|
Name |
Accession |
Description |
Interval |
E-value |
| GCP6_N |
pfam19340 |
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal ... |
28-342 |
0e+00 |
|
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal alpha-helical region of Gamma-tubulin complex component 6 (GCP6), a protein indispensable for assembly of the gamma-tubulin complex and for microtubule nucleation. It is located at the centrioles and the pericentriolar material, being required for centriole formation and reduplication. It has been shown that the N-terminal domains define the functional identity of gamma-tubulin complex proteins. GCP6 carries a large internal insertion phosphorylated by Plk4 and contains a domain of interaction with keratins.
:
Pssm-ID: 466048 Cd Length: 315 Bit Score: 551.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 28 VNRKRAKRSLKKVAYNALFTNLFQDETQQLQPDMSKLPARNKILMLSFDLRVGGLGPKADRLEELVEELEAAPCCPLLEV 107
Cdd:pfam19340 1 VSRPRFKRALKKAAYGALFEKLFQEETAKWPSELAKTPVRNKLLMLSFDLRVAGLGDEADRLEELVEKLEAGPSSPLAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 108 GSVLDLLVQLAGSGPPQVLPRKRDYFLNNKHVGRNVPYSGYDCDDLSVFEMDVQSLISREECLCHSMIQETLQVMEAAPG 187
Cdd:pfam19340 81 EAVLDLLVQLAGSGPPQPLSFKRDYFRREKHVLRRVPLLGYDSYDLRVLEADAWSLVCREEWLFLHYIQYTLQLMEAAPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 188 TGLPTVGLFSFGDPCGDRFERDTRVSLFGALVHSRTYDMDVRLGLPPVPDNADLSGLAIKVPPSVDQWEDEGFQSASNLT 267
Cdd:pfam19340 161 TGLPTLGLFSLQLEAEDRFEKETRVSLFGALVHSRTYDMDVRLDLPPVPSNADLSGLAIKVPQSLDQSEDEGFQSASNLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 268 PDSQSEPSVTPDVDLWEAALTYEASKRRCWERVGCPPGHREEPYLTEAGRDAFDKFCRLHQGELQLLAGGVLQAP 342
Cdd:pfam19340 241 PDSQSEPSMTPDIDVWEAALTYEPSKRRCWERVGCPPGKREEPYLTEAGREAFDQLYRLREGELQVLSSPLLQLP 315
|
|
| GCP_C_terminal |
pfam04130 |
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ... |
1505-1808 |
2.06e-66 |
|
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.
:
Pssm-ID: 461187 Cd Length: 297 Bit Score: 227.12 E-value: 2.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1505 LEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGagqTPGELLNPLVLNSVLSKALQCSlhgdtpHASNLSLA-LKYLPEVF 1583
Cdd:pfam04130 1 LLDHLRALKRYLLLGQGDFISRLMDALFDELW---KPASSLLRHNLTGLLEEAIRSS------NAQRDLPDvLRRLDARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1584 APNAPDVLSCLELRYKVDWPLNIVITEGCLSKYSGVFSFLLQLKLMMWALKDVcfHLKRTALLSHmagSVQFRQLQLFKH 1663
Cdd:pfam04130 72 DPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSL--WRRRQMSGSR---SVLWHRARLLRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1664 EMQHFVKVIQGYIANQILHVTWCEFRARLAT-VGDLEEIQRAHAEYLHEAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQ 1742
Cdd:pfam04130 147 EMIHFVSQLQYYVMFEVIEPSWREFEEKLQKaASDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187956495 1743 LISQAWGPPGGPRGAEHPNFALMQQS-----YNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYY 1808
Cdd:pfam04130 227 LDGLYLSVSESARAEAEDELPELERErlrrlEKQFRKKVSLLLKVLRGLKSHPDESHLRQLLLRLDFNGYY 297
|
|
| GCP_N_terminal |
pfam17681 |
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ... |
353-633 |
6.02e-36 |
|
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.
:
Pssm-ID: 465456 Cd Length: 298 Bit Score: 139.34 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 353 VKDVLNVLIGVVSATFSLCQPAQAFVVKrgVHVSGASPESISSLLSEVAEYGTCYTRLSHFSLQPvldSLYSKGLVFQAF 432
Cdd:pfam17681 1 LRDLLFALQGISGSYIRFDESDSRIVDD--IRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESS---SSFEYGLVLQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 433 TSGLRRYLQ-YYRACV-------LSTPPTLSLLTIGFLFKKLGRQLRYLAELcgVGAVLPGTCGGGpraafptgvKLLSY 504
Cdd:pfam17681 76 CAALQEELTeYYRLIAqlesqllEASDSILTLLRLVVWLQPPLLLLRVLSNL--VEAVEKQNLKGG---------ALLSL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 505 LYQEALHNcSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDAYGEFMIQVNHEYLSFRDKL--YWTHGYVLiskeVED 582
Cdd:pfam17681 145 LHEATSHG-DPFVRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAKESLTSddLWEDKYTL----RPE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 583 CVPVFL-KHIAHDIYVCGKTINLLKLCCPRHY--------LCWSDVPVPRISVIFSLEEL 633
Cdd:pfam17681 220 MLPSFLsPDLAEKILLTGKSLNFLRECCGDSWriedtaseLEYGDDLSESSIFSLSLEEL 279
|
|
| TPH super family |
cl38442 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
658-806 |
1.31e-09 |
|
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.
The actual alignment was detected with superfamily member pfam13868:
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.86 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 658 KEEKELRMEIAKQELIAHAREAASRvlsalSDRQMSERMALDARKREQFQRLKEQFVKDQERRqaARQEELDDDFsyare 737
Cdd:pfam13868 143 KELEKEEEREEDERILEYLKEKAER-----EEEREAEREEIEEEKEREIARLRAQQEKAQDEK--AERDELRAKL----- 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 738 lrdrerrlksLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLL------EDEKHIQEMLKAVSEAHQ 806
Cdd:pfam13868 211 ----------YQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRlaeeaeREEEEFERMLRKQAEDEE 275
|
|
| DUF4573 super family |
cl25719 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1033-1200 |
4.96e-03 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
The actual alignment was detected with superfamily member pfam15140:
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 39.81 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1033 SEIAPTRPRWNTHGHVSDASIRVGENVSDVAPTQPRWNTHGHVSNASISLGESVSDVAPTRPRWNIHGHVSNASIRVGEN 1112
Cdd:pfam15140 18 REIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERDPLGAVEEIEPPQAASEMKPLGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1113 VSDVAPTRPRWNTHGHvsnasirvgENVSDVAPTRPRWNTHGHVSDASISLGESVSDMAPARPRWNTHGHVSDASISLGE 1192
Cdd:pfam15140 98 AENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEIEPLEPVQLIEPLGEVEQIQPLE 168
|
....*...
gi 187956495 1193 SVSDMAPT 1200
Cdd:pfam15140 169 TVPKENPT 176
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GCP6_N |
pfam19340 |
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal ... |
28-342 |
0e+00 |
|
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal alpha-helical region of Gamma-tubulin complex component 6 (GCP6), a protein indispensable for assembly of the gamma-tubulin complex and for microtubule nucleation. It is located at the centrioles and the pericentriolar material, being required for centriole formation and reduplication. It has been shown that the N-terminal domains define the functional identity of gamma-tubulin complex proteins. GCP6 carries a large internal insertion phosphorylated by Plk4 and contains a domain of interaction with keratins.
Pssm-ID: 466048 Cd Length: 315 Bit Score: 551.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 28 VNRKRAKRSLKKVAYNALFTNLFQDETQQLQPDMSKLPARNKILMLSFDLRVGGLGPKADRLEELVEELEAAPCCPLLEV 107
Cdd:pfam19340 1 VSRPRFKRALKKAAYGALFEKLFQEETAKWPSELAKTPVRNKLLMLSFDLRVAGLGDEADRLEELVEKLEAGPSSPLAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 108 GSVLDLLVQLAGSGPPQVLPRKRDYFLNNKHVGRNVPYSGYDCDDLSVFEMDVQSLISREECLCHSMIQETLQVMEAAPG 187
Cdd:pfam19340 81 EAVLDLLVQLAGSGPPQPLSFKRDYFRREKHVLRRVPLLGYDSYDLRVLEADAWSLVCREEWLFLHYIQYTLQLMEAAPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 188 TGLPTVGLFSFGDPCGDRFERDTRVSLFGALVHSRTYDMDVRLGLPPVPDNADLSGLAIKVPPSVDQWEDEGFQSASNLT 267
Cdd:pfam19340 161 TGLPTLGLFSLQLEAEDRFEKETRVSLFGALVHSRTYDMDVRLDLPPVPSNADLSGLAIKVPQSLDQSEDEGFQSASNLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 268 PDSQSEPSVTPDVDLWEAALTYEASKRRCWERVGCPPGHREEPYLTEAGRDAFDKFCRLHQGELQLLAGGVLQAP 342
Cdd:pfam19340 241 PDSQSEPSMTPDIDVWEAALTYEPSKRRCWERVGCPPGKREEPYLTEAGREAFDQLYRLREGELQVLSSPLLQLP 315
|
|
| GCP_C_terminal |
pfam04130 |
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ... |
1505-1808 |
2.06e-66 |
|
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.
Pssm-ID: 461187 Cd Length: 297 Bit Score: 227.12 E-value: 2.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1505 LEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGagqTPGELLNPLVLNSVLSKALQCSlhgdtpHASNLSLA-LKYLPEVF 1583
Cdd:pfam04130 1 LLDHLRALKRYLLLGQGDFISRLMDALFDELW---KPASSLLRHNLTGLLEEAIRSS------NAQRDLPDvLRRLDARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1584 APNAPDVLSCLELRYKVDWPLNIVITEGCLSKYSGVFSFLLQLKLMMWALKDVcfHLKRTALLSHmagSVQFRQLQLFKH 1663
Cdd:pfam04130 72 DPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSL--WRRRQMSGSR---SVLWHRARLLRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1664 EMQHFVKVIQGYIANQILHVTWCEFRARLAT-VGDLEEIQRAHAEYLHEAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQ 1742
Cdd:pfam04130 147 EMIHFVSQLQYYVMFEVIEPSWREFEEKLQKaASDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187956495 1743 LISQAWGPPGGPRGAEHPNFALMQQS-----YNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYY 1808
Cdd:pfam04130 227 LDGLYLSVSESARAEAEDELPELERErlrrlEKQFRKKVSLLLKVLRGLKSHPDESHLRQLLLRLDFNGYY 297
|
|
| GCP_N_terminal |
pfam17681 |
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ... |
353-633 |
6.02e-36 |
|
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.
Pssm-ID: 465456 Cd Length: 298 Bit Score: 139.34 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 353 VKDVLNVLIGVVSATFSLCQPAQAFVVKrgVHVSGASPESISSLLSEVAEYGTCYTRLSHFSLQPvldSLYSKGLVFQAF 432
Cdd:pfam17681 1 LRDLLFALQGISGSYIRFDESDSRIVDD--IRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESS---SSFEYGLVLQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 433 TSGLRRYLQ-YYRACV-------LSTPPTLSLLTIGFLFKKLGRQLRYLAELcgVGAVLPGTCGGGpraafptgvKLLSY 504
Cdd:pfam17681 76 CAALQEELTeYYRLIAqlesqllEASDSILTLLRLVVWLQPPLLLLRVLSNL--VEAVEKQNLKGG---------ALLSL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 505 LYQEALHNcSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDAYGEFMIQVNHEYLSFRDKL--YWTHGYVLiskeVED 582
Cdd:pfam17681 145 LHEATSHG-DPFVRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAKESLTSddLWEDKYTL----RPE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 583 CVPVFL-KHIAHDIYVCGKTINLLKLCCPRHY--------LCWSDVPVPRISVIFSLEEL 633
Cdd:pfam17681 220 MLPSFLsPDLAEKILLTGKSLNFLRECCGDSWriedtaseLEYGDDLSESSIFSLSLEEL 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
658-806 |
1.31e-09 |
|
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: 61.86 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 658 KEEKELRMEIAKQELIAHAREAASRvlsalSDRQMSERMALDARKREQFQRLKEQFVKDQERRqaARQEELDDDFsyare 737
Cdd:pfam13868 143 KELEKEEEREEDERILEYLKEKAER-----EEEREAEREEIEEEKEREIARLRAQQEKAQDEK--AERDELRAKL----- 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 738 lrdrerrlksLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLL------EDEKHIQEMLKAVSEAHQ 806
Cdd:pfam13868 211 ----------YQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRlaeeaeREEEEFERMLRKQAEDEE 275
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
631-806 |
1.86e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKdcavyvgrmERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLK 710
Cdd:COG1196 323 EELAELEE---------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 711 EQFVKDQERRQAARQEELDDDfsyarelrdrerRLKSLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLLED 790
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLE------------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170
....*....|....*.
gi 187956495 791 EKHIQEMLKAVSEAHQ 806
Cdd:COG1196 462 LELLAELLEEAALLEA 477
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
627-771 |
4.87e-05 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 45.00 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 627 IFSLEELKEIEKDcavyvgRMERVARHSSVSKEEKElRMEIAKQELIAHAREAASRVL----SALSDRQMSER----MAL 698
Cdd:TIGR02473 1 EFRLQKLLDLREK------EEEQAKLELAKAQAEFE-RLETQLQQLIKYREEYEQQALekvgAGTSALELSNYqrfiRQL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956495 699 DARKREQFQ---RLKEQFVKDQERRQAARQEEldddfsyarelrdrerrlKSLEEELERKASKLSAEAARREQKAL 771
Cdd:TIGR02473 74 DQRIQQQQQelaLLQQEVEAKRERLLEARREL------------------KALEKLKEKKQKEYRAEEAKREQKEM 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
631-803 |
8.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKDCAVYVGRMERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLK 710
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 711 EQFVKDQERRQAARQEELDDDfsyARELRDRERRLKSLEEELERKASKL--SAEAARREQKALWRIQRHRLESARLRFLL 788
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
170
....*....|....*
gi 187956495 789 EDEKHIQEMLKAVSE 803
Cdd:PTZ00121 1712 AEEKKKAEELKKAEE 1726
|
|
| DUF4573 |
pfam15140 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1033-1200 |
4.96e-03 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 39.81 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1033 SEIAPTRPRWNTHGHVSDASIRVGENVSDVAPTQPRWNTHGHVSNASISLGESVSDVAPTRPRWNIHGHVSNASIRVGEN 1112
Cdd:pfam15140 18 REIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERDPLGAVEEIEPPQAASEMKPLGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1113 VSDVAPTRPRWNTHGHvsnasirvgENVSDVAPTRPRWNTHGHVSDASISLGESVSDMAPARPRWNTHGHVSDASISLGE 1192
Cdd:pfam15140 98 AENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEIEPLEPVQLIEPLGEVEQIQPLE 168
|
....*...
gi 187956495 1193 SVSDMAPT 1200
Cdd:pfam15140 169 TVPKENPT 176
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GCP6_N |
pfam19340 |
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal ... |
28-342 |
0e+00 |
|
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal alpha-helical region of Gamma-tubulin complex component 6 (GCP6), a protein indispensable for assembly of the gamma-tubulin complex and for microtubule nucleation. It is located at the centrioles and the pericentriolar material, being required for centriole formation and reduplication. It has been shown that the N-terminal domains define the functional identity of gamma-tubulin complex proteins. GCP6 carries a large internal insertion phosphorylated by Plk4 and contains a domain of interaction with keratins.
Pssm-ID: 466048 Cd Length: 315 Bit Score: 551.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 28 VNRKRAKRSLKKVAYNALFTNLFQDETQQLQPDMSKLPARNKILMLSFDLRVGGLGPKADRLEELVEELEAAPCCPLLEV 107
Cdd:pfam19340 1 VSRPRFKRALKKAAYGALFEKLFQEETAKWPSELAKTPVRNKLLMLSFDLRVAGLGDEADRLEELVEKLEAGPSSPLAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 108 GSVLDLLVQLAGSGPPQVLPRKRDYFLNNKHVGRNVPYSGYDCDDLSVFEMDVQSLISREECLCHSMIQETLQVMEAAPG 187
Cdd:pfam19340 81 EAVLDLLVQLAGSGPPQPLSFKRDYFRREKHVLRRVPLLGYDSYDLRVLEADAWSLVCREEWLFLHYIQYTLQLMEAAPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 188 TGLPTVGLFSFGDPCGDRFERDTRVSLFGALVHSRTYDMDVRLGLPPVPDNADLSGLAIKVPPSVDQWEDEGFQSASNLT 267
Cdd:pfam19340 161 TGLPTLGLFSLQLEAEDRFEKETRVSLFGALVHSRTYDMDVRLDLPPVPSNADLSGLAIKVPQSLDQSEDEGFQSASNLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 268 PDSQSEPSVTPDVDLWEAALTYEASKRRCWERVGCPPGHREEPYLTEAGRDAFDKFCRLHQGELQLLAGGVLQAP 342
Cdd:pfam19340 241 PDSQSEPSMTPDIDVWEAALTYEPSKRRCWERVGCPPGKREEPYLTEAGREAFDQLYRLREGELQVLSSPLLQLP 315
|
|
| GCP_C_terminal |
pfam04130 |
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ... |
1505-1808 |
2.06e-66 |
|
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.
Pssm-ID: 461187 Cd Length: 297 Bit Score: 227.12 E-value: 2.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1505 LEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGagqTPGELLNPLVLNSVLSKALQCSlhgdtpHASNLSLA-LKYLPEVF 1583
Cdd:pfam04130 1 LLDHLRALKRYLLLGQGDFISRLMDALFDELW---KPASSLLRHNLTGLLEEAIRSS------NAQRDLPDvLRRLDARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1584 APNAPDVLSCLELRYKVDWPLNIVITEGCLSKYSGVFSFLLQLKLMMWALKDVcfHLKRTALLSHmagSVQFRQLQLFKH 1663
Cdd:pfam04130 72 DPDSLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSL--WRRRQMSGSR---SVLWHRARLLRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1664 EMQHFVKVIQGYIANQILHVTWCEFRARLAT-VGDLEEIQRAHAEYLHEAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQ 1742
Cdd:pfam04130 147 EMIHFVSQLQYYVMFEVIEPSWREFEEKLQKaASDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187956495 1743 LISQAWGPPGGPRGAEHPNFALMQQS-----YNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYY 1808
Cdd:pfam04130 227 LDGLYLSVSESARAEAEDELPELERErlrrlEKQFRKKVSLLLKVLRGLKSHPDESHLRQLLLRLDFNGYY 297
|
|
| GCP_N_terminal |
pfam17681 |
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ... |
353-633 |
6.02e-36 |
|
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.
Pssm-ID: 465456 Cd Length: 298 Bit Score: 139.34 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 353 VKDVLNVLIGVVSATFSLCQPAQAFVVKrgVHVSGASPESISSLLSEVAEYGTCYTRLSHFSLQPvldSLYSKGLVFQAF 432
Cdd:pfam17681 1 LRDLLFALQGISGSYIRFDESDSRIVDD--IRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESS---SSFEYGLVLQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 433 TSGLRRYLQ-YYRACV-------LSTPPTLSLLTIGFLFKKLGRQLRYLAELcgVGAVLPGTCGGGpraafptgvKLLSY 504
Cdd:pfam17681 76 CAALQEELTeYYRLIAqlesqllEASDSILTLLRLVVWLQPPLLLLRVLSNL--VEAVEKQNLKGG---------ALLSL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 505 LYQEALHNcSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDAYGEFMIQVNHEYLSFRDKL--YWTHGYVLiskeVED 582
Cdd:pfam17681 145 LHEATSHG-DPFVRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSVAKESLTSddLWEDKYTL----RPE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 583 CVPVFL-KHIAHDIYVCGKTINLLKLCCPRHY--------LCWSDVPVPRISVIFSLEEL 633
Cdd:pfam17681 220 MLPSFLsPDLAEKILLTGKSLNFLRECCGDSWriedtaseLEYGDDLSESSIFSLSLEEL 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
658-806 |
1.31e-09 |
|
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: 61.86 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 658 KEEKELRMEIAKQELIAHAREAASRvlsalSDRQMSERMALDARKREQFQRLKEQFVKDQERRqaARQEELDDDFsyare 737
Cdd:pfam13868 143 KELEKEEEREEDERILEYLKEKAER-----EEEREAEREEIEEEKEREIARLRAQQEKAQDEK--AERDELRAKL----- 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956495 738 lrdrerrlksLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLL------EDEKHIQEMLKAVSEAHQ 806
Cdd:pfam13868 211 ----------YQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRlaeeaeREEEEFERMLRKQAEDEE 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
635-796 |
2.64e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 635 EIEKDCAVYVGR----MERVARHSSVSKEEKELRMEIAKQELIAHAREAasrvLSALSDRQMsERMALDARKREQFQRLK 710
Cdd:pfam17380 328 EMDRQAAIYAEQermaMERERELERIRQEERKRELERIRQEEIAMEISR----MRELERLQM-ERQQKNERVRQELEAAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 711 EQFVKDQERRQAARQEELDDDFSYARELRDRERRLKSLEEELERKASKLSAEAARREQKaLWRIQRHRLESARLRFLLED 790
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ-VERLRQQEEERKRKKLELEK 481
|
....*.
gi 187956495 791 EKHIQE 796
Cdd:pfam17380 482 EKRDRK 487
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
648-803 |
6.55e-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: 51.28 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 648 ERVARHSSVSKEEKElrmeiAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFVKDQERRQAARQEE 727
Cdd:pfam17380 417 QQKVEMEQIRAEQEE-----ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 728 LDddfsyarelrdrerrLKSLEEELERKASKLSAEAARRE---------QKALWRIQRHRL--ESARLRFLLEDEKHIQE 796
Cdd:pfam17380 492 QR---------------RKILEKELEERKQAMIEEERKRKllekemeerQKAIYEEERRREaeEERRKQQEMEERRRIQE 556
|
....*..
gi 187956495 797 MLKAVSE 803
Cdd:pfam17380 557 QMRKATE 563
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
678-810 |
6.64e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 47.73 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 678 EAASRvlsALSDRQmseRMALDARKREQFQRL----KEQFVKDQERRQAA----RQEEldddfsyarELRDRERRLKSLE 749
Cdd:pfam05672 10 EEAAR---ILAEKR---RQAREQREREEQERLekeeEERLRKEELRRRAEeeraRREE---------EARRLEEERRREE 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187956495 750 EELERKASKLSAEAARREQKALWRIQRHRLES-ARLRfllED-EKHIQEMlkavsEAHQPQEP 810
Cdd:pfam05672 75 EERQRKAEEEAEEREQREQEEQERLQKQKEEAeAKAR---EEaERQRQER-----EKIMQQEE 129
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
631-806 |
1.86e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKdcavyvgrmERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLK 710
Cdd:COG1196 323 EELAELEE---------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 711 EQFVKDQERRQAARQEELDDDfsyarelrdrerRLKSLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLLED 790
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLE------------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170
....*....|....*.
gi 187956495 791 EKHIQEMLKAVSEAHQ 806
Cdd:COG1196 462 LELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
631-806 |
2.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKDCAvyvgrmERVARHSSVSKEEKELRMEIAK-----QELIAHAREAASRVLSALSDRQMSERMALDARKREQ 705
Cdd:COG1196 246 AELEELEAELE------ELEAELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 706 fqRLKEQFVKDQERRQAARQEELDDDfsyarelrdreRRLKSLEEELERKASKLSAEAARREQKALWRIQRHRLESARLR 785
Cdd:COG1196 320 --ELEEELAELEEELEELEEELEELE-----------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180
....*....|....*....|.
gi 187956495 786 FLLEDEKHIQEMLKAVSEAHQ 806
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEE 407
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
631-806 |
3.57e-05 |
|
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: 47.99 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKDCAVYVG-RMERVARhssvsKEEKELRMEIAKQELIAHAREAASRVLSALSDR-QMSERMALDARKREQFQR 708
Cdd:pfam13868 148 EEEREEDERILEYLKeKAEREEE-----REAEREEIEEEKEREIARLRAQQEKAQDEKAERdELRAKLYQEEQERKERQK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 709 lkeqfvkdqERRQAARQEELDDDfsyarelrdrerRLKSLEEELERKASKLSAEAAR---------REQKALWRIQrhRL 779
Cdd:pfam13868 223 ---------EREEAEKKARQRQE------------LQQAREEQIELKERRLAEEAEReeeefermlRKQAEDEEIE--QE 279
|
170 180
....*....|....*....|....*..
gi 187956495 780 ESARLRflLEDEKHIQEMLKAVSEAHQ 806
Cdd:pfam13868 280 EAEKRR--MKRLEHRRELEKQIEEREE 304
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
627-771 |
4.87e-05 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 45.00 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 627 IFSLEELKEIEKDcavyvgRMERVARHSSVSKEEKElRMEIAKQELIAHAREAASRVL----SALSDRQMSER----MAL 698
Cdd:TIGR02473 1 EFRLQKLLDLREK------EEEQAKLELAKAQAEFE-RLETQLQQLIKYREEYEQQALekvgAGTSALELSNYqrfiRQL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956495 699 DARKREQFQ---RLKEQFVKDQERRQAARQEEldddfsyarelrdrerrlKSLEEELERKASKLSAEAARREQKAL 771
Cdd:TIGR02473 74 DQRIQQQQQelaLLQQEVEAKRERLLEARREL------------------KALEKLKEKKQKEYRAEEAKREQKEM 131
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
630-804 |
5.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 630 LEELKEIEKDCAVYVGRMER----VARHSSVSKEEKELRmeiAKQELIAHAREAASRVLSALSDRQmsERMALDARKR-- 703
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEyaelQEELEELEEELEELE---AELEELREELEKLEKLLQLLPLYQ--ELEALEAELAel 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 704 -EQFQRLKEQF--VKDQERRQAARQEELDDdfsyarelrdrerrlksLEEELERKASKLSAEAARREQKALWRIQRHRle 780
Cdd:COG4717 145 pERLEELEERLeeLRELEEELEELEAELAE-----------------LQEELEELLEQLSLATEEELQDLAEELEELQ-- 205
|
170 180
....*....|....*....|....
gi 187956495 781 sARLRFLLEDEKHIQEMLKAVSEA 804
Cdd:COG4717 206 -QRLAELEEELEEAQEELEELEEE 228
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-803 |
7.81e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 645 GRMERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFVKDQERRQAAR 724
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 725 QEELDDDFSYARELRDRERRLKslEEELERKASKLSAE---------AARREQKALwriqrhrleSARLRFL---LED-E 791
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPD--LEELERELERLEREiealgpvnlLAIEEYEEL---------EERYDFLseqREDlE 808
|
170
....*....|..
gi 187956495 792 KHIQEMLKAVSE 803
Cdd:COG1196 809 EARETLEEAIEE 820
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
631-803 |
8.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKDCAVYVGRMERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLK 710
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 711 EQFVKDQERRQAARQEELDDDfsyARELRDRERRLKSLEEELERKASKL--SAEAARREQKALWRIQRHRLESARLRFLL 788
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
170
....*....|....*
gi 187956495 789 EDEKHIQEMLKAVSE 803
Cdd:PTZ00121 1712 AEEKKKAEELKKAEE 1726
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
631-803 |
8.74e-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: 43.75 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEiekdcavyvgrMERVARHSSVSKE------EKELRMEIAKQELIAHAREAASRVLSALsDRQMSERMALDARKRE 704
Cdd:pfam13868 6 DELRE-----------LNSKLLAAKCNKErdaqiaEKKRIKAEEKEEERRLDEMMEEERERAL-EEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 705 QFQRLKEQFVKDQERRQAARQEELDDdfsyarELRDRERRLKSLEEELERKASKLS-AEAARREQKALWRIQRHRLESAR 783
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQE------REQMDEIVERIQEEDQAEAEEKLEkQRQLREEIDEFNEEQAEWKELEK 147
|
170 180
....*....|....*....|
gi 187956495 784 LRFLLEDEKhIQEMLKAVSE 803
Cdd:pfam13868 148 EEEREEDER-ILEYLKEKAE 166
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
677-804 |
1.27e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.19 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 677 REAASRVLSALSDRQMSErmALDARKREQFQRLKEQFVKDQERRQAARQEELDddfsyarelrdrerrlKSLEEELERK- 755
Cdd:pfam15346 1 KEAESKLLEEETARRVEE--AVAKRVEEELEKRKDEIEAEVERRVEEARKIME----------------KQVLEELEREr 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 187956495 756 -----ASKLSAEAARREQKALWRIQRHR---LESARLRFLLEDEKHIQEMLKAVSEA 804
Cdd:pfam15346 63 eaeleEERRKEEEERKKREELERILEENnrkIEEAQRKEAEERLAMLEEQRRMKEER 119
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
690-820 |
1.32e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 40.24 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 690 RQMSE-RMALDArKREQFQRLKEQFvKDQERRQAARQEELDDDFsyarelrdrERRLKSLEE-ELERKASKLSAEAARRE 767
Cdd:pfam13863 6 REMFLvQLALDA-KREEIERLEELL-KQREEELEKKEQELKEDL---------IKFDKFLKEnDAKRRRALKKAEEETKL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 187956495 768 QKALWR-IQRHRLESARLRflledeKHIQEMLKAVSEaHQPQEppDVLLSVHPQ 820
Cdd:pfam13863 75 KKEKEKeIKKLTAQIEELK------SEISKLEEKLEE-YKPYE--DFLEKVVPK 119
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
649-810 |
1.39e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.21 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 649 RVARHSSVSKEEKElRMEIAKQELIAHAReaasrvlsALSDRQMSERMALDARKREQFQRLKEQfvkdqERRQAARQEEL 728
Cdd:pfam11600 1 RRSQKSVQSQEEKE-KQRLEKDKERLRRQ--------LKLEAEKEEKERLKEEAKAEKERAKEE-----ARRKKEEEKEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 729 DDdfsyarelrdrerrlKSLEEELER----KASKLSAEAARREQK-----ALWRIQRHRLESARLRfllEDEKHIQ---- 795
Cdd:pfam11600 67 KE---------------KERREKKEKdekeKAEKLRLKEEKRKEKqealeAKLEEKRKKEEEKRLK---EEEKRIKaeka 128
|
170
....*....|....*
gi 187956495 796 EMLKAVSEAHQPQEP 810
Cdd:pfam11600 129 EITRFLQKPKTQQAP 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
630-788 |
3.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 630 LEELKEIEKDCAVYVGRMERVARHSSVSKEEKELRMEIA-KQELIAHAREAASRVLSALSDRQmsermaldaRKREQFQR 708
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAeLPERLEELEERLEELRELEEELE---------ELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 709 LKEQFVKDQERRQAARQEELDDDFSYARELRDRERRLKSLEEELERKASKLSAEAARREQKALWRIQRHRLESARLRFLL 788
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| DUF4573 |
pfam15140 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1033-1200 |
4.96e-03 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 39.81 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1033 SEIAPTRPRWNTHGHVSDASIRVGENVSDVAPTQPRWNTHGHVSNASISLGESVSDVAPTRPRWNIHGHVSNASIRVGEN 1112
Cdd:pfam15140 18 REIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERDPLGAVEEIEPPQAASEMKPLGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 1113 VSDVAPTRPRWNTHGHvsnasirvgENVSDVAPTRPRWNTHGHVSDASISLGESVSDMAPARPRWNTHGHVSDASISLGE 1192
Cdd:pfam15140 98 AENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEIEPLEPVQLIEPLGEVEQIQPLE 168
|
....*...
gi 187956495 1193 SVSDMAPT 1200
Cdd:pfam15140 169 TVPKENPT 176
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
631-800 |
5.35e-03 |
|
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: 41.06 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 631 EELKEIEKDCAVyvgRMERVARHSSVSKEEKELR----MEIAKQELIAH----------AREAASR----VLSALSDRQM 692
Cdd:pfam13868 36 AEEKEEERRLDE---MMEEERERALEEEEEKEEErkeeRKRYRQELEEQieereqkrqeEYEEKLQereqMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 693 SERMALDARKREQfQRLKEQFVKDQE----RRQAARQEELDDD---FSYARELRdrerrlkslEEELERkasklsaEAAR 765
Cdd:pfam13868 113 EDQAEAEEKLEKQ-RQLREEIDEFNEeqaeWKELEKEEEREEDeriLEYLKEKA---------EREEER-------EAER 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 187956495 766 REQKAlwriqRHRLESARLRFLLE---DEKHIQEMLKA 800
Cdd:pfam13868 176 EEIEE-----EKEREIARLRAQQEkaqDEKAERDELRA 208
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
632-790 |
6.25e-03 |
|
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: 41.06 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 632 ELKEIEKdcavyvgRMERVARHSSVSKEEKELRMEiAKQELIAHAREAASRVL--SALSDRQmsERMALDAR--KREQFQ 707
Cdd:pfam13868 223 EREEAEK-------KARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLrkQAEDEEI--EQEEAEKRrmKRLEHR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956495 708 RLKEQFVKDQER-RQAARQEELDddfsyarelrdrerrlkslEEELERKasklsAEAARREqkalwriqrhRLESARLRf 786
Cdd:pfam13868 293 RELEKQIEEREEqRAAEREEELE-------------------EGERLRE-----EEAERRE----------RIEEERQK- 337
|
....
gi 187956495 787 LLED 790
Cdd:pfam13868 338 KLKE 341
|
|
| |
