- 518
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907162022 573 gaqesmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEEP 611
Cdd:COG1196 519 -------LRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-610 |
2.23e-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: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 388 LGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEkYSELVQNHADLLRKNAEVTKQVSVARQ 467
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 468 AQVDLEREKKELADSFARVsDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE----LEKEQ 543
Cdd:COG4913 683 SSDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaAALGD 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 544 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrkAAEREIQEALSQLEE 610
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL--ESLPEYLALLDRLEE 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-610 |
3.45e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRsLTEIERKAQANEQRYSKLKEK 440
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 441 YSELVQ----NHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVL----ENLKHELATSR 512
Cdd:PTZ00121 1536 ADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 513 QELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAG 592
Cdd:PTZ00121 1616 EEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250
....*....|....*...
gi 1907162022 593 IRKAAEREIQEALSQLEE 610
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEA 1712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-608 |
3.53e-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: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 363 ESQRAMLQLKGRVSELEAELAEQQhlgrqamddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYS 442
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALK----------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 443 ELvqnHADLLRKNAEVTKQVsvaRQAQVDLEREKKELADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNL 522
Cdd:COG4942 94 EL---RAELEAQKEELAELL---RALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 523 ETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQ 602
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1907162022 603 EALSQL 608
Cdd:COG4942 246 AGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-610 |
6.95e-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: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 409 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsd 488
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 489 qaQRKTQEQQDVLENLKHELATSRQELQ----------VLHSNLETSAQSEAKWLTQIAELEKEQG-----SLATVAAQR 553
Cdd:COG4942 89 --EKEIAELRAELEAQKEELAELLRALYrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAeelraDLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 554 EEeLSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKaAEREIQEALSQLEE 610
Cdd:COG4942 167 AE-LEAERAELEALLAELEEERAAL-EALKAERQKLLARLEK-ELAELAAELAELQQ 220
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-608 |
8.29e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 336 KDEKDHLIE--RLYREISGLTGQLDNMKIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQRED 412
Cdd:TIGR02169 204 RREREKAERyqALLKEKREYEGYELLKEKEALERQKeAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 413 T-------------------EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvaRQAQVDLE 473
Cdd:TIGR02169 284 LgeeeqlrvkekigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---DKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 474 REKKELADSFARV------SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLA 547
Cdd:TIGR02169 361 ELKEELEDLRAELeevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 548 TVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGIRKAAEREIQEALSQL 608
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQA 499
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
8-117 |
1.13e-08 |
|
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.
Pssm-ID: 340767 Cd Length: 120 Bit Score: 54.20 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 8 VSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVN---RLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYK 84
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHalaKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907162022 85 NELSDMSRmW--GHLSEGYGQ--LCSIYLKLLRTRME 117
Cdd:cd03564 83 GHIFNLSN-FkdDSSPEAWDLsaFIRRYARYLEERLE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-610 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF--LRTELDELKRQREDTEKAQRSL 420
Cdd:COG4913 612 LAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 421 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLE-REKKELADSFARVSDQAQRKTQEQQd 499
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGDAVERE- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 500 VLENLKHELATSRQELQVLHSNLEtSAQSEAK--WLTQIAELEkeqgslATVAAqrEEELSALRDQLEstQIKLAGAQES 577
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELE-RAMRAFNreWPAETADLD------ADLES--LPEYLALLDRLE--EDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 1907162022 578 MCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG4913 836 FKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-610 |
1.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 344 ERLYReISGLTGQLDNMKIESQRAMLQ-LKGRVSELEAELAEQQHLGRQamddCEFLRTELDELKRQREDTEKAQRSLTE 422
Cdd:COG4717 56 DELFK-PQGRKPELNLKELKELEEELKeAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 423 IERKAQANEQ------RYSKLKEKYSELVQNHADLLRKNAEVtkqvsvaRQAQVDLEREKKELADSFARVSDQAQRKTQE 496
Cdd:COG4717 131 YQELEALEAElaelpeRLEELEERLEELRELEEELEELEAEL-------AELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 497 QQDVLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEQGSLATVAAQReeELSALRDQLESTQIKLAGAQ- 575
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALL--ALLGLGGSLLSLILTIAGVLf 280
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162022 576 ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG4717 281 lvlGLLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
366-597 |
1.82e-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: 54.90 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 366 RAMLqLKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELKRQRedtekaqrslTEIERKAQANEQRYSKLKEKY 441
Cdd:pfam07888 28 RAEL-LQNRLEECLQERAEllqaQEAANRQREKEKERYKRDREQWERQR----------RELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 442 SELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSN 521
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 522 LETSAQSEAKWLTQiaeLEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQ------ESMCQQVKDQRKTLLAGIRK 595
Cdd:pfam07888 176 LQAKLQQTEEELRS---LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHrkeaenEALLEELRSLQERLNASERK 252
|
..
gi 1907162022 596 AA 597
Cdd:pfam07888 253 VE 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-572 |
2.88e-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: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 341 HLIERLYREISGLTGQldnmkIESQRAML-QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELK-----------R 408
Cdd:TIGR02168 747 ERIAQLSKELTELEAE-----IEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaaN 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 409 QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSD 488
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 489 QAQ---RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwltQIAELEK-EQGSLATVAAQREEELSALRDQL 564
Cdd:TIGR02168 902 ELReleSKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-------RLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
....*...
gi 1907162022 565 ESTQIKLA 572
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-573 |
3.16e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 54.25 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 328 FNNQNGVNKDekdhLIERLYREISGLTGQLDNMK---------IESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEF 398
Cdd:PHA02562 165 LSEMDKLNKD----KIRELNQQIQTLDMKIDHIQqqiktynknIEEQRK--KNGENIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYselvqnhadllRKNAEV---TKQVSVARQAQVDLERE 475
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----------EKGGVCptcTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 476 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 555
Cdd:PHA02562 308 LKELQHSL--------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
250
....*....|....*...
gi 1907162022 556 ELSALRDQLESTQIKLAG 573
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSE 397
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
330-603 |
3.85e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 330 NQNGVNKDEKDHLIERLYREisgltgqldNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELD---EL 406
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQE---------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErerEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 407 KRQREDTEKaqRSLTEIERKAQANEQrysklkEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdLEREKkeladsfarv 486
Cdd:pfam17380 351 ERIRQEERK--RELERIRQEEIAMEI------SRMRELERLQMERQQKNERVRQELEAARKVKI-LEEER---------- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 487 sdqaQRKTQEQQDVLENLKHELATSRQ-ELQVLHsnletsaQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLE 565
Cdd:pfam17380 412 ----QRKIQQQKVEMEQIRAEQEEARQrEVRRLE-------EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907162022 566 STQIKLAGAQES----MCQQVKDQRKTLL--AGIRKAAEREIQE 603
Cdd:pfam17380 481 KEKRDRKRAEEQrrkiLEKELEERKQAMIeeERKRKLLEKEMEE 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
379-566 |
4.56e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 379 EAELAEQQ--HLG--RQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLL 452
Cdd:COG4913 243 ALEDAREQieLLEpiRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 453 RKNAEVTKQVSVARQAQVD-LEREKKELADSFARVSDQAQRktqeQQDVLENLKHELATSRQELQVLHSNLETSAQSEAK 531
Cdd:COG4913 323 EELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRAR----LEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190
....*....|....*....|....*....|....*
gi 1907162022 532 WLTQIAELEKEQGSLATVAAQREEELSALRDQLES 566
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-593 |
5.35e-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: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 336 KDEKDHLIERLYREISGLTGQLD---------NMKIES-QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDE 405
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEelrlevselEEEIEElQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 406 LKRQREDTEKA------------------QRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR- 466
Cdd:TIGR02168 328 LESKLDELAEElaeleekleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEa 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 467 ---QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAELEKEq 543
Cdd:TIGR02168 408 rleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE---EALEELREELEEAEQALDAAERE- 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907162022 544 gslatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVKDQRKtlLAGI 593
Cdd:TIGR02168 484 ----------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSG--LSGI 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-610 |
6.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 370 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 449
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 450 DLLRKNAEVTKQVSvarqaqvDLErEKKELADSFARVSdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLE--TSAQ 527
Cdd:PRK03918 270 ELKKEIEELEEKVK-------ELK-ELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 528 SEAKWLT-QIAELEKEQGSLATvAAQREEELSALRDQLESTQIKLAGAQesmcqqvKDQRKTLLAGIRKAAErEIQEALS 606
Cdd:PRK03918 338 ERLEELKkKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLT-------PEKLEKELEELEKAKE-EIEEEIS 408
|
....
gi 1907162022 607 QLEE 610
Cdd:PRK03918 409 KITA 412
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-538 |
9.95e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 377 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:PRK04863 500 ELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 457 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENLKH------ELATSRQ 513
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAarapawlaaqDALARLREQsgeefedSQDVTEYMQQLLEREREltverdELAARKQ 655
|
170 180
....*....|....*....|....*
gi 1907162022 514 ELQVLHSNLETSAQSEAKWLTQIAE 538
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
390-610 |
1.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 390 RQAMDDCEFLRTELDELKRQREDTEKAQR---SLTEIERKAQaneqRYSKLKEKYSELVQnhadllrknaevtkqvsVAR 466
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqieLLEPIRELAE----RYAAARERLAELEY-----------------LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 467 QAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLetSAQSEAKWLTQIAELEKEQGSL 546
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 547 ATVAAQREEELSALRDQLESTQIKLAGAQESmCQQVKDQRKTLLAGIRKA---AEREIQEALSQLEE 610
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAE-AAALLEALEEELEALEEAlaeAEAALRDLRRELRE 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-595 |
1.32e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 337 DEKDHLIERLYREISGLTGQLDNMKIEsqraMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKA 416
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 417 QRSLTEI------------ERKAQANEQRYSKLKEKYSelVQNHADLLRKNAE-VTKQVSVARQAQVDLEREKKELADSF 483
Cdd:TIGR02168 847 IEELSEDieslaaeieeleELIEELESELEALLNERAS--LEEALALLRSELEeLSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 484 ARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETsaqSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQ 563
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED---DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
250 260 270
....*....|....*....|....*....|....
gi 1907162022 564 LE--STQIKlagaqesmcqQVKDQRKTLLAGIRK 595
Cdd:TIGR02168 1002 YDflTAQKE----------DLTEAKETLEEAIEE 1025
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
329-612 |
1.37e-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: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 329 NNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKR 408
Cdd:COG5185 140 VEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 409 QREDTEKAQRSLTEIERKAQANEQRYSKLK---EKYSELVQNHADL----LRKNAEVTKQVSVARQAQVDL-EREKKELA 480
Cdd:COG5185 220 TLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLIKQfENTKEKIA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 481 DSFARVSD-------QAQRKTQEQQDVLENLKHELATSRQELQvlhSNLETSAQSEAKWLTQIAElEKEQGSLATVAAQR 553
Cdd:COG5185 300 EYTKSIDIkkateslEEQLAAAEAEQELEESKRETETGIQNLT---AEIEQGQESLTENLEAIKE-EIENIVGEVELSKS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 554 EEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEEPT 612
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
365-521 |
1.41e-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: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 365 QRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREdtEKAQRSLTEIERKAQANEQRYSKLKEKYSEL 444
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARL 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 445 vQNHADLLRKNAEVTKQVSVARQAQVdlerekKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSN 521
Cdd:COG4913 365 -EALLAALGLPLPASAEEFAALRAEA------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
343-610 |
1.93e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDNmKIESQRAMlQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQRedtEKAQRSLTE 422
Cdd:PRK02224 178 VERVLSDQRGSLDQLKA-QIEEKEEK-DLHERLNGLESELAE--------------LDEEIERYEEQR---EQARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 423 IERKAQANEQR---YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQRKTQEQQD 499
Cdd:PRK02224 239 ADEVLEEHEERreeLETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 500 VLEN----LKHELATSRQELQVLHSNLETSA------QSEAKWL-TQIAELEKEQGSLATVAAQREEELSALRDQLESTQ 568
Cdd:PRK02224 318 ELEDrdeeLRDRLEECRVAAQAHNEEAESLRedaddlEERAEELrEEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162022 569 IKLAGAQE-------------SMCQQVKDQRKTLLAGIRKAAEReIQEALSQLEE 610
Cdd:PRK02224 398 ERFGDAPVdlgnaedfleelrEERDELREREAELEATLRTARER-VEEAEALLEA 451
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-610 |
2.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSK-LKE 439
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 440 KYSElvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKElADSfARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLH 519
Cdd:PTZ00121 1465 KAEE--AKKADEAKKKAEEAKK---ADEAKKKAEEAKKK-ADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 520 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEE--LSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAA 597
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVM-KLYEEEKKMKAEEAKKAE 1616
|
250
....*....|....
gi 1907162022 598 EREIQ-EALSQLEE 610
Cdd:PTZ00121 1617 EAKIKaEELKKAEE 1630
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
335-610 |
2.19e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 335 NKDEKDHLIER---LYREISGLTGQLDNMK---IESQRAMLQLKGRVSELEAEL-AEQQHLGR-----QAMDDCEFLRTE 402
Cdd:COG3096 276 HANERRELSERaleLRRELFGARRQLAEEQyrlVEMARELEELSARESDLEQDYqAASDHLNLvqtalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 403 LDEL----KRQREDTEKAQRSLTEIERKAQANEQRYSKLK---------------------------EKYSELVQNhADL 451
Cdd:COG3096 356 LEELterlEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqqaldvqqtraiqyqqavqalEKARALCGL-PDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 452 LRKNAEVTKQVSVARQAQVD---LEREKK-ELADSFARVSDQA-------------QRKTQEQQDVLE---NLKHeLATS 511
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATeevLELEQKlSVADAARRQFEKAyelvckiageverSQAWQTARELLRryrSQQA-LAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 512 RQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQE--SMCQQVKDQRKTL 589
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrSELRQQLEQLRAR 593
|
330 340
....*....|....*....|...
gi 1907162022 590 LAGIRKAAE--REIQEALSQLEE 610
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 ... |
361-610 |
2.89e-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: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKaqaNEQRYSKLKEK 440
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK---REQEVTELKKA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 441 YSELVQNH----ADLLRKNA----EVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVlENLKHELATSR 512
Cdd:pfam01576 336 LEEETRSHeaqlQEMRQKHTqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS-EHKRKKLEGQL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 513 QELQVLHSNLETSAQSEAKWLTQI-AELEKEQGSLATVAAQR---EEELSALRDQL--------ESTQIKLAGAqeSMCQ 580
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLqSELESVSSLLNEAEGKNiklSKDVSSLESQLqdtqellqEETRQKLNLS--TRLR 492
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162022 581 QVKDQRKTLLAGI------RKAAEREIQEALSQLEE 610
Cdd:pfam01576 493 QLEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSD 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
337-610 |
3.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 337 DEKDHLIERLYREISGLTGQLDNmkIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQA------------------- 392
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGN--AEDFLEELReerdeLREREAELEATLRTARERVEEAealleagkcpecgqpvegs 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 393 -----MDDC----EFLRTELDELKRQREDTEKAQRSLTEierkAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVS 463
Cdd:PRK02224 465 phvetIEEDrervEELEAELEDLEEEVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 464 VARQAQVDLEREKKELADSFARVSDQAQrKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAkwltQIAELEKEQ 543
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAELKERIESLERIRTLLAAIADAED----EIERLREKR 615
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 544 GSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgirkaaerEIQEALSQLEE 610
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE--------QVEEKLDELRE 674
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
397-607 |
3.73e-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: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 397 EFLRTELDELKRQREDTE------KAQRSLTEIERKAQANEQRYSKLKEKYSEL------VQNHADLLRKNAEVTKQVSV 464
Cdd:COG3206 178 EFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEAraelaeAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 465 ARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLEnLKHELATSRQELQVLHSNLETSAQSEAKwltqiaelekeqg 544
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILASLEAELE------------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162022 545 slatVAAQREEELSALRDQLESTQIKLAGAQ---ESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 607
Cdd:COG3206 324 ----ALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
342-547 |
4.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 342 LIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQamddceflrTELDELKRQrEDTEKAQRSLT 421
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ---------PPLALLLSP-EDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 422 EIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQdvl 501
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--- 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162022 502 enlkhELATSRQELQVLHSNLETSAQSEAKwLTQIAELEKEQGSLA 547
Cdd:COG4942 217 -----ELQQEAEELEALIARLEAEAAAAAE-RTPAAGFAALKGKLP 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-610 |
6.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTE----LDELKRQREDTEKAQRSLTEIERKA-----QANE 431
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEaeaaADEAEAAEEKAEAAEKKKEEAKKKAdaakkKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 432 QRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLER--EKKELADSfARVSDQAQRKTQEQQDVlENLKHELA 509
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEE-AKKADEAKKKAEEAKKA-EEAKKKAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 510 TSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTL 589
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260
....*....|....*....|.
gi 1907162022 590 LAGIRKAAEREIQEALSQLEE 610
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEE 1568
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
347-565 |
8.50e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 347 YREISGLTGQLDNMKIESQRAMLQL---KGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEi 423
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQLELdnlRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKE- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 424 erkaqanEQRYskLKEKYSELVqnhADLLRKNAEVTKQVSVARQAQVDL---------------EREKKELADSFARVSD 488
Cdd:pfam00038 132 -------ELAF--LKKNHEEEV---RELQAQVSDTQVNVEMDAARKLDLtsalaeiraqyeeiaAKNREEAEEWYQSKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 489 QAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEkEQGSLATVAAQR-----EEELSALRDQ 563
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETE-ERYELQLADYQEliselEAELQETRQE 278
|
..
gi 1907162022 564 LE 565
Cdd:pfam00038 279 MA 280
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
339-609 |
1.42e-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: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 339 KDHLIERLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEA----ELAEQQHLG------RQAMDDCEFLRTELDE--- 405
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSrvdlKLQELQHLKnegdhlRNVQTECEALKLQMAEkdk 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 406 ----LKRQRED----------------TEKAQRSLTEIERKAQANEQRYSKLKE--KYSELVQNHADLLRKNAEVTKQVS 463
Cdd:pfam15921 563 vieiLRQQIENmtqlvgqhgrtagamqVEKAQLEKEINDRRLELQEFKILKDKKdaKIRELEARVSDLELEKVKLVNAGS 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 464 VARQAQVDLEREKKELADSFARVSDQAQRKTQEqqdvLENLKHELATSRQELQVLHSNLET---SAQSEAKWL-TQIAEL 539
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMqlkSAQSELEQTrNTLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 540 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQ-------------------RKTLLAG---IRKAA 597
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhflkeeknklsqelstvatEKNKMAGeleVLRSQ 798
|
330
....*....|..
gi 1907162022 598 EREIQEALSQLE 609
Cdd:pfam15921 799 ERRLKEKVANME 810
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
377-538 |
1.67e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 377 ELEAELAEQQHLGRQAmddcEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNA 456
Cdd:COG3096 499 ELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 457 EVTKQVSVARQAQVDLEREKKELA----------DSFARVSDQ-------AQRKTQEQQDVLENL------KHELATSRQ 513
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAarapawlaaqDALERLREQsgealadSQEVTAAMQQLLEREreatveRDELAARKQ 654
|
170 180
....*....|....*....|....*
gi 1907162022 514 ELQVLHSNLETSAQSEAKWLTQIAE 538
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLALAE 679
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-610 |
1.85e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 398 FLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADL----------LRKNAEVTKQVSVA-R 466
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqleqeEEKLKERLEELEEDlS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 467 QAQVDLEREKKELADSFARVSDQaQRKTQEQQDVLENLKHELATSR-QELQVLHSNLETSAQseaKWLTQIAELEKEQGS 545
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEEL-EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVS---RIEARLREIEQKLNR 823
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162022 546 LATVAAQREEELSALRDQLESTQIklagaQESMCQQVKDQRKTLLAGIrKAAEREIQEALSQLEE 610
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEEL-EEELEELEAALRDLES 882
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
414-602 |
1.87e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 414 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVAR----QAQVDLEREKKELADSFARVsDQ 489
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAReeleQLEEELEQARSELEQLEEEL-EE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 490 AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 569
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190
....*....|....*....|....*....|...
gi 1907162022 570 KLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQ 602
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-610 |
2.03e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 329 NNQNGVNKDEkdhlIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCE----------F 398
Cdd:TIGR04523 376 KKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAQRSLT-EIERKAQANEQRYSKLKEKYSE---LVQNHADLLRKNAEVTKQVSVARQAQVDLER 474
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 475 EKKELADSFarvsDQAQRKTQEQQDVL--ENLKHELATSRQELQVLHSNLE--TSAQSEAKWL-----TQIAELEKEQGS 545
Cdd:TIGR04523 532 EKKEKESKI----SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKslKKKQEEKQELidqkeKEKKDLIKEIEE 607
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 546 LATVAAQREEELSALRDQ---LESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE--REIQEALSQLEE 610
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEiiKKIKESKTKIDD 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-610 |
2.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 358 DNMKIESQRAMLQLKGRVSELEAElAEQQHLGRQAMDDCEFLRtELDELKRQREDTEKAQRSLTEIER-------KAQAN 430
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEakkadeaKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 431 EQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSfARVSDQAQ-----------RKTQEQQD 499
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKkaeekkkadelKKAEELKK 1559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 500 VLENLKHELATSRQELQVLHS-NLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESM 578
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162022 579 CQQVKDQRKTllAGIRKAAE----REIQEALSQLEE 610
Cdd:PTZ00121 1640 KKEAEEKKKA--EELKKAEEenkiKAAEEAKKAEED 1673
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-610 |
2.21e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAMLQLKGRvselEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSlteieRKAQANEQRYSKLKEK 440
Cdd:PTZ00121 1571 KAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 441 YSELVQNhADLLRKnAEVTKQVSVARQAQVDLEREKKeladsfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHS 520
Cdd:PTZ00121 1642 EAEEKKK-AEELKK-AEEENKIKAAEEAKKAEEDKKK---------AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 521 NLETSAQSEakwltQIAELEKEQGSLATVAAQREEElsalrDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAERE 600
Cdd:PTZ00121 1711 EAEEKKKAE-----ELKKAEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
250
....*....|
gi 1907162022 601 IQEALSQLEE 610
Cdd:PTZ00121 1781 IEEELDEEDE 1790
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
365-610 |
2.28e-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: 48.43 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 365 QRAMLQLKGRVSELEAELAEQQHLGRQamddceflrteldELKRQREDTEKAQRSLTEIERKAQAnEQRYSKLKEKYSEL 444
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTS-------------ERKQRASLKEQMQEIQQSFSILTQC-DNRSKEDIPNLQNI 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 445 VQNHADLLRKNAEVTKQVSVARQAQvdleREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQElQVLHSNLET 524
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHAL----LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE-RVREHALSI 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 525 SAQSEAKWLTQIAELEKEQGSLATVAAQREE---ELSALRDQLEStqIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREI 601
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMlaqCQTLLRELETH--IEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
....*....
gi 1907162022 602 QEALSQLEE 610
Cdd:TIGR00618 746 KELMHQART 754
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-610 |
4.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 397 EFLRTEL-DELKRQREDTEKAQrslteiERKAQANEQRYSKLKEKYSELVQNHADLlrknAEVTKQVSVARQAQVDLERE 475
Cdd:COG4717 41 AFIRAMLlERLEKEADELFKPQ------GRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 476 KKELADSFARVSDQAQRKTQEQQdvLENLKHELATSRQELQVLHSNLETSAQseakWLTQIAELEKEQGSLATVAAQREE 555
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162022 556 ELS-ALRDQLESTQIKLAGAQesmcqqvkdQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG4717 185 QLSlATEEELQDLAEELEELQ---------QRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
374-536 |
5.22e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 374 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 453
Cdd:PRK12705 37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 454 KNAEvtkqvsvarqaqvdLEREKKELADSFARVSDQAQRktQEQQDVLENLKHELatsRQELQVLHSNLETSAQSEAKWL 533
Cdd:PRK12705 117 RELE--------------LEELEKQLDNELYRVAGLTPE--QARKLLLKLLDAEL---EEEKAQRVKKIEEEADLEAERK 177
|
...
gi 1907162022 534 TQI 536
Cdd:PRK12705 178 AQN 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
405-610 |
9.77e-05 |
|
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: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 405 ELKRQREDTEKaqrsltEIERkAQANEQRyskLKEKYSELvQNHADLLRKNAEVTKQvsvARQAQVDLEREKKELADSFA 484
Cdd:COG1196 169 KYKERKEEAER------KLEA-TEENLER---LEDILGEL-ERQLEPLERQAEKAER---YRELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 485 RVSDQAQRKTQEQQDVLEN-----------LKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 553
Cdd:COG1196 235 RELEAELEELEAELEELEAeleeleaelaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162022 554 EEELSALRDQLESTQIKLAGAQESmcQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
353-565 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 353 LTGQLDNMKIESQRAMLQLKG----RVSELEAELA----EQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQrslteIE 424
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDsaneRLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ-----LA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 425 RKAQANEQRYSKLKEKYSEL-VQNHADLlrknaevtKQVSVARQAQVDLEREKKELADSFARVS---------DQAQRKT 494
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALeTWYKRDL--------ASLGVDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQET 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 495 QEQQDvlENLKHELATSRQELQVLHSNLeTSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLE 565
Cdd:pfam12128 805 WLQRR--PRLATQLSNIERAISELQQQL-ARLIADTK--LRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
337-605 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 337 DEKDHLIERLYREISGLTGQLDNM----------------KIES--------QRAMLQLKGRVSELEAE----------- 381
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkinvlqkKIENlqeqlrdkDKQLAGLKERVKSLQTDssntdtalttl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 382 ---LAEQQHL-----------GRQAMDDCEFLRTELDELKRQRE--DTEKAQRSLTEIERKAQANEQRYSKLKeKYSELV 445
Cdd:pfam10174 442 eeaLSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSalQPELTEKESSLIDLKEHASSLASSGLK-KDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 446 QNHADLLRKNAEVTKQVSVARQAQ--VDLEREKKELADSFARVSDQAQRKTQE----QQDV---------LENLKH---- 506
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHnaEEAVRTNPEINDRIRLLEQEVARYKEEsgkaQAEVerllgilreVENEKNdkdk 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 507 -----ELATSRQ--ELQVLHSNLETSAQSE-AKWLTQIAELEKEQGSLATVAAQR--EEELSAL---RDQLESTQIKLAG 573
Cdd:pfam10174 601 kiaelESLTLRQmkEQNKKVANIKHGQQEMkKKGAQLLEEARRREDNLADNSQQLqlEELMGALektRQELDATKARLSS 680
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907162022 574 AQESMCQqvKDQRKTLLAGIRKAAEREI----QEAL 605
Cdd:pfam10174 681 TQQSLAE--KDGHLTNLRAERRKQLEEIlemkQEAL 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-610 |
1.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 342 LIERLYREISGLTGQLDnmKIESQRAML-QLKGRVSELEAELAEQQHLGRqAMDDCEFLRTELDELKrqredTEKAQRSL 420
Cdd:PRK03918 315 RLSRLEEEINGIEERIK--ELEEKEERLeELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK-----KRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 421 TEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDL--------EREKKELADSFARVSDQAQR 492
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 493 KTQEQQDVLENLKHELATSRQELqvlhsNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSalrDQLESTQIKLA 572
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLK 538
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907162022 573 GAQESMCQQVKdqRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:PRK03918 539 GEIKSLKKELE--KLEELKKKLAELEKKLDELEEELAE 574
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
346-583 |
1.50e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 346 LYREISGLTGQldnmkIESQRAML-QLKGRVSELeaelaeQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRS----- 419
Cdd:PRK04863 849 LERALADHESQ-----EQQQRSQLeQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFvqqhg 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 420 --LTEIERKA---QANEQRYSKLKEKY-----------------SELVQNHA--------DLLRKNAEVTKQVSVA-RQA 468
Cdd:PRK04863 918 naLAQLEPIVsvlQSDPEQFEQLKQDYqqaqqtqrdakqqafalTEVVQRRAhfsyedaaEMLAKNSDLNEKLRQRlEQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 469 QVDLEREKKELADSFARVSDQAQRKTQEQQ--DVLENLKHELATSRQELQV-LHSNLETSAQSEAKWL--------TQIA 537
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSsyDAKRQMLQELKQELQDLGVpADSGAEERARARRDELharlsanrSRRN 1077
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907162022 538 ELEKEQGSLatvaaqrEEELSALRDQLESTQIKLAGAQESMCQQVK 583
Cdd:PRK04863 1078 QLEKQLTFC-------EAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
412-570 |
1.75e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 412 DTEKAQRSLTEIERKAQANEQRYSKLKEkyseLVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFArvsdqaq 491
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEA----ELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAV------- 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 492 rkTQEQqdvLENLKHELATSRQELQVLHSNLEtSAQSEAKWLTQIAELEKEqgslatvAAQREEELSALRDQLESTQIK 570
Cdd:COG1566 146 --SQQE---LDEARAALDAAQAQLEAAQAQLA-QAQAGLREEEELAAAQAQ-------VAQAEAALAQAELNLARTTIR 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
428-593 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 428 QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDV-----LE 502
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 503 NLKHELATSRQELQVLhsnletsAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQEsmcqQV 582
Cdd:COG1579 93 ALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE----EL 161
|
170
....*....|.
gi 1907162022 583 KDQRKTLLAGI 593
Cdd:COG1579 162 EAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
353-555 |
1.83e-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: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 353 LTGQLDNMKIESQRAMLQLKG-RVSELEAELAEQQHLGRQAMDDcefLRTELDELKRQREDTE------KAQRSLTEIER 425
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSE---LESQLAEARAELAEAEarlaalRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 426 KAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVsvarqaqVDLEREKKELAdsfARVSDQAQRKTQEQQDVLENLK 505
Cdd:COG3206 257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV-------IALRAQIAALR---AQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907162022 506 HELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 555
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
370-609 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 370 QLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQAN---------------EQRY 434
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQmkdlqreleearasrDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 435 SKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVdlerEKKELADsfaRVSDQAQRKTQeQQDVLENLKHELATSRQE 514
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQ----ERDELAD---EIASGASGKSA-LQDEKRRLEARIAQLEEE 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 515 LQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREeelsALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAgir 594
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE----SARQQLERQNKELKAKLQEMEGTVKSKFKSSIA--- 970
|
250
....*....|....*
gi 1907162022 595 kAAEREIQEALSQLE 609
Cdd:pfam01576 971 -ALEAKIAQLEEQLE 984
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-444 |
2.06e-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: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDNmkiESQRAMLQLKGRVSELEAELAEqqhlgrqamddcefLRTELDELKRQREDTEKAQRSLTE 422
Cdd:COG3206 293 VIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREAS--------------LQAQLAQLEARLAELPELEAELRR 355
|
90 100
....*....|....*....|..
gi 1907162022 423 IERKAQANEQRYSKLKEKYSEL 444
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEA 377
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
366-571 |
2.19e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 366 RAMLQLKGRVSEleAELAEQQHlgRQAMddcEFLRTELDELkrQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELV 445
Cdd:COG3096 455 EEVLELEQKLSV--ADAARRQF--EKAY---ELVCKIAGEV--ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 446 Q---NHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdQAQRKTQEQQdvLENLKHELATSRQELQVLHSNL 522
Cdd:COG3096 526 QrlrQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL---------EAQLEELEEQ--AAEAVEQRSELRQQLEQLRARI 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162022 523 ETSAQSEAKWLTQIAELEK--EQG--SLATVAA---------QREEELSALRDQLESTQIKL 571
Cdd:COG3096 595 KELAARAPAWLAAQDALERlrEQSgeALADSQEvtaamqqllEREREATVERDELAARKQAL 656
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
334-524 |
2.31e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 334 VNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQ-----LKGRVSELEAELAEQQHLGRQamddcefLRTELDELKR 408
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeienLNGKKEELEEELEELEAALRD-------LESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 409 QREDTEK----AQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVtKQVSVARQAQVDLEREKKELADSFA 484
Cdd:TIGR02169 890 ERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEELSLEDVQAELQRVEEEIR 968
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162022 485 RVSDQAQRKTQEQQDVLENL-----KHE-LATSRQELQVLHSNLET 524
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLdelkeKRAkLEEERKAILERIEEYEK 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-576 |
3.35e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 360 MKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQR-EDTEKAQ--RSLTEIERKAQANEQRYSK 436
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEeaKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 437 LKEKYSELVQNHADLLRKNAEVTKQVSV----ARQAQVDLEREKKELADsfARVSDQ-----AQRKTQEQQDVLENLKHE 507
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEE--AKKDEEekkkiAHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 508 LATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLAT--VAAQREEELSALRDQLESTQIKLAGAQE 576
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
343-566 |
3.95e-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: 44.56 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDNMKIES--QRAMLQLKGRVSELEAELA-----EQQHlgRQAMD-------------------DC 396
Cdd:COG3096 811 LQRLHQAFSQFVGGHLAVAFAPdpEAELAALRQRRSELERELAqhraqEQQL--RQQLDqlkeqlqllnkllpqanllAD 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 397 EFLRTELDELKRQREDTEKAQRS-------LTEIERKA---QANEQRYSKLKEKY-----------------SELVQN-- 447
Cdd:COG3096 889 ETLADRLEELREELDAAQEAQAFiqqhgkaLAQLEPLVavlQSDPEQFEQLQADYlqakeqqrrlkqqifalSEVVQRrp 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 448 H------ADLLRKNAEVTKQV-SVARQAQVDLEREKKELADSFARVSDQAQRKT------QEQQDVLENLKHEL------ 508
Cdd:COG3096 969 HfsyedaVGLLGENSDLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLAslkssrDAKQQTLQELEQELeelgvq 1048
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162022 509 ------ATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 566
Cdd:COG3096 1049 adaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-577 |
4.26e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 391 QAMDDCEFLRTELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEKY----SELVQNHADLLRKNAEVTKQVSVAR 466
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 467 QAQVDLEREKKEL--------ADSFA----------RVSDQ----------AQRKTQEQQDVLENLKHELATSRQELQVL 518
Cdd:COG3883 90 ERARALYRSGGSVsyldvllgSESFSdfldrlsalsKIADAdadlleelkaDKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 519 HSNLEtSAQSEAKwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQES 577
Cdd:COG3883 170 KAELE-AQQAEQE--ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-550 |
4.74e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 343 IERLYREISGLTGQLDNMKIEsqRAMLQ-----LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQ 417
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKR--RDKLTeeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 418 -RSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELadsfarvsdqaqRKTQE 496
Cdd:TIGR02169 409 dRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------------YDLKE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162022 497 QQDVLENlkhELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKE-QGSLATVA 550
Cdd:TIGR02169 477 EYDRVEK---ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiQGVHGTVA 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
362-571 |
5.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 362 IESQRAMLQ-LKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIER---KAQANEQRYSKL 437
Cdd:PRK02224 532 IEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllaAIADAEDEIERL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 438 KEKYSELvqnhadllrknAEVTKQvsvaRQAQVDLERE-KKELADSF--ARVsDQAQRKTQEQQDVLENLKHELATSRQE 514
Cdd:PRK02224 612 REKREAL-----------AELNDE----RRERLAEKRErKRELEAEFdeARI-EEAREDKERAEEYLEQVEEKLDELREE 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 515 lqvlhsnlETSAQSEAKWLT-QIAELEKEQGSLATVAAqREEELSALRD---QLESTQIKL 571
Cdd:PRK02224 676 --------RDDLQAEIGAVEnELEELEELRERREALEN-RVEALEALYDeaeELESMYGDL 727
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
371-542 |
5.39e-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: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 371 LKGRVSELEAELAEQQHLGRQAMDDCEFLRTEL-DELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHA 449
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALkRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 450 DLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKhELATSRQELQVLHSNLETSAQSE 529
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNLEKQQSSL 165
|
170
....*....|...
gi 1907162022 530 AKWLTQIAELEKE 542
Cdd:pfam05557 166 AEAEQRIKELEFE 178
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
399-524 |
6.53e-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: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAQRSLTEiERKAQAneQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREkke 478
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAE--- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907162022 479 lADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQ----VLHSNLET 524
Cdd:pfam07926 80 -AESAKAELEESEESWEEQKKELEKELSELEKRIEDLNeqnkLLHDQLES 128
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
414-610 |
6.58e-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: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 414 EKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSvarQAQVDLEREKKELADSFARVSDQAQR- 492
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERARAl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 493 -KTQEQQDVLENLKheLATSRQEL--QVlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQI 569
Cdd:COG3883 96 yRSGGSVSYLDVLL--GSESFSDFldRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162022 570 KLAGAQESmcqqvKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:COG3883 172 ELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
405-610 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 405 ELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQvdlEREKKELADSFA 484
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 485 RVSDQAQRKTQEQQDVLENLKHELATSRQElqvlhSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQL 564
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907162022 565 ESTQIKLAgaqESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:PTZ00121 1439 KAEEAKKA---DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
335-568 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 335 NKDEKDHLIERLYREISGLTGQLDNMK-----IESQRAMLQLKGR---------VSELEAELAEqqhlgrqamddcefLR 400
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARsqansIQSQLEIIQEQARnqnsmymrqLSDLESTVSQ--------------LR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 401 TELDELKRQREDT-EKAQRSLteIERKAQANEQRYSKlkEKYSELVQNHADLLRKN-AEVTKqvsvaRQAQVDLEREK-K 477
Cdd:pfam15921 331 SELREAKRMYEDKiEELEKQL--VLANSELTEARTER--DQFSQESGNLDDQLQKLlADLHK-----REKELSLEKEQnK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 478 ELADSFARVS---DQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQRE 554
Cdd:pfam15921 402 RLWDRDTGNSitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV 481
|
250
....*....|....
gi 1907162022 555 EELSALRDQLESTQ 568
Cdd:pfam15921 482 EELTAKKMTLESSE 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
405-610 |
1.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 405 ELKRQREDTEKAQRSLTEIERKA----QANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAqvdlEREKKELA 480
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVE 1636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 481 DSFARVSDQAQRKTQEQQDVLENL--KHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELS 558
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907162022 559 ALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
391-610 |
1.65e-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: 42.42 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 391 QAMDDCEFLRTELDELKRQREDTEKAQRslteiERKAQANEQRYSKLKEKYSELVQNHADLlrKNAEVTKQVSVARQAQV 470
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKL--EEAEKARQAEMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 471 DLEREKKELadsfarvsdqaQRKTQEQQDVLENLKHELATSRQElqvlhsnletsaqSEAKWLTQIAELEKEQgslatva 550
Cdd:pfam17380 336 YAEQERMAM-----------ERERELERIRQEERKRELERIRQE-------------EIAMEISRMRELERLQ------- 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 551 AQREEELSALRDQLEST-QIKLagaQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEE 610
Cdd:pfam17380 385 MERQQKNERVRQELEAArKVKI---LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
408-603 |
1.95e-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: 41.86 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 408 RQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDlEREKKELADSFARVS 487
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-ERQRQEEEERKQRLQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 488 DQ-AQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAElekEQGSLATVAaqREEELSALRDQLES 566
Cdd:pfam15709 414 LQaAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE--MQLAE---EQKRLMEMA--EEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907162022 567 TQIKLAGAQESMcQQVKDQRKTLLAGIRKAAEREIQE 603
Cdd:pfam15709 487 EEKARLEAEERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
374-607 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 374 RVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLR 453
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 454 KNAEVTKQVSVARQ---AQVDLEREKKELADSFARV-SDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSE 529
Cdd:pfam02463 251 EEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162022 530 AKWLTQIAELEKEqgsLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQ 607
Cdd:pfam02463 331 KKEKEEIEELEKE---LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
401-561 |
2.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 401 TELDELKRQ-----------REDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQaq 469
Cdd:PRK09039 53 SALDRLNSQiaeladllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 470 vdlerekkeladsfarVSDQAQRKtqeqqdvLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELekeqGSLATV 549
Cdd:PRK09039 131 ----------------VSARALAQ-------VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL----GRRLNV 183
|
170
....*....|...
gi 1907162022 550 A-AQREEELSALR 561
Cdd:PRK09039 184 AlAQRVQELNRYR 196
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-569 |
2.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 390 RQAMDDCEFLRTELDELKRQREDTE----KAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVA 465
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEeeleQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 466 RQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKwlTQIAELEKEQGS 545
Cdd:COG4372 121 QKERQDLEQQRKQLEAQ----IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE--QALDELLKEANR 194
|
170 180
....*....|....*....|....
gi 1907162022 546 LATVAAQREEELSALRDQLESTQI 569
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAE 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
344-608 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 344 ERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLG-RQAMDDCEFLRTELDELKRQ-------REDTEK 415
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGELKLRlnqatatPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 416 AQRSLTEIERKAQANEQRYSKLKEKYSELVQnhADLLRKNAEVTKQVSVARQAQVD--------------------LERE 475
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELRQ--ARKRRDQASEALRQASRRLEERQsaldelelqlfpqagtllhfLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 476 KKELADSFARVSDQAQ--RKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQR 553
Cdd:pfam12128 544 APDWEQSIGKVISPELlhRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 554 EEELSALRDQLESTQIKLAGAQESM------CQQVKDQRKTLLAGIRKAAEREIQEALSQL 608
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALknarldLRRLFDEKQSEKDKKNKALAERKDSANERL 684
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
370-570 |
2.98e-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: 40.87 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 370 QLKGRVSELEAELAEQQHLgrqamddceflrteldelkrqredtekaqrslteiERKAQANEQRYSKLKEKYSELVQNHA 449
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQ-----------------------------------VARLQAELDRLQALESELAISRQDYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 450 DLLRKNAEVTKQVSVArQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQse 529
Cdd:pfam00529 100 GATAQLRAAQAAVKAA-QAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907162022 530 akwlTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIK 570
Cdd:pfam00529 177 ----ENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIR 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-609 |
3.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 337 DEKDHLIERLYREISgltgQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGR------------------------QA 392
Cdd:PRK03918 448 EHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaeqlkeleeklkkynleeleKK 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 393 MDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELvqnHADLLRKNAEVTKqvsvarqaqvDL 472
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---LKELEELGFESVE----------EL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 473 EREKKELA---DSFARVSDqAQRKTQEQQDVLENLKHELATSRQELQVLHSNLEtsaqsEAKwlTQIAELEKEQGslatv 549
Cdd:PRK03918 591 EERLKELEpfyNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR--KELEELEKKYS----- 657
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162022 550 aaqrEEELSALRDQLESTQIKLAGAQESMcQQVKDQRKTLLAGIRKAAER--EIQEALSQLE 609
Cdd:PRK03918 658 ----EEEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEEleEREKAKKELE 714
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
402-610 |
3.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 402 ELDELKRQREDTEKA---QRSLTEIERKAQANEQRySKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKE 478
Cdd:PTZ00121 1303 KADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 479 LADSFA---RVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREE 555
Cdd:PTZ00121 1382 AAKKKAeekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 556 ELSALRDQLESTQIKLAGAQESMCQQVK---DQRKTLLAGIRKAAE-REIQEALSQLEE 610
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEaKKKADEAKKAEE 1520
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
348-568 |
3.42e-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: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 348 REISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQqhLGRQAMDDCEFLRTElDELKRQREDTEKAQRSLTEIERKA 427
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKE-KEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 428 QANEQRYSKL--KEKYSELVQNHADLLRKNAEVTKQVS------VARQAQVDLER----------EKKELADSFARVSDQ 489
Cdd:TIGR00606 768 EEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVErkiaqqAAKLQGSDLDRtvqqvnqekqEKQHELDTVVSKIEL 847
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162022 490 AQRKTQEQQDVLENLKHELatsrQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQ 568
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKT----NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
478-610 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 478 ELADSFarVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLE--------TSAQSEAKWLT-QIAELEKEQGSLAT 548
Cdd:COG3206 156 ALAEAY--LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglVDLSEEAKLLLqQLSELESQLAEARA 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162022 549 VAAQREEELSALRDQLESTQIKLAGAQES-MCQQVKDQRKTL---LAGIR----------KAAEREIQEALSQLEE 610
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpVIQQLRAQLAELeaeLAELSarytpnhpdvIALRAQIAALRAQLQQ 309
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
411-584 |
3.69e-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: 39.66 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 411 EDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHAD------LLRKNAEVTKQVSVARQAQV---------DLERE 475
Cdd:pfam05010 8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEfektiaQMIEEKQKQKELEHAEIQKVleekdqalaDLNSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 476 KKELADSFarvsdqaqRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAE-LEKEQGSLATVAAQRE 554
Cdd:pfam05010 88 EKSFSDLF--------KRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEkLDQANEEIAQVRSKAK 159
|
170 180 190
....*....|....*....|....*....|
gi 1907162022 555 EELSALRDQLESTQIKLAGAQESMCQQVKD 584
Cdd:pfam05010 160 AETAALQASLRKEQMKVQSLERQLEQKTKE 189
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
353-544 |
3.86e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 353 LTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQR-------SLTEIER 425
Cdd:PLN02939 199 LEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKerslldaSLRELES 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 426 K---AQANEQRYSKLK-EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSF--ARVSDQAQRKTQEQQD 499
Cdd:PLN02939 279 KfivAQEDVSKLSPLQyDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLkeANVSKFSSYKVELLQQ 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907162022 500 VLENLKHELATSRQElqvLHSNLETSAQSEAKWLTQIAELEKEQG 544
Cdd:PLN02939 359 KLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
368-598 |
4.52e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 368 MLQLKGRVSELEAELAEQQHLGRQAMDdceflrtELDELKRQREDtekAQRSLTEIERKAQANEQRYSKLKEkyselvqn 447
Cdd:PRK10929 111 ILQVSSQLLEKSRQAQQEQDRAREISD-------SLSQLPQQQTE---ARRQLNEIERRLQTLGTPNTPLAQ-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 448 hADLLRKNAEvtkqvSVARQAQVDlerekkELadsfarvsDQAQRKTQEQQDvLENLKHELATSRQE-----LQVLHSNL 522
Cdd:PRK10929 173 -AQLTALQAE-----SAALKALVD------EL--------ELAQLSANNRQE-LARLRSELAKKRSQqldayLQALRNQL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 523 ETSAQSEA-KWLTQIAELEKEQGSLATVAA---QREEELSALRDQlESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAE 598
Cdd:PRK10929 232 NSQRQREAeRALESTELLAEQSGDLPKSIVaqfKINRELSQALNQ-QAQRMDLIASQQRQAASQTLQVRQALNTLREQSQ 310
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
434-568 |
4.56e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.39 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 434 YSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADsfarvsdQAQRKTQEQQDVLENLKHELATSRQ 513
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD-------RAKEKLKKLLQEIMIKVKKLEELEE 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162022 514 ELQVLHSNLETSAQSEAKWLTQIAELEKeqgSLATVAAQREEELSALRDQLESTQ 568
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEK---KLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
319-566 |
4.61e-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: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 319 SSLSSDPFNFNNQNGVNKDEKDhlieRLYREISGLTGQLDnmkiESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEF 398
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKN----KLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAqrsLTEIERKAQANEQRYSKLK---EKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLERE 475
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKN---IDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 476 KKE-------LADSFARVSDQAQRKTQE-----------------------------QQDVLENLKHELATSRQELQVLH 519
Cdd:TIGR04523 248 ISNtqtqlnqLKDEQNKIKKQLSEKQKEleqnnkkikelekqlnqlkseisdlnnqkEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907162022 520 SNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLES 566
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
471-576 |
4.94e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 471 DLEREKKELADSFArvsdQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVA 550
Cdd:PRK09039 57 RLNSQIAELADLLS----LERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100
....*....|....*....|....*.
gi 1907162022 551 AQREEELSALRDQLESTQIKLAGAQE 576
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEA 158
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
402-581 |
5.10e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.21 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 402 ELDELKRQREDTEKAQR-SLTEIERKA-------QANEQRYSKLKE-KYSELVQNHADLLRKNAEVTKQVSVARQAQVDL 472
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQeRQKKLEQQAeeaekqrAAEQARQKELEQrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 473 EREKKELADSFARVSDQAQRKTQEqqdvlENLKHELATSRQELQVLHSNLETSAQSEA-------------KWLTQIAEL 539
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEE-----EAKAKAAAEAKKKAEEAKKKAEAEAKAKAeaeakakaeeakaKAEAAKAKA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907162022 540 EKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQ 581
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
383-610 |
5.39e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 383 AEQQHLGRQAMDDCEFLRTELDELKR--QREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTK 460
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAERIRtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESA 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 461 QvSVARQAQVDLEREKKELADSFARVSDQAQRKTQEQQDVLENLKHELATSRQELQVLHSNLETSAQseakwlTQIAELE 540
Cdd:NF041483 680 D-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASAR------KRVEEAQ 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162022 541 KEQGSLATVAAQREEEL-SALRDQLESTQIKLAGAQESMCQQVkdqrktllAGIRKAAEREIQEALSQLEE 610
Cdd:NF041483 753 AEAQRLVEEADRRATELvSAAEQTAQQVRDSVAGLQEQAEEEI--------AGLRSAAEHAAERTRTEAQE 815
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
361-564 |
5.55e-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: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 361 KIESQRAmlQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQredtekaqrsLTEIERKAQANEQRYSKLKEK 440
Cdd:COG1579 14 ELDSELD--RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----------IKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 441 YSElVQNHADLlrknAEVTKQVSVARQAQVDLEREKKELADSfarvSDQAQRKTQEQQDVLENLKHELATSRQELQvlhs 520
Cdd:COG1579 82 LGN-VRNNKEY----EALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELD---- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907162022 521 nletsaqseakwlTQIAELEKEqgsLATVAAQREEELSALRDQL 564
Cdd:COG1579 149 -------------EELAELEAE---LEELEAEREELAAKIPPEL 176
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
335-588 |
8.67e-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: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 335 NKDEKDHLIERLYREISGLTGQLDNMK--IESQRAMLQ-LKGRVSELEAELAE----QQHLGRQAMDDCEFLRTELDELK 407
Cdd:smart00806 72 NVEELDEVKKHIDDEIDTLQNELDEVKqaLESQREAIQrLKERQQNSAANIARpaasPSPVLASSSSAISLANNPDKLNK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 408 RQREDTEKAQRSLTEIeRKAQANEQrySKLKEKYSELVQNHADLLRKNAEVTKQVSVAR--QAQVDLEREKKELADSFAR 485
Cdd:smart00806 152 EQRAELKSLQRELAVL-RQTHNSFF--TEIKESIKDILEKIDKFKSSSLSASGSSNRAYveSSKKKLSEDSDSLLTKVDD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 486 VSDQ--------AQRKTQEQQDVLENLKHELATSRQELQvlhsNLETSAQSEAKWLTQI--AELEK---EQGSLATvaaq 552
Cdd:smart00806 229 LQDIiealrkdvAQRGVRPSKKQLETVQKELETARKELK----KMEEYIDIEKPIWKKIweAELDKvceEQQFLTL---- 300
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162022 553 REEELSALRDQLESTQIKLAGAQESMCQQVKDQRKT 588
Cdd:smart00806 301 QEDLIADLKEDLEKAEETFDLVEQCCEEQEKGPSKN 336
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
399-585 |
8.79e-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: 40.00 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 399 LRTELDELKRQREDTEKAQ-RSLTEIERKaqanEQRYSKLKEKYSelvqnhadllrknaevtkqvsvarqaqvDLEREKK 477
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIdKFLTEIKKK----EKELEKLNNKYN----------------------------DLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162022 478 ELADSFARVSDQAQRKtqeqQDVLENLKHELAtsrqELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEEL 557
Cdd:TIGR04523 170 ELENELNLLEKEKLNI----QKNIDKIKNKLL----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
170 180
....*....|....*....|....*...
gi 1907162022 558 SALRDQLESTQIKLAGAQESMcQQVKDQ 585
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQ-NKIKKQ 268
|
|
| |
