|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
30-299 |
7.84e-90 |
|
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: 289.20 E-value: 7.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 30 TQAISISKAINSQEAPVKEKHARRIILGTHH-EKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRY 108
Cdd:pfam07651 1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSsAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 109 RSNIREIGDLWGHLRDQ-YGHLVNIYTKLLLTKISFHLKHPQFPAGLEVTDEVLeKAAGTDVNNIFqLTVEMFDYMDCEL 187
Cdd:pfam07651 81 RRRISSLLRISSFSLSWdYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGS-LVAVGDPNERY-LTMSMEDLLDSIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 188 KLSESVFRQLNTAIAVSQMsSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSCLP------ADTLQGHRDRFHEQFHSLR 261
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNAL-SNECIIAALILLVKESFGLYRAINEGIINLLEKFFelskpdADRALGIYKRFVKQFERLK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 672073093 262 NFFRRASDMLYFKRLIqIPRLPEGPPNFLRasALAEHI 299
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLE--ALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
822-1020 |
3.75e-89 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 284.26 E-value: 3.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 822 GVKLEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVESADKV 901
Cdd:smart00307 1 GVELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 902 VLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVNERAANVVASTKSGQEQ-IEDRDTMDFSGLS 980
Cdd:smart00307 81 VTGKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 672073093 981 LIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHYVLA 1020
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
1.71e-80 |
|
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: 257.49 E-value: 1.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 31 QAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17014 1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 672073093 111 NIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFH 144
Cdd:cd17014 81 NIRETGSLWGHLHDRYGQLVSLYTKLLCTKIEFH 114
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
1.18e-65 |
|
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: 216.38 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 31 QAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17006 1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80
|
90 100 110
....*....|....*....|....*....|....
gi 672073093 111 NIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFH 144
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 ... |
872-1017 |
1.58e-53 |
|
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: 183.55 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 872 KNSRWTEGLISASKAVGWGATQLVESADKVVLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVN 951
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQGQGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 952 ERAANVVASTKSGQEQIEDRD--TMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHY 1017
Cdd:pfam01608 81 DATKNLVAAVKSAAELQEEEIeeEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHY 148
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
31-144 |
3.15e-51 |
|
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: 175.61 E-value: 3.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 31 QAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRS 110
Cdd:cd17013 1 QTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKN 80
|
90 100 110
....*....|....*....|....*....|....
gi 672073093 111 NIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFH 144
Cdd:cd17013 81 ELSDMSRMWGHLSEGYGQLCSIYLKLLITKMEFH 114
|
|
| HIP1_clath_bdg |
pfam16515 |
Clathrin-binding domain of Huntingtin-interacting protein 1; HIP1_clath_bdg is the coiled-coil ... |
462-560 |
6.09e-37 |
|
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: 134.37 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 462 HAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQ 541
Cdd:pfam16515 1 HADLLRKNAETTKQLTVAQQAQEEVEREKKQLEFELERAKEEAQMKLEEQKEELERLKRELESSRAELATLQSTLQSSEQ 80
|
90
....*....|....*....
gi 672073093 542 SGSELSSRLDTLNAEKEAL 560
Cdd:pfam16515 81 SGSQLSSQLAALQAEKEGL 99
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
30-151 |
2.80e-36 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 133.52 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 30 TQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSS--ILSWKFCHVLHKVLRDGHPNVLHDCQR 107
Cdd:smart00273 2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKnwRVVYKALILLHYLLRNGSPRVILEALR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 672073093 108 YRSNIREIGDLWGHLRDQ--YGHLVNIYTKLLLTKISFHLKHPQFP 151
Cdd:smart00273 82 NRNRILNLSDFQDIDSRGkdQGANIRTYAKYLLERLEDDRRLKEER 127
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
34-144 |
3.83e-24 |
|
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: 98.22 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 34 SISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIR 113
Cdd:cd16986 4 AVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSLLGGYLDAWLP 83
|
90 100 110
....*....|....*....|....*....|....
gi 672073093 114 EIGDL---WGHLRDQYGHLVNIYTKLLLTKISFH 144
Cdd:cd16986 84 ELVRVkntQQSLSEFYSQLIKKYVRYLELKVVFH 117
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
33-144 |
1.58e-22 |
|
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: 93.52 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 33 ISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNI 112
Cdd:cd17007 3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82
|
90 100 110
....*....|....*....|....*....|...
gi 672073093 113 REIGDLW-GHLRDQYGHLVNIYTKLLLTKISFH 144
Cdd:cd17007 83 ESLGRQSsGSGAKGYGRLIKEYVRYLLDKLAFH 115
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
356-639 |
1.36e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVET------LRAELEKIKMEAQ-RYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLK----ALQ 424
Cdd:COG1196 201 QLEPLERQAEKaeryreLKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRleleELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 425 LEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAfQMEQVKRES 504
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELE-EAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALsgaiRQREAELLAAQSLVREKEEA 584
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERLERLEEELEELEEALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 672073093 585 LSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDA 639
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-686 |
1.09e-19 |
|
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: 95.51 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKReVETLRAELEKikmeaqryisqlkgQVNSLEA---------ELEEQRKQKQKALVDNEQLRHElAQLKALQLEGA 428
Cdd:TIGR02168 186 ENLDR-LEDILNELER--------------QLKSLERqaekaerykELKAELRELELALLVLRLEELR-EELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNadtakqltvtQQSQEEVARVKEQLAFQMEQVKReSEMKM 508
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----------YALANEISRLEQQKQILRERLAN-LERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 509 EEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLV---REKEEAL 585
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 586 SQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDplHLRCTSSPDYLVSRAQAA 665
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEEAEQA 476
|
330 340
....*....|....*....|.
gi 672073093 666 LDSVSGLEKGHTQYLASSEAL 686
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-634 |
1.81e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRY---ISQLKGQVNSLEAELEEQRKQKQKAlvdNEQLRHELAQLKALQLEGAR 429
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELeaeLEELEAELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqmEQVKRESEMKME 509
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA----EEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQ 589
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 672073093 590 QRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEA 634
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-617 |
1.82e-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: 81.64 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRYISQ---LKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQlegar 429
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEEleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 nQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQMEQVKRESEMKME 509
Cdd:TIGR02168 298 -SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQ 589
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260
....*....|....*....|....*....
gi 672073093 590 QRSAQEKGE-LQGRLAEKESQEQGLQQKL 617
Cdd:TIGR02168 456 LERLEEALEeLREELEEAEQALDAAEREL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-615 |
9.25e-15 |
|
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: 79.34 E-value: 9.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEaqryISQLKGQVNSLEAELEEQRKqKQKALVDNEQLRHElAQLKALQLEGARNQGLRE 435
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEE----ISELEKRLEEIEQLLEELNK-KIKDLGEEEQLRVK-EKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSD-- 513
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyr 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 514 -QLEKLKRELVAKAGELAHAQEALSRTEQSGSELS-------SRLDTLNAEKEALSGAIRQREAEL--LAAQ-SLVREKE 582
Cdd:TIGR02169 392 eKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieAKINELEEEKEDKALEIKKQEWKLeqLAADlSKYEQEL 471
|
250 260 270
....*....|....*....|....*....|...
gi 672073093 583 EALSQEQQRSAQEKGELQGRLAEKESQEQGLQQ 615
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
356-1016 |
4.86e-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: 73.94 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKAlvdNEQLRHELAQLKALQLEGARNQGLRE 435
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQL----TVTQQSQEEVARVKEQLAFQMEQVKRESEmKMEEQ 511
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleEQLETLRSKVAQLELQIASLNNEIERLEA-RLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRELVA-----KAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALS 586
Cdd:TIGR02168 413 EDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 587 QEQQRSAQEKGELQGRLAEKESQEQ-GLQQKLLDEQFAVLRGAAAEAEAILQDAVSklddplhlrctsspDYLVSRAQAA 665
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGlSGILGVLSELISVDEGYEAAIEAALGGRLQ--------------AVVVENLNAA 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 666 LDSVSGLEKghtqylASSEALAFVPADasALVAALTRFSHLAADTIVNG--GATSHLAPTDPADR-----LIDTCR--EC 736
Cdd:TIGR02168 559 KKAIAFLKQ------NELGRVTFLPLD--SIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRkalsyLLGGVLvvDD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 737 GARALELMGQLQDQTKLPRAQPSLMRAplqGILQLGQDLKPKSLDV-RQEELgamvdKEMAATSAAIEDAVRRIEDMMNQ 815
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLDGDLVRP---GGVITGGSAKTNSSILeRRREI-----EELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 816 ARHESSgvklEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLV 895
Cdd:TIGR02168 703 LRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 896 ESADKVVLHMGKYEELivcSHEIAASTAQLVAASKVkanknsphLSRLQECSRTVNERAANVVASTKSGQEQIEDrdtmd 975
Cdd:TIGR02168 779 EAEAEIEELEAQIEQL---KEELKALREALDELRAE--------LTLLNEEAANLRERLESLERRIAATERRLED----- 842
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 672073093 976 fsglslikLKKQEMETQVRVLELEKTLEAERVRLGELRKQH 1016
Cdd:TIGR02168 843 --------LEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-644 |
6.54e-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: 73.55 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 379 QRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQlegarnqglrEEAERKASATEARYSKLKEKHNEL 458
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----------EELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 459 INTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKREsemkMEEQSDQLEKLKRELVAKAGEL-------AH 531
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ----IEQLKEELKALREALDELRAELtllneeaAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 532 AQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQ 611
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270
....*....|....*....|....*....|...
gi 672073093 612 GLQQklLDEQFAVLRGAAAEAEAILQDAVSKLD 644
Cdd:TIGR02168 902 ELRE--LESKRSELRRELEELREKLAQLELRLE 932
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
356-637 |
9.58e-13 |
|
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: 72.84 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLR---AELEKIKM---EAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKalqLEGAR 429
Cdd:pfam15921 532 ELQHLKNEGDHLRnvqTECEALKLqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR---LELQE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQ----LTVTQQSQEEVARVKEQlafqMEQVKRESE 505
Cdd:pfam15921 609 FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQErdqlLNEVKTSRNELNSLSED----YEVLKRNFR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 MKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSE-------LSSRLDTLNAEKEALSGAIRQREAELLAA---Q 575
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNAnkeK 764
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672073093 576 SLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAA--AEAEAILQ 637
Cdd:pfam15921 765 HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLqfAECQDIIQ 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
358-639 |
1.80e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKReVETLRAELEKikmeaqryisQLKgqvnsleaELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARnqglreea 437
Cdd:COG1196 186 ENLER-LEDILGELER----------QLE--------PLERQAEKAERYRELKEELKELEAELLLLKLRELE-------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 438 erkasateARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVarvkeqlafqmeqvkresEMKMEEQSDQLEK 517
Cdd:COG1196 239 --------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL------------------ELELEEAQAEEYE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 518 LKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQ-EQQRSAQEK 596
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 672073093 597 gelqgRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDA 639
Cdd:COG1196 373 -----ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-645 |
2.49e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKA--LVDNEQLRHELAQLKALQL---EGARNQG 432
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAkkaEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LREeAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQS 512
Cdd:PTZ00121 1580 LRK-AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 513 DQLEklKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEE-ALSQEQQR 591
Cdd:PTZ00121 1659 NKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAK 1736
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 672073093 592 SAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-621 |
5.61e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGArnqglrEEA 437
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA------DEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 438 ERKASatEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEevARVKEQLAFQMEQVKRESEMKMEEQSDQLEK 517
Cdd:PTZ00121 1476 KKKAE--EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 518 LKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAE-LLAAQSLVREKEEALSQEQQRSAQEK 596
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
250 260
....*....|....*....|....*
gi 672073093 597 GELQGRLAEKESQEQGLQQKLLDEQ 621
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAE 1656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-609 |
6.48e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQ---RYISQLKGQVNSLEAELEEQRKQ---KQKAlvdnEQLRHELAQLKALQLEGARNQ 431
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKAdeaKKKA----EEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAERKASATEARySKLKEKHNelinthAELLRKNADTAKQLTVTQQSQEEvARVKEQLAFQMEQVKRESEM--KME 509
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAK-KKAEEAKK------ADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKADEAkkKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKR--ELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEalsgairQREAELLAAQSLVREKEEALSQ 587
Cdd:PTZ00121 1494 EAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE-------KKKADELKKAEELKKAEEKKKA 1566
|
250 260
....*....|....*....|..
gi 672073093 588 EQQRSAQEKGELQGRLAEKESQ 609
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKK 1588
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
434-645 |
1.13e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSKLKEKHNELiNTHAELLRKNADTAKQltVTQQSQEEVARVKEQLAFQMEQVKREsemkMEEQSD 513
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGEL-ERQLEPLERQAEKAER--YRELKEELKELEAELLLLKLRELEAE----LEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 514 QLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALsgaiRQREAELLAAQSLVREKEEALSQEQQRSA 593
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL----LAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 672073093 594 QEKGELQGRLAEKESQEQGLQQKL--LDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-645 |
1.65e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRA----------ELEKIKMEAQRYISQLKGQVNSLEAELEEQRKqkqkALVDNEQLRHELAQL 420
Cdd:PRK02224 380 EDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREERDELREREAELEATLRTARE----RVEEAEALLEAGKCP 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 421 KALQ-LEGARNQGLREEAERKASATEARYSKLKEKHNELINTH--AELLRKNADTAKQLtvtqqsQEEVARVKEQLAFQM 497
Cdd:PRK02224 456 ECGQpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLerAEDLVEAEDRIERL------EERREDLEELIAERR 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 498 EQVKRESEmKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALsGAIRQREAELLAAQSL 577
Cdd:PRK02224 530 ETIEEKRE-RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDE 607
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 578 VREKEEALSQEQQRSAQEKGelqgRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:PRK02224 608 IERLREKREALAELNDERRE----RLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
358-616 |
3.54e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKiKMEAQRYISQLKGQVNSLEaELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEA 437
Cdd:PTZ00121 1209 EEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 438 ERKASATEARYSKLKEKHNEL------------INTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQ----MEQVK 501
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAkkkaeeakkadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeaeaAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 502 RESEMKMEEQSDQLEKLKRelvaKAGELAHAQEALSRTEqsgsELSSRLDTLNAEKEALSGA--IRQREAELLAAQSLVR 579
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKK----KAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKK 1438
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672073093 580 EKEEAL-SQEQQRSAQE--KGELQGRLAEKESQEQGLQQK 616
Cdd:PTZ00121 1439 KAEEAKkADEAKKKAEEakKAEEAKKKAEEAKKADEAKKK 1478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-643 |
8.93e-11 |
|
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: 66.24 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETLRAELEKIkmeaQRYISQLKGQVNSLEAELEEqrKQKQKALvdNEQLRHELAQLKALQLEGARNQgl 433
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERL----DLIIDEKRQQLERLRREREK--AERYQAL--LKEKREYEGYELLKEKEALERQ-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQltVTQQSQEEVARVKEQLAfqmeqvkrESEMKMEEQSD 513
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIG--------ELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 514 QLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKE-------EALS 586
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELK 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672073093 587 QEQQRSAQ---EKGELQGRLAEKESQEQGLQQKLLD--EQFAVLRGAAAEAEAILQDAVSKL 643
Cdd:TIGR02169 389 DYREKLEKlkrEINELKRELDRLQEELQRLSEELADlnAAIAGIEAKINELEEEKEDKALEI 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
377-627 |
3.57e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 377 EAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQlegarnqglrEEAERKASATEARYSKLKEKHN 456
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----------RALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 457 ELintHAELLRKNADTAKQLTVTQQSQEEvarvkEQLAFQMEQvkrESEMKMEEQSDQLEKLKRELVAKAGELAHAQEAL 536
Cdd:COG4942 94 EL---RAELEAQKEELAELLRALYRLGRQ-----PPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 537 SRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQK 616
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|.
gi 672073093 617 LLDEQFAVLRG 627
Cdd:COG4942 243 TPAAGFAALKG 253
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-643 |
3.59e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQryisQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGAR 429
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELE----EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKME 509
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSelSSRLDTLNAEKEALSGAIRQ------------REAELLAAQSL 577
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLE--GVKAALLLAGLRGLAGAVAVligveaayeaalEAALAAALQNI 551
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 578 VREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKL 643
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-615 |
6.02e-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: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETLRAELEKikmeAQRY--ISQLKGQVNS--LEAELEEQRKQKQKALVDNEQLRHELAQLKALQLE--- 426
Cdd:TIGR02169 190 DLIIDEKRQQLERLRREREK----AERYqaLLKEKREYEGyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISElek 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 427 --GARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQVkRES 504
Cdd:TIGR02169 266 rlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLAKLEAEIDKLLAEI-EEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKRELVAKAGEL----AHAQE---ALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSL 577
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELedlrAELEEvdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
250 260 270
....*....|....*....|....*....|....*...
gi 672073093 578 VREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQ 615
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
434-645 |
7.10e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSKLKEKHNELiNTHAELLRKNADTAKQLtvtqqsQEEVARVKE-QLAFQMEQVKRESEmKMEEQS 512
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNEL-ERQLKSLERQAEKAERY------KELKAELRElELALLVLRLEELRE-ELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 513 DQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQ---SLVREKEEALSQEQ 589
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRerlANLERQLEELEAQL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 590 QRSAQEKGELQGRLAEKESQEQGLQqklldEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELK-----EELESLEAELEELEAELEELESRLEE 376
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-647 |
8.31e-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: 63.16 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 357 IENLKREVETLRAELEKIKMEaqryISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKalqlegarnqglree 436
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENR----LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE--------------- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 437 aerkasatearySKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLE 516
Cdd:TIGR02169 744 ------------EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 517 K----LKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQ-EQQR 591
Cdd:TIGR02169 812 ArlreIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlKKER 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 592 SAQEKgelQGRLAEKESQEQGLQQKLLDEQFAVLrgaaAEAEAILQDAVSKLDDPL 647
Cdd:TIGR02169 892 DELEA---QLRELERKIEELEAQIEKKRKRLSEL----KAKLEALEEELSEIEDPK 940
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-558 |
1.77e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQRYIsQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLegarnqglREEA 437
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--------LEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 438 ERKASATEARYSKLKEKHNELINTHAELlrknadtakqltvtQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEK 517
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEEL--------------EELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 672073093 518 LKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKE 558
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
356-645 |
2.53e-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: 61.57 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQryisQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLK----ALQLEGARNQ 431
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQ----QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsVKELIIKNLD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAERKASATEARYSKLKekhNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKR-ESE----- 505
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlESEkkeke 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 ------------MKMEEQSDQLEKLKRELVAKAGELAHAQEALsrtEQSGSELSSRLDTLNAEKEALsgaIRQREAELLA 573
Cdd:TIGR04523 538 skisdledelnkDDFELKKENLEKEIDEKNKEIEELKQTQKSL---KKKQEEKQELIDQKEKEKKDL---IKEIEEKEKK 611
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672073093 574 AQSLVREKEEALSQEQQRSAQEKgelqGRLAEKESQEQglQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIK----NIKSKKNKLKQ--EVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
355-598 |
3.66e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 355 LQIENLKREVETLR-AELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARN-QG 432
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LR--EEAERKASATEARYSKLKEKHNELINTHAELLRKnadtAKQLtvtqQSQEEVARVK-EQLAFQMEQVKRESE--MK 507
Cdd:PTZ00121 1680 AKkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK----AEEL----KKAEEENKIKaEEAKKEAEEDKKKAEeaKK 1751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 508 MEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDT------------------------LNAEKEALSGA 563
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdkkikdifdnfaniieggkegnlvINDSKEMEDSA 1831
|
250 260 270
....*....|....*....|....*....|....*
gi 672073093 564 IRqreaELLAAQSLVREKEEALSQEQQRSAQEKGE 598
Cdd:PTZ00121 1832 IK----EVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
356-563 |
6.95e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKM---EAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELA-QLKALQLEGaRNQ 431
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRALYRLG-RQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAERKASATEARYSKLKEKHNELINTHAELLRKnadTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQ 511
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA---DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 672073093 512 SDQLEKLKRELVAKAGELAhaqeALSRTEQSGSELSSRLDTLNAEKEALSGA 563
Cdd:COG4942 198 QKLLARLEKELAELAAELA----ELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
350-625 |
7.03e-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: 60.03 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDL--QIENLKREVETLRAELEKIkmeaQRYISQLKGQVNSLEAELEEQRKQKQKalvdNEQLRHELAQLKAlqleg 427
Cdd:TIGR04523 159 NKYNDLkkQKEELENELNLLEKEKLNI----QKNIDKIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKK----- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 428 aRNQGLREEAERKASATEARYSKLKEKHNELINthaeLLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRE-SEM 506
Cdd:TIGR04523 226 -QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ----LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 507 KMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALsgairqrEAELLAAQSLVREKEEALS 586
Cdd:TIGR04523 301 NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS-------ESENSEKQRELEEKQNEIE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 672073093 587 QEQQRSAQEKGELQGRLAEKESQEQGLQQ-----KLLDEQFAVL 625
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNqeklnQQKDEQIKKL 417
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-643 |
1.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEKIKMEAQRYiSQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLE-GAR 429
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEH-EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEElEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEAER---KASATEARYSKLKEKHNEL-------------INTHAELLRKNADTAkqltvtqqsqEEVARVKEQL 493
Cdd:PRK02224 295 RDDLLAEAGLddaDAEAVEARREELEDRDEELrdrleecrvaaqaHNEEAESLREDADDL----------EERAEELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 494 AFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSrteqsgsELSSRLDTLNAEKEALSGAIRQREAELLA 573
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-------NAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 574 AQSLVREKEEALS--------QEQQRSA---------QEKGELQGRLAEKESQEQGLQQKLldEQFAVLRGAAAEAEAIL 636
Cdd:PRK02224 438 ARERVEEAEALLEagkcpecgQPVEGSPhvetieedrERVEELEAELEDLEEEVEEVEERL--ERAEDLVEAEDRIERLE 515
|
....*....
gi 672073093 637 Q--DAVSKL 643
Cdd:PRK02224 516 ErrEDLEEL 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
350-641 |
1.25e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQR----------YISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQ 419
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 420 LKalqlegARNQGLREEAERKASATEARYSKLKEKHNEL-----------------------INTHAELLRKNADTAKQ- 475
Cdd:PRK02224 354 LE------ERAEELREEAAELESELEEAREAVEDRREEIeeleeeieelrerfgdapvdlgnAEDFLEELREERDELREr 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 476 ---LTVTQQSQEEVARVKEQL-----AFQMEQVKRESEM--KMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSgSE 545
Cdd:PRK02224 428 eaeLEATLRTARERVEEAEALleagkCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 546 LSSRLDTLNAEKEALSGAIRQREAEL----LAAQSLVREKEE--ALSQEQQRSAQEK----GELQGRLAEKESQEQGLQQ 615
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIeekrERAEELRERAAEleAEAEEKREAAAEAeeeaEEAREEVAELNSKLAELKE 586
|
330 340
....*....|....*....|....*.
gi 672073093 616 KLldEQFAVLRGAAAEAEAILQDAVS 641
Cdd:PRK02224 587 RI--ESLERIRTLLAAIADAEDEIER 610
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
417-643 |
2.20e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 417 LAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQ 496
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 497 MEQVKREsemkMEEQSDQLEKLKRELvAKAGELAHAQEALSRTEQSGSELSSR-LDTLNAEKEALSGAIRQREAELLAAQ 575
Cdd:COG4942 92 IAELRAE----LEAQKEELAELLRAL-YRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 576 SLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEaiLQDAVSKL 643
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIARL 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
354-603 |
2.30e-08 |
|
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: 58.43 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETLRAELEkikmeaqryisQLKGQVNSLEAEL---EEQRKQKQKALvdnEQLRHELAQLKALQLEGARN 430
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQ-----------QATEEVLELEQKLsvaDAARRQFEKAY---ELVCKIAGEVERSQAWQTAR 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASAteARYSKLKEKHNEL---INTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVK------ 501
Cdd:COG3096 499 ELLRRYRSQQALA--QRLQQLRAQLAELeqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEeqaaea 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 502 RESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSR-TEQSGSELSSRLDTLNAEKEALsgairQREAELLAAQSLVRE 580
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlREQSGEALADSQEVTAAMQQLL-----EREREATVERDELAA 651
|
250 260
....*....|....*....|...
gi 672073093 581 KEEALSQEQQRSAQEKGELQGRL 603
Cdd:COG3096 652 RKQALESQIERLSQPGGAEDPRL 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-563 |
2.63e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKmEAQRYISQLKGQVNSLEA---ELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQG 432
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQ-LAFQMEQVKRES--EMKME 509
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhELYEEAKAKKEEleRLKKR 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 672073093 510 EQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGA 563
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-632 |
2.63e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 349 MKDDRDL--QIENLKREVETLraelekikMEAQRYISQLKGQVNSLEaELEEQRKQKQKALVDNEQLRHELAQLKA--LQ 424
Cdd:COG4913 217 MLEEPDTfeAADALVEHFDDL--------ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 425 LEGARNQGLREEAERKASATEARYSKLKEKHNELinthaellrknadtakqltvtqqsQEEVARVKEQLAfqmeqvkres 504
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDAL------------------------REELDELEAQIR---------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 emkmEEQSDQLEKLKRelvakagELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEA 584
Cdd:COG4913 334 ----GNGGDRLEQLER-------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 672073093 585 LSQEQQRSAQEKGELQGRLAEKESQEQGLQQK--LLDEQFAVLRGAAAEA 632
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRksNIPARLLALRDALAEA 452
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-611 |
2.72e-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: 58.21 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 348 SMKDDRDL---QIENLKREVETLRAELEKIKMEAQRYISQLkgqvnsleaELEEQRKqkqkalvdNEQLRHELaqlkalq 424
Cdd:pfam17380 343 AMERERELeriRQEERKRELERIRQEEIAMEISRMRELERL---------QMERQQK--------NERVRQEL------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 425 lEGARNQGLREEAerkasateaRYSKLKEKHNELinthaELLRKNADTAKQltvtqqsqEEVARVKEQLAFQMEQVkRES 504
Cdd:pfam17380 399 -EAARKVKILEEE---------RQRKIQQQKVEM-----EQIRAEQEEARQ--------REVRRLEEERAREMERV-RLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRldTLNAEKEALSGAIRQR---EAELLAAQSLVREK 581
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK--ELEERKQAMIEEERKRkllEKEMEERQKAIYEE 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 672073093 582 EEALSQEQQRSAQ------------------EKGELQGRLAEKESQEQ 611
Cdd:pfam17380 533 ERRREAEEERRKQqemeerrriqeqmrkateERSRLEAMEREREMMRQ 580
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
346-616 |
3.10e-08 |
|
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: 57.72 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 346 NGSMKDDRDlQIENLKREVETLRAELEKIKMEAQRY---ISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKA 422
Cdd:TIGR04523 109 NSEIKNDKE-QKNKLEVELNKLEKQKKENKKNIDKFlteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 423 lQLEGARNQGLREEaeRKASATEarysKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQVKr 502
Cdd:TIGR04523 188 -NIDKIKNKLLKLE--LLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNI---EKKQQEINEKTTEISNTQTQLN- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 503 esemkmeEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEA-----LSGAIRQREAELLAAQSL 577
Cdd:TIGR04523 257 -------QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQ 329
|
250 260 270
....*....|....*....|....*....|....*....
gi 672073093 578 VREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQK 616
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
353-634 |
3.72e-08 |
|
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: 58.04 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRY--------------------------ISQLKGQVNSLEAELEEQRKQKQKA 406
Cdd:COG3096 783 REKRLEELRAERDELAEQYAKASFDVQKLqrlhqafsqfvgghlavafapdpeaeLAALRQRRSELERELAQHRAQEQQL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 407 LVDNEQLRHELAQLKALQLE---------GARNQGLREEAErkaSATEA-RYSKLKEKHNELINTHAELLRKNADTAKQL 476
Cdd:COG3096 863 RQQLDQLKEQLQLLNKLLPQanlladetlADRLEELREELD---AAQEAqAFIQQHGKALAQLEPLVAVLQSDPEQFEQL 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 477 TV-TQQSQEEVARVKEQlAFQMEQVKR--------ESEMKMEEQSDQLEKLKRELVakagelaHAQEALSRTEQSGSELS 547
Cdd:COG3096 940 QAdYLQAKEQQRRLKQQ-IFALSEVVQrrphfsyeDAVGLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 548 SRLDTLNAEKEALSGAIRQREAELLA-------------------AQSLVREKEEALSQeqqrSAQEKGELQGRLAEKES 608
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQEleqeleelgvqadaeaeerARIRRDELHEELSQ----NRSRRSQLEKQLTRCEA 1087
|
330 340
....*....|....*....|....*...
gi 672073093 609 QEQGLQQKL--LDEQFAVLRGAAAEAEA 634
Cdd:COG3096 1088 EMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-566 |
3.81e-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: 57.77 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQRYISQL---KGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKA-LQLEGARNQ 431
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAerkaSATEARYSKLKEKHNELINT------------------HAELLRKNADTAKQLTVTQQSQEEVARVKEQL 493
Cdd:TIGR02169 382 ETRDEL----KDYREKLEKLKREINELKREldrlqeelqrlseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672073093 494 AfQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQ 566
Cdd:TIGR02169 458 E-QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
365-612 |
4.34e-08 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 57.56 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 365 ETLRAELEKIKMEAQ-RYISQLKGQVNSLEAELEeqrkQKQKALVDNEQLRHELAQLKA-LQLEGAR-----NQGLREEA 437
Cdd:PLN03229 531 LSLKYKLDMLNEFSRaKALSEKKSKAEKLKAEIN----KKFKEVMDRPEIKEKMEALKAeVASSGASsgdelDDDLKEKV 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 438 ERKASATEARYSKLKEKhnelINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKmeeqsDQLEK 517
Cdd:PLN03229 607 EKMKKEIELELAGVLKS----MGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLK-----SKIEL 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 518 LKRElVAKAGelahaqealsrteqsgselsSRLDTLNAEK-EALSGAIRQREAELLAAQSLvREKEEALSQEQQRSAQEK 596
Cdd:PLN03229 678 LKLE-VAKAS--------------------KTPDVTEKEKiEALEQQIKQKIAEALNSSEL-KEKFEELEAELAAARETA 735
|
250
....*....|....*.
gi 672073093 597 GELQGRLAEKESQEQG 612
Cdd:PLN03229 736 AESNGSLKNDDDKEED 751
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
439-632 |
4.47e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTV-TQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEK 517
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEeLEQLREELEQAREELE-QLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 518 LKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAqekg 597
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE---- 160
|
170 180 190
....*....|....*....|....*....|....*
gi 672073093 598 ELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEA 632
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQALDELLKEANRN 195
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
344-616 |
6.16e-08 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 55.97 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 344 PPNGSMKD------DRDLQIENLKREVETLRAELEKIKMEAQRYISQLKG------QVNSLEAELEEQRKQKQKALVDNE 411
Cdd:pfam15905 39 PNLNNSKDastpatARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQErgeqdkRLQALEEELEKVEAKLNAAVREKT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 412 QLRHELAQLKALQLEGARNQglrEEAERKASAT------EARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQ----Q 481
Cdd:pfam15905 119 SLSASVASLEKQLLELTRVN---ELLKAKFSEDgtqkkmSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQknleH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 482 SQEEVARVKEQLAfQMEQVKRESEMKMEEQ----------SDQLEKLKRELV-------AKAGELAHAQEALSRTEQSGS 544
Cdd:pfam15905 196 SKGKVAQLEEKLV-STEKEKIEEKSETEKLleyitelscvSEQVEKYKLDIAqleellkEKNDEIESLKQSLEEKEQELS 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 545 ----ELSSRLDTLNAEKEalsgairqreaellaaqSLVREKEEalsQEQQRSAqEKGELQGRLAEKESQEQGLQQK 616
Cdd:pfam15905 275 kqikDLNEKCKLLESEKE-----------------ELLREYEE---KEQTLNA-ELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
384-609 |
9.75e-08 |
|
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: 56.34 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 384 QLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlQLEGArNQGlREEAERKASATEARYSKLKEKHNELINTHA 463
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA-QIDAA-NKG-REEAVKQLKKLQAQMKDLQRELEEARASRD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 464 ELLRKNADTAKQLtvtQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSG 543
Cdd:pfam01576 823 EILAQSKESEKKL---KNLEAELLQLQEDLA-ASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEEL 898
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 544 SELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEAlsqEQQRSAQEKgELQGRLAEKESQ 609
Cdd:pfam01576 899 EEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA---RQQLERQNK-ELKAKLQEMEGT 960
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
354-612 |
1.13e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETLRAELEkikmEAQRYISQLKGQVNSLEAELE--EQRKQKQKALVDneQLRHELAQLKALQLEG-ARN 430
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQ----EATEELLSLEQKLSVAQAAHSqfEQAYQLVRKIAG--EVSRSEAWDVARELLRrLRE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QglREEAERkASATEARYSKLKEKHNElintHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVK------RES 504
Cdd:PRK04863 508 Q--RHLAEQ-LQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSesvseaRER 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKRELVAKAGELAHAQEALSR-TEQSGSELSSRldtlnaekEALSGAIRQreaellaaqslVREKEE 583
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARlREQSGEEFEDS--------QDVTEYMQQ-----------LLERER 641
|
250 260
....*....|....*....|....*....
gi 672073093 584 ALSQEQQRSAQEKGELQGRlAEKESQEQG 612
Cdd:PRK04863 642 ELTVERDELAARKQALDEE-IERLSQPGG 669
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
356-624 |
1.25e-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: 55.80 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAEL---EKIKMEAQRYISQLKGQVNSLEAE---LEEQRKQKQKALV----DNEQLRHELAQLK---- 421
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEklkkENQSYKQEIKNLEsqin 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 422 ALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVK 501
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 502 ResEMKMEEQSdqLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREK 581
Cdd:TIGR04523 475 R--SINKIKQN--LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 672073093 582 EEALS--------QEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAV 624
Cdd:TIGR04523 551 DFELKkenlekeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
356-605 |
1.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEkikmEAQRYISQLKGQVNSLEAELE--EQRKQKQKALVDNEQLRHELAQLKAlQLEGAR--NQ 431
Cdd:COG4913 611 KLAALEAELAELEEELA----EAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEA-ELERLDasSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLReEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQ 511
Cdd:COG4913 686 DLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRELVAKAGELAHAQEALSRT-EQSGSELSSRLDTLNAEKEALSGAIRQREAelLAAQSLVREKEEALSQEQQ 590
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDR--LEEDGLPEYEERFKELLNE 842
|
250
....*....|....*
gi 672073093 591 RSAQEKGELQGRLAE 605
Cdd:COG4913 843 NSIEFVADLLSKLRR 857
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
471-645 |
1.43e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 471 DTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEmKMEEQSDQLEKLKR------ELVAKAGELAHAQEALSRTEQSGS 544
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 545 ELS---SRLDTLNAEKEALSGAIRQreaellaaqslVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQ 621
Cdd:COG4913 686 DLAaleEQLEELEAELEELEEELDE-----------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
170 180
....*....|....*....|....*.
gi 672073093 622 FAVLRGAAAEAE--AILQDAVSKLDD 645
Cdd:COG4913 755 FAAALGDAVERElrENLEERIDALRA 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-645 |
1.53e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKalqlegarn 430
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE--------- 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASATEARysklkEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEmkmee 510
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDI-----ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE----- 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 511 qsDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLdtlnAEKEalsgairQREAELLAAQSLVREKEEALSQEQQ 590
Cdd:TIGR02168 908 --SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----SEEY-------SLTLEEAEALENKIEDDEEEARRRL 974
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 591 RSAQEKGELQGR---LAEKESQEQGLQQKLLDEQFAVLRgaaaEAEAILQDAVSKLDD 645
Cdd:TIGR02168 975 KRLENKIKELGPvnlAAIEEYEELKERYDFLTAQKEDLT----EAKETLEEAIEEIDR 1028
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
358-609 |
1.97e-07 |
|
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: 55.57 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREvETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQK---------ALVDNEQLRHELAQLKALQLEgA 428
Cdd:pfam01576 194 ERLKKE-EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelqaalARLEEETAQKNNALKKIRELE-A 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQL-------AFQMEQVK 501
Cdd:pfam01576 272 QISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALeeetrshEAQLQEMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 502 RESEMKMEEQSDQLEKLKRELVAkageLAHAQEALsrtEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREK 581
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKAN----LEKAKQAL---ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES 424
|
250 260 270
....*....|....*....|....*....|.
gi 672073093 582 EEALSQEQQRSAQEKGELQ---GRLAEKESQ 609
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELEsvsSLLNEAEGK 455
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
365-627 |
2.62e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 365 ETLRAELEKIKMeaqryISQLKGQVNSLEAELEE-----QRKQKQKAlvDNEQLRHELAQLKALQLEGARN-QGLREEAE 438
Cdd:PRK11281 39 ADVQAQLDALNK-----QKLLEAEDKLVQQDLEQtlallDKIDRQKE--ETEQLKQQLAQAPAKLRQAQAElEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSkLKEKHNELINTHAEL--LRKNADTAKQLTVTQQSQEEvaRVKEQL---AFQMEQVKRE----SEMKME 509
Cdd:PRK11281 112 EETRETLSTLS-LRQLESRLAQTLDQLqnAQNDLAEYNSQLVSLQTQPE--RAQAALyanSQRLQQIRNLlkggKVGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKRELVakageLAHAQEALSRTEQSGSELssRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQ 589
Cdd:PRK11281 189 LRPSQRVLLQAEQA-----LLNAQNDLQRKSLEGNTQ--LQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKT 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672073093 590 ---QRSAQEKGELQG-RLAEKESQ--------------------EQGLQ-----------QKLLDEQFAVLRG 627
Cdd:PRK11281 262 vqeAQSQDEAARIQAnPLVAQELEinlqlsqrllkateklntltQQNLRvknwldrltqsERNIKEQISVLKG 334
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-608 |
3.12e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQRY--ISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGL 433
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYeeAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSK---------LKEKHNEliNTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafQMEQVKRES 504
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgreLTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKREL-VAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEE 583
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
250 260
....*....|....*....|....*
gi 672073093 584 ALSQEQQRSAQEKGELQGRLAEKES 608
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEP 599
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
356-579 |
3.18e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKmeAQRYISQLKGQVNSLEAELEEQRKQKQkalvdneQLRHELAQLKAlQLEGARNQGLRE 435
Cdd:COG3206 183 QLPELRKELEEAEAALEEFR--QKNGLVDLSEEAKLLLQQLSELESQLA-------EARAELAEAEA-RLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQL 515
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV---IALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672073093 516 EKLKRELVAKAGELAhaqeALSRTEQSGSELSSRLDTLNAEKEALSGaiRQREAELLAAQSLVR 579
Cdd:COG3206 330 ASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQ--RLEEARLAEALTVGN 387
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
361-621 |
3.61e-07 |
|
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: 54.59 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 361 KREVETLRAELEKIKMEAQRYISQLKGQVnsLEAELEEQRKQKQKALVDNEQLRHEL-AQLKALQLEGARNQGLREeaER 439
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHLREALQQTQQSHAYLTQKReAQEEQLKKQQLLKQLRAR--IE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 440 KASATEARYSKLKEKhnelINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLA-FQMEQVKRESEMKMEEQSDQLEKL 518
Cdd:TIGR00618 271 ELRAQEAVLEETQER----INRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRsRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 519 KRELVAKAGELAHAQE-ALSRTEQSGSELS--SRLDTLNAEKEALsgairqREAELLAAQSLVREKEEALSQEQQRSAQE 595
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEvATSIREISCQQHTltQHIHTLQQQKTTL------TQKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260
....*....|....*....|....*.
gi 672073093 596 kgELQGRLAEKESQEQgLQQKLLDEQ 621
Cdd:TIGR00618 421 --DLQGQLAHAKKQQE-LQQRYAELC 443
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
363-602 |
3.76e-07 |
|
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: 54.41 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 363 EVETLRAELEKIKMEAQRYISQLKGQVNSLE---AELEEQRKQKQKALVD-NEQLRHELAQLKALQLEgarnqglREEAE 438
Cdd:pfam01576 58 EAEEMRARLAARKQELEEILHELESRLEEEEersQQLQNEKKKMQQHIQDlEEQLDEEEAARQKLQLE-------KVTTE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTvtqqSQEEVARVKEQLAFQMEQVKRESE--MKMEEQSDQ-L 515
Cdd:pfam01576 131 AKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA----EEEEKAKSLSKLKNKHEAMISDLEerLKKEEKGRQeL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 516 EKLKRELVAKAGELahaQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQ-----EQQ 590
Cdd:pfam01576 207 EKAKRKLEGESTDL---QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISElqedlESE 283
|
250
....*....|..
gi 672073093 591 RSAQEKGELQGR 602
Cdd:pfam01576 284 RAARNKAEKQRR 295
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
409-631 |
4.32e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.29 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 409 DNEQLRHELAQLKALQ----------LEGArnqgLREEAERKASATEAR-YSKLKEKHNELINTHAELLRKNADTAKQLT 477
Cdd:PRK10929 24 DEKQITQELEQAKAAKtpaqaeiveaLQSA----LNWLEERKGSLERAKqYQQVIDNFPKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 478 VTQQSQE---EVARVKEQLAFQMEQVKRESEmKMEEQSDQLEKLkrelvakAGELAHAQEALSrteqsgsELSSRLDTLN 554
Cdd:PRK10929 100 PNMSTDAleqEILQVSSQLLEKSRQAQQEQD-RAREISDSLSQL-------PQQQTEARRQLN-------EIERRLQTLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 555 AEKEALSGA-IRQREAELLAAQSLVREKEeaLSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAE 631
Cdd:PRK10929 165 TPNTPLAQAqLTALQAESAALKALVDELE--LAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAE 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
346-672 |
4.49e-07 |
|
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: 54.41 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 346 NGSMKDDRDLQIENLKREVETLRAELEKIKMeaqryISQLKGQVNSLEAELEEQRKQKqkalvdnEQLRHELAQLKAlQL 425
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-----LSKLKNKHEAMISDLEERLKKE-------EKGRQELEKAKR-KL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 426 EGARNQGLREEAERKASATEARySKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQMEQVKRESE 505
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELR-AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE-SERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 MKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAEllAAQSLVREKEEA- 584
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQ--ALEELTEQLEQAk 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 585 -----LSQEQQRSAQEKGELQG--RLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLddplhlrctsspdy 657
Cdd:pfam01576 370 rnkanLEKAKQALESENAELQAelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL-------------- 435
|
330
....*....|....*
gi 672073093 658 lvSRAQAALDSVSGL 672
Cdd:pfam01576 436 --SKLQSELESVSSL 448
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
356-644 |
6.85e-07 |
|
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: 53.58 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQK----QKALVDNEQLRHELAQL----KALQLEG 427
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsQESGNLDDQLQKLLADLhkreKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 428 ARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNAD----TAKQLTVTQQSQEEVARVkEQLAFQMEQVKRE 503
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNESLEKV-SSLTAQLESTKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 504 SEMKMEEQSDQ---LEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDT-------LNAEKEALSGAirQREAELLA 573
Cdd:pfam15921 477 LRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLklqelqhLKNEGDHLRNV--QTECEALK 554
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 574 AQSLVREKE-EALSQEQQRSAQEKGElQGRLA-----EKESQEQGLQQKLLD-EQFAVLRGAAAEAEAILQDAVSKLD 644
Cdd:pfam15921 555 LQMAEKDKViEILRQQIENMTQLVGQ-HGRTAgamqvEKAQLEKEINDRRLElQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
349-645 |
6.91e-07 |
|
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: 53.57 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 349 MKDDRDLQIENLKREVET---LRAELEKIKMEAQRYISQLKgqvnSLEAELEEQRKQKQKALVDNEqlrhelAQLKALQL 425
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKkdhLTKELEDIKMSLQRSMSTQK----ALEEDLQIATKTICQLTEEKE------AQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 426 EGARNQGLREEAERKASATEarysklkekhnELINTHAELLRKNADTAKQLTVTQQSQ----EEVARVKEQLAFQMEQVK 501
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLE-----------ELLRTEQQRLEKNEDQLKIITMELQKKsselEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 502 R--ESEMKMEEQSDQLEKLKRELVAKAGELAHaqeALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAEL-------- 571
Cdd:pfam05483 412 KilAEDEKLLDEKKQFEKIAEELKGKEQELIF---LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELekeklkni 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 572 -LAAQS--LVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQ-KLLDEQFAVLRGaaaEAEAILQDAVSKLDD 645
Cdd:pfam05483 489 eLTAHCdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQiENLEEKEMNLRD---ELESVREEFIQKGDE 563
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
356-636 |
7.96e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQryisQLKGQVNSLEAELEEQRKQKQKAlvdNEQLRHELAQLKALQLEGARNQGLRE 435
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEEL---NEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQL 515
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL---KELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 516 EKLKRELVAKAGELAHAQEalSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQE 595
Cdd:COG4372 189 LKEANRNAEKEEELAEAEK--LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672073093 596 KGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAIL 636
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| ANTH_N |
cd03564 |
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ... |
33-116 |
8.26e-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: 48.81 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 33 ISISKAINSQEAPVKEKHARRIILGThhekgaftfwsYAIGLPLPSSSIL----------SW----KFCHVLHKVLRDGH 98
Cdd:cd03564 3 VAVVKATNHDEVPPKEKHVRKLLLAT-----------SNGGGRADVAYIVhalakrlhkkNWivvlKTLIVIHRLLREGS 71
|
90
....*....|....*...
gi 672073093 99 PNVLHDCQRYRSNIREIG 116
Cdd:cd03564 72 PSFLEELLRYSGHIFNLS 89
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
447-594 |
1.25e-06 |
|
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: 49.12 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 447 RYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLkrELVAKA 526
Cdd:pfam01608 4 RWTEGLISAAKAVAAATNLLVEAADGVVQG---QGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRL--EAASKA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 527 geLAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAirQREAELLAAQSLVREKEEALSQEQQRSAQ 594
Cdd:pfam01608 79 --VTDATKNLVAAVKSAAELQEEEIEEEMDFSKLSLH--QAKRQEMEAQVEILKLEKELEEARKKLAE 142
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
350-594 |
1.46e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEaqryISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQ--------LK 421
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgerAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 422 ALQLEGARNQGLR--------EEAERKASATearySKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQL 493
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSAL----SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 494 AFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQS--GSELSSRLDTLNAEKEALSGAIRQREAEL 571
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAaaAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
250 260
....*....|....*....|...
gi 672073093 572 LAAQSLVREKEEALSQEQQRSAQ 594
Cdd:COG3883 250 GAAGAAGAAAGSAGAAGAAAGAA 272
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
376-621 |
1.48e-06 |
|
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: 52.43 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 376 MEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLK--E 453
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 454 KHNELINTHAELLRKNADTAKQLTVTQ-QSQEEVARVKEQL--AFQMEQVKRESEMKMEEQSDQLEKLKRElvakagELA 530
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELERLQmERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEMEQIRAE------QEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 531 HAQEALSRTEQsgsELSSRLDTLNAEKEAlsgaiRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQE 610
Cdd:pfam17380 432 ARQREVRRLEE---ERAREMERVRLEEQE-----RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250
....*....|.
gi 672073093 611 QglQQKLLDEQ 621
Cdd:pfam17380 504 R--KQAMIEEE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
367-594 |
2.38e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 367 LRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRK-----QKQKALVD-NEQLRHELAQLKALQLEgarnqglREEAERK 440
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefRQKNGLVDlSEEAKLLLQQLSELESQ-------LAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 441 ASATEARYSKLKEKHNELINTHAELLrknadtakQLTVTQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEKLKR 520
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELL--------QSPVIQQLRAQLAELEAELA-ELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672073093 521 ELVAKAgelahaQEALSRTEQSGSELSSRLDTLNAEKEALSGAIR---QREAELLAAQSLVREKEEALSQEQQRSAQ 594
Cdd:COG3206 306 QLQQEA------QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
480-647 |
2.53e-06 |
|
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: 49.92 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 480 QQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSR-TEQSGSELSSR-LDTLNAEK 557
Cdd:COG1579 20 DRLEHRLKELPAELA-ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVRNNKeYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 558 EALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAqekgELQGRLAEKESQeqglqqklLDEQFAVLRGAAAEAEAILQ 637
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELA----ELEAELEEKKAE--------LDEELAELEAELEELEAERE 166
|
170
....*....|
gi 672073093 638 DAVSKLDDPL 647
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
353-634 |
2.57e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVnslEAELEEQRKQKQKALVDNEQLRHELAQL--KALQLEGARN 430
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE---ARKAEEAKKKAEDARKAEEARKAEDARKaeEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASATEARYSKLKEKhnelinthAELLRKNADTAKQLTVtqQSQEEVARVKEqlAFQMEQVKRESEMKMEE 510
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKK--------AEAARKAEEVRKAEEL--RKAEDARKAEA--ARKAEEERKAEEARKAE 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 511 QSDQLEKLKR-ELVAKAGELAHAQEALSRTEQSGSELSSRLDTLnAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQ 589
Cdd:PTZ00121 1222 DAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF-ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 672073093 590 QRSAQE---------KGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEA 634
Cdd:PTZ00121 1301 KKKADEakkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
403-538 |
2.64e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.73 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 403 KQKALvdnEQLRHELAQL-KALQLEGARNQGLREEAER---KASATEARYSKLKEKHNELINTHAELLRKNADTAKQL-- 476
Cdd:PRK09039 51 KDSAL---DRLNSQIAELaDLLSLERQGNQDLQDSVANlraSLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELds 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672073093 477 --TVTQQSQEEVARVKEQLAFQMEQVKR------ESEMKMEEQSDQLEKLKREL-VAKAGElahAQEaLSR 538
Cdd:PRK09039 128 ekQVSARALAQVELLNQQIAALRRQLAAleaaldASEKRDRESQAKIADLGRRLnVALAQR---VQE-LNR 194
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
355-611 |
3.00e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 355 LQIENLKREVETLRAELEKIKmEAQRYISQLKGQVNSLEAELEEQRKQKQkalvDNEQLRHELAQLKAlQLEGARNQ--G 432
Cdd:PRK04863 887 LADETLADRVEEIREQLDEAE-EAKRFVQQHGNALAQLEPIVSVLQSDPE----QFEQLKQDYQQAQQ-TQRDAKQQafA 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LREEAERKA--SATEArysklkekhnelinthAELLRKNADTAKQLTVTQ-QSQEEVARVKEQLafqmeqvkRESEMKME 509
Cdd:PRK04863 961 LTEVVQRRAhfSYEDA----------------AEMLAKNSDLNEKLRQRLeQAEQERTRAREQL--------RQAQAQLA 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 510 EQSDQLEKLKRELVAKAGELAHAQEALSrteqsgsELSSRLDTlNAEKEAlsgaiRQREAELLAAQSLVREKEEALSQEQ 589
Cdd:PRK04863 1017 QYNQVLASLKSSYDAKRQMLQELKQELQ-------DLGVPADS-GAEERA-----RARRDELHARLSANRSRRNQLEKQL 1083
|
250 260
....*....|....*....|....
gi 672073093 590 QRSAQEKGELQGRL--AEKESQEQ 611
Cdd:PRK04863 1084 TFCEAEMDNLTKKLrkLERDYHEM 1107
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
361-621 |
3.29e-06 |
|
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: 51.18 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 361 KREVETLRAELEKIKMEAQRyisqLKGQVNSLEAELEeqrkqKQKALVDNEQLRHELAQLKALQLEgarnqglrEEAERK 440
Cdd:pfam05701 299 KKELEEVKANIEKAKDEVNC----LRVAAASLRSELE-----KEKAELASLRQREGMASIAVSSLE--------AELNRT 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 441 ASATEARYSKLKEKHNELINTHAEL--LRKNADTAKQLtvTQQSQEEVARVKEqlafQMEQVKRESEMkMEEqsdQLEKL 518
Cdd:pfam05701 362 KSEIALVQAKEKEAREKMVELPKQLqqAAQEAEEAKSL--AQAAREELRKAKE----EAEQAKAAAST-VES---RLEAV 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 519 KRELVA-KAGE-LAHA-----QEALSRTEQSGSELSSRLDTLNAEK-EALSGaiRQREAELLA------AQSLVREKEEA 584
Cdd:pfam05701 432 LKEIEAaKASEkLALAaikalQESESSAESTNQEDSPRGVTLSLEEyYELSK--RAHEAEELAnkrvaeAVSQIEEAKES 509
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 672073093 585 -------LSQEQQRSAQEKGELQGRLAEKESQEQGlqqKLLDEQ 621
Cdd:pfam05701 510 elrslekLEEVNREMEERKEALKIALEKAEKAKEG---KLAAEQ 550
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
389-590 |
3.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 389 VNSLEAELEE-QRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLR---EEAERKASATEARYSKLKEKHNELinthaE 464
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 465 LLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVkRESEMKMEEQSDQLEKLKRELVAKAGEL-AHAQEALSRTEQSG 543
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 672073093 544 SELSSRLDTLNAEKEALSGAIRQREAEL--LAAQSLVREKEEALSQEQQ 590
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARL 250
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
360-620 |
3.78e-06 |
|
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: 51.12 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 360 LKREVETLRAELEKIKMEAQRYISQLKGQVNslEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAER 439
Cdd:TIGR00618 648 LHALQLTLTQERVREHALSIRVLPKELLASR--QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 440 KASATEARYSKLKEKHNELINthaELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLK 519
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLK---ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 520 RELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELlaaqSLVREKEEALSQEQQRSAQEKGEL 599
Cdd:TIGR00618 803 TLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY----EECSKQLAQLTQEQAKIIQLSDKL 878
|
250 260
....*....|....*....|.
gi 672073093 600 QGRLAEKESQEQGLQQKLLDE 620
Cdd:TIGR00618 879 NGINQIKIQFDGDALIKFLHE 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-568 |
4.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLraELEKIKMEAQRY------ISQLKGQVNSLEAELEE-QRKQKQKALVDNE--QLRHELAQLKALQLE 426
Cdd:PRK03918 504 QLKELEEKLKKY--NLEELEKKAEEYeklkekLIKLKGEIKSLKKELEKlEELKKKLAELEKKldELEEELAELLKELEE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 427 gaRNQGLREEAERKASATEARYsklkEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfqmEQVKRESEM 506
Cdd:PRK03918 582 --LGFESVEELEERLKELEPFY----NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE---ELRKELEEL 652
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672073093 507 KMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQRE 568
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
355-639 |
5.70e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 355 LQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELA----QLKALQLEGARN 430
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEqleeELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQS----QEEVARVKEQLAFQMEQVKRESEM 506
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 507 KMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALS 586
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 672073093 587 QEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDA 639
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
392-617 |
5.98e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 392 LEAELEEQRKQKqkalvdNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLK-------EKHNELINTHAE 464
Cdd:pfam07888 32 LQNRLEECLQER------AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelrqsrEKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 465 LLRKNADTAKQL-TVTQQSQEEVARVKE--QLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALsrtEQ 541
Cdd:pfam07888 106 LSASSEELSEEKdALLAQRAAHEARIREleEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL---QQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 542 SGSELSSrldtLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQ------EKGELQGRLAEKESQEQGLQQ 615
Cdd:pfam07888 183 TEEELRS----LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleELRSLQERLNASERKVEGLGE 258
|
..
gi 672073093 616 KL 617
Cdd:pfam07888 259 EL 260
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
340-607 |
7.42e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 340 QTFGPPNGSMKDDRDLQIENLKREVETLRAELEKIKMEAQRYI----SQLKGQVNSLEAELE-EQRKQKQKALVDNEQLR 414
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEvEITGLTEKASSARSQAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 415 HELAQLKALQlEGARNQG---LREEAERKASATEARySKLKEK----HNELINTHAELLRKNADTAKQLTVTQQSQEEVA 487
Cdd:pfam15921 296 SIQSQLEIIQ-EQARNQNsmyMRQLSDLESTVSQLR-SELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 488 RVKEQLAFQMEQV-KRESEMKMEEQSDQ------------LEKLKRELVAKAGELAHAqEALSRTEQS--GSELSSRLDT 552
Cdd:pfam15921 374 NLDDQLQKLLADLhKREKELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRL-EALLKAMKSecQGQMERQMAA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 553 LNAEKEALSgAIRQREAELLAAQSLVREKEEALSQEQ---QRSAQEKGELQGRLAEKE 607
Cdd:pfam15921 453 IQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKE 509
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
348-663 |
1.04e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 348 SMKDDRDLQIENLKREvETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQlrHELAQLKALQLEG 427
Cdd:pfam02463 201 KLKEQAKKALEYYQLK-EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEE--EKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 428 ARNQGLREEaERKASATEARYSKLKEKHNELINTHA--ELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQmeQVKRESE 505
Cdd:pfam02463 278 EKEKKLQEE-ELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKKEKEEIEELEKELKEL--EIKREAE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 MKMEEQSDQL----EKLKRELVAKAGEL-AHAQEALSRTEQSGSELSSRLDTLNAEKEALSgaIRQREAELLAAQSLVRE 580
Cdd:pfam02463 355 EEEEEELEKLqeklEQLEEELLAKKKLEsERLSSAAKLKEEELELKSEEEKEAQLLLELAR--QLEDLLKEEKKEELEIL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 581 KEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVS 660
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
...
gi 672073093 661 RAQ 663
Cdd:pfam02463 513 LAL 515
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
349-524 |
1.23e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 349 MKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKgqvnslEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGA 428
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER------AREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAE--------------RKASATEARYSKLKEKHNELINT--HAELLRKNADTAKQltvTQQSQEEVARVKEQ 492
Cdd:pfam17380 481 KEKRDRKRAEeqrrkilekeleerKQAMIEEERKRKLLEKEMEERQKaiYEEERRREAEEERR---KQQEMEERRRIQEQ 557
|
170 180 190
....*....|....*....|....*....|....*.
gi 672073093 493 LAFQMEQVKR----ESEMKMEEQSDQLEKLKRELVA 524
Cdd:pfam17380 558 MRKATEERSRleamEREREMMRQIVESEKARAEYEA 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
411-620 |
1.34e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 411 EQLRHELAQlKALQLEGARNqglreEAERKASATEARYSKLKEKHNELInTHAELLRKNADTAKQltvTQQSQEEVARVK 490
Cdd:pfam05557 12 SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQ-KRIRLLEKREAEAEE---ALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 491 EQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDtlnaEKEALSGAIRQREAE 570
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKASEAEQLRQN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 672073093 571 LLAAQSLVREKEE---ALSQEQQRSAQEKGEL------QGRLAEKESqeqgLQQKLLDE 620
Cdd:pfam05557 158 LEKQQSSLAEAEQrikELEFEIQSQEQDSEIVknskseLARIPELEK----ELERLREH 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-726 |
1.60e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 480 QQSQEEVARVKEQLAFQMEQVKrESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSR-------------------TE 540
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 541 QSGSELSSRLDTLN----AEKEALSgAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGL--Q 614
Cdd:COG3883 112 ESFSDFLDRLSALSkiadADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLsaE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 615 QKLLDEQFAVLRGAAAEAEAILQDAVSKLDDplhlrcTSSPDYLVSRAQAALDSVSGLEKGHTQYLASSEALAFVPADAS 694
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAA------AAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
250 260 270
....*....|....*....|....*....|..
gi 672073093 695 ALVAALTRFSHLAADTIVNGGATSHLAPTDPA 726
Cdd:COG3883 265 AGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
366-635 |
1.73e-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: 48.96 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 366 TLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALvdneqlrhELaqlkALQLEGARNQGLREEAERKASATE 445
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI--------EL----LLQQHQDRIEQLISEHEVEITGLT 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 446 ARYSKLKEKHNElINTHAELLRKNADTAKQLTVTQQSqeEVARVKEQLAFQMEQVKRESEmkmeeqsDQLEKLKRELVAK 525
Cdd:pfam15921 285 EKASSARSQANS-IQSQLEIIQEQARNQNSMYMRQLS--DLESTVSQLRSELREAKRMYE-------DKIEELEKQLVLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 526 AGELAHAQEALSRTEQSGSELSSRLDTLNAEkealsgaIRQREAELlaaqSLVREKEEALSQEQQRSAQEKGELQGRLAE 605
Cdd:pfam15921 355 NSELTEARTERDQFSQESGNLDDQLQKLLAD-------LHKREKEL----SLEKEQNKRLWDRDTGNSITIDHLRRELDD 423
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672073093 606 KESQEQGLQ----------QKLLDEQFAVLRGAAAEAEAI 635
Cdd:pfam15921 424 RNMEVQRLEallkamksecQGQMERQMAAIQGKNESLEKV 463
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
365-644 |
1.77e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 365 ETLRAELEKIKMEAQRYIS---QLKGQVNSLEA--ELEEQRKQKQKAL-VDNEQLRHELAQLKALQLEGARNQGLREEAE 438
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSrlgELKLRLNQATAtpELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQAS 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSKLKEKHNELI-------NTHAELLRKNA-------------------DTAKQLTVTQQSQE-------- 484
Cdd:pfam12128 506 EALRQASRRLEERQSALDELElqlfpqaGTLLHFLRKEApdweqsigkvispellhrtDLDPEVWDGSVGGElnlygvkl 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 485 EVARVKEQLAFQMEQVKRESEMKMEE----QSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEAL 560
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEalqsAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSE 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 561 SGAI-RQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKL---LDEQFAVLRGAAAEAEAIL 636
Cdd:pfam12128 666 KDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVegaLDAQLALLKAAIAARRSGA 745
|
....*...
gi 672073093 637 QDAVSKLD 644
Cdd:pfam12128 746 KAELKALE 753
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-650 |
2.07e-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: 48.96 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 361 KREVETLRAELEKIKMEAQ-------RYISQLKGQVNSLEAELEEQRKQKQKALvdnEQLRHELAqLKALQLEGARNQgl 433
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKI---EELEKQLV-LANSELTEARTE-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSKL------KEKHNELINTHAELLRkNADTAKQLTVTQQSQE------EVARV-------KEQLA 494
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLW-DRDTGNSITIDHLRRElddrnmEVQRLeallkamKSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 495 FQME------QVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDtlnaEKEAlsgAIRQRE 568
Cdd:pfam15921 444 GQMErqmaaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKER---AIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 569 AELLAAQSLVREKEEALSQ-----EQQRSAQEKGE-LQGRLAEKESQEQGLQQKLldEQFAVLRGAAAEAEAILQDAVSK 642
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHlknegDHLRNVQTECEaLKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQ 594
|
....*...
gi 672073093 643 LDDPLHLR 650
Cdd:pfam15921 595 LEKEINDR 602
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-526 |
2.15e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQRYISQ---LKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlQLE 426
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA-KLE 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 427 GARNQGLREEAERKA----SATEARYSKLKEKHNELinthAELLRKNADTakQLTVTQQSQEEVARVKEqLAFQMEQVKR 502
Cdd:TIGR02169 928 ALEEELSEIEDPKGEdeeiPEEELSLEDVQAELQRV----EEEIRALEPV--NMLAIQEYEEVLKRLDE-LKEKRAKLEE 1000
|
170 180
....*....|....*....|....
gi 672073093 503 ESEmKMEEQSDQLEKLKRELVAKA 526
Cdd:TIGR02169 1001 ERK-AILERIEEYEKKKREVFMEA 1023
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
378-641 |
2.27e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 378 AQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlQLEGARNQglREEAERKASATEARYsklkEKHNE 457
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAE--IDKLQAEIAEAEAEI----EERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 458 LINTHAELLRKNADTAKQLTVTQQSQ---------EEVARVKEQLAFQMEQVKRESEmKMEEQSDQLEKLKRELVAKAGE 528
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKA-ELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 529 LAHAQEALsrteqsgselssrlDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKES 608
Cdd:COG3883 166 LEAAKAEL--------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250 260 270
....*....|....*....|....*....|...
gi 672073093 609 QEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVS 641
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
353-617 |
2.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRY---ISQLKGQVNSLEAELEEQRK-QKQKALVDneQLRHELAQLKALQLEga 428
Cdd:PRK03918 443 RELTEEHRKELLEEYTAELKRIEKELKEIeekERKLRKELRELEKVLKKESElIKLKELAE--QLKELEEKLKKYNLE-- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 rnqglreEAERKASateaRYSKLKEKHNEL---INTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESE 505
Cdd:PRK03918 519 -------ELEKKAE----EYEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 MKMEEQSDQLEKL----------KRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLaaq 575
Cdd:PRK03918 588 EELEERLKELEPFyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL--- 664
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 672073093 576 slvREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKL 617
Cdd:PRK03918 665 ---REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
361-524 |
2.88e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 361 KREVETLRAELEKiKMEAQRYISQLKgqvnSLEAELEEQRKQKQKALVDNEQLRHELAQLKA----LQLEGARNQGLREE 436
Cdd:pfam05262 180 KKVVEALREDNEK-GVNFRRDMTDLK----ERESQEDAKRAQQLKEELDKKQIDADKAQQKAdfaqDNADKQRDEVRQKQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 437 AERKASATEARYSKLKEKHNElinthAELLRKNADTAKQltVTQQSQEEVARVKEQLAFQMEQVKRESEmKMEEQSDQLE 516
Cdd:pfam05262 255 QEAKNLPKPADTSSPKEDKQV-----AENQKREIEKAQI--EIKKNDEEALKAKDHKAFDLKQESKASE-KEAEDKELEA 326
|
....*...
gi 672073093 517 KLKRELVA 524
Cdd:pfam05262 327 QKKREPVA 334
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
347-636 |
2.91e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 347 GSMKDDRDLQIENLKREVEtlraelEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKA----------LVDNEQLRHE 416
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIE------EKEEKDLHERLNGLESELAELDEEIERYEEQREQAretrdeadevLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 417 LAQLKALQlegarnqglrEEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfq 496
Cdd:PRK02224 253 LETLEAEI----------EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 497 meqvKRESEMKmeeqsDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQS 576
Cdd:PRK02224 321 ----DRDEELR-----DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672073093 577 LVREKEEALSQeqqrSAQEKGELQGRLAEKESQEQGLQQKL--LDEQFAVLRGAAAEAEAIL 636
Cdd:PRK02224 392 EIEELRERFGD----APVDLGNAEDFLEELREERDELREREaeLEATLRTARERVEEAEALL 449
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
357-622 |
3.25e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 357 IENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKAlvdneqlrhelaqlkalqlegarnqglREE 436
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA---------------------------EEE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 437 AERKASATEARYSKLKEKHNEL--INTHAELLRKNADTAkqltvtqqsqEEVARVKEQLAfQMEQVKRESEMKMEEQSDQ 514
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIesLERIRTLLAAIADAE----------DEIERLREKRE-ALAELNDERRERLAEKRER 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 515 leklKRELVAKAGE--LAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLvREKEEALSQEQQR- 591
Cdd:PRK02224 636 ----KRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL-RERREALENRVEAl 710
|
250 260 270
....*....|....*....|....*....|....*..
gi 672073093 592 -----SAQEKGELQGRL-AEKESQEQGLQQKLLDEQF 622
Cdd:PRK02224 711 ealydEAEELESMYGDLrAELRQRNVETLERMLNETF 747
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
365-616 |
3.46e-05 |
|
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: 47.79 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 365 ETLRAELEKI-KMEAQRYISQLKGQVNSleAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEaerkasa 443
Cdd:pfam05483 363 ELLRTEQQRLeKNEDQLKIITMELQKKS--SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 444 tearyskLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESeMKMEEQSDQLEKLKRELV 523
Cdd:pfam05483 434 -------LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN-IELTAHCDKLLLENKELT 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 524 AKAG----ELAHAQEALSRTEQSGSELSSRLDTLNaEKEAlsgairQREAELLAAQSLVREKEEALSQEQQRSAQEKGEL 599
Cdd:pfam05483 506 QEASdmtlELKKHQEDIINCKKQEERMLKQIENLE-EKEM------NLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
250
....*....|....*..
gi 672073093 600 QGRLAEKESQEQGLQQK 616
Cdd:pfam05483 579 EYEVLKKEKQMKILENK 595
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
463-621 |
3.58e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 463 AELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEqs 542
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 543 gselsSRLDTLNAEKEALSGAIRQREAELLAAQSLVRE---KEEALSQEQQRSAQEK-GELQGRLAEKESQEQGLQQKLL 618
Cdd:TIGR02169 244 -----RQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELE 318
|
...
gi 672073093 619 DEQ 621
Cdd:TIGR02169 319 DAE 321
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
400-621 |
3.61e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 400 RKQKQKAlvdneQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLT-V 478
Cdd:TIGR00618 160 AKSKEKK-----ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLReA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 479 TQQSQEEVARVKEQLAFQMEQVKRESEM--------KMEEQSDQLEKL--KRELVAKAGELAHAQEALSRTEQSGSELSS 548
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLkqlrarieELRAQEAVLEETqeRINRARKAAPLAAHIKAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 549 RLDtlnaEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQ---RSAQEKGELQGRLAEKEsQEQGLQQKLLDEQ 621
Cdd:TIGR00618 315 ELQ----SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISC-QQHTLTQHIHTLQ 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-607 |
3.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETlRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKA---LVDNEQLRHELAQLKalQLEGARN 430
Cdd:PRK03918 175 KRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELE--KELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKaSATEARYSKLKEKHNELINTHAEL--LRKNADT--------AKQLTVTQQSQEEVARVKEQLAFQMEQV 500
Cdd:PRK03918 252 GSKRKLEEKI-RELEERIEELKKEIEELEEKVKELkeLKEKAEEyiklsefyEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 501 KRESEmkMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQsgseLSSRLDTLNAEKEALSgaIRQREAELLAAQslvRE 580
Cdd:PRK03918 331 KELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLT--PEKLEKELEELE---KA 399
|
250 260
....*....|....*....|....*..
gi 672073093 581 KEEaLSQEQQRSAQEKGELQGRLAEKE 607
Cdd:PRK03918 400 KEE-IEEEISKITARIGELKKEIKELK 425
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
346-583 |
3.97e-05 |
|
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: 47.79 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 346 NGSMKDDRDL-QIENLKREVETLRAELEKIKMEAQRYISQLKGQV-----NSLEAELEEQRKQKQKALVDN------EQL 413
Cdd:pfam05483 524 NCKKQEERMLkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdkseeNARSIEYEVLKKEKQMKILENkcnnlkKQI 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 414 RHELAQLKALQLEgarNQGLREE--AERKA-SATEARYSKL-------KEKHNELINTH-AELLRKNADTAKQLTVTQQS 482
Cdd:pfam05483 604 ENKNKNIEELHQE---NKALKKKgsAENKQlNAYEIKVNKLelelasaKQKFEEIIDNYqKEIEDKKISEEKLLEEVEKA 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 483 Q---EEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEalsrtEQSGSELSSRLDTLNAEKEA 559
Cdd:pfam05483 681 KaiaDEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ-----EQSSAKAALEIELSNIKAEL 755
|
250 260
....*....|....*....|....
gi 672073093 560 LSgAIRQREAELLAAQSLVREKEE 583
Cdd:pfam05483 756 LS-LKKQLEIEKEEKEKLKMEAKE 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
335-681 |
4.29e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 335 ADLFDQTFGPPNGSMKDDR----DLQIE--NLKREVETLRAEL----EKIKMEAQR-YISQLKGQVNSLEAELEEQRKQ- 402
Cdd:NF041483 414 ADQAEQLKGAAKDDTKEYRaktvELQEEarRLRGEAEQLRAEAvaegERIRGEARReAVQQIEEAARTAEELLTKAKADa 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 403 ---KQKALVDNEQLRHE-------LAQLKALQLEGARNQG--LREEAERKA----SATEARYSKLKEKHNELINTHA--- 463
Cdd:NF041483 494 delRSTATAESERVRTEaierattLRRQAEETLERTRAEAerLRAEAEEQAeevrAAAERAARELREETERAIAARQaea 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 464 --ELLRKNADTAKQLTVTQQS----QEEVARVKEQLAFQMEQVKRESEMK---MEEQSDQ-LEKLKRELVAKAGEL-AHA 532
Cdd:NF041483 574 aeELTRLHTEAEERLTAAEEAladaRAEAERIRREAAEETERLRTEAAERirtLQAQAEQeAERLRTEAAADASAArAEG 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 533 QEALSRTEQSGSELSSRLDTlnaekEALSGAIRQREAELLAAQSLVREKEEALSQEQQ---RSAQEKGELQGRLAEKESQ 609
Cdd:NF041483 654 ENVAVRLRSEAAAEAERLKS-----EAQESADRVRAEAAAAAERVGTEAAEALAAAQEeaaRRRREAEETLGSARAEADQ 728
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672073093 610 EQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDplhlRCTSSPDYLVSRAQAALDSVSGLEKGHTQYLA 681
Cdd:NF041483 729 ERERAREQSEELLASARKRVEEAQAEAQRLVEEADR----RATELVSAAEQTAQQVRDSVAGLQEQAEEEIA 796
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
396-534 |
5.06e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 47.35 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 396 LEEQRKQKQKaLVDNEQLRH-------ELAQLKALQ-LEGARNQgLREEAERKASateaRYSKLKEKHNELINTHAELLR 467
Cdd:pfam10168 544 FREEYLKKHD-LAREEIQKRvkllklqKEQQLQELQsLEEERKS-LSERAEKLAE----KYEEIKDKQEKLMRRCKKVLQ 617
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672073093 468 KNADTAKQLTVTQQS-QEEVARVKEQ---LAFQMEQVKreseMKMEEQSDQLEKLKRELVAKAGELAHAQE 534
Cdd:pfam10168 618 RLNSQLPVLSDAEREmKKELETINEQlkhLANAIKQAK----KKMNYQRYQIAKSQSIRKKSSLSLSEKQR 684
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
357-617 |
5.29e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 357 IENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQK---QKALVDN-EQLRHELAQLKALQLEGARNQ- 431
Cdd:pfam07111 308 LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailQRALQDKaAEVEVERMSAKGLQMELSRAQe 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARV---KEQLA--FQMEQVKRESEM 506
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVhtiKGLMArkVALAQLRQESCP 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 507 KME-------EQSDQLEKLKRELVAKAGEL---AH-AQEALSRTEQSGSelssrldtlnAEKEALSGAIRQREAELLAAQ 575
Cdd:pfam07111 468 PPPpappvdaDLSLELEQLREERNRLDAELqlsAHlIQQEVGRAREQGE----------AERQQLSEVAQQLEQELQRAQ 537
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 672073093 576 -SLVR--EKEEALSQEQQRSAQEKGELQGRLA-EKESQEQGLQQKL 617
Cdd:pfam07111 538 eSLASvgQQLEVARQGQQESTEEAASLRQELTqQQEIYGQALQEKV 583
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
354-648 |
5.54e-05 |
|
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: 47.26 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 354 DLQIENLKREVETLRAELEKIKMEA--------QRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLK---A 422
Cdd:COG5185 209 ESETGNLGSESTLLEKAKEIINIEEalkgfqdpESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAnnlI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 423 LQLEGARnQGLREEAERKASATEARYSKLKEKHNELINTHAELLRK-NADTAKQLTVTQQSQ----EEVARVKEQLA-FQ 496
Cdd:COG5185 289 KQFENTK-EKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKREtETGIQNLTAEIEQGQesltENLEAIKEEIEnIV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 497 MEQVKRESEMKMEEQSDQLEKLKRELVAKAGELA-HAQEALSRTEQSGSELSSRLdtlnaekEALSGAIRQREAELLAAQ 575
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRgYAQEILATLEDTLKAADRQI-------EELQRQIEQATSSNEEVS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 576 SLVRE------------KEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLldeqfAVLRGAAAEAEAILQDAVSKL 643
Cdd:COG5185 441 KLLNEliselnkvmreaDEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV-----STLKATLEKLRAKLERQLEGV 515
|
....*
gi 672073093 644 DDPLH 648
Cdd:COG5185 516 RSKLD 520
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
443-648 |
5.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 443 ATEARYSKLKEKHNELINTHAELLRKnADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKReseMKMEEQSDQLEKLKREL 522
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 523 VAKAGELAHAQEALSRTEQsgselssRLDTLNAEKEALSGAIRQREAELLAA-QSLVREKEEALSQEQQRSAQekgeLQG 601
Cdd:COG4913 298 EELRAELARLEAELERLEA-------RLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRAR----LEA 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 672073093 602 RLAEkesqeQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDPLH 648
Cdd:COG4913 367 LLAA-----LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
363-574 |
6.04e-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: 45.69 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 363 EVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRkqkqkalvdneqlrhelAQLKALQLEgarnqglREEAERKAS 442
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK-----------------TELEDLEKE-------IKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 443 ATEARYSKLKEKHNelinthaellrkNADTAKQLtvtQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEKLKREL 522
Cdd:COG1579 70 EVEARIKKYEEQLG------------NVRNNKEY---EALQKEIESLKRRIS-DLEDEILELMERIEELEEELAELEAEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 672073093 523 VAKAGELAHAQEALsrtEQSGSELSSRLDTLNAEKEALSGAIrqrEAELLAA 574
Cdd:COG1579 134 AELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI---PPELLAL 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
513-651 |
6.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 513 DQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKE---------ALSGAIRQREAE---LLAAQSLVR- 579
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAElerLDASSDDLAa 689
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672073093 580 --EKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLldeqfavlrgaaAEAEAILQDAVSKLDDPLHLRC 651
Cdd:COG4913 690 leEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL------------DELQDRLEAAEDLARLELRALL 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-645 |
7.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKM------------EAQRYISQLKGQVNSLEAELEEQRkqkqkalvdneQLRHELAQLKAl 423
Cdd:COG4717 103 ELEELEAELEELREELEKLEKllqllplyqeleALEAELAELPERLEELEERLEELR-----------ELEEELEELEA- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 424 QLEGARNQgLREEAERKASATEARYSKLKEKHNELINTHAELlrknadtakqltvtqqsQEEVARVKEQLAFQMEQVKR- 502
Cdd:COG4717 171 ELAELQEE-LEELLEQLSLATEEELQDLAEELEELQQRLAEL-----------------EEELEEAQEELEELEEELEQl 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 503 ESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALS----------------------RTEQSGSELSSRLDTLNAEKEAL 560
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 561 SGAIRQRE-AELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQglQQKLLDEQFAVLRGAAAEAEAILQDA 639
Cdd:COG4717 313 LEELEEEElEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAA 390
|
....*.
gi 672073093 640 VSKLDD 645
Cdd:COG4717 391 LEQAEE 396
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-640 |
9.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKM----EAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQ 431
Cdd:COG4717 164 ELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 GLREEAERKASAT---------------------------------EARYSKLKEKHNELINTHAELLRKNADTAKQLTV 478
Cdd:COG4717 244 RLKEARLLLLIAAallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 479 --------TQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAG-----ELAHAQEALSRTEqsgsE 545
Cdd:COG4717 324 llaalglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGvedeeELRAALEQAEEYQ----E 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 546 LSSRLDTLNAEKEALSGAIRQREAELLAAQslVREKEEALSQEQQRSAQEKGELQGRLAEKESQeqgLQQKLLDEQFAVL 625
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAE---LEQLEEDGELAEL 474
|
330
....*....|....*
gi 672073093 626 RGAAAEAEAILQDAV 640
Cdd:COG4717 475 LQELEELKAELRELA 489
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
377-597 |
1.13e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 377 EAQRYISQLKGQVNSLEA---ELEEQRKQKQKALvdneqlrhelaqlkALQLEGARNQG--------LREEAERKASATE 445
Cdd:PRK11637 93 ETQNTLNQLNKQIDELNAsiaKLEQQQAAQERLL--------------AAQLDAAFRQGehtglqliLSGEESQRGERIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 446 ARYSKLKEKHNELINthaELlrknadtakqltvtQQSQEEVARVKEQLafqmEQVKRESEMKMEEQSDQLEKLKRELVAK 525
Cdd:PRK11637 159 AYFGYLNQARQETIA---EL--------------KQTREELAAQKAEL----EEKQSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 526 AGELAHAQEALSRTEQSGSEL---SSRL-DTL-NAEKEALSGAIRQ-REAEllaaqsLVREKeealsqeqQRSAQEKG 597
Cdd:PRK11637 218 KKTLTGLESSLQKDQQQLSELranESRLrDSIaRAEREAKARAEREaREAA------RVRDK--------QKQAKRKG 281
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-612 |
1.15e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 352 DRDLQIENLK----REVETLRAELEKI------KMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLK 421
Cdd:pfam01576 226 ELQAQIAELRaqlaKKEEELQAALARLeeetaqKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 422 AlQLEG-----ARNQGLREEAERK-----------ASATEARYSKLKEKHNELINTHAELL------------------R 467
Cdd:pfam01576 306 T-ELEDtldttAAQQELRSKREQEvtelkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLeqakrnkanlekakqaleS 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 468 KNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVK---RESEMKMEEQSDQLEKLKREL--------------------VA 524
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQarlSESERQRAELAEKLSKLQSELesvssllneaegkniklskdVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 525 KAG-ELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSgaiRQREAELLAAQSLVREkeeaLSQEQQRSAQEKGELQGRL 603
Cdd:pfam01576 465 SLEsQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ---EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDA 537
|
....*....
gi 672073093 604 AEKESQEQG 612
Cdd:pfam01576 538 GTLEALEEG 546
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
347-634 |
1.22e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 347 GSMKDDRDLQIENLKREVETLRAELEKIkMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLE 426
Cdd:pfam19220 23 RSLKADFSQLIEPIEAILRELPQAKSRL-LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 427 G-ARNQGLREEAERKASATEARYSKLKEKHNELINTHAEL--LRKNADTAKQLTvtQQSQEEVARVKEQLAFqMEQVKRE 503
Cdd:pfam19220 102 AeAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENkaLREEAQAAEKAL--QRAEGELATARERLAL-LEQENRR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 504 SEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSS-----------RLDTLNAEKEALSGAIRQREAELL 572
Cdd:pfam19220 179 LQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAereraeaqleeAVEAHRAERASLRMKLEALTARAA 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672073093 573 AAQSLV-------REKEEALSQEQQRSAqekgELQGRLAEKESQEQGLQQKLLD--EQFAVLRGAAAEAEA 634
Cdd:pfam19220 259 ATEQLLaearnqlRDRDEAIRAAERRLK----EASIERDTLERRLAGLEADLERrtQQFQEMQRARAELEE 325
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
409-605 |
1.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 409 DNEQLRhELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELlrknadtakqltvtqqsQEEVAR 488
Cdd:COG1579 2 MPEDLR-ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-----------------EKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 489 VKEQLAFQMEQVKRESEmKMEEQSDQleklkRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQRE 568
Cdd:COG1579 64 LELEIEEVEARIKKYEE-QLGNVRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 672073093 569 AELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAE 605
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
356-617 |
1.46e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQRYISQLKGQVN---SLEAELEEQRKQkqkalVDNEQLRHelaqlkaLQLEgARNQG 432
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNlrtSAENDLVGLRKD-----LDEATLAR-------VDLE-AKIES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LREEAERkasatearyskLKEKHNELINthaELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQ- 511
Cdd:pfam00038 129 LKEELAF-----------LKKNHEEEVR---ELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWy 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRElVAKAGElahaqeALSRTEQSGSELSSRLDTLNAEKEALSGairQREAellaaqslvreKEEALSQEQQR 591
Cdd:pfam00038 195 QSKLEELQQA-AARNGD------ALRSAKEEITELRRTIQSLEIELQSLKK---QKAS-----------LERQLAETEER 253
|
250 260
....*....|....*....|....*.
gi 672073093 592 SAQEKGELQGRLAEKESQEQGLQQKL 617
Cdd:pfam00038 254 YELQLADYQELISELEAELQETRQEM 279
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
363-609 |
1.70e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.67 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 363 EVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKAlvdNEQLRHELAQLKALQleGARNQGLReeaeRKAS 442
Cdd:pfam15964 214 EDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDL---KERLKHKESLVAAST--SSRVGGLC----LKCA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 443 ATEArysKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFqmEQVKRESEMKMEEQSD------QLE 516
Cdd:pfam15964 285 QHEA---VLAQTHTNVHMQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAY--EQVKQAVQMTEEANFEktkaliQCE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 517 KLKRELVAKAgelahaqealSRTEQsgsELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEK 596
Cdd:pfam15964 360 QLKSELERQK----------ERLEK---ELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREK 426
|
250
....*....|...
gi 672073093 597 GELQGRLAEKESQ 609
Cdd:pfam15964 427 NSLVSQLEEAQKQ 439
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
348-526 |
1.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 348 SMKDDRDLQIENLKREVETLRaelEKIKMEAQRYISQLKgqvnsleAELEEQRKQKQKALVDNEQ--LRHELA---QLKA 422
Cdd:PRK12704 35 EAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLR-------NEFEKELRERRNELQKLEKrlLQKEENldrKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 423 LQLEGARNQGLREEAERKASATEARYSKLKEKHNELInthAELLRknadtAKQLTVTQQSQEEVARVKEQLAFQMEQVKR 502
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL---QELER-----ISGLTAEEAKEILLEKVEEEARHEAAVLIK 176
|
170 180
....*....|....*....|....
gi 672073093 503 ESEMKMEEQSDqleKLKRELVAKA 526
Cdd:PRK12704 177 EIEEEAKEEAD---KKAKEILAQA 197
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
352-634 |
1.75e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 352 DRDLQIENLKREVETLR----------AELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQlrhelaQLK 421
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQtdssntdtalTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKE------KVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 422 ALQlegarnqglREEAERKASATEaryskLKEKHNELinthAELLRKNADTAKQLTVT-QQSQEEVARVKEQLafQMEQV 500
Cdd:pfam10174 486 ALQ---------PELTEKESSLID-----LKEHASSL----ASSGLKKDSKLKSLEIAvEQKKEECSKLENQL--KKAHN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 501 KRESEMKMEEQSDQLEKLKRELVAKAGELAHAQealsrteqsgSELSSRLDTL-NAEKEALSGAIRQREAELLAA----- 574
Cdd:pfam10174 546 AEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ----------AEVERLLGILrEVENEKNDKDKKIAELESLTLrqmke 615
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 575 QSLVREKEEALSQEQQRSAQEkgELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEA 634
Cdd:pfam10174 616 QNKKVANIKHGQQEMKKKGAQ--LLEEARRREDNLADNSQQLQLEELMGALEKTRQELDA 673
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
480-639 |
1.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 480 QQSQEEVARVKEQ-LAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSEL--SSRLDTLNAE 556
Cdd:COG3206 192 EEAEAALEEFRQKnGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 557 KEALsgaiRQREAELLA--------AQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKL--LDEQFAVLR 626
Cdd:COG3206 272 LAEL----EAELAELSArytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLaqLEARLAELP 347
|
170
....*....|...
gi 672073093 627 GAAAEAEAILQDA 639
Cdd:COG3206 348 ELEAELRRLEREV 360
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
356-616 |
2.02e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAEL---EKIKMEAQRYISQL-------KGQVNSLEAELEEQRK-------QKQKA--LVDNEQLRHE 416
Cdd:pfam10174 476 ENKDLKEKVSALQPELtekESSLIDLKEHASSLassglkkDSKLKSLEIAVEQKKEecsklenQLKKAhnAEEAVRTNPE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 417 LA-QLKALQLEGARNqglREEAERKASATEARYSKLKEKHNE-------LINTHAELLRKNADTAKQLTVTQQSQEEVAR 488
Cdd:pfam10174 556 INdRIRLLEQEVARY---KEESGKAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 489 -----VKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAkagelahAQEALSRTEQSGSELSSRLDTLNAE-KEALSG 562
Cdd:pfam10174 633 kgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDA-------TKARLSSTQQSLAEKDGHLTNLRAErRKQLEE 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 672073093 563 AIRQREAELLAAQSlvrEKEE-----ALSQEQQRSAQEKGELQGRlaEKESQEQGLQQK 616
Cdd:pfam10174 706 ILEMKQEALLAAIS---EKDAniallELSSSKKKKTQEEVMALKR--EKDRLVHQLKQQ 759
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-616 |
2.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQI----ENLKREVETLRAElEKIKMEAQRYISQLKGQVNSLEAEleEQRKQKQKALVDNEQLRHELAQLKalql 425
Cdd:PTZ00121 1149 EDAKRVEIarkaEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRKAE--DARKAEAARKAEEERKAEEARKAE---- 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 426 EGARNQGLREEAERKASATEARYSKlKEKHNELINTHAEllrknADTAKQLTVTQQSQEEVARVKEQLAfqmeqvKRESE 505
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEE-----ARMAHFARRQAAIKAEEARKADELK------KAEEK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 506 MKMEEQSDQLEKLK-RELVAKAGELAHAQEALSRTEqsgsELSSRLDTL--NAEKEALSGAIRQREAELLAAQSLVREKE 582
Cdd:PTZ00121 1290 KKADEAKKAEEKKKaDEAKKKAEEAKKADEAKKKAE----EAKKKADAAkkKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270
....*....|....*....|....*....|....
gi 672073093 583 EALSQEQQRSAQEKGELQGRLAEKESQEQGLQQK 616
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
449-634 |
2.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 449 SKLKEKHNELINTHAELLRKNADTAKQLtvtqQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKREL--VAKA 526
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 527 GELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGA---IRQREAELLAAQSLVREKEEALSQEQ----QRSAQEKGEL 599
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLSLATeeelQDLAEELEEL 204
|
170 180 190
....*....|....*....|....*....|....*..
gi 672073093 600 QGRLAEKESQEQGLQQKL--LDEQFAVLRGAAAEAEA 634
Cdd:COG4717 205 QQRLAELEEELEEAQEELeeLEEELEQLENELEAAAL 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
474-647 |
2.31e-04 |
|
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: 44.89 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 474 KQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTL 553
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 554 NAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQ-----KLLDEQFAVLRGA 628
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelRSLSKEFQELRNS 200
|
170 180
....*....|....*....|..
gi 672073093 629 AAEAEA---ILQDAVSKLDDPL 647
Cdd:pfam07888 201 LAQRDTqvlQLQDTITTLTQKL 222
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
356-596 |
2.45e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.42 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKmeaQRYISQL-KGQVNSLEAELEEQRKQKQKALvdNEQLRHELAQlKALQLEGARNQGLR 434
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLK---NTTPKDMwLEDLDKFEEALEEQEEVEEKEI--AKEQRLKSKT-KGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 435 EEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQ 514
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSED 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 515 LEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNA----EKEALSGAIRQREAELLAAQSLVREKEEALSQEQQ 590
Cdd:PTZ00108 1257 NDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNggskPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK 1336
|
....*.
gi 672073093 591 RSAQEK 596
Cdd:PTZ00108 1337 SKTRVK 1342
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
350-456 |
2.83e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLK---REVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlQLe 426
Cdd:PRK09039 76 NQDLQDSVANLRaslSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRR-QL- 153
|
90 100 110
....*....|....*....|....*....|
gi 672073093 427 gARNQGLREEAERKASATEARYSKLKEKHN 456
Cdd:PRK09039 154 -AALEAALDASEKRDRESQAKIADLGRRLN 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-522 |
3.38e-04 |
|
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: 45.05 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQryisQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlqlegar 429
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRR------- 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 nqgLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVT-----QQSQEEVARVKEQLA-------FQM 497
Cdd:TIGR02168 916 ---ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKieddeEEARRRLKRLENKIKelgpvnlAAI 992
|
170 180
....*....|....*....|....*..
gi 672073093 498 EQVKRESEMK--MEEQSDQLEKLKREL 522
Cdd:TIGR02168 993 EEYEELKERYdfLTAQKEDLTEAKETL 1019
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
385-581 |
3.45e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 385 LKGQVNSLEAELEEQRKQKQKALVDNE----QLRHELAQLKALQlegarnqglrEEAERKASATEARYSKLKEKhnelin 460
Cdd:COG1842 10 IRANINALLDKAEDPEKMLDQAIRDMEedlvEARQALAQVIANQ----------KRLERQLEELEAEAEKWEEK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 461 thAEL-LRKNA-DTAKQ-LTVTQQSQEEVARVKEQLAFQMEQVKresemKMEEQSDQLEKLKRELVAKAGELAhAQEALS 537
Cdd:COG1842 74 --ARLaLEKGReDLAREaLERKAELEAQAEALEAQLAQLEEQVE-----KLKEALRQLESKLEELKAKKDTLK-ARAKAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 672073093 538 RTEQSGSELSSRLDTLNAEK--EALSGAIRQREAELLAAQSLVREK 581
Cdd:COG1842 146 KAQEKVNEALSGIDSDDATSalERMEEKIEEMEARAEAAAELAAGD 191
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
360-651 |
3.59e-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: 44.57 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 360 LKREVETLRAELEKIKMEAQRYisqlKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQL-KALQLEGARNQGLREEAE 438
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASL----KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqDLTEKLSEAEDMLACEQH 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKL 518
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 519 KRELvAKAGELAHAQEALSRT-----EQSGSELSSRLDTLNAEKEALSGAIRQreaellaAQSLVREKEEALSQEQQRSA 593
Cdd:TIGR00618 696 KEML-AQCQTLLRELETHIEEydrefNEIENASSSLGSDLAAREDALNQSLKE-------LMHQARTVLKARTEAHFNNN 767
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 594 QEKGELQGRLAEKESQEQGLQQKllDEQFAVLRGAAAEAEAILQDAVSKLDDPLHLRC 651
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFF--NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
435-719 |
3.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 435 EEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQMEQV-KRESEMKMEEQS- 512
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELgERARALYRSGGSv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 513 DQLEKLkreLVAK-AGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQR 591
Cdd:COG3883 103 SYLDVL---LGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 592 SAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVSRAQAALDSVSG 671
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 672073093 672 LEKGHTQYLASSEALAFVPADASALVAALTRFSHLAADTIVNGGATSH 719
Cdd:COG3883 260 GSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGS 307
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
350-621 |
3.81e-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: 44.57 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAE-LEEQRKQKQKALVDNEQLRHELAQLKALQLEGA 428
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHV 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTakQLTVTQQSQEEVARVKEQLAfqmeqvKRESEMKM 508
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT--QHIHTLQQQKTTLTQKLQSL------CKELDILQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 509 EEQSDQLEKLKRELVAKaGELAHAqealsRTEQSGSELSSRLDTLNAEKEALSgaIRQREAELLAAQSLVREKEEALSQE 588
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQ-GQLAHA-----KKQQELQQRYAELCAAAITCTAQC--EKLEKIHLQESAQSLKEREQQLQTK 478
|
250 260 270
....*....|....*....|....*....|...
gi 672073093 589 QQRSAQEKGelQGRLAEKESQEQGLQQKLLDEQ 621
Cdd:TIGR00618 479 EQIHLQETR--KKAVVLARLLELQEEPCPLCGS 509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-595 |
4.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERKASATEARYSKLKEKHNELI----NTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQ 511
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDakedNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRldtlnaEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQR 591
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER 1212
|
....
gi 672073093 592 SAQE 595
Cdd:PTZ00121 1213 KAEE 1216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
362-617 |
4.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 362 REVETLRAELEKIKMEAQRYISQLKGQVNSLEAE----LEEQRKQKQKALVD-----NEQLRHELAQL--KALQLEGARN 430
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAKRVEiarkaEDARKAEEARKaeDAKKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASATEARYSKLKEKHNELinTHAELLRKNADTAKQltvtqqsqEEVARVkEQLAFQMEQVKRESEMKMEE 510
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAARKAEEE--RKAEEARKAEDAKKA--------EAVKKA-EEAKKDAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 511 QSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTL-NAEKEALSGAIRQREAELLAAQSLVREKEEAlsQEQ 589
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKK 1330
|
250 260
....*....|....*....|....*....
gi 672073093 590 QRSAQEKGELQGRLAE-KESQEQGLQQKL 617
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEaAKAEAEAAADEA 1359
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
391-642 |
4.75e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 391 SLEAELEEQRKQKQKALVDNEQLRHELAQLKALQL-EGarnqglrEEAErkasatearyskLKEKHNELinTHAELLRKN 469
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAALqPG-------EEEE------------LEEERRRL--SNAEKLREA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 470 ADTAKQLTvtqqSQEEVArvkeqLAFQMEQVKRESEmKMEEQSDQLEKLKRELvakagelahaQEALSRTEQSGSELSSR 549
Cdd:COG0497 228 LQEALEAL----SGGEGG-----ALDLLGQALRALE-RLAEYDPSLAELAERL----------ESALIELEEAASELRRY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 550 LDTLNAEKEALSgAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQG---RLAEKESQEQGLQQKLLD--EQFAV 624
Cdd:COG0497 288 LDSLEFDPERLE-EVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENsdeRLEELEAELAEAEAELLEaaEKLSA 366
|
250
....*....|....*...
gi 672073093 625 LRGAAAEAeaiLQDAVSK 642
Cdd:COG0497 367 ARKKAAKK---LEKAVTA 381
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
353-617 |
5.04e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKMEAQRY--------------------------ISQLKGQVNSLEAELEEQRKQKQKA 406
Cdd:PRK04863 784 REKRIEQLRAEREELAERYATLSFDVQKLqrlhqafsrfigshlavafeadpeaeLRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 407 LVDNEQLRHELAQLKALQ------LEGARNQGLREEAERKASATEARYSklkekhnelINTHAELLRKnadTAKQLTVTQ 480
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLprlnllADETLADRVEEIREQLDEAEEAKRF---------VQQHGNALAQ---LEPIVSVLQ 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 481 QSQEEVARVKEQLAfQMEQVKRESEMkmeeqsdQLEKLKrELVAKAGELAH--AQEALSRTEQSGSELSSRLDTLNAEKE 558
Cdd:PRK04863 932 SDPEQFEQLKQDYQ-QAQQTQRDAKQ-------QAFALT-EVVQRRAHFSYedAAEMLAKNSDLNEKLRQRLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 559 ALSGAIRQREAE-------LLAAQSLVREKEE---ALSQE------------QQRSAQEKGELQGRLAEKESQEQGLQQK 616
Cdd:PRK04863 1003 RAREQLRQAQAQlaqynqvLASLKSSYDAKRQmlqELKQElqdlgvpadsgaEERARARRDELHARLSANRSRRNQLEKQ 1082
|
.
gi 672073093 617 L 617
Cdd:PRK04863 1083 L 1083
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
348-610 |
5.26e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 348 SMKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKgqvnSLEAELEEQRKQKqKALVdnEQLRHELAQLKALQLEG 427
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELK----ELAEKRDELNAQV-KELR--EEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 428 ARNQGLREEAERKASATEARYSKLKEKHNELINTHAEL--LRKNADtakQLTVTQQSQ-----------EEVARVKEQLA 494
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIdkLRKEIE---RLEWRQQTEvlspeeekelvEKIKELEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 495 FQMEQVKRESEMK-----MEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREA 569
Cdd:COG1340 151 KAKKALEKNEKLKelraeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672073093 570 ELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQE 610
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
358-458 |
5.40e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAE----LEEQRKQKQKALvdnEQLRHELAQ----LKALQLEGAR 429
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEedklLEEAEKEAQQAI---KEAKKEADEiikeLRQLQKGGYA 602
|
90 100
....*....|....*....|....*....
gi 672073093 430 NQGLREeaerkasATEARySKLKEKHNEL 458
Cdd:PRK00409 603 SVKAHE-------LIEAR-KRLNKANEKK 623
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
358-645 |
6.12e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIKMEAQRYISQLKGQV--NSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLRE 435
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 436 EAERkaSATEARYSKLKEKHNELinthaELLRKNADTAKQLTVTQQS----QEEVARVKEQLAFQMEQVKRESEMKMEEQ 511
Cdd:pfam13868 131 EIDE--FNEEQAEWKELEKEEER-----EEDERILEYLKEKAEREEEreaeREEIEEEKEREIARLRAQQEKAQDEKAER 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAE---LLAAQSLVREKEEALSQE 588
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEferMLRKQAEDEEIEQEEAEK 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 589 Q-QRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:pfam13868 284 RrMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-556 |
6.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEkikmEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARN 430
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELE----ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASAT-EARYSKLKEKHN----ELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqmeqvkRESE 505
Cdd:COG4913 757 AALGDAVERELRENlEERIDALRARLNraeeELERAMRAFNREWPAETADLDADLESLPEYLALLDRL--------EEDG 828
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 672073093 506 mkMEEQSDQLEKLKRElvAKAGELAHAQEALSRTEQSGSElssRLDTLNAE 556
Cdd:COG4913 829 --LPEYEERFKELLNE--NSIEFVADLLSKLRRAIREIKE---RIDPLNDS 872
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
398-574 |
7.20e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.05 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 398 EQRKQKQKALvdNEQLRHELAQLKALQLEGARnqgLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLT 477
Cdd:cd00176 36 EALLKKHEAL--EAELAAHEERVEALNELGEQ---LIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 478 VTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSS-----RLDT 552
Cdd:cd00176 111 FFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADeeieeKLEE 190
|
170 180
....*....|....*....|..
gi 672073093 553 LNAEKEALSGAIRQREAELLAA 574
Cdd:cd00176 191 LNERWEELLELAEERQKKLEEA 212
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
360-609 |
8.33e-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: 43.63 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 360 LKREVETLRAELE-----KIKMEAQRyiSQLKGQVNSLEAELEEQRK------QKQKALvdnEQLrheLAQLKALQlegA 428
Cdd:pfam01576 550 LQRELEALTQQLEekaaaYDKLEKTK--NRLQQELDDLLVDLDHQRQlvsnleKKQKKF---DQM---LAEEKAIS---A 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLafqmEQVKRESEMKM 508
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHEL----ERSKRALEQQV 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 509 EEQSDQLEKLKRELVAkagelahAQEALSRTE--------QSGSELSSRLDTLNAEKEALSGAIRQREAELlaaqslvre 580
Cdd:pfam01576 695 EEMKTQLEELEDELQA-------TEDAKLRLEvnmqalkaQFERDLQARDEQGEEKRRQLVKQVRELEAEL--------- 758
|
250 260
....*....|....*....|....*....
gi 672073093 581 kEEALSQEQQRSAQEKgELQGRLAEKESQ 609
Cdd:pfam01576 759 -EDERKQRAQAVAAKK-KLELDLKELEAQ 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
388-645 |
8.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 388 QVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALqlEGARNQGLREEAERKASATEARYSKLKEKHNElinthAELLR 467
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEA--ESDLEQDYQAASDHLNLVQTALRQQEKIERYQ-----ADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 468 KNADTAKQLTVTQQSQEEVARVKEQlafqmeqvKRESEMKMEEQSDQLEKLKRELVA---KAGELAHAQEALSRTEQ--- 541
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEAR--------AEAAEEEVDELKSQLADYQQALDVqqtRAIQYQQAVQALERAKQlcg 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 542 ----SGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALS-------------------------QEQQRS 592
Cdd:PRK04863 432 lpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiagevsrseawdvarellrrlREQRHL 511
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 593 AQEKGELQGRLAEKE--SQEQGLQQKLLDE---QFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:PRK04863 512 AEQLQQLRMRLSELEqrLRQQQRAERLLAEfckRLGKNLDDEDELEQLQEELEARLES 569
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
349-450 |
9.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 349 MKDDRDL--QIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLE 426
Cdd:COG3883 128 ADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|....
gi 672073093 427 GARNQGLREEAERKASATEARYSK 450
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
410-645 |
1.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 410 NEQLRHELAQLKALQLEGARnqgLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARV 489
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQ---LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 490 KEQLafqmeqvkresemkmEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREA 569
Cdd:COG4372 107 QEEA---------------EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672073093 570 ELLA-AQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDD 645
Cdd:COG4372 172 ELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
363-600 |
1.03e-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: 43.50 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 363 EVETLRAELEKIKMEAQRYISQLKGQVNSL---EAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAER 439
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIdlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 440 KASATEARYSKLKEKHNELINTHAELLRKNADtakqLTVTQQSQEevarvKEQLAFQMEQVKRESEMK---MEEQSDQLE 516
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLD----RTVQQVNQE-----KQEKQHELDTVVSKIELNrklIQDQQEQIQ 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 517 KLKrelvAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELL----AAQSLVREKEEALSQEQQRS 592
Cdd:TIGR00606 861 HLK----SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpletFLEKDQQEKEELISSKETSN 936
|
....*...
gi 672073093 593 AQEKGELQ 600
Cdd:TIGR00606 937 KKAQDKVN 944
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
377-529 |
1.05e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 377 EAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKalqlegarnQGLREEAERKASATEARYSKLKEKHN 456
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLK---------EELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672073093 457 ELINThaelLRKNADTAKQLTVTQQsQEEVARVKEQlafQMEQVKResemKMEEQSDQLEKLKRELVAKAGEL 529
Cdd:PRK00409 577 QAIKE----AKKEADEIIKELRQLQ-KGGYASVKAH---ELIEARK----RLNKANEKKEKKKKKQKEKQEEL 637
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
356-586 |
1.12e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKM------EAQRYISQLKGQVNSLEAELEEQRkqkqkalvdNEQLRHELAQLKALQLEGAR 429
Cdd:PRK01156 516 KSINEYNKIESARADLEDIKIkinelkDKHDKYEEIKNRYKSLKLEDLDSK---------RTSWLNALAVISLIDIETNR 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQglREEAERKASATEARYSKLkEKHNELINTHAE-LLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKm 508
Cdd:PRK01156 587 SR--SNEIKKQLNDLESRLQEI-EIGFPDDKSYIDkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI- 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 509 eeqsDQLEKLKRELVAKAGE----LAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAEL------LAAQSLV 578
Cdd:PRK01156 663 ----DSIIPDLKEITSRINDiednLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLesmkkiKKAIGDL 738
|
....*...
gi 672073093 579 REKEEALS 586
Cdd:PRK01156 739 KRLREAFD 746
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
355-645 |
1.19e-03 |
|
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: 42.79 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 355 LQIENLKREVETLRAELEKIkMEAQR-YISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGA----R 429
Cdd:pfam05483 95 VSIEAELKQKENKLQENRKI-IEAQRkAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAektkK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEA-------------------ERKASATEAR---YSKLKEKHNELINTHAELLRKNADTAKQLT---------- 477
Cdd:pfam05483 174 YEYEREETrqvymdlnnniekmilafeELRVQAENARlemHFKLKEDHEKIQHLEEEYKKEINDKEKQVSllliqiteke 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 478 --------VTQQSQEEVARVKEQLAFQMEQVKRESEmKMEEQSDQLEKLK----RELVAKAGELAHAQEALSRTEQSGSE 545
Cdd:pfam05483 254 nkmkdltfLLEESRDKANQLEEKTKLQDENLKELIE-KKDHLTKELEDIKmslqRSMSTQKALEEDLQIATKTICQLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 546 LSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQ-------------- 611
Cdd:pfam05483 333 KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkeveleelkk 412
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 672073093 612 --GLQQKLLDEQFAV------LRGAAAEAEAILQDAVSKLDD 645
Cdd:pfam05483 413 ilAEDEKLLDEKKQFekiaeeLKGKEQELIFLLQAREKEIHD 454
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
356-521 |
1.39e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKmeaQRYI---------SQLKGQVNSLEAELEE--QRKQKQKA----LVDN-EQLRHELAQ 419
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVK---QSYTlneselesvRQLEKQLESLEKQYDEitERIAEQEIayseLQEElEEILKQLEE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 420 LKALQLEGARN-QGLREEaERKASATEARYSklkekhNELINTHAELLRKN-----ADTAKQLTVTQQSQEEVARVKEQL 493
Cdd:PRK04778 395 IEKEQEKLSEMlQGLRKD-ELEAREKLERYR------NKLHEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEEK 467
|
170 180
....*....|....*....|....*...
gi 672073093 494 AFQMEQVKREsemkMEEQSDQLEKLKRE 521
Cdd:PRK04778 468 PINMEAVNRL----LEEATEDVETLEEE 491
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
448-609 |
1.40e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 448 YSKLKEK------HNELINTHAELLRKNADTAKQ-LTVTQQSQEEVARVKEQLafqmeqvkRESEMKMEEQSDQLEKLKR 520
Cdd:smart00787 125 FARLEAKkmwyewRMKLLEGLKEGLDENLEGLKEdYKLLMKELELLNSIKPKL--------RDRKDALEEELRQLKQLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 521 EL-VAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGEL 599
Cdd:smart00787 197 ELeDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
170
....*....|
gi 672073093 600 QGRLAEKESQ 609
Cdd:smart00787 277 KEQLKLLQSL 286
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
351-639 |
1.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKgqvNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlQLEGARN 430
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQE-ELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 431 QGLREEAERKASATEARYSKLKEK--------------------------------------HNELINTHAELLRKNADT 472
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 473 AKQLTVTQQSQEEVARVKEQLAF--------------QMEQVKRESEMKMEEQS----DQLEKLKRELVAKAG------- 527
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLppdlspeellelldRIEELQELLREAEELEEelqlEELEQEIAALLAEAGvedeeel 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 528 -ELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGA-----IRQREAELLAAQSLVREKEEALSQEQQRSAQEKGEL-- 599
Cdd:COG4717 388 rAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldeeeLEEELEELEEELEELEEELEELREELAELEAELEQLee 467
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 672073093 600 QGRLAEKESQEQGLQQKL--LDEQFAVLRGAAAEAEAILQDA 639
Cdd:COG4717 468 DGELAELLQELEELKAELreLAEEWAALKLALELLEEAREEY 509
|
|
| PriC |
COG3923 |
Primosomal replication protein N'' [Replication, recombination and repair]; |
376-542 |
1.62e-03 |
|
Primosomal replication protein N'' [Replication, recombination and repair];
Pssm-ID: 443127 [Multi-domain] Cd Length: 179 Bit Score: 40.67 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 376 MEAQRYISQLKGQVNSLEAELEEQ-RKQKQKALVD-------NEQLRHELAQLKAL--QLEGARNQGLREEAERKASATE 445
Cdd:COG3923 1 MKTSQLLQTLEQQLDQLAQQIAPLaDHRTLQARFDrqlfstrSTRLQDYLQEARQNlaQLEQAVEANRTQQVAFLAERLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 446 ARYSKLKEkhnELINTHaelLRKNaDTAKQLTVTQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEK--LKRELV 523
Cdd:COG3923 81 AQIAALQR---ELATQS---LRKQ-EPRSASKPILDLYQKLAQHQEYER-RLLAMIRDRESQLEQATTLAEQqrLQKELA 152
|
170
....*....|....*....
gi 672073093 524 AKAGELAHAQEALSRTEQS 542
Cdd:COG3923 153 ALEGRLARCRQALARIERQ 171
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
356-593 |
1.87e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQ--RYISQL-KGQVNSLEAELEEQRKQKQKALVDNEQLRHE--LAQLKAL--QLEGA 428
Cdd:pfam05701 71 ELESTKRLIEELKLNLERAQTEEAqaKQDSELaKLRVEEMEQGIADEASVAAKAQLEVAKARHAaaVAELKSVkeELESL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKASATEARYSKLKEKHN---------ELINTHAEL------------------LRKNADTAKQLTVTQQ 481
Cdd:pfam05701 151 RKEYASLVSERDIAIKRAEEAVSASKEIektveeltiELIATKESLesahaahleaeehrigaaLAREQDKLNWEKELKQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 482 SQEEVARVKEQLAfqmeqVKRESEMKMEEQSDQLEKLKRELVAKA-GELAHAQEALSRTEQSGSELSSRLDTLNAEKEAL 560
Cdd:pfam05701 231 AEEELQRLNQQLL-----SAKDLKSKLETASALLLDLKAELAAYMeSKLKEEADGEGNEKKTSTSIQAALASAKKELEEV 305
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672073093 561 SGAIRQREAEL----LAAQSLV----REKEEaLSQEQQRSA 593
Cdd:pfam05701 306 KANIEKAKDEVnclrVAAASLRseleKEKAE-LASLRQREG 345
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
322-515 |
2.05e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 322 SSGPPAGEPVQVVADLFDQTFGPPNGSMKDDRDLQIENLK-REVETLRAELEKIKMEAQRYIS----QLKGQVNSLEAEL 396
Cdd:PRK10929 92 RDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRaREISDSLSQLPQQQTEARRQLNeierRLQTLGTPNTPLA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 397 EEQRKQKQ------KALVDN---EQL----RHELAQLKA-----------LQLEGARNQgLREEAERKASATEARYSKLK 452
Cdd:PRK10929 172 QAQLTALQaesaalKALVDElelAQLsannRQELARLRSelakkrsqqldAYLQALRNQ-LNSQRQREAERALESTELLA 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672073093 453 EKHNELINTHAELLRKNADTAKQLTvtQQSQE--EVARVKEQLAFQMEQVkRESEMKMEEQSDQL 515
Cdd:PRK10929 251 EQSGDLPKSIVAQFKINRELSQALN--QQAQRmdLIASQQRQAASQTLQV-RQALNTLREQSQWL 312
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
358-561 |
2.17e-03 |
|
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: 42.08 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAEL----------------EKIKMEAQryISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLK 421
Cdd:pfam01576 853 ERARRQAQQERDELadeiasgasgksalqdEKRRLEAR--IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAER 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 422 AL--QLEGARNQGLREEAERKASATEARySKLKEKHNELInthAELLRKNADTAKQLTVT----QQSQEEVARVKEQLAF 495
Cdd:pfam01576 931 STsqKSESARQQLERQNKELKAKLQEME-GTVKSKFKSSI---AALEAKIAQLEEQLEQEsrerQAANKLVRRTEKKLKE 1006
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672073093 496 QMEQVkrESEMKMEEQ-SDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALS 561
Cdd:pfam01576 1007 VLLQV--EDERRHADQyKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
349-639 |
2.26e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 349 MKDDRDLqiENLKREVETLRAELEKIKMEAQRYISQlkgqvnsleAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGA 428
Cdd:PRK07735 1 MDPEKDL--EDLKKEAARRAKEEARKRLVAKHGAEI---------SKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 429 RNQGLREEAERKAS-ATEARYSKLKEK-HNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKR---- 502
Cdd:PRK07735 70 KAAALAKQKREGTEeVTEEEKAKAKAKaAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQkreg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 503 ESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSL----- 577
Cdd:PRK07735 150 TEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASqgngd 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672073093 578 -------------VREKEEALSQEQQRSAQEKGElqgrlAEKESQEQGLQQKLLDEQFAVLRGAAaeAEAILQDA 639
Cdd:PRK07735 230 sgdedakakaiaaAKAKAAAAARAKTKGAEGKKE-----EEPKQEEPSVNQPYLNKYVEVIKEKL--GEDVLEDS 297
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
481-668 |
2.34e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 481 QSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQS------------------ 542
Cdd:pfam15921 138 QSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAsgkkiyehdsmstmhfrs 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 543 -GSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRS-----AQEKGELQGrLAEKES-------- 608
Cdd:pfam15921 218 lGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieqliSEHEVEITG-LTEKASsarsqans 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672073093 609 --------QEQGLQQKL--------LDEQFAVLRGAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVSRAQAALDS 668
Cdd:pfam15921 297 iqsqleiiQEQARNQNSmymrqlsdLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
395-559 |
2.56e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 395 ELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEK---------HNELINTHAEL 465
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQaaqerarqqQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 466 LRKnadtaKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKlKRELVAKAgelahAQEALSRTEQsgSE 545
Cdd:pfam15709 436 QRK-----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ-KQEAEEKA-----RLEAEERRQK--EE 502
|
170
....*....|....
gi 672073093 546 LSSRLDTLNAEKEA 559
Cdd:pfam15709 503 EAARLALEEAMKQA 516
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
353-637 |
2.58e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 353 RDLQIENLKREVETLRAELEKIKmEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLrhELAQLKALQ-------- 424
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLK-NRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSEL--ELKMEKVFQgtdeqlnd 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 425 LEGARNQGLREEAERKASAtEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRES 504
Cdd:TIGR00606 306 LYHNHQRTVREKERELVDC-QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 505 EMKMEEQSDQLEKLKRE-------LVAK-----AGELAHAQEALSRTEqsgSELSSRLDTLNAEKEALSGAIRQREAELL 572
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIErqedeakTAAQlcadlQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVIK 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 573 AAQSLVREKEEALSQEQqrsAQEKGELQGRLAEKESQEQGLQQK---LLDEQFAVLRGAAAEAEAILQ 637
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEvksLQNEKADLDRKLRKLDQEMEQ 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
465-640 |
3.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 465 LLRKNADTAKQLtvtqQSQEEVARVKEQLAFQMEQVKREsemKMEEQSDQLEKLKRELvakagelahaqealsrteqsgs 544
Cdd:PRK12704 23 FVRKKIAEAKIK----EAEEEAKRILEEAKKEAEAIKKE---ALLEAKEEIHKLRNEF---------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 545 elssrldtlnaEKEalsgaIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQK------LL 618
Cdd:PRK12704 74 -----------EKE-----LRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKeeeleeLI 137
|
170 180
....*....|....*....|....*.
gi 672073093 619 DEQFAVLRGAAA----EAEAILQDAV 640
Cdd:PRK12704 138 EEQLQELERISGltaeEAKEILLEKV 163
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
480-611 |
3.90e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 480 QQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQL-EKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKE 558
Cdd:PRK12705 29 QRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRErNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 672073093 559 ALSGAIRQREAELLAAQSLVREK-EEAlsqEQQRSAQEKGELQGRLaEKESQEQ 611
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNElYRV---AGLTPEQARKLLLKLL-DAELEEE 158
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
378-590 |
4.27e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 378 AQRYISQLKGQVNSLEAELEEQRKQKQKAlvdnEQLRHELA--QLKALQLEGARnqgLREEAERKASATEARYSKLKEKH 455
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQA----EELQQKQAaeQERLKQLEKER---LAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 456 NElinthaellrknADTAKQLTVTQQSQEEVARVKEQLAFQME---QVKRESEMKMEEQSDQLEKLKRELVAKAGELAHA 532
Cdd:PRK09510 134 AE------------EAAAKAAAAAKAKAEAEAKRAAAAAKKAAaeaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 672073093 533 QEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQslvREKEEALSQEQQ 590
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA---KAAEKAAAAKAA 256
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
417-645 |
4.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 417 LAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVAR----VKEQ 492
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTlegeGGSA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 493 LAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELL 572
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 573 AAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGL--------------QQKL--LDEQFAVLRGAAAEaeaiL 636
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYdfLSEQREDLEEARET----L 814
|
....*....
gi 672073093 637 QDAVSKLDD 645
Cdd:COG1196 815 EEAIEEIDR 823
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
417-595 |
4.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 417 LAQLKALQLEGARNQGLrEEAERKASAtearysklkEKHNELINTHAELLRKNADTAKQLtvtQQSQEEVARVKEQLAFQ 496
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL-EEAKKEAEA---------IKKEALLEAKEEIHKLRNEFEKEL---RERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 497 MEQVKRESEmkmeeqsdQLEKLKRELVAKAGELAHAQEALSRTEQsgsELSSRLDTLNAEKEALSG---------AIRQR 567
Cdd:PRK12704 95 EENLDRKLE--------LLEKREEELEKKEKELEQKQQELEKKEE---ELEELIEEQLQELERISGltaeeakeiLLEKV 163
|
170 180
....*....|....*....|....*....
gi 672073093 568 EAELLA-AQSLVREKEEALSQEQQRSAQE 595
Cdd:PRK12704 164 EEEARHeAAVLIKEIEEEAKEEADKKAKE 192
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
350-570 |
5.21e-03 |
|
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: 40.71 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 350 KDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALvdnEQLRHELAQLKALqlegar 429
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQI---EQATSSNEEVSKL------ 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 NQGLREEAERK-ASATEARYSKLKEKHNELINTHAELLRKNADTAKQL-----TVTQQSQEEVARVKEQLAF---QMEQV 500
Cdd:COG5185 443 LNELISELNKVmREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIesrvsTLKATLEKLRAKLERQLEGvrsKLDQV 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672073093 501 KRESEMKMEEQSDQLEKLKRELVAKAGelAHAQEALSRTEQSGSELSSRLDTLNAEKEAL-SGAIRQREAE 570
Cdd:COG5185 523 AESLKDFMRARGYAHILALENLIPASE--LIQASNAKTDGQAANLRTAVIDELTQYLSTIeSQQAREDPIP 591
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
512-639 |
5.31e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 512 SDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNA-------EKEALSGAIRQREAELLAAQSLVREKEEA 584
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAslsaaeaERSRLQALLAELAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 672073093 585 LSQEQQrsaqekgelqgrlaekESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDA 639
Cdd:PRK09039 125 LDSEKQ----------------VSARALAQVELLNQQIAALRRQLAALEAALDAS 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
360-459 |
5.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 360 LKREVETLRAELEkikmEAQRYISQLKGQVNSLEAELEEQRKQK------QKALVDNEQLRHELAQLKALQLEGARNQGL 433
Cdd:PRK03918 671 LSRELAGLRAELE----ELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
90 100
....*....|....*....|....*...
gi 672073093 434 REEAERKASATEARYS--KLKEKHNELI 459
Cdd:PRK03918 747 EIASEIFEELTEGKYSgvRVKAEENKVK 774
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
362-638 |
5.70e-03 |
|
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: 40.93 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 362 REVETLRA---ELEKIKMEAQRYISQLKgQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKAlqlegaRNQGLREEAE 438
Cdd:pfam01576 2 RQEEEMQAkeeELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRA------RLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 439 RKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLtvtqqSQEEVARVKeqlaFQMEQVKRESEMK--------MEE 510
Cdd:pfam01576 75 EILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-----DEEEAARQK----LQLEKVTTEAKIKkleedillLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 511 QSDQLEKLKRELVAKAGE----LAHAQEAL-------SRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVR 579
Cdd:pfam01576 146 QNSKLSKERKLLEERISEftsnLAEEEEKAkslsklkNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672073093 580 EKEEALSQEQQRSAQEKGELQG---RLAEKESQEQGLQQKL---------LDEQFAVLRGAAAEAEAILQD 638
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAalaRLEEETAQKNNALKKIreleaqiseLQEDLESERAARNKAEKQRRD 296
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
362-644 |
6.76e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 362 REVETLRAELEKIKMEAQRYISQLKGQVNS--------LEAELEEQRKQKQKALVDN----EQLRHELAQLKALQLEGAR 429
Cdd:NF041483 94 RELRDARAQTQRILQEHAEHQARLQAELHTeavqrrqqLDQELAERRQTVESHVNENvawaEQLRARTESQARRLLDESR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 430 ---NQGL---REEAERkaSATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQL----AFQMEQ 499
Cdd:NF041483 174 aeaEQALaaaRAEAER--LAEEARQRLGSEAESARAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLrsstAAESDQ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 500 VKRES-------EMKMEEQSDQLEKLKRE---LVAKAGELAHAQ--EALSRTEQSGSELSSRLDTLNAEKEALSGAIRQR 567
Cdd:NF041483 252 ARRQAaelsraaEQRMQEAEEALREARAEaekVVAEAKEAAAKQlaSAESANEQRTRTAKEEIARLVGEATKEAEALKAE 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672073093 568 EAELLAAQSLVREKEEALSQEQQRSAQEKgELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLD 644
Cdd:NF041483 332 AEQALADARAEAEKLVAEAAEKARTVAAE-DTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEAD 407
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
348-474 |
7.09e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 348 SMKDDRDLQIENLKREVETL-----RAELEKIKMEAQRYISQLKGQVNSLEA---ELEEQRKQKQKALVDneqLRHELAQ 419
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKD---LIKEIEE 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 672073093 420 LKALQLEGARNQglrEEAERKASATEARYSKLKEKHNELiNTHAELLRKNADTAK 474
Cdd:TIGR04523 608 KEKKISSLEKEL---EKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIR 658
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-621 |
7.34e-03 |
|
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: 40.48 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 382 ISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINt 461
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 462 haellrkNADTAKQLTVTQQ-----SQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEAL 536
Cdd:pfam05483 342 -------KAKAAHSFVVTEFeattcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 537 SRTEQ---SGSELSSRLDTLNAEKEALSGAIRQREAEL--LAAQ-SLVREKEEALSQE--QQRSAQEKGELQGRLAEKES 608
Cdd:pfam05483 415 AEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIhdLEIQlTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHC 494
|
250
....*....|...
gi 672073093 609 QEQGLQQKLLDEQ 621
Cdd:pfam05483 495 DKLLLENKELTQE 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-611 |
7.58e-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: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEKIKMEAQRYISQLK-----GQVNSLEAELEEQRKQKQKALVDN--------EQLRHEL 417
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALargaiGAAVDLVASDLREADARYYVLGDTllgrtlvaARLEAAL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 418 AQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQM 497
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 498 EQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALsGAIRQREAELLAAqsl 577
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-GPVNLLAIEEYEE--- 792
|
250 260 270
....*....|....*....|....*....|....*.
gi 672073093 578 VREKEEALSQEQQRSAQEKGELQGRLAE--KESQEQ 611
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLEEAIEEidRETRER 828
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-502 |
7.66e-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: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 351 DDRDLQIENLKREVETLRAELEKIKmEAQRYISQLKgQVNSLEAELEEQRKQKQKAlvdNEQLRHELAQLkalqlegarn 430
Cdd:COG1579 55 EDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNK-EYEALQKEIESLKRRISDL---EDEILELMERI---------- 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672073093 431 qglrEEAERKASATEARYSKLKEKHNELInthAELLRKNADTAKQL-TVTQQSQEEVARVKEQLAFQMEQVKR 502
Cdd:COG1579 120 ----EELEEELAELEAELAELEAELEEKK---AELDEELAELEAELeELEAEREELAAKIPPELLALYERIRK 185
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
358-593 |
8.08e-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: 40.42 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 358 ENLKREVETLRAELEKIK--MEAQRYISQLKGQVNSLEAELEEQRKQKQKaLVDNEQLRHELAQLKALQLEGARNQ--GL 433
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTevQSLIREIKDAKEQDSPLETFLEKDQQEKEE-LISSKETSNKKAQDKVNDIKEKVKNihGY 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 434 REEAERKASATEARYSKLKE--------------KHNELINTHAELLRKNADTAKQltvtqqsQEEVarvkeqLAFQMEQ 499
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKEtelntvnaqleeceKHQEKINEDMRLMRQDIDTQKI-------QERW------LQDNLTL 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 500 VKRESEMKmeeqsdqleKLKRELVAKAGELAhaQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVR 579
Cdd:TIGR00606 1024 RKRENELK---------EVEEELKQHLKEMG--QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
250
....*....|....
gi 672073093 580 EKEEALSQEQQRSA 593
Cdd:TIGR00606 1093 EPQFRDAEEKYREM 1106
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
355-489 |
8.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 355 LQIENLKREVETLRAELEKIKMEAQryisqlkgqvnslEAELEEQRKQKQKAlvdnEQLRHELAQLKAlQLEGARNQ--- 431
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKE-------------ALKKEQDEASFERL----AELRDELAELEE-ELEALKARwea 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 432 --GLREEAERKASATEARYSKLKEKHNELINTHAELlrKNADTAKQLTVTqqsQEEVARV 489
Cdd:COG0542 466 ekELIEEIQELKEELEQRYGKIPELEKELAELEEEL--AELAPLLREEVT---EEDIAEV 520
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
449-591 |
8.20e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.20 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 449 SKLKEKHNELIN-THAELLRKNaDTAKQL-------TVTQQSQEEVARVKEQLAFQMEQVK------RESEMKMEEQSD- 513
Cdd:pfam15066 366 NKLKENVEELIEdKYNVILEKN-DINKTLqnlqeilANTQKHLQESRKEKETLQLELKKIKvnyvhlQERYITEMQQKNk 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 514 ---QLEKLKRELVAKAGELAHAQEALSRTEQSgseLSSRLDTLNAEKEAlsgairqREAELLAAQSLVREKEEALSQEQQ 590
Cdd:pfam15066 445 svsQCLEMDKTLSKKEEEVERLQQLKGELEKA---TTSALDLLKREKET-------REQEFLSLQEEFQKHEKENLEERQ 514
|
.
gi 672073093 591 R 591
Cdd:pfam15066 515 K 515
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
357-621 |
8.58e-03 |
|
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: 39.88 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 357 IENLKREVETLRAELEKIKMEAQRYISQLKgqvnsleaELEEQRKQKQKALVDNEQLRHELaqlkALQLEGARNQglreE 436
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRK--------EEEAERKQLQAKLQQTEEELRSL----SKEFQELRNS----L 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 437 AERKASATearysKLKEKHNELINTHAELLRKNADtakqltvTQQSQEEVARVKEQLAfqmeqvkresemkMEEQSdqLE 516
Cdd:pfam07888 202 AQRDTQVL-----QLQDTITTLTQKLTTAHRKEAE-------NEALLEELRSLQERLN-------------ASERK--VE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 517 KLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLN-AEKEALSGAIRQREAELLAAQsLVREKEEALSQEQQRsaqe 595
Cdd:pfam07888 255 GLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASlALREGRARWAQERETLQQSAE-ADKDRIEKLSAELQR---- 329
|
250 260
....*....|....*....|....*.
gi 672073093 596 kgeLQGRLAEKESQEQGLQQKLLDEQ 621
Cdd:pfam07888 330 ---LEERLQEERMEREKLEVELGREK 352
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
356-616 |
8.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 356 QIENLKREVETLRAELEKIKMEAQR---YISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQG 432
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDleqQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 433 LREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQS 512
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 513 DQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRS 592
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
250 260
....*....|....*....|....
gi 672073093 593 AQEKGELQGRLAEKESQEQGLQQK 616
Cdd:COG4372 342 LLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
450-649 |
9.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 450 KLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAfQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGEL 529
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073093 530 AHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQ 609
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 672073093 610 EQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDPLHL 649
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
|
| |
