|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
40-306 |
2.17e-89 |
|
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: 287.66 E-value: 2.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 40 QAVSINKAINTQEVAVKEKHARTCILGTHH-EKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:pfam07651 2 LEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 119 ADLNDMSRMWGH-LSEGYGKLCSIYLKLLITKMEFHIKNPRFPGNLQMSNRQLDEAGENDVNNFfqLTVEMFDYLECELN 197
Cdd:pfam07651 82 RRISSLLRISSFsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 198 LFLGVFSSLDMSRSVSVTaAGQCRLAPLIQVILDSSHLYDYTVKLLFKLHSCLP------ADTLQGHRDRFQEQFKKLKS 271
Cdd:pfam07651 160 LQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLKE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 261244998 272 LFYRSSNLQYFKRLIqIPQLPENPPNFLRASALSE 306
Cdd:pfam07651 239 FYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
836-1034 |
1.76e-83 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 268.85 E-value: 1.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 836 GIKMEVNERILASCTDLMQAIRVLVLSSKDLQRDIVESGRGAASMKEFYAKNSRWTEGLISASKAVGWGATMLVDAADQV 915
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 916 VQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQ-IEDTETMDFSAMT 994
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 261244998 995 LTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYELA 1034
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
4.38e-83 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 264.21 E-value: 4.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 261244998 120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
4.71e-70 |
|
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: 228.32 E-value: 4.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 261244998 120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17006 81 RLKELGKLWGHLKDGYGKLIAQYCKLLITKLEFH 114
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
886-1032 |
1.06e-59 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 200.89 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 886 KNSRWTEGLISASKAVGWGATMLVDAADQVVQGKGKFEELMVCSHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVT 965
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261244998 966 QATAGVVASTKSGKSQIED--TETMDFSAMTLTQIKRQEMDAQVLVLELETRLQKERERLGELRKKHYE 1032
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEeiEEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
40-153 |
2.46e-56 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 190.08 E-value: 2.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKA 119
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 261244998 120 DLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
42-153 |
6.19e-37 |
|
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: 134.81 E-value: 6.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHP--NVIKDSMRH-K 118
Cdd:cd16986 3 KAVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDAwL 82
|
90 100 110
....*....|....*....|....*....|....*
gi 261244998 119 ADLNDMSRMWGHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd16986 83 PELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
40-160 |
1.47e-35 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 131.21 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 40 QAVSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNA--VLCWKFCHVFHKLLRDGHPNVIKDSMRH 117
Cdd:smart00273 3 LEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEALRN 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 261244998 118 KADLNDMSRMWGHLSEG--YGKLCSIYLKLLITKMEFHIKNPRFP 160
Cdd:smart00273 83 RNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
483-581 |
2.65e-33 |
|
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. It carries a highly conserved HADLLRKN sequence motif at its N-terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. this binding then stimulates clathrin lattice assembly. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding.
Pssm-ID: 465154 [Multi-domain] Cd Length: 99 Bit Score: 123.58 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 483 HADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 261244998 563 SNEQLGTQLSALVAEKAGL 581
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
42-153 |
5.80e-28 |
|
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: 108.93 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 42 VSINKAINTQEVAVKEKHARTCILGTHHEKGAHTFWLAVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHKADL 121
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 261244998 122 NDMSRMW-GHLSEGYGKLCSIYLKLLITKMEFH 153
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-825 |
7.56e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIERKAQANEQRY-TKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQ 528
Cdd:COG1196 323 EELAELEEELEELEEELEELeEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 529 EKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTN 608
Cdd:COG1196 403 EELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 609 ERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQVALD 688
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 689 CVERLRSSRDGfvsdntDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQESMG 768
Cdd:COG1196 562 AIEYLKAAKAG------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 261244998 769 AADCSRLRTALDSVKALGEKLRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEE 825
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-1032 |
7.21e-16 |
|
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: 82.80 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 376 RLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQAlgesEFLRAELDDLRRVKEDTEKEqrsL 455
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----QILRERLANLERQLEELEAQ---L 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 456 SEIERKAQANEQRYTKLKEKYTELVQSHADLlrknaevtrqmtvaRAAQDEVENVKKEMQDRLKVAQDSASQQEKAQ--- 532
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESL--------------EAELEELEAELEELESRLEELEEQLETLRSKVaql 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 533 LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSAlvAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERES 612
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 613 GVKAAEALQ---NQLNEKESREQALES--ELVSLRWASLRAALEEAGKI------VQDSLN---QLEDPAHISCTSSADY 678
Cdd:TIGR02168 470 LEEAEQALDaaeRELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLsgilgvLSELISvdeGYEAAIEAALGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 679 LVSR-CQVALDCVERLRSSRDGFVS--DNTDVSGLVRAVTQFAHLVGDVIVQGSATSHMVPVEQADALADS------VKA 749
Cdd:TIGR02168 550 VVVEnLNAAKKAIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 750 CGAEALTLLCQLKEQESMGAADcsrlrtaldsvkalGEKLRPRGLELQQGELGDLVEQEmaaTSAAVESAAARIEEMLNK 829
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLD--------------GDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 830 SRAvdtgIKMEVNErILASCTDLMQAIRVLVLSSKDLQRDIVEsgrGAASMKEFYAKNSRWTEGLISASKAVGWGATMLV 909
Cdd:TIGR02168 693 IAE----LEKALAE-LRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 910 DAADQVVQgkgKFEELMVCSHEIAASTAQlVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQIEDTETMd 989
Cdd:TIGR02168 765 ELEERLEE---AEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR- 839
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 261244998 990 fSAMTLTQIKRQEMDAQVLVLELE------TRLQKERERLGELRKKHYE 1032
Cdd:TIGR02168 840 -LEDLEEQIEELSEDIESLAAEIEeleeliEELESELEALLNERASLEE 887
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-655 |
1.04e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSE 457
Cdd:COG1196 234 LRELEAELEELEAELEELEAEL----EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 458 IERKAQANEQRYTK-LKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQL 536
Cdd:COG1196 310 RRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 537 QALQAELmSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESgVKA 616
Cdd:COG1196 390 EALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL-LAE 467
|
250 260 270
....*....|....*....|....*....|....*....
gi 261244998 617 AEALQNQLNEKESREQALESELVSLRWASLRAALEEAGK 655
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-665 |
4.15e-15 |
|
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: 80.49 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 398 ESGRLCQA-----LRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTkl 472
Cdd:TIGR02168 669 NSSILERRreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE-- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 473 kEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELET 552
Cdd:TIGR02168 747 -ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 553 LKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ---NSLTNERESGVKAAEALQNQLNEKES 629
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSE 901
|
250 260 270
....*....|....*....|....*....|....*.
gi 261244998 630 REQALESELVslrwaSLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02168 902 ELRELESKRS-----ELRRELEELREKLAQLELRLE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-653 |
1.14e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 409 RVNELEAELAEQ-THLKQQA---------LGESEFLRAEL--DDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKY 476
Cdd:COG1196 190 RLEDILGELERQlEPLERQAekaeryrelKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 477 TELVQSHADLLRKNAEVTRQMTVARAAQDEVEN---VKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETL 553
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 554 KSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQA 633
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260
....*....|....*....|
gi 261244998 634 LESELVSLrwASLRAALEEA 653
Cdd:COG1196 430 LAELEEEE--EEEEEALEEA 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
366-826 |
2.10e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 366 QNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVK 445
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 446 EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSA 525
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 526 SQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEkAGLVETVSRKEVELSGLGAELERLQNS 605
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG-AVAVLIGVEAAYEAALEAALAAALQNI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 606 LTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDPAHiscTSSADYLVSRCQV 685
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 686 ALDCVERLRSSRdGFVSDNTDVSGLVRAVTQFAHLVGDvIVQGSATSHMVPVEQADALADSVKACGAEALTLLCQLKEQE 765
Cdd:COG1196 629 AARLEAALRRAV-TLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261244998 766 SMGAADCSRLRTALDSVKALGEK------------LRPRGLELQQGELGDLVEQEMAATSAAVESAAARIEEM 826
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQleaereelleelLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-666 |
2.19e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALK---EELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKE----DTEK 450
Cdd:TIGR02168 693 IAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleeRLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 451 EQRSLSEIERKAQANEQRYTKLKEkytELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEK 530
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKE---ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 531 AQlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLT--N 608
Cdd:TIGR02168 850 LS-EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261244998 609 ERESGVKAAEA-LQNQLNEKESREQALESELVSL----------RWASLRAALEEAGKIVQDSLNQLED 666
Cdd:TIGR02168 929 LRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKieddeeearrRLKRLENKIKELGPVNLAAIEEYEE 997
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-1030 |
5.33e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 366 QNGMRKDDKDRLIEQLTAELQALKEELESFRL---ESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLR 442
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 443 RVKEDTEKEQRSLSEiERKAQANEQRYTKLKEKYTELvqshadllrknAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQ 522
Cdd:TIGR02168 407 ARLERLEDRRERLQQ-EIEELLKKLEEAELKELQAEL-----------EELEEELEELQEELERLEEALEELREELEEAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 523 dSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAekagLVETVSRKEVELS-GLGaelER 601
Cdd:TIGR02168 475 -QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE----LISVDEGYEAAIEaALG---GR 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 602 LQNSLTNERESGVKAAEALqnqlnEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLEDpaHISCTSSA----D 677
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFL-----KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--LVKFDPKLrkalS 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 678 YLVSRCQVA--LDCVERLRSSRDgfvsdntdvsGLVRAVTQFAHLV--GDVIVQGSATSHMVPVEQADALADSVKACgaE 753
Cdd:TIGR02168 620 YLLGGVLVVddLDNALELAKKLR----------PGYRIVTLDGDLVrpGGVITGGSAKTNSSILERRREIEELEEKI--E 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 754 ALTLLCQLKEQEsmgaadCSRLRTALDSVKALGEKLRPRGLELQQgeLGDLVEQEMAATSAAVESAAARIEEmLNKSRAV 833
Cdd:TIGR02168 688 ELEEKIAELEKA------LAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQ-LSKELTE 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 834 DTGIKMEVNERILASCTDLMQAIRVLVlsskDLQRDIvesgrgaasmKEFYAKNSRWTEGLISASKAVgwgaTMLVDAAD 913
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIE----ELEAQI----------EQLKEELKALREALDELRAEL----TLLNEEAA 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 914 QVVQGKGKFEELMvcsHEIAASTAQLVAASKVKAEKGSSNLSRLQQASKGVTQATAGVVASTKSGKSQIEdtetmdfsAM 993
Cdd:TIGR02168 821 NLRERLESLERRI---AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE--------AL 889
|
650 660 670
....*....|....*....|....*....|....*..
gi 261244998 994 TLTQIKRQEMDAQvlVLELETRLQKERERLGELRKKH 1030
Cdd:TIGR02168 890 ALLRSELEELSEE--LRELESKRSELRRELEELREKL 924
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
404-650 |
1.14e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 404 QALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEqrsLSEIERKAQANEQRYTKLKEKYTELVQSH 483
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 484 ADLLRKNAEVTRQ--MTVARAAQDEVENVkkemqdRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQ 561
Cdd:COG4942 107 AELLRALYRLGRQppLALLLSPEDFLDAV------RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 562 QSNEQLGTQLSALVAEKAGLVETVSRKEVELSglgAELERLQnsltneresgvKAAEALQNQLNEKESREQALESELVSL 641
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELA---AELAELQ-----------QEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 261244998 642 RWASLRAAL 650
Cdd:COG4942 247 GFAALKGKL 255
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-618 |
4.17e-10 |
|
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: 64.32 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRlesgRLCQALRGRVNELEAELAEQThLKQQALGESEFLR---------AELDD 440
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLT----EEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLRvkekigeleAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 441 LRRVKEDTEKEQRSLSEIERKAQANEQRY------------------TKLKEKYTELVQSHADLLRKNAEVTRQMTVARA 502
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLlaeieelereieeerkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 503 AQD----EVENVKKEM------QDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLS 572
Cdd:TIGR02169 386 ELKdyreKLEKLKREInelkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261244998 573 ALVAEKAGLVETVSRKEVELSGLGAELERL--QNSLTNERESGVKAAE 618
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGRAVE 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-666 |
6.42e-10 |
|
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: 63.55 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 375 DRLIEQLTAELQALKEELESFRLesgrLCQALRGRVNELEAELAEQthLKQQALgESEFLRAELDDLRRVKEDTEKEqrs 454
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDL----IIDEKRQQLERLRREREKA--ERYQAL-LKEKREYEGYELLKEKEALERQ--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQmtVARAAQDEVENVKKEMQDrLKVAQDSASQQEKAQLE 534
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGE-LEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 535 QLQALQAELMSSRTELETLKSTVtssqqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERE--- 611
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEI-------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelk 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 612 SGVKAAEALQNQLNEKESREQALESELVSLRwaSLRAALEEAGKIVQDSLNQLED 666
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLS--EELADLNAAIAGIEAKINELEE 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
385-578 |
9.35e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 385 LQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLK---QQALGESEFLRAELDDLRRVKEDTEKEQRSLsEIERK 461
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKL-EKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 462 AQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQA 541
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 261244998 542 ELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEK 578
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
378-652 |
1.97e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlkqqALGESEFLRAELDDLRRVKEDTEKE----QR 453
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRdeelRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 454 SLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAA----QDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedrREEIEELEEEIEELRERFGDAPVDLG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 530 KAQ--LEQLQALQAELMSSRTELETLKSTVTSSQQSNEQL---------GTQLsalvaEKAGLVETVSRKEVELSGLGAE 598
Cdd:PRK02224 409 NAEdfLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecGQPV-----EGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 261244998 599 LERLQNSlTNERESGVKAAEALQNQLNEKESREQalESELVSLRWASLRAALEE 652
Cdd:PRK02224 484 LEDLEEE-VEEVEERLERAEDLVEAEDRIERLEE--RREDLEELIAERRETIEE 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-576 |
3.98e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRlesgrlcqALRGRVNELEAELAEQthlkQQALGEsefLRAELDDLRRVKEDTEKEQRsLSE 457
Cdd:COG4717 73 LKELEEELKEAEEKEEEYA--------ELQEELEELEEELEEL----EAELEE---LREELEKLEKLLQLLPLYQE-LEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 458 IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*....
gi 261244998 538 ALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVA 576
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
378-663 |
4.62e-09 |
|
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: 60.42 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLE---SGRLCQALRGRVNELEAELAEqthLKQQAlgeseflraELDDLRRVKEDTEKEQRS 454
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKEleqNNKKIKELEKQLNQLKSEISD---LNNQK---------EQDWNKELKSELKNQEKK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvarAAQDEVENVKKEMQDRLKVAQDSASQ------- 527
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQNEIEKLKKENQSYKQEIKNLESQindlesk 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 528 -----QEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQ---------------------QSNEQLGTQLSALVAE--- 577
Cdd:TIGR04523 400 iqnqeKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKNNseikdltnqdsvkeliiknldNTRESLETQLKVLSRSink 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 578 -KAGLVETV---SRKEVELSGLGAE---LERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAAL 650
Cdd:TIGR04523 480 iKQNLEQKQkelKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
330
....*....|...
gi 261244998 651 EEagkiVQDSLNQ 663
Cdd:TIGR04523 560 EK----EIDEKNK 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-608 |
5.15e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR----VK 445
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 446 EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLkvaqDSA 525
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EEL 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 526 SQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRK-EVELSGLGAELERLQN 604
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRLEN 979
|
....
gi 261244998 605 SLTN 608
Cdd:TIGR02168 980 KIKE 983
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
326-666 |
6.67e-09 |
|
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: 60.24 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 326 VVETEDLVDTDI-PPLTGTGDSKFDDLFGTSAATDPFNFNSQNGMRkddkdrliEQLTAELQALKEELESFRLESGRLCQ 404
Cdd:pfam12128 554 VISPELLHRTDLdPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASE--------EELRERLDKAEEALQSAREKQAAAEE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 405 ALRGRVNELEAELAEQThLKQQALGESEflraelDDLRRVKEDTEKEQRSLSE--IERKAQANEQRyTKLKEKYTELVQS 482
Cdd:pfam12128 626 QLVQANGELEKASREET-FARTALKNAR------LDLRRLFDEKQSEKDKKNKalAERKDSANERL-NSLEAQLKQLDKK 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 483 HADLLRKNAEVTRQMTVAR-AAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSR-----------TEL 550
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKqAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkREI 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 551 ETLKSTVTSSQQsNEQLGTQL-----SALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNER---ESGVKAAEALQN 622
Cdd:pfam12128 778 RTLERKIERIAV-RRQEVLRYfdwyqETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRaklEMERKASEKQQV 856
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 261244998 623 QLNEKESREQALESELVSLRwasLRAALEEAGKIVQDSLNQLED 666
Cdd:pfam12128 857 RLSENLRGLRCEMSKLATLK---EDANSEQAQGSIGERLAQLED 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
376-665 |
7.02e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 376 RLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQthlkQQALG--ESEFLRAELDDLRRVKEDTEKEQR 453
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHKL----EEALNdlEARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 454 SLSEIERKAQANEQRYTKLKEKYTELVQshaDLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQdsasqqekAQL 533
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQ---ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE--------AAL 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 534 EQLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQnsltnERESG 613
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLREL---ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-----EIPEE 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261244998 614 VKAAEALQNQLNEKESREQALES---------ELVSLRWASL---RAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPvnmlaiqeyEEVLKRLDELkekRAKLEEERKAILERIEEYE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-665 |
1.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRvkedtEKEQRsLSEIERKA-QAneQRYTKLKEKYTELvQSHADLLRKNaEVTRQMTVARAAQDEVENVKKEM 514
Cdd:COG1196 189 ERLEDILG-----ELERQ-LEPLERQAeKA--ERYRELKEELKEL-EAELLLLKLR-ELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 515 QDRLKVAQ------DSASQQEKAQLEQLQALQAELMSSRTELET----LKSTVTSSQQSNEQLGTQLSALVAEKAGLVET 584
Cdd:COG1196 259 EAELAELEaeleelRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 585 VSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLrwASLRAALEEAGKIVQDSLNQL 664
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERL 416
|
.
gi 261244998 665 E 665
Cdd:COG1196 417 E 417
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
418-666 |
2.64e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 418 AEQTHLKQQALGESEFLRAELDDLRRvKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSH----ADLLRKNAEV 493
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkkADELKKAEEL 1557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 494 TRQMTVARAAQDEVENVKKEMQDRlkvAQDSASQQEKAQLEQLQALQAELMSSRTEL------ETLKSTVTSSQQSNEQL 567
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeAKIKAEELKKAEEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 568 GTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNS-------LTNERESGVKAAEALQNQLNEKESREQALESELVS 640
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
250 260
....*....|....*....|....*.
gi 261244998 641 LRWASLRAALEEAGKIVQDSLNQLED 666
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAE 1740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-652 |
2.80e-08 |
|
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: 58.21 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 372 DDKDRLIEQLTAELQALKEELESfrlESGRLCQALRGRVNELEaelaEQTHLKQQALGESEFLRAELDDLRRVKEDTEKE 451
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLE----KVSSLTAQLESTKEMLRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 452 QR-------SLSEIERKAQANEQRYTKLKE----KYTEL------------VQSHADLLR-------KNAEVTRQ----M 497
Cdd:pfam15921 495 ERtvsdltaSLQEKERAIEATNAEITKLRSrvdlKLQELqhlknegdhlrnVQTECEALKlqmaekdKVIEILRQqienM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 498 T--------VARAAQDEVENVKKEMQDR---------LKVAQDSASQQEKAQLEQLQALQAELMSS-----------RTE 549
Cdd:pfam15921 575 TqlvgqhgrTAGAMQVEKAQLEKEINDRrlelqefkiLKDKKDAKIRELEARVSDLELEKVKLVNAgserlravkdiKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 550 LETLKSTVTSSQQSNEQLGTQLSAL---VAEKAGLVETVSRK-EVELSGLGAELERLQNSLTNERES---GVKAAEALQN 622
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLkrnFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSdghAMKVAMGMQK 734
|
330 340 350
....*....|....*....|....*....|
gi 261244998 623 QLNEKESREQALESELVSLRWASLRAALEE 652
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMTNANKEK 764
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-636 |
2.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 372 DDKDRLIEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHLKQqalgesefLRAELDDLRRVKEDTEKe 451
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELK----EIEEKERKLRKELRELEKVLKKESELIK--------LKELAEQLKELEEKLKK- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 452 qRSLSEIERKAQaneqRYTKLKEKYTEL---VQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLK--------- 519
Cdd:PRK03918 515 -YNLEELEKKAE----EYEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvee 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 520 ---------------VAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSalVAEKAGLVET 584
Cdd:PRK03918 590 leerlkelepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREE 667
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 261244998 585 VSRKEVELSGLGAELERLQNSltneRESGVKAAEALQNQLNEKESREQALES 636
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKR----REEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
371-652 |
3.33e-08 |
|
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: 57.21 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 371 KDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGrVNELEAELAEQTHLKQQALGESEFLRAELDDlrRVKEDTEK 450
Cdd:pfam07888 68 REQWERQRRELESRVAELKEELRQSREKHEELEEKYKE-LSASSEELSEEKDALLAQRAAHEARIRELEE--DIKTLTQR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 451 EQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTR---QMTVARAAQDE-------VENVKKEMQDRLKV 520
Cdd:pfam07888 145 VLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSlskEFQELRNSLAQrdtqvlqLQDTITTLTQKLTT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 521 AQDSASQQEkAQLEQLQALQAELMSSRTELETLKSTVTS--SQQSN------------EQLGTQLSAL-----------V 575
Cdd:pfam07888 225 AHRKEAENE-ALLEELRSLQERLNASERKVEGLGEELSSmaAQRDRtqaelhqarlqaAQLTLQLADAslalregrarwA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 576 AEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQnqlNEKE-SREQALES--ELVSLRwASLRAALEE 652
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG---REKDcNRVQLSESrrELQELK-ASLRVAQKE 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
367-666 |
4.37e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 367 NGMRKDDKDRLIEQLTAELQAL---KEELESFRLESGRLCQALRGRVNELEAELAEqthLKQqALGESEFLRAELDD--- 440
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEE---LKK-AKGKCPVCGRELTEehr 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 441 ---LRRVK---EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSH--ADLLRKNAEVTRQMTV--ARAAQDEVENV 510
Cdd:PRK03918 451 kelLEEYTaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKLKKYNLeeLEKKAEEYEKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 511 KKEMqDRLKVAQDSAsqqeKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEV 590
Cdd:PRK03918 531 KEKL-IKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 591 ELSGLGAELERLQNSLTNERESGVKA----------AEALQNQLNEKESR-----EQALESELVSLR--WASLRAALEEA 653
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAfeelaetekrLEELRKELEELEKKyseeeYEELREEYLELSreLAGLRAELEEL 685
|
330
....*....|...
gi 261244998 654 GKIVQDSLNQLED 666
Cdd:PRK03918 686 EKRREEIKKTLEK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-665 |
5.37e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 412 ELEAELAEQTHLKQQALGESEFLRAELDDLR-RVKEDTEK---EQRSLSEIERKAQANEQRYTKLKEKYTELvqshadll 487
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDELSQElsdASRKIGEIEKEIEQLEQEEEKLKERLEEL-------- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 488 rknaevtrqMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQlEQLQALQAELMSSR-----TELETLKSTVTSSQQ 562
Cdd:TIGR02169 743 ---------EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE-EALNDLEARLSHSRipeiqAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 563 SNEQLGTQLSALVAEKAGLVETVSRKEVELsglgAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLR 642
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQR----IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260
....*....|....*....|...
gi 261244998 643 waSLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR02169 889 --KERDELEAQLRELERKIEELE 909
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
389-665 |
5.42e-08 |
|
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: 57.06 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 389 KEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQA--LGESEFLRAELD-DLRRVKEdtEKEQRSLSEIERKAQAN 465
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiYAEQERMAMERErELERIRQ--EERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 466 EQrytklkEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAElms 545
Cdd:pfam17380 373 EI------SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE--- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 546 SRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGL-VETVSRKEVELSG---LGAELE-RLQNSLTNERESGV--KAAE 618
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRrkiLEKELEeRKQAMIEEERKRKLleKEME 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 261244998 619 ALQNQLNEKESREQAlESELVSLRWASLRAALEEAGKIVQDSLNQLE 665
Cdd:pfam17380 524 ERQKAIYEEERRREA-EEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-553 |
5.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRL-------------IEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHLKQQALGESEF--L 434
Cdd:COG4913 591 EKDDRRRIrsryvlgfdnrakLAALEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDEIDVasA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 435 RAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEM 514
Cdd:COG4913 667 EREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261244998 515 Q------DRLKVAQDSASQQEKAQLE-QLQALQAELMSSRTELETL 553
Cdd:COG4913 747 LralleeRFAAALGDAVERELRENLEeRIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
378-584 |
2.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLESGRLCQAL-RGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR------------V 444
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdrleqL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 445 KEDTEKEQRSLSEIERKAQANEQRYTKLKEkytELVQSHADLLRKNAEVTRQMTVARAAQDEVENvkkemqdrlkvAQDS 524
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGL---PLPASAEEFAALRAEAAALLEALEEELEALEE-----------ALAE 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 525 ASQQEKAQLEQLQALQAELmssrTELETLKSTVTSSQQsneqlgtQLSALVAEKAGLVET 584
Cdd:COG4913 410 AEAALRDLRRELRELEAEI----ASLERRKSNIPARLL-------ALRDALAEALGLDEA 458
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
42-126 |
2.87e-07 |
|
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: 50.35 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 42 VSINKAINTQEVAVKEKHARTCILGTH-HEKGAHTFWL--AVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVIKDSMRHK 118
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLATSnGGGRADVAYIvhALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYS 82
|
....*...
gi 261244998 119 ADLNDMSR 126
Cdd:cd03564 83 GHIFNLSN 90
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-652 |
5.99e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 384 ELQALKEELESFRLESGRLcqalRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQ 463
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENI----EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 464 ANEQRYTKLKEKYTELVQSHADL---LRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDsaSQQEKAQLEQ-LQAL 539
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELkkeIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEeINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 540 QAELmssrTELETLKSTVTSSQQSNEQLGTQLSALvAEKAGLVETVSRKEVELSGLGAELERLQ-NSLTNERESGVKAAE 618
Cdd:PRK03918 327 EERI----KELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKE 401
|
250 260 270
....*....|....*....|....*....|....
gi 261244998 619 ALQNQLNEKESREQALESELvslrwASLRAALEE 652
Cdd:PRK03918 402 EIEEEISKITARIGELKKEI-----KELKKAIEE 430
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
411-663 |
6.15e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 411 NELEAeLAEQTHLK------QQALGESEFLraeLDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKytelvqsha 484
Cdd:PRK11281 43 AQLDA-LNKQKLLEaedklvQQDLEQTLAL---LDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 485 dllrkNAEVTRQmTVARAAQdevenvkKEMQDRLKVAQDsasQQEKAQlEQLQALQAELMSSRTELETLKSTVTSSQQSN 564
Cdd:PRK11281 110 -----NDEETRE-TLSTLSL-------RQLESRLAQTLD---QLQNAQ-NDLAEYNSQLVSLQTQPERAQAALYANSQRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 565 EQLGTQLSALVAEKAGLVET-VSRKEVELSGLGAELERLQNSLTNEresgVKAAEALQNQLNEKESREQALESELVSLRW 643
Cdd:PRK11281 173 QQIRNLLKGGKVGGKALRPSqRVLLQAEQALLNAQNDLQRKSLEGN----TQLQDLLQKQRDYLTARIQRLEHQLQLLQE 248
|
250 260
....*....|....*....|
gi 261244998 644 ASLRAALEEAGKIVQDSLNQ 663
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQ 268
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
364-637 |
6.23e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 364 NSQNGMRKDDKdrLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlKQQALGESEFLRAELDDLRR 443
Cdd:TIGR04523 325 EIQNQISQNNK--IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE----NQSYKQEIKNLESQINDLES 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 444 VKEDTEKEQRslsEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQD 523
Cdd:TIGR04523 399 KIQNQEKLNQ---QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 524 SAsQQEKAQLEQLQAlqaELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ 603
Cdd:TIGR04523 476 SI-NKIKQNLEQKQK---ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
250 260 270
....*....|....*....|....*....|....
gi 261244998 604 NSLTNERESGVKaaEALQNQLNEKESREQALESE 637
Cdd:TIGR04523 552 FELKKENLEKEI--DEKNKEIEELKQTQKSLKKK 583
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
439-737 |
8.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 439 DDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMtvaRAAQDEVENVKKEMQ--- 515
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 516 -------------------DRLkVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVA 576
Cdd:COG3883 100 gsvsyldvllgsesfsdflDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 577 EKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKI 656
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 657 VQDSLNQLEDPAHISCTSSADYLVSRCQVALDCVERLRSSRDGFVSDNTDVSGLVRAVTQFAHLVGDVIVQGSATSHMVP 736
Cdd:COG3883 259 AGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGG 338
|
.
gi 261244998 737 V 737
Cdd:COG3883 339 G 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
436-650 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRVKEDTEKEQRSLSEIERKAQ--------ANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEV 507
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAEryaaarerLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 508 ENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLkstvtsSQQSNEQLGTQLSALVAEKAGLVETVSR 587
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERR------RARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261244998 588 KEVELSGLGAELERLQNSLT---NERESGVKAAEALQNQLNEKESREQALESELVSLRwASLRAAL 650
Cdd:COG4913 389 AAALLEALEEELEALEEALAeaeAALRDLRRELRELEAEIASLERRKSNIPARLLALR-DALAEAL 453
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
373-638 |
1.09e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.84 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 373 DKDRLIEQLTAELQA-LKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRrVKEDTEKE 451
Cdd:pfam00038 18 DKVRFLEQQNKLLETkISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR-QKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 452 QRSLSEIE---RKAQANEQRYTKLK-EKYTELVQSHADLLRKN--AEVtRQMTvaraAQDEVENVKKEMQDRLKVAQDSA 525
Cdd:pfam00038 97 LRTSAENDlvgLRKDLDEATLARVDlEAKIESLKEELAFLKKNheEEV-RELQ----AQVSDTQVNVEMDAARKLDLTSA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 526 SQQEKAQLEQLQALqaelmsSRTELE-TLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQN 604
Cdd:pfam00038 172 LAEIRAQYEEIAAK------NREEAEeWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270
....*....|....*....|....*....|....
gi 261244998 605 SLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELEAELQETRQEM 279
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
370-642 |
1.31e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELEsfrlESGRLCQALRGRVNELEAELAEQTHL---KQQALGESEFLRAELDDLRRVKE 446
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 447 DTEKEQRSLSEIERKAQANEQRYTK-LKEKYTEL---------VQSHAD-LLRKNAEVTRQmtvaraAQDEVENVKKEMQ 515
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKeVEDLKTELekeklknieLTAHCDkLLLENKELTQE------ASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 516 DrlkvaQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGL 595
Cdd:pfam05483 521 D-----IINCKKQEERMLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261244998 596 GAELERLQNSLTN----------ERESGVKAAEALQNQLNEKESREQALESELVSLR 642
Cdd:pfam05483 593 ENKCNNLKKQIENknknieelhqENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
410-633 |
2.13e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 410 VNEL-EAELAEQTHLKQQALGES-EFLRAELDDLRRVKEDTE------KEQRSLSEIERKAQANEQRYTKLKEKYTEL-- 479
Cdd:COG3206 154 ANALaEAYLEQNLELRREEARKAlEFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEAra 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 480 ----VQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDrLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKS 555
Cdd:COG3206 234 elaeAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 556 TVTSSQQSN-EQLGTQLSALVAEKAGL---VETVSRKEVELSGLGAELERLQNSLtneresgvkaaEALQNQLNEKESRE 631
Cdd:COG3206 313 RILASLEAElEALQAREASLQAQLAQLearLAELPELEAELRRLEREVEVARELY-----------ESLLQRLEEARLAE 381
|
..
gi 261244998 632 QA 633
Cdd:COG3206 382 AL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
369-638 |
2.37e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 369 MRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRG---RVNELEA---ELAEQTHLKQQALGESEFLRAELDDLR 442
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKlekEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 443 RVKEDTEKEQRSLSEIER---KAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVK-------- 511
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerleelkk 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 512 --KEMQDRLKVAQDSASQQE--KAQLEQLQALQAELmsSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSR 587
Cdd:PRK03918 346 klKELEKRLEELEERHELYEeaKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261244998 588 KEVELSGL----------GAEL-----ERLQNSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:PRK03918 424 LKKAIEELkkakgkcpvcGRELteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-655 |
2.70e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAeqthlKQQALGESEFLRaELDDLRRVKEDTE 449
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR-KADELKKAEEKKK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIERKA-----QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDS 524
Cdd:PTZ00121 1292 ADEAKKAEEKKKAdeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 525 ASQQEKAQLEQL-----QALQAELMSSRTE-----LETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSG 594
Cdd:PTZ00121 1372 KKEEAKKKADAAkkkaeEKKKADEAKKKAEedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261244998 595 LGAELERLQNsLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGK 655
Cdd:PTZ00121 1452 KAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
369-525 |
3.17e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.24 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 369 MRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQAlrgRVNELEAELAEqthlkqqalgesefLRAELDDLrrvKEDT 448
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFE---RLAELRDELAE--------------LEEELEAL---KARW 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKN------------AEVTRQMT---VARAAQDEVENVKKe 513
Cdd:COG0542 464 EAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELApllreevteediAEVVSRWTgipVGKLLEGEREKLLN- 542
|
170
....*....|....*
gi 261244998 514 MQDRLK---VAQDSA 525
Cdd:COG0542 543 LEEELHervIGQDEA 557
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
384-601 |
3.25e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.14 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 384 ELQALKEELESFRLESGRLCQALRGRVNELeaelaeQTHLKQQALGESEFLRAELDDLRRvkedtEKEQrSLSEIERKAQ 463
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASL------KEGSGVEGLDSSTALTLELEELRQ-----ERDL-LREEIQKLRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 464 ANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAEL 543
Cdd:pfam09787 69 QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261244998 544 MSSRTELeTLKSTVTSSQQSNE-----------QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELER 601
Cdd:pfam09787 149 EKLRNQL-TSKSQSSSSQSELEnrlhqltetliQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSN 216
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
375-630 |
4.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 375 DRLIEQLTaELQALKEELESFRLESGRLcQALRGRVNELEAELAEQTHLKQqalgesefLRAELDDLRRvkedtekeQRS 454
Cdd:COG4913 228 DALVEHFD-DLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEY--------LRAALRLWFA--------QRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 455 LSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMtvARAAQDEVENVKKEMqDRLKVAQDSASQQEKAQLE 534
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREI-ERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 535 QLQALQAELMSSRTELETLKSTVTSSQqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGV 614
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250
....*....|....*.
gi 261244998 615 KAAEALQNQLNEKESR 630
Cdd:COG4913 444 ALRDALAEALGLDEAE 459
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
378-586 |
4.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLESGRLcqALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRvkedtekeQRSLSE 457
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA--------QLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 458 IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:COG3206 254 DALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQ 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261244998 538 ALQAELMS-------SRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVS 586
Cdd:COG3206 334 AQLAQLEArlaelpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
370-551 |
6.38e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFR---LESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRV-- 444
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALErriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 445 -------------KEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVK 511
Cdd:COG4942 115 rlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 261244998 512 KEMQDRLKVAQDSASQQEkAQLEQLQALQAELMSSRTELE 551
Cdd:COG4942 195 AERQKLLARLEKELAELA-AELAELQQEAEELEALIARLE 233
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
368-666 |
8.73e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 368 GMRKDDKDRLieqltaelQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQ-------------------QAL 428
Cdd:pfam10174 46 ALRKEEAARI--------SVLKEQYRVTQEEN----QHLQLTIQALQDELRAQRDLNQllqqdfttspvdgedkfstPEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 429 GESEFLRAELDDLRRVKEdTEKEQRSLSEIERKAQANEQRYTKLKE---KYTELVQSHADLLRKNAEV---TRQMTVARA 502
Cdd:pfam10174 114 TEENFRRLQSEHERQAKE-LFLLRKTLEEMELRIETQKQTLGARDEsikKLLEMLQSKGLPKKSGEEDwerTRRIAEAEM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 503 A---------QDEVENV--KKEMQDRLKVAQDSASQQEKAQL-----EQLQALQAELMSSRTELETLKST-VTSSQQSNE 565
Cdd:pfam10174 193 QlghlevlldQKEKENIhlREELHRRNQLQPDPAKTKALQTViemkdTKISSLERNIRDLEDEVQMLKTNgLLHTEDREE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 566 QLgTQL------SALVAEKAG-LVETVSRKEVELSGLGAELErlqnSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:pfam10174 273 EI-KQMevykshSKFMKNKIDqLKQELSKKESELLALQTKLE----TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEV 347
|
330 340
....*....|....*....|....*...
gi 261244998 639 VSLRwasLRaaLEEAGKIVQDSLNQLED 666
Cdd:pfam10174 348 DALR---LR--LEEKESFLNKKTKQLQD 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
370-666 |
8.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQE 529
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 530 KAQLEQLQalQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERlqnsltnE 609
Cdd:PTZ00121 1545 KKKADELK--KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------A 1615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261244998 610 RESGVKaAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLED 666
Cdd:PTZ00121 1616 EEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
386-537 |
9.50e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 386 QALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEK---EQRSLSEIERKA 462
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKA 1690
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 463 QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVEnvKKEMQDRLKVAQDSASQQEKAQLEQLQ 537
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK--KEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
376-661 |
1.05e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 376 RLIEQLTAELQALKEELESFRLESGRLCQALR---------GRVNELEAELAEQTHLKQQAlgeseflRAELDDLRRVKE 446
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAASDHLNLVQTALRqqekieryqADLEELEERLEEQNEVVEEA-------DEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 447 DTEKE-----------QRSLSEIERKAQANEQRYTKLkEKYTELVQShADLLRKNAEVTrqMTVARAAQDEVENVKKEMQ 515
Cdd:PRK04863 387 AAEEEvdelksqladyQQALDVQQTRAIQYQQAVQAL-ERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 516 DRLKVAQDSASQQEKA-------------------------QLEQLQALQAELMSSRTELETLKSTVtSSQQSNEQLGTQ 570
Cdd:PRK04863 463 QKLSVAQAAHSQFEQAyqlvrkiagevsrseawdvarellrRLREQRHLAEQLQQLRMRLSELEQRL-RQQQRAERLLAE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 571 LSalvaEKAGLVETvsrKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESElvSLRWASLRAAL 650
Cdd:PRK04863 542 FC----KRLGKNLD---DEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR--APAWLAAQDAL 612
|
330
....*....|.
gi 261244998 651 EEAGKIVQDSL 661
Cdd:PRK04863 613 ARLREQSGEEF 623
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
374-637 |
1.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 374 KDRLIEQLTAELQALKEELESFRLESgRLCQALRGRVNELEAelaeqTHLKQQALGESEflrAELDDLRRvkEDTEKEqR 453
Cdd:PRK04863 784 REKRIEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRFIG-----SHLAVAFEADPE---AELRQLNR--RRVELE-R 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 454 SLSEIERKAQANEQRYTKLKEKYTEL--VQSHADLLRKNAevtrqmtvaraAQDEVEnvkkEMQDRLKVAQDSAS--QQE 529
Cdd:PRK04863 852 ALADHESQEQQQRSQLEQAKEGLSALnrLLPRLNLLADET-----------LADRVE----EIREQLDEAEEAKRfvQQH 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 530 KAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSAlvaekagLVETVSRKE-------VELSGLGAEL-ER 601
Cdd:PRK04863 917 GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFA-------LTEVVQRRAhfsyedaAEMLAKNSDLnEK 989
|
250 260 270
....*....|....*....|....*....|....*....
gi 261244998 602 LQNSLTNERESGVKAAEAL---QNQLNEKESREQALESE 637
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaQAQLAQYNQVLASLKSS 1028
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-634 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 369 MRKDDKDRLIEQLT---AELQALKEELESFRLESG-------RLCQALRGRVNELEAELAEQTHLKQQALGES---EFLR 435
Cdd:pfam15921 339 MYEDKIEELEKQLVlanSELTEARTERDQFSQESGnlddqlqKLLADLHKREKELSLEKEQNKRLWDRDTGNSitiDHLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRVKEDTEKEQRSLS-----EIERKAQANEQRYTKLkEKYTEL---VQSHADLLRKNAE--VTRQMTVaRAAQD 505
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKsecqgQMERQMAAIQGKNESL-EKVSSLtaqLESTKEMLRKVVEelTAKKMTL-ESSER 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 506 EVENVKKEMQDRLKVAQDSASQQEKA------QLEQLQALQAE---LMSSRTELETLKSTVTSSQQSNEQLGTQLS---- 572
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEITKLrsrvdlKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtq 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 573 ----------ALVAEKAGLVETVSRKEVELSGLGA----------ELERLQNSLTNERESGVKA-AEALQNQLNEKESRE 631
Cdd:pfam15921 577 lvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKIlkdkkdakirELEARVSDLELEKVKLVNAgSERLRAVKDIKQERD 656
|
...
gi 261244998 632 QAL 634
Cdd:pfam15921 657 QLL 659
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
493-665 |
1.30e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 493 VTRQMTVARAAQDEVENVKKEMQDRLKVAQD------------SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSS 560
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 561 QQSNE----------------QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNEREsgvKAAEALQNQL 624
Cdd:COG3206 246 RAQLGsgpdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ---RILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 261244998 625 NEKESREQALESELvslrwASLRAALEEAGKIVQDsLNQLE 665
Cdd:COG3206 323 EALQAREASLQAQL-----AQLEARLAELPELEAE-LRRLE 357
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
371-635 |
1.57e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 371 KDDKDRLIEQLTAELQAlKEELEsfrlesgrlcqaLRGRVNELEAELAEQTHL-------KQQA----------LGESEF 433
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-KEEKD------------LHERLNGLESELAELDEEieryeeqREQAretrdeadevLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 434 LRAELDDLrrvKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKE 513
Cdd:PRK02224 249 RREELETL---EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 514 MQDRL---KVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEV 590
Cdd:PRK02224 326 LRDRLeecRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 261244998 591 ELSGLGAELERLQNSLTNERESgVKAAEA-LQNQLNEKESREQALE 635
Cdd:PRK02224 406 DLGNAEDFLEELREERDELRER-EAELEAtLRTARERVEEAEALLE 450
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
369-517 |
1.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 369 MRKDDKDRLIEQLTAELQAL--------KEELESfRLESGRLCQALRGRVNELEAELAEQTHLKQQAL--GESEFLRAEL 438
Cdd:COG4717 356 AEELEEELQLEELEQEIAALlaeagvedEEELRA-ALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEEL 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261244998 439 DDLRRVKEDTEKEQRSLSEiERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDR 517
Cdd:COG4717 435 EELEEELEELEEELEELRE-ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
371-655 |
2.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 371 KDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNEleAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEK 450
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 451 --EQRSLSEIERKAQANEQRYTKLKEKYTElvQSHADLLRK-----NAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQD 523
Cdd:PTZ00121 1479 aeEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKaeeakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 524 SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGlGAELERLQ 603
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKV 1635
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 261244998 604 NSLTNERESGVKAAEALQNQLNEKESR--EQALESELVSLRWASLRAALEEAGK 655
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
371-636 |
2.69e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 371 KDDKDRLIEQLTAELQAL----------KEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELD- 439
Cdd:pfam01576 652 KEELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFEr 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 440 DLRRVKEDTEKEQRSLS----------EIERKAQANEQRYTKLKEKYTELVQSHADLLRKNA-EVTRQMtvaRAAQDEVE 508
Cdd:pfam01576 732 DLQARDEQGEEKRRQLVkqvreleaelEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGReEAVKQL---KKLQAQMK 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 509 NVKKEMQDrLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRK 588
Cdd:pfam01576 809 DLQRELEE-ARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRL 887
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261244998 589 EVELSGLGAELERLQNS--LTNER-ESGVKAAEALQNQLNEKESREQALES 636
Cdd:pfam01576 888 EARIAQLEEELEEEQSNteLLNDRlRKSTLQVEQLTTELAAERSTSQKSES 938
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
525-666 |
2.95e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 525 ASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQN 604
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261244998 605 SLTNEResGVKAAEALQNQLNEKESREQALESELVSL--RWASLRAALEEAGKIVQDSLNQLED 666
Cdd:COG1579 81 QLGNVR--NNKEYEALQKEIESLKRRISDLEDEILELmeRIEELEEELAELEAELAELEAELEE 142
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
500-653 |
3.33e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 500 ARAAQDEVENVKKEMQD---RLKVAQD------------SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSN 564
Cdd:COG3524 172 ERAREDAVRFAEEEVERaeeRLRDAREallafrnrngilDPEATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 565 EQLGTQLSAL----VAEKAGLVETVSRKevELSGLGAELERLQnsltneresgvkaaealqnqlNEKESREQALESELvs 640
Cdd:COG3524 252 RQLRRRIAALekqiAAERARLTGASGGD--SLASLLAEYERLE---------------------LEREFAEKAYTSAL-- 306
|
170
....*....|...
gi 261244998 641 lrwASLRAALEEA 653
Cdd:COG3524 307 ---AALEQARIEA 316
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
366-665 |
3.56e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 366 QNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEA---EL-------AEQTHLKQQALGESEFLR 435
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlktELedtldttAAQQELRSKREQEVTELK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRVKED--TEKEQRSLSEIERKAQANEQrytkLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKE 513
Cdd:pfam01576 334 KALEEETRSHEAqlQEMRQKHTQALEELTEQLEQ----AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 514 MQDRLKVAQDSASQQEKA---QLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSalvaEKAGLVETVSRKEV 590
Cdd:pfam01576 410 LEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ----DTQELLQEETRQKL 485
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 591 ELSGLGAELERLQNSltneresgvkaaeaLQNQLNEKESREQALESELvslrwASLRAALEEAGKIVQDSLNQLE 665
Cdd:pfam01576 486 NLSTRLRQLEDERNS--------------LQEQLEEEEEAKRNVERQL-----STLQAQLSDMKKKLEEDAGTLE 541
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
438-660 |
5.02e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 438 LDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTEL--VQSHADLLRKNAEVTRQ-MTVARAAQDEvenvkkem 514
Cdd:PRK10929 57 LEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVppNMSTDALEQEILQVSSQlLEKSRQAQQE-------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 515 QDRLKVAQDSASQQEKAQLEQLQALQAelMSSRteLETLKSTVTSSQQSneqlgtQLSALVAEKAGLVETVSrkEVELSG 594
Cdd:PRK10929 129 QDRAREISDSLSQLPQQQTEARRQLNE--IERR--LQTLGTPNTPLAQA------QLTALQAESAALKALVD--ELELAQ 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 595 LGA----ELERLQnsltneresgvkaAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDS 660
Cdd:PRK10929 197 LSAnnrqELARLR-------------SELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQS 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
374-626 |
5.05e-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: 47.32 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 374 KDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDL----RRVKEDTE 449
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLekeiERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLR--KNAEVTRQMTVARAAQDEVE-----NVKKEMQDRLKVAQ 522
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKELKSKEKElkklnEEKKELEEKVKDLT 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 523 DSASQ---------QEKAQLEQ-----------------LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVA 576
Cdd:TIGR04523 517 KKISSlkekiekleSEKKEKESkisdledelnkddfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 577 EKAGLVETVSRKEVELSGLGAELERLQ----------NSLTNERESGVKAAEALQNQLNE 626
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKkeneklssiiKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-635 |
5.46e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEELESFRLESGRLCQalrgrvnelEAELAEQTHLKQQALG-------ESEFLRAELDDLRRVKEDTEKE 451
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQ---------KREAQEEQLKKQQLLKqlrarieELRAQEAVLEETQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 452 QRSLSEIERKAQANEQR---YTKLKEKYTELvqshADLLRKNAEVTRQmTVARAAQDEVENVKKEMQDRLKVAQDSA--- 525
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAqriHTELQSKMRSR----AKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVAtsi 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 526 ---SQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVetVSRKEVELSGLGAELERL 602
Cdd:TIGR00618 368 reiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA--HAKKQQELQQRYAELCAA 445
|
250 260 270
....*....|....*....|....*....|....*
gi 261244998 603 --QNSLTNERESGVKAAEALQnQLNEKESREQALE 635
Cdd:TIGR00618 446 aiTCTAQCEKLEKIHLQESAQ-SLKEREQQLQTKE 479
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
372-694 |
6.20e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 372 DDKDRLIE------QLTAELQALKEELESFRLESGRLCQALRGR---------VNELEAELAEQTHL-----KQQALGES 431
Cdd:COG3096 303 EEQYRLVEmareleELSARESDLEQDYQAASDHLNLVQTALRQQekieryqedLEELTERLEEQEEVveeaaEQLAEAEA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 432 EFLRAElDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLkEKYTELVQShADLLRKNAEvTRQMTvARAAQDEVENVK 511
Cdd:COG3096 383 RLEAAE-EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQAL-EKARALCGL-PDLTPENAE-DYLAA-FRAKEQQATEEV 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 512 KEMQDRLKVAQDSASQQEKA--------------------------------QLEQLQALQAELMSSRTELETLKSTVTS 559
Cdd:COG3096 458 LELEQKLSVADAARRQFEKAyelvckiageversqawqtarellrryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 560 SQQSNEQLGTQLSALvaekaglvetvsrkevelsglgAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELV 639
Cdd:COG3096 538 LEEFCQRIGQQLDAA----------------------EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 640 SLRwaslraALEEAGKIVQDSLNQLEDPAHISCTSSADYLVSRCQValdcVERLR 694
Cdd:COG3096 596 ELA------ARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL----LERER 640
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
373-578 |
7.85e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 373 DKDRLIEQL----TAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQ-----------THLKQQALGESEFLRAE 437
Cdd:pfam10174 447 EKERIIERLkeqrEREDRERLEELESLKKEN----KDLKEKVSALQPELTEKesslidlkehaSSLASSGLKKDSKLKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 438 LDDLRRVKEDTEKEQRSL---SEIERKAQANEQRYTKLKEKYTElVQSHADLLRK-NAEVTRQMTVARAAQDE------- 506
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQE-VARYKEESGKaQAEVERLLGILREVENEkndkdkk 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 507 ------------------VENVK-KEMQDRLKVAQ-------DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSS 560
Cdd:pfam10174 602 iaelesltlrqmkeqnkkVANIKhGQQEMKKKGAQlleearrREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST 681
|
250
....*....|....*...
gi 261244998 561 QQSNEQLGTQLSALVAEK 578
Cdd:pfam10174 682 QQSLAEKDGHLTNLRAER 699
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-638 |
1.46e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 333 VDTDIPPLTGTgdskfddLFGTSAATDPFNFNSQNGMR------KDDKDRLIEQLTAELQALKEELESFRLESGR----- 401
Cdd:pfam15921 229 LDTEISYLKGR-------IFPVEDQLEALKSESQNKIElllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSiqsql 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 402 --------------LCQ--ALRGRVNELEAELAEQTHL---------KQQALGESEFLRAE------------LDD-LRR 443
Cdd:pfam15921 302 eiiqeqarnqnsmyMRQlsDLESTVSQLRSELREAKRMyedkieeleKQLVLANSELTEARterdqfsqesgnLDDqLQK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 444 VKEDTEKEQRSLSeIERkaQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENvkkEMQDRLKVAQD 523
Cdd:pfam15921 382 LLADLHKREKELS-LEK--EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 524 SASQQEK-----AQLEQ----LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSG 594
Cdd:pfam15921 456 KNESLEKvssltAQLEStkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH 535
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 261244998 595 LGAELERLQNSLTNeresgvkaAEALQNQLNEKESREQALESEL 638
Cdd:pfam15921 536 LKNEGDHLRNVQTE--------CEALKLQMAEKDKVIEILRQQI 571
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
371-515 |
1.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 371 KDDKDRLIEQLTAELQALKEELEsfrLESGRLCQALRgrvNELEAELAEQT-HLKQQalgESEFLRAElDDLRRVKEDTE 449
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLR---NEFEKELRERRnELQKL---EKRLLQKE-ENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261244998 450 KEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLrknaEVTRQMTVARAAQDEVENVKKEMQ 515
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAEEAKEILLEKVEEEAR 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-551 |
1.91e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEqthlKQQALGEsefLRAELDDLRRVKEDTE 449
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE----LEAALRD---LESRLGDLKKERDELE 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KE----QRSLSEIERKAQANEQRYTKLKEKYTELVQSHA---DLLRKNAEVTRQMTVARAAQDEVENVKKEMQD----RL 518
Cdd:TIGR02169 896 AQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNM 975
|
170 180 190
....*....|....*....|....*....|...
gi 261244998 519 KVAQDSASqqEKAQLEQLQALQAELMSSRTELE 551
Cdd:TIGR02169 976 LAIQEYEE--VLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-642 |
1.93e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 435 RAELDDLRRVKEDTEKEQRSLSEIE-----------------------RKAQANEQRYTKLKEK-----YTELVQSHADL 486
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEeveenierldliidekrqqlerlRREREKAERYQALLKEkreyeGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 487 LRKNAEVTRQMTVARAAQD----EVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQ 562
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 563 SNEQLGTQLSALVAEkaglvetVSRKEVELSGLGAELERLQ---NSLTNERESGVKAAEALQNQLNEKESREQALESELV 639
Cdd:TIGR02169 316 ELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
...
gi 261244998 640 SLR 642
Cdd:TIGR02169 389 DYR 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-642 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 484 ADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQ----------DSASQQE-----KAQLEQLQALQAELMSSRT 548
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeiDVASAEReiaelEAELERLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 549 ELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNER-------ESGVKAAEALQ 621
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaalgdAVERELRENLE 772
|
170 180
....*....|....*....|.
gi 261244998 622 NQLNEKESREQALESELVSLR 642
Cdd:COG4913 773 ERIDALRARLNRAEEELERAM 793
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
476-643 |
2.75e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.00 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 476 YTELVQSHADLLRKnaevtrqmtvARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTEL-ETLK 554
Cdd:pfam08614 2 FLELIDAYNRLLDR----------TALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELaELYR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 555 STVTSSQQ---SNEQLGT----------QLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLtneresgvkaaEALQ 621
Cdd:pfam08614 72 SRGELAQRlvdLNEELQElekklrederRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDEL-----------VALQ 140
|
170 180
....*....|....*....|....*
gi 261244998 622 NQLNEKESREQALESE---LVSlRW 643
Cdd:pfam08614 141 LQLNMAEEKLRKLEKEnreLVE-RW 164
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
352-666 |
2.98e-04 |
|
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: 44.56 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 352 FGTSAATDPFNFNSQNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQaLRGRVNELEAELAEQTHLKQQALGES 431
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELED-LAQTSDKLEKLVEQNTDLRLEKLGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 432 EflraelDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEkytelvqshadlLRKNAEVTRQMtvarAAQDEVENVK 511
Cdd:COG5185 274 A------ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA------------TESLEEQLAAA----EAEQELEESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 512 KEMQDRLKVAQDSASQQEKAQLEQLQALQAELMS---------SRTELETLKSTVTSSQQSNEQLGTQLSALVAE-KAGL 581
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIENivgevelskSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLATL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 582 VETVSRKEVELsglgAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSL 661
Cdd:COG5185 412 EDTLKAADRQI----EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEEL 487
|
....*
gi 261244998 662 NQLED 666
Cdd:COG5185 488 TQIES 492
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
377-543 |
3.13e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 377 LIEQLTAELQALKEELESFRLESGRLcQALRGRVNELEAELAeqtHLKQQALGESEFLRAELDDLRRV-----------K 445
Cdd:PRK11637 73 LLAQLKKQEEAISQASRKLRETQNTL-NQLNKQIDELNASIA---KLEQQQAAQERLLAAQLDAAFRQgehtglqlilsG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 446 EDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLkVAQDSA 525
Cdd:PRK11637 149 EESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTL-TGLESS 227
|
170
....*....|....*...
gi 261244998 526 SQQEKAQLEQLQALQAEL 543
Cdd:PRK11637 228 LQKDQQQLSELRANESRL 245
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
437-664 |
3.33e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.44 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 437 ELDDLRRVKEDTEKEQRSLSEIER------KAQANEQRytklKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENV 510
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDLQQalslldKIDASKQR----AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 511 K---KEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVET-VS 586
Cdd:pfam12795 77 SlslEELEQRLLQTSAQLQELQ----NQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAqRW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 587 RKEVELSGLGAE---LERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQ 663
Cdd:pfam12795 153 ALQAELAALKAQidmLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
.
gi 261244998 664 L 664
Cdd:pfam12795 233 H 233
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
383-567 |
3.36e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 383 AELQALKEELESFRlesgrlcqalrGRVNELEAELAEQTHLKQQALGESEFLRAEL----DDLRRVKEDTEKEQRSLSE- 457
Cdd:pfam00261 1 KKMQQIKEELDEAE-----------ERLKEAMKKLEEAEKRAEKAEAEVAALNRRIqlleEELERTEERLAEALEKLEEa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 458 -------------IERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTV-------ARAAQDEVENVKKEMQDR 517
Cdd:pfam00261 70 ekaadesergrkvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVvegdlerAEERAELAESKIVELEEE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 518 LKVA----------QDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQL 567
Cdd:pfam00261 150 LKVVgnnlksleasEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-635 |
3.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 369 MRKDDKDRLIEQLTAELQALKEELEsfRLESGRLCQALRGRVNELEAELAEQT-HLKQQALGESEFLRaeLDDLRRVKED 447
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAAAAIeYLKAAKAGRATFLP--LDKIRARAAL 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 448 TEKEQRSLSEIERKAQANEQRYTKLKEK---YTELVQSHADLLRKNA------------EVTRQMTVARAAQDEVENVKK 512
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYvlgDTLLGRTLVAARLEAAlrravtlagrlrEVTLEGEGGSAGGSLTGGSRR 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 513 EMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKstvtssQQSNEQLGTQLSALVAEKAGLVETVSRKEVEL 592
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA------EAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 261244998 593 SGLGAELERLQnsltnERESGVKAAEALQNQLNEKESREQALE 635
Cdd:COG1196 743 EEEELLEEEAL-----EELPEPPDLEELERELERLEREIEALG 780
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
362-601 |
4.67e-04 |
|
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: 44.27 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 362 NFNSQNGMRKDDKDRLIEQLTAELQAlKEELESFRLESGRLCQALRGRVNELEAEL--AEQTHLKQQaLGESEFLRAELD 439
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQS-KERLKQEQADEIRDEKKGLGRTIELKKEIleKKQEELKFV-IKELQQLEGSSD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 440 DLRRVKEDTEKEQRSLSEIERKA--QANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvaraAQDEVENVKKEMQDR 517
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT----TRTQMEMLTKDKMDK 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 518 LKVAQDSASQQE------------KAQLEQ-LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVET 584
Cdd:TIGR00606 548 DEQIRKIKSRHSdeltsllgyfpnKKQLEDwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
250 260
....*....|....*....|...
gi 261244998 585 V------SRKEVELSGLGAELER 601
Cdd:TIGR00606 628 LfdvcgsQDEESDLERLKEEIEK 650
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
432-666 |
4.93e-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: 44.40 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 432 EFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKytelVQSHADLLRKnAEVTRQMTVARaaQDEVENVK 511
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQ----LQAETELCAE-AEEMRARLAAR--KQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 512 KEMQDRLKVAQDSASQ--QEKAQLEQ-LQALQAEL---MSSRTELETLKSTVTSSQQSNEQ----LGTQLSALVAEKAGL 581
Cdd:pfam01576 78 HELESRLEEEEERSQQlqNEKKKMQQhIQDLEEQLdeeEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 582 VETVSrkevELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALE----------SEL------VSLRWAS 645
Cdd:pfam01576 158 EERIS----EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEkakrklegesTDLqeqiaeLQAQIAE 233
|
250 260
....*....|....*....|.
gi 261244998 646 LRAALEEAGKIVQDSLNQLED 666
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEE 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
402-666 |
5.68e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 402 LCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEierkaqaNEQRYTKLKEKYTELVQ 481
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-------DLQIATKTICQLTEEKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 482 SHADLLRKnAEVTRQMTVAraaqdEVENVKKEMQDRLKVAQDSASQQEkaqlEQLQALQAELMSSRTELETLKSTVTSSQ 561
Cdd:pfam05483 335 AQMEELNK-AKAAHSFVVT-----EFEATTCSLEELLRTEQQRLEKNE----DQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 562 QSNEQLGTQLS---ALVAEKA---GLVETVSRKEVELSGLGA-------ELERLQNSLTNERESGVKAAEALQNQL-NEK 627
Cdd:pfam05483 405 VELEELKKILAedeKLLDEKKqfeKIAEELKGKEQELIFLLQarekeihDLEIQLTAIKTSEEHYLKEVEDLKTELeKEK 484
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 261244998 628 -ESREQALESELVSLRWASLraaLEEAGKIVQDSLNQLED 666
Cdd:pfam05483 485 lKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQED 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
500-665 |
7.68e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 500 ARAAQDEVENVKKEMQDrlkvaqdsASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKA 579
Cdd:COG4372 33 LRKALFELDKLQEELEQ--------LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 580 GLVETVSRKEVELSGLGAELERLQ---NSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKI 656
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
....*....
gi 261244998 657 VQDSLNQLE 665
Cdd:COG4372 185 LDELLKEAN 193
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-642 |
7.69e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQaLGESEflrAELDDLRRVKEDTEKEQRSLSEI 458
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ-TQQSH---AYLTQKREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 459 ERK---AQANEQRYTKLKEKYTE-------------LVQSHADLLRKNAEVTRQMTvaraaqdeveNVKKEMQDRLKVAQ 522
Cdd:TIGR00618 266 RARieeLRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMR----------SRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 523 DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQ-----------LGTQLSALVAEKAGLVETVSRKEVE 591
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqkttLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 261244998 592 LSG---LGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLR 642
Cdd:TIGR00618 416 TSAfrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
361-638 |
8.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 361 FNFNSQNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQalgesefLRAELDD 440
Cdd:COG4372 16 FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 441 LRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKV 520
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 521 AQDSASQQEKAQLEQ-LQALQAELMSSRTELETLKST-VTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAE 598
Cdd:COG4372 169 LEQELQALSEAEAEQaLDELLKEANRNAEKEEELAEAeKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 261244998 599 LERLQNSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
424-655 |
9.30e-04 |
|
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: 43.19 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 424 KQQalgESEFLRAELDDLRRVKEDTEKE---QRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVA 500
Cdd:pfam17380 287 RQQ---QEKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 501 RAAQDEVENVKKEMQ--DRLKVAQDSASQQEKAQLE---QLQALQAELMSSRTELETLKSTVTSSQQSNEQLgtQLSALV 575
Cdd:pfam17380 364 RIRQEEIAMEISRMRelERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 576 AEKAGLVETVSRKEVELSglgAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRwaslRAALEEAGK 655
Cdd:pfam17380 442 EERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK----QAMIEEERK 514
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
378-652 |
9.37e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRL-----ESGRLCQALRGRvnelEAELAEQTHLKQqalgeseflrAElDDLRRVKEDTekeq 452
Cdd:pfam05701 182 VEELTIELIATKESLESAHAahleaEEHRIGAALARE----QDKLNWEKELKQ----------AE-EELQRLNQQL---- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 453 RSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTvaRAAQDEVENVKKEMQD-RLKVaqdsasqqEKA 531
Cdd:pfam05701 243 LSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTS--TSIQAALASAKKELEEvKANI--------EKA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 532 QLEqLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAE---KAGLVETVSRKEVELSGLGAELERLQNSLTN 608
Cdd:pfam05701 313 KDE-VNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAElnrTKSEIALVQAKEKEAREKMVELPKQLQQAAQ 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 261244998 609 ERESGVKAAEALQNQLNE-KESREQALESelVSLRWASLRAALEE 652
Cdd:pfam05701 392 EAEEAKSLAQAAREELRKaKEEAEQAKAA--ASTVESRLEAVLKE 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
471-641 |
9.84e-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: 41.83 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 471 KLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQD-RLKVAQ-DSASQQEKAQLEQLQALQAELMSSRt 548
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlEKEIKRlELEIEEVEARIKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 549 ELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQnsltNERESGVKAAEALQNQLNEK- 627
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK----AELDEELAELEAELEELEAEr 165
|
170
....*....|....
gi 261244998 628 ESREQALESELVSL 641
Cdd:COG1579 166 EELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
377-665 |
1.03e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 377 LIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQrsls 456
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---- 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 457 eierKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQdrlkvaqdsASQQEKAQLEQ- 535
Cdd:TIGR00618 477 ----TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ---------RGEQTYAQLETs 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 536 LQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGL----------VETVSRKEVELSGLG-AELERLQN 604
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqnitvrlqdlTEKLSEAEDMLACEQhALLRKLQP 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261244998 605 SLTNERESGV--KAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQDSLNQLE 665
Cdd:TIGR00618 624 EQDLQDVRLHlqQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
456-653 |
1.04e-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: 43.29 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 456 SEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQ 535
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 536 LQALQAELMSSRTELETLkstvTSSQQSNEQLGTQLSALVAEKaglvetvsrkevelsgLGAELERLQNSLTNERESGVK 615
Cdd:pfam12128 349 LPSWQSELENLEERLKAL----TGKHQDVTAKYNRRRSKIKEQ----------------NNRDIAGIKDKLAKIREARDR 408
|
170 180 190
....*....|....*....|....*....|....*...
gi 261244998 616 AAEALQNQLnekesreQALESELVSLRWASLRAALEEA 653
Cdd:pfam12128 409 QLAVAEDDL-------QALESELREQLEAGKLEFNEEE 439
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
370-653 |
1.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLEsgrlCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIERKAQA-------------------------NEQRYTKLKEKYTELVQSHADLlrkNAEVTRQMTVARAAQ 504
Cdd:PRK02224 433 ATLRTARERVEEAEAlleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEV---EERLERAEDLVEAED 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 505 --DEVENVKKEMQDRLKVAQDSA-SQQEKAQL--EQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKA 579
Cdd:PRK02224 510 riERLEERREDLEELIAERRETIeEKRERAEElrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 580 GLvETVSRKEVELSGLGAELERLqnsltNERESGVKAAEAL-QNQLNEKESREQALESELVSLRWASLRAALEEA 653
Cdd:PRK02224 590 SL-ERIRTLLAAIADAEDEIERL-----REKREALAELNDErRERLAEKRERKRELEAEFDEARIEEAREDKERA 658
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
404-648 |
1.12e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 404 QALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRV---------------KEDTEKEQRSLSEIERKAQANEQR 468
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLlpqanlladetladrLEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 469 YTKLKEKYTEL---VQSHADLLRKNAEVTRQMTVARAA----------------QDEVENVKK--EMQDRLKVAQDSASQ 527
Cdd:COG3096 919 LAQLEPLVAVLqsdPEQFEQLQADYLQAKEQQRRLKQQifalsevvqrrphfsyEDAVGLLGEnsDLNEKLRARLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 528 QEKAQLEQLQALQAELMSSRTELETLKS-------TVTSSQQSNEQLGTQLSALVAEKAGlvETVSRKEVELSGLGAELE 600
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLASLKSsrdakqqTLQELEQELEELGVQADAEAEERAR--IRRDELHEELSQNRSRRS 1076
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261244998 601 RLQNSLT-NERESgvkaaEALQNQLNEKESREQALESELVS--LRWASLRA 648
Cdd:COG3096 1077 QLEKQLTrCEAEM-----DSLQKRLRKAERDYKQEREQVVQakAGWCAVLR 1122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
436-638 |
1.35e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRVKEDTEKEqrsLSEIERKAQANEQRYTKLKEKYTELvqsHADLLRKNAEVtrqmtvaraaqDEVENVKKEMQ 515
Cdd:COG1579 17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDL---EKEIKRLELEI-----------EEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 516 DRLKVAQDSasqqekaqlEQLQALQAELmssrteletlkstvtssqqsnEQLGTQLSALVAEKAGLVETVSRKEVELSGL 595
Cdd:COG1579 80 EQLGNVRNN---------KEYEALQKEI---------------------ESLKRRISDLEDEILELMERIEELEEELAEL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261244998 596 GAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESEL 638
Cdd:COG1579 130 EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
370-443 |
1.79e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261244998 370 RKDDKDRLIEQLTAEL---QALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRR 443
Cdd:PRK09039 75 GNQDLQDSVANLRASLsaaEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRR 151
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
502-658 |
1.98e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 502 AAQDEVENVKKEMQDRLKVAQDSASQ-QEKAQ--LEQLQALQAELMSSRTELETLKSTVtssqqsNEQLGTQLSALVAEk 578
Cdd:cd22656 107 TDDEELEEAKKTIKALLDDLLKEAKKyQDKAAkvVDKLTDFENQTEKDQTALETLEKAL------KDLLTDEGGAIARK- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 579 aglvetvsrkevELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWA--SLRAALEEAGKI 656
Cdd:cd22656 180 ------------EIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDldNLLALIGPAIPA 247
|
..
gi 261244998 657 VQ 658
Cdd:cd22656 248 LE 249
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
378-658 |
2.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 378 IEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEqthlkqqalgesefLRAELDDLR-RVKEDTEKEQrslS 456
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEI----EELKEKRDELNEELKE--------------LAEKRDELNaQVKELREEAQ---E 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 457 EIERKAQANEQrYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQdRLKVAQDSAS---QQEKAQL 533
Cdd:COG1340 62 LREKRDELNEK-VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE-RLEWRQQTEVlspEEEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 534 EQLQALQAELMSSRTELETLKSTVTSSQQSnEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ---NSLTNER 610
Cdd:COG1340 140 EKIKELEKELEKAKKALEKNEKLKELRAEL-KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRkeaDELHKEI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261244998 611 ESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQ 658
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
381-669 |
2.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 381 LTAELQALKEELESFRLESgrlcqalrGRVNELEAELaeQTHLKQQalgeseflrAELDDLRR-VKedtEKEQRSLSEIE 459
Cdd:pfam05622 109 LAEEAQALKDEMDILRESS--------DKVKKLEATV--ETYKKKL---------EDLGDLRRqVK---LLEERNAEYMQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 460 RKAQANEQrytklkekytelvqshadlLRKnaevtrqmtvARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLE----- 534
Cdd:pfam05622 167 RTLQLEEE-------------------LKK----------ANALRGQLETYKRQVQELHGKLSEESKKADKLEFEykkle 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 535 -QLQALQAELMSSRTELETLKSTVTS---SQQSNEQLgTQLSALVAEKAGLVETVSrKEVELSGLGAELERLQNS----L 606
Cdd:pfam05622 218 eKLEALQKEKERLIIERDTLRETNEElrcAQLQQAEL-SQADALLSPSSDPGDNLA-AEIMPAEIREKLIRLQHEnkmlR 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 607 TNERESGVKAAEALQNQLNEKESREQALESE--LVSLRWASLRAALEEAGKIVQDSLNQLEDPAH 669
Cdd:pfam05622 296 LGQEGSYRERLTELQQLLEDANRRKNELETQnrLANQRILELQQQVEELQKALQEQGSKAEDSSL 360
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
434-555 |
2.70e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.16 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 434 LRAELDDLRRVKEDTEKEQRSLSEiERKAQAneQRYTKLKEKYTELVQSHadllrknAEVTRQMTVARAAQDEVENVKKE 513
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQE-DLEKQA--EIAREAQQNYERELVLH-------AEDIKALQALREELNELKAEIAE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 261244998 514 MQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKS 555
Cdd:pfam07926 76 LKAEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
432-566 |
2.78e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.53 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 432 EFLRAELD-DLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELvQSHADLLRKNAEVTRQMTvaRAAQDEVENV 510
Cdd:pfam05262 184 EALREDNEkGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKA-QQKADFAQDNADKQRDEV--RQKQQEAKNL 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261244998 511 KK-----EMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQ 566
Cdd:pfam05262 261 PKpadtsSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAED 321
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
379-637 |
2.88e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEELESFRLESGRL---CQALRGRVNELEAELAEQTHLKQQ-ALGES-----EFLRAEL--DDLRRVKED 447
Cdd:pfam05622 207 DKLEFEYKKLEEKLEALQKEKERLiieRDTLRETNEELRCAQLQQAELSQAdALLSPssdpgDNLAAEImpAEIREKLIR 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 448 TEKEQRSLSEieRKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAqdeVENVKKEMQDRLKVAQDSASQ 527
Cdd:pfam05622 287 LQHENKMLRL--GQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ---VEELQKALQEQGSKAEDSSLL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 528 QEK--AQLEQLQALQAELMSSRTELETLKSTVTSS-QQSNEQLGTQLSALVAEKAGLVETVSR-----KEVeLSGLGAel 599
Cdd:pfam05622 362 KQKleEHLEKLHEAQSELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEDMKAMEERYKKyvekaKSV-IKTLDP-- 438
|
250 260 270
....*....|....*....|....*....|....*...
gi 261244998 600 eRLQNSLTNEresgvkaAEALQNQLNEKESREQALESE 637
Cdd:pfam05622 439 -KQNPASPPE-------IQALKNQLLEKDKKIEHLERD 468
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
379-665 |
2.89e-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: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEELESFRLESGR-----------LCQALRGRVNELEAELAEQTHLKQQALGESEFLraeLDDLRRVKED 447
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLR---LNQATATPEL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 448 TEKEQRSLSEIERKAQANEQRytklkekytelvqshadllRKNAE-VTRQMTVARAAQDEvenvkkemqdrlkvaQDSAS 526
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAA-------------------NAEVErLQSELRQARKRRDQ---------------ASEAL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 527 QQEKAQLEQLQALQAELM-----SSRTELETLKSTVTSSQQS------NEQLGTqlSALVAEkagLVETVSRKEVELSGL 595
Cdd:pfam12128 509 RQASRRLEERQSALDELElqlfpQAGTLLHFLRKEAPDWEQSigkvisPELLHR--TDLDPE---VWDGSVGGELNLYGV 583
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261244998 596 GAELERLQNSLTNERESGVKA-AEALQNQLNEKESREQALESELVslrwaSLRAALEEAGKIVQDSLNQLE 665
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRErLDKAEEALQSAREKQAAAEEQLV-----QANGELEKASREETFARTALK 649
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
379-573 |
3.53e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEEL---ESFRLESGRLCQALRGRVNELEAELAEQT-------HLKQQAL-GESEFLRAELDDLRRVKED 447
Cdd:COG3096 451 QQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTarellrrYRSQQALaQRLQQLRAQLAELEQRLRQ 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 448 TEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKV---AQDS 524
Cdd:COG3096 531 QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDA 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 525 ASQ---QEKAQLEQLQALQA---ELMSSRTELETLKSTVTSSQQSNEQLGTQLSA 573
Cdd:COG3096 611 LERlreQSGEALADSQEVTAamqQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
366-642 |
3.62e-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: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 366 QNGMRKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGR------VNELEAELAEQTHLKQQALGEsefLRAELD 439
Cdd:TIGR00606 360 QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQedeaktAAQLCADLQSKERLKQEQADE---IRDEKK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 440 DLRRV----KEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADL--LRKNAEVTRQMTVARAAQDEVENVKKE 513
Cdd:TIGR00606 437 GLGRTielkKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 514 MQdrlKVAQDSAS-QQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQS-------NEQLGTQLSALVAEKAGLVETV 585
Cdd:TIGR00606 517 LR---KLDQEMEQlNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnKKQLEDWLHSKSKEINQTRDRL 593
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261244998 586 SRKEVELsglgAELERLQNSLTNERESGVKAAEALQNQLNEKESrEQALESELVSLR 642
Cdd:TIGR00606 594 AKLNKEL----ASLEQNKNHINNELESKEEQLSSYEDKLFDVCG-SQDEESDLERLK 645
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
391-637 |
3.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 391 ELESFRLESGRLCQALRGRVNELEAELAEQTHLK--QQALGESEFLRAEldDLRRVKEDTEKEQRSLSEIERKAQ----- 463
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKkaEDARKAEEARKAE--DARKAEEARKAEDAKRVEIARKAEdarka 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 464 -----ANEQRYTKLKEKYTELvqSHADLLRKnAEVTRQMTVARAAQDE--VENVKK-------EMQDRLKVAQDSASQQE 529
Cdd:PTZ00121 1167 eearkAEDAKKAEAARKAEEV--RKAEELRK-AEDARKAEAARKAEEErkAEEARKaedakkaEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 530 KAQLEQLQALQAELMSSRTELETLKSTVTSSQQSN--EQLGTQLSALVAEKAGLVETVsrKEVELSGLGAELERLQNSLT 607
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADEAK 1321
|
250 260 270
....*....|....*....|....*....|
gi 261244998 608 NERESGVKAAEALQNQLNEKESREQALESE 637
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
372-580 |
4.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 372 DDKDRLIEQLTAELQALKEELESFRLESgrlcQALRGRVNELEAELAEQTH-LKQQA---------------LGESEFLR 435
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEI----DKLQAEIAEAEAEIEERREeLGERAralyrsggsvsyldvLLGSESFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 436 AELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQ 515
Cdd:COG3883 116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261244998 516 DRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAG 580
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
526-640 |
4.60e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 526 SQQEKAQL-EQLQALQAELMSSRTELETLKST----VTSSQQSNEQLGTQLSAlvaekaglvETVSRKEVElsglgAELE 600
Cdd:pfam09787 52 LRQERDLLrEEIQKLRGQIQQLRTELQELEAQqqeeAESSREQLQELEEQLAT---------ERSARREAE-----AELE 117
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 261244998 601 RLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVS 640
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTS 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
525-621 |
4.64e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 525 ASQQEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQ 603
Cdd:COG4942 17 AQADAAAEAEaELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90
....*....|....*...
gi 261244998 604 NSLTNERESGVKAAEALQ 621
Cdd:COG4942 97 AELEAQKEELAELLRALY 114
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-586 |
4.86e-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: 39.91 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 375 DRLIEQLTAELQALKEELEsfrlesgrlcqalrgrvnELEAELAEqthlkqqalgesefLRAELDDLRRVKEDTEKEQRs 454
Cdd:COG1579 16 DSELDRLEHRLKELPAELA------------------ELEDELAA--------------LEARLEAAKTELEDLEKEIK- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 455 lsEIERKAQANEQRYTKLKEKYTElvqshadlLRKNAEVTrqmtvarAAQDEVENVKKEMQDRLKVAQDSASQQEKAQlE 534
Cdd:COG1579 63 --RLELEIEEVEARIKKYEEQLGN--------VRNNKEYE-------ALQKEIESLKRRISDLEDEILELMERIEELE-E 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 261244998 535 QLQALQAELMSSRTELETLKSTVtssQQSNEQLGTQLSALVAEKAGLVETVS 586
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKIP 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
370-610 |
4.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESfrlesgrlcqaLRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEE-----------LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 450 KEQRSLSEIER---KAQANEQRYTKLKEKYTELvqshadllrknAEVTRQmtvARAAQDEVENVKKEMQDRLKVAQDSAS 526
Cdd:PRK02224 586 ERIESLERIRTllaAIADAEDEIERLREKREAL-----------AELNDE---RRERLAEKRERKRELEAEFDEARIEEA 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 527 QQEKAQLEQLQALQA----ELMSSRTELETLKSTVTSSQQSNEQLGTQLSALvAEKAGLVETVSRKEVELSGLGAELE-- 600
Cdd:PRK02224 652 REDKERAEEYLEQVEekldELREERDDLQAEIGAVENELEELEELRERREAL-ENRVEALEALYDEAEELESMYGDLRae 730
|
250
....*....|.
gi 261244998 601 -RLQNSLTNER 610
Cdd:PRK02224 731 lRQRNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-497 |
5.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTE 449
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261244998 450 KEQRSLSEIERKAQA----N----------EQRYTKLKEKYTELVQSHADLLRKNAEVTRQM 497
Cdd:COG1196 764 ELERELERLEREIEAlgpvNllaieeyeelEERYDFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
409-652 |
6.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 409 RVNELEAELAEqthlkqqalgesefLRAELDDLRRVKEDTEKE-QRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLL 487
Cdd:COG4372 39 ELDKLQEELEQ--------------LREELEQAREELEQLEEElEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 488 RKNAEVTRQMTVARAAQDEVENVKKEmQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTV--TSSQQSNE 565
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqaLSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 566 QLGTQLSALVAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWAS 645
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
....*..
gi 261244998 646 LRAALEE 652
Cdd:COG4372 264 ELAILVE 270
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
370-663 |
6.87e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEE-LESFRLESGRLcqALRGRVNELEAELAEQTHLKQQalgesefLRAELDDLRRVKEDT 448
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKILDEiLEINSLERNYD--KLKDVIDMLRAEISNIDYLEEK-------LKSSNLELENIKKQI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTR-QMTVARA----AQDEVENVK-KEMQDRLKVAQ 522
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyESEIKTAesdlSMELEKNNYyKELEERHMKII 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 523 DSASQQEKAQLEQLQALQAELMSSRTELETLKSTVtssqQSNEQLGTQLSALVAEKAGLVETVSRKEvELSGLGAELERL 602
Cdd:PRK01156 287 NDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEI----NKYHAIIKKLSVLQKDYNDYIKKKSRYD-DLNNQILELEGY 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261244998 603 Q---NSLTNE-------RESGVKAAEALQNQLNEKESREQALESELVSlRWASLRAALEE-AGKIvqDSLNQ 663
Cdd:PRK01156 362 EmdyNSYLKSieslkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKK-ELNEINVKLQDiSSKV--SSLNQ 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
431-658 |
6.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 431 SEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQrytklkekytELVQSHADLLRKNAEVTRQMTVARAAQDEVENV 510
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEE----------ELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 511 KKEMQDRLKVAQDSASQQEKAQLEQlQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEV 590
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKER-QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261244998 591 ELsgLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKIVQ 658
Cdd:COG4372 179 AE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
413-543 |
7.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 413 LEAELAEQTHLKQQALGES--EFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKN 490
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAkeLLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 261244998 491 AevtrqmtvaraaqdEVENVKKEMQDRLKVAQDSASQQEKAQLeqLQALQAEL 543
Cdd:PRK12705 119 L--------------ELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAEL 155
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-553 |
7.39e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 370 RKDDKDRLIEQLTAELQALKEELESFRLESGRLCQALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLR-RVKEDT 448
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeEERELA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 449 EKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQD----RLKVAQDS 524
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvNLLAIEEY 790
|
170 180
....*....|....*....|....*....
gi 261244998 525 ASQQEkaQLEQLQALQAELMSSRTELETL 553
Cdd:COG1196 791 EELEE--RYDFLSEQREDLEEARETLEEA 817
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
524-665 |
7.56e-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: 39.71 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 524 SASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQQSNEQLGTQLSALVAekaglveTVSRKEVELSGLGAELERLQ 603
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA-------AVKAAQAQLAQAQIDLARRR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261244998 604 ----------NSLTNEREsgvkAAEALQNQLNEKESREQALESELVSLRWASLRAALEEAGKiVQDSLNQLE 665
Cdd:pfam00529 131 vlapiggisrESLVTAGA----LVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSG-AQLQIAEAE 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
505-661 |
7.62e-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: 39.14 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 505 DEVENVKKEMQDRLKVAQDsasqqEKAQLE-QLQALQAELMSSRTELETLKSTVTSSQQ----SNEQLGT-----QLSAL 574
Cdd:COG1579 20 DRLEHRLKELPAELAELED-----ELAALEaRLEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLGNvrnnkEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 575 VAEKAGLVETVSRKEVELSGLGAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESELvslrwASLRAALEEAG 654
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-----EELEAEREELA 169
|
....*..
gi 261244998 655 KIVQDSL 661
Cdd:COG1579 170 AKIPPEL 176
|
|
| F-BAR_FCHSD |
cd07654 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains ... |
497-637 |
7.97e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains proteins (FCHSD); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of FCH and double SH3 domain (FCHSD) proteins, so named as they contain an N-terminal F-BAR domain and two SH3 domains at the C-terminus. Vertebrates harbor two subfamily members, FCHSD1 and FCHSD2, which have been characterized only in silico. Their biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153338 [Multi-domain] Cd Length: 264 Bit Score: 39.49 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 497 MTVARAAQDEVENVKKEMQDRLKVAQDSASQQEKAQLEQLQALQAELMSSRTELETLKSTVTSSQqsneqlgtQLSALVA 576
Cdd:cd07654 80 DAVAQSRQNRCEAYRRYISEPAKTGRSAKEQQLKKCTEQLQRAQAEVQQTVRELSKSRKTYFERE--------QVAHLAR 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261244998 577 EKAGLVEtvsrkevelsglgAELERLQNSLTNERESGVKAAEALQNQLNEKESREQALESE 637
Cdd:cd07654 152 EKAADVQ-------------AREARSDLSIFQSRTSLQKASVKLSARKAECSSKATAARND 199
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
405-610 |
8.29e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.09 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 405 ALRGRVNELEAELAEQTHLKQQALGESEFLRAELDDLRRVKEDTEKEQRSLSEIERKAQANEQRYTKLKEKYTELVQSHA 484
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 485 DLlrknAEVTRQMT---VARAAQDEVENVKKEMQDRLK---VAQDSASQQEKAQLEQL-QALQAELMSSRTEL------E 551
Cdd:pfam03528 85 TV----SENTKQEAideVKSQWQEEVASLQAIMKETVReyeVQFHRRLEQERAQWNQYrESAEREIADLRRRLsegqeeE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 552 TLKSTVTSSQQSNEQLGTQLSALVAEKAGLVETVSRKEVELSGLGA-ELERLQNSLTNER 610
Cdd:pfam03528 161 NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEAsKMKELNHYLEAEK 220
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
379-637 |
8.98e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 379 EQLTAELQALKEELESFRLESGRLCQALR--GRVNELEAELAEQTHLKQQALGESEFLRAELDDL------RRVKEDTEK 450
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALslaqpaRQLRPHWER 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 451 EQRSLSEIERKAQANEQRYTKLKEKYTELVQSHADLLRKNAEvtRQMTVARAAQDEVENvkkemqDRLKV-AQDSAS--- 526
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAE--LQAQQQSLNTWLAEH------DRFRQwNNELAGwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 527 --QQEKAQLEQLQALQAELMSSRTELETL-KSTVTSS--------QQSNEQ--LGTQLSALVAEKAGLVETVSRKEVELS 593
Cdd:PRK10246 371 qfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTadevaaalAQHAEQrpLRQRLVALHGQIVPQQKRLAQLQVAIQ 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 261244998 594 GLGAELERLQNSLTNERESGVKAAEALQN--QLNEKESREQALESE 637
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLADvkTICEQEARIKDLEAQ 496
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
553-666 |
9.62e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 553 LKSTVTSSQQSNEQLGTQLSALV-------AEKAGLVETVSRKEVELSGLGAELERLQNsLTNERESGVKAAEALQNQLN 625
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELAdllslerQGNQDLQDSVANLRASLSAAEAERSRLQA-LLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 261244998 626 EKESREQA-----------LESELVSLR--WASLRAALEEAGKIVQDSLNQLED 666
Cdd:PRK09039 123 QELDSEKQvsaralaqvelLNQQIAALRrqLAALEAALDASEKRDRESQAKIAD 176
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
406-543 |
9.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261244998 406 LRGRVNELEAELAEQT--HLKQQALGESEFLRAEL-----DDLRRVKEDTEKEQRS-LSEIERKAQANEQRYTKLKEKYT 477
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEakRILEEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRErRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261244998 478 ELVQSHADLLRKNAEVTRQMTVARAAQDEVENVKKEMQDRLKVAqdSASQQEKAQLEQLQALQAEL 543
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAEEAKEILLEKVEEEA 167
|
|
| |
