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Conserved domains on  [gi|7270120|emb|CAB79934|]
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putative protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
 48-187 2.56e-82

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


:

Pssm-ID: 132789  Cd Length: 138  Bit Score: 257.64  E-value: 2.56e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   48 YCVTIPSWIVLPKSRNSDPVVSFIAVhvIRYSNIVELAYIYNILDEQFYRVQVSVQSPEGITTMRGVLRRFNDFLKLLTD 127
Cdd:cd06879   1 YCVFIPSWVVLPKSKESDGKAINPKV--GNMSVVYSEYQPLNNAVDKFYRVQVGVQSPEGITTMRGVLRRFNDFLKLHTD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  128 LKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLELE 187
Cdd:cd06879  79 LKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFLELE 138
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 396-614 1.60e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     396 ELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQAIMSERER------F 469
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     470 NQMQWDMEELRQKSYEMEMKLKSREDGSSHAEPTVQStisekhvLSKELDARKQQLEDLSRRYEELEAkskaDMKVLVKE 549
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSE----DIESLAAE 860

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7270120     550 VKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVA-------ARKKLLSDCRILHDRLKEYNLNLS 614
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEelrelesKRSELRRELEELREKLAQLELRLE 932
 
Name Accession Description Interval E-value
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
 48-187 2.56e-82

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132789  Cd Length: 138  Bit Score: 257.64  E-value: 2.56e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   48 YCVTIPSWIVLPKSRNSDPVVSFIAVhvIRYSNIVELAYIYNILDEQFYRVQVSVQSPEGITTMRGVLRRFNDFLKLLTD 127
Cdd:cd06879   1 YCVFIPSWVVLPKSKESDGKAINPKV--GNMSVVYSEYQPLNNAVDKFYRVQVGVQSPEGITTMRGVLRRFNDFLKLHTD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  128 LKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLELE 187
Cdd:cd06879  79 LKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFLELE 138
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 95-185 2.90e-18

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 80.47  E-value: 2.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120      95 FYRVQVSVQSPEgitTMRGVLRRFNDFLKLLTDLKRTFPRKGFPSAPPK---GLLRMKSRAVLEERRCSLEEWITKLLSD 171
Cdd:smart00312  14 YYVIEIETKTGL---EEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKklfGRLNNFSEEFIEKRRRGLEKYLQSLLNH 90

                           90
                   ....*....|....*
gi 7270120     172 IELAR-SVVVASFLE 185
Cdd:smart00312  91 PELINhSEVVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 114-185 1.92e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.81  E-value: 1.92e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7270120    114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLE 185
Cdd:pfam00787  11 VRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLE 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 396-614 1.60e-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: 55.06  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     396 ELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQAIMSERER------F 469
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     470 NQMQWDMEELRQKSYEMEMKLKSREDGSSHAEPTVQStisekhvLSKELDARKQQLEDLSRRYEELEAkskaDMKVLVKE 549
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSE----DIESLAAE 860

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7270120     550 VKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVA-------ARKKLLSDCRILHDRLKEYNLNLS 614
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEelrelesKRSELRRELEELREKLAQLELRLE 932
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-716 2.62e-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: 54.35  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     414 NAKTDMEDLIARLNQEIAvkdYLNKKVNDLEGELETTKQRSKENLEQAIMSERERFNQMqwdmeelrqkSYEMEMKLKSR 493
Cdd:pfam15921  217 SLGSAISKILRELDTEIS---YLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQL----------ISEHEVEITGL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     494 EDGSSHAEPTVQSTISEKHVLSKEldARKQ------QLEDLSRRYEELEAKSKADMKVLVKEVKSLRRSHVELEKELTHS 567
Cdd:pfam15921  284 TEKASSARSQANSIQSQLEIIQEQ--ARNQnsmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     568 LTDKtnaEKLLQEERKLLENTvaarKKLLSDcriLHDRLKEynLNLSMDGNGNFVD----DSTTISDVLRLLsisDDQIE 643
Cdd:pfam15921  362 RTER---DQFSQESGNLDDQL----QKLLAD---LHKREKE--LSLEKEQNKRLWDrdtgNSITIDHLRREL---DDRNM 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     644 EAQLLSGF------------DENAAA-----EDIDKTLSMDTETRIMEDELRKILANIFVENAKLR--KQVNSAMLRALQ 704
Cdd:pfam15921  427 EVQRLEALlkamksecqgqmERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQ 506

                          330
                   ....*....|..
gi 7270120     705 KDVKTTEDVNEE 716
Cdd:pfam15921  507 EKERAIEATNAE 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-608 5.92e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  395 LELRNKLNRILLatnERLVNAKTDMEDLIARLNQEIAVkdyLNKKVNDLEGELETTKQRsKENLEQAIMSERERFNQMQW 474
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAE-LEELRLELEELELELEEAQA 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  475 DMEELRQKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAK----------SKADMK 544
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeaelaeAEEALL 368

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7270120  545 VLVKEVKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-611 3.98e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   395 LELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKEnleqaIMSERERFNQMQW 474
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-----LEKRLEELEERHE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   475 DMEELRQKSYEMEmKLKSREDGSS--HAEPTVQSTISEKHVLSKELD---ARKQQLE----DLSRRYEELE-AKSKAD-- 542
Cdd:PRK03918 363 LYEEAKAKKEELE-RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISkitARIGELKkeikELKKAIEELKkAKGKCPvc 441

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   543 ------------MKVLVKEVKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENtvaarKKLLSDCRILHDRLKEYN 610
Cdd:PRK03918 442 grelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN 516


                 .
gi 7270120   611 L 611
Cdd:PRK03918 517 L 517
 
Name Accession Description Interval E-value
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
 48-187 2.56e-82

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132789  Cd Length: 138  Bit Score: 257.64  E-value: 2.56e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   48 YCVTIPSWIVLPKSRNSDPVVSFIAVhvIRYSNIVELAYIYNILDEQFYRVQVSVQSPEGITTMRGVLRRFNDFLKLLTD 127
Cdd:cd06879   1 YCVFIPSWVVLPKSKESDGKAINPKV--GNMSVVYSEYQPLNNAVDKFYRVQVGVQSPEGITTMRGVLRRFNDFLKLHTD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  128 LKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLELE 187
Cdd:cd06879  79 LKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFLELE 138
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 95-185 2.90e-18

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 80.47  E-value: 2.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120      95 FYRVQVSVQSPEgitTMRGVLRRFNDFLKLLTDLKRTFPRKGFPSAPPK---GLLRMKSRAVLEERRCSLEEWITKLLSD 171
Cdd:smart00312  14 YYVIEIETKTGL---EEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKklfGRLNNFSEEFIEKRRRGLEKYLQSLLNH 90

                           90
                   ....*....|....*
gi 7270120     172 IELAR-SVVVASFLE 185
Cdd:smart00312  91 PELINhSEVVLEFLE 105
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 95-186 1.01e-14

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 70.46  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   95 FYRVQVSVQSPEGITtmrgVLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIEL 174
Cdd:cd06093  19 VYIIEVTTQGGEEWT----VYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQLEQYLQSLLNHPEL 94

                        90
                ....*....|..
gi 7270120  175 ARSVVVASFLEL 186
Cdd:cd06093  95 RNSEELKEFLEL 106
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 114-185 1.92e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 68.81  E-value: 1.92e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7270120    114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLE 185
Cdd:pfam00787  11 VRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLE 82
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 117-184 1.15e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 56.18  E-value: 1.15e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7270120  117 RFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMkSRAVLEERRCSLEEWITKLLSDIELARSVVVASFL 184
Cdd:cd06885  34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPL-TPAQLEERRLQLEKYLQAVVQDPRIANSDIFNSFL 100
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 97-185 3.66e-08

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 52.33  E-value: 3.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   97 RVQVSVQSPEGITTmrgvLRRFNDFLKLLTDLKRTFP---RKGFPSAPPK-----GLLRMkSRAVLEERRCSLEEWITKL 168
Cdd:cd07280  28 TIETKDLIGSSIVA----YKRYSEFVQLREALLDEFPrhkRNEIPQLPPKvpwydSRVNL-NKAWLEKRRRGLQYFLNCV 102

                        90
                ....*....|....*..
gi 7270120  169 LSDIELARSVVVASFLE 185
Cdd:cd07280 103 LLNPVFGGSPVVKEFLL 119
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 396-614 1.60e-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: 55.06  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     396 ELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQAIMSERER------F 469
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     470 NQMQWDMEELRQKSYEMEMKLKSREDGSSHAEPTVQStisekhvLSKELDARKQQLEDLSRRYEELEAkskaDMKVLVKE 549
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQIEELSE----DIESLAAE 860

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7270120     550 VKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVA-------ARKKLLSDCRILHDRLKEYNLNLS 614
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEelrelesKRSELRRELEELREKLAQLELRLE 932
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-716 2.62e-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: 54.35  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     414 NAKTDMEDLIARLNQEIAvkdYLNKKVNDLEGELETTKQRSKENLEQAIMSERERFNQMqwdmeelrqkSYEMEMKLKSR 493
Cdd:pfam15921  217 SLGSAISKILRELDTEIS---YLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQL----------ISEHEVEITGL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     494 EDGSSHAEPTVQSTISEKHVLSKEldARKQ------QLEDLSRRYEELEAKSKADMKVLVKEVKSLRRSHVELEKELTHS 567
Cdd:pfam15921  284 TEKASSARSQANSIQSQLEIIQEQ--ARNQnsmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     568 LTDKtnaEKLLQEERKLLENTvaarKKLLSDcriLHDRLKEynLNLSMDGNGNFVD----DSTTISDVLRLLsisDDQIE 643
Cdd:pfam15921  362 RTER---DQFSQESGNLDDQL----QKLLAD---LHKREKE--LSLEKEQNKRLWDrdtgNSITIDHLRREL---DDRNM 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     644 EAQLLSGF------------DENAAA-----EDIDKTLSMDTETRIMEDELRKILANIFVENAKLR--KQVNSAMLRALQ 704
Cdd:pfam15921  427 EVQRLEALlkamksecqgqmERQMAAiqgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQ 506

                          330
                   ....*....|..
gi 7270120     705 KDVKTTEDVNEE 716
Cdd:pfam15921  507 EKERAIEATNAE 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 395-608 5.92e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  395 LELRNKLNRILLatnERLVNAKTDMEDLIARLNQEIAVkdyLNKKVNDLEGELETTKQRsKENLEQAIMSERERFNQMQW 474
Cdd:COG1196 216 RELKEELKELEA---ELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAE-LEELRLELEELELELEEAQA 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  475 DMEELRQKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAK----------SKADMK 544
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeaelaeAEEALL 368

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7270120  545 VLVKEVKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 395-598 6.49e-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: 52.80  E-value: 6.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    395 LELRNKLNRILLAtNERLVNAKTDMEdliarlnqeIAVKDYLNKKVNDLEGELETTKQrsKENLEQAIMSERerfNQMQW 474
Cdd:pfam05483 488 IELTAHCDKLLLE-NKELTQEASDMT---------LELKKHQEDIINCKKQEERMLKQ--IENLEEKEMNLR---DELES 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    475 DMEELRQKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVKSLR 554
Cdd:pfam05483 553 VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 7270120    555 RSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSD 598
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 96-185 1.08e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 48.03  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   96 YRVQVSVQSPEGITTMRGVLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELA 175
Cdd:cd06873  25 YAISVTRIYPNGQEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQSLLNPEVLD 104

                        90
                ....*....|....
gi 7270120  176 RS----VVVASFLE 185
Cdd:cd06873 105 ANpglqEIVLDFLE 118
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 108-184 1.10e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 47.61  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  108 ITTMRG---VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFL 184
Cdd:cd06866  23 VSSKRFkstVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLNLVARHPVLSEDELVRTFL 102
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 99-186 1.60e-06

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 47.27  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   99 QVSVQSPEGITTMRgvlRRFNDFLKLLTDLKRTFPRKgFPSA-PPK--GLLRMKSRAVLEERRCSLEEWITKLL--SDIE 173
Cdd:cd06897  19 NIQVRLPLRSYTVS---RRYSEFVALHKQLESEVGIE-PPYPlPPKswFLSTSSNPKLVEERRVGLEAFLRALLndEDSR 94

                        90
                ....*....|...
gi 7270120  174 LARSVVVASFLEL 186
Cdd:cd06897  95 WRNSPAVKEFLNL 107
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 395-731 3.35e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.56  E-value: 3.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     395 LELRNKLNRillaTNERLvnaKTDMEDLIARlnqeiavKDYLNKKVNDLEgelettkqRSKENLEQAimsererfnqmqw 474
Cdd:pfam01576  649 LEAKEELER----TNKQL---RAEMEDLVSS-------KDDVGKNVHELE--------RSKRALEQQ------------- 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     475 dMEELRQKSYEMEMKLKSREDGSSHAEPTVQstisekhvlskeldARKQQLE-DLSRRYEELEAKSKAdmkvLVKEVKSL 553
Cdd:pfam01576  694 -VEEMKTQLEELEDELQATEDAKLRLEVNMQ--------------ALKAQFErDLQARDEQGEEKRRQ----LVKQVREL 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     554 RRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKEY-----NLNLSMDGNGNFVDDS--- 625
Cdd:pfam01576  755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLqreleEARASRDEILAQSKESekk 834

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     626 --TTISDVLRL---LSISDDQIEEAQ---------LLSGFDENAAAEDIDKTLsmdtETRI--MEDELRKILANIFVENA 689
Cdd:pfam01576  835 lkNLEAELLQLqedLAASERARRQAQqerdeladeIASGASGKSALQDEKRRL----EARIaqLEEELEEEQSNTELLND 910

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 7270120     690 KLRKQVnsamlraLQKDVKTTEDVNEENSDEKDEASRETLKR 731
Cdd:pfam01576  911 RLRKST-------LQVEQLTTELAAERSTSQKSESARQQLER 945
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 401-584 5.60e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.72  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    401 LNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKEnlEQAIMSERERFNQMQwdmEELR 480
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIA---EELK 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    481 QKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDlsRRYEELEAKSKADMkvLVKEVKSLRRSHVEL 560
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK--EKLKNIELTAHCDK--LLLENKELTQEASDM 511

                         170       180
                  ....*....|....*....|....
gi 7270120    561 EKELTHSLTDKTNAEKllQEERKL 584
Cdd:pfam05483 512 TLELKKHQEDIINCKK--QEERML 533
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 396-597 6.77e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 6.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     396 ELRNKLNRILLATNERLVNAKTDMEDLIARLN-----QEIAVKDY--LNKKVNDLEGELETTKQRsKENLEQAImserer 468
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSeleeeIEELQKELyaLANEISRLEQQKQILRER-LANLERQL------ 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     469 fNQMQWDMEELRQKSYEMEMKLKSREDGSSHAEPTVQStisekhvLSKELDARKQQLEDLSRRYEELEAKS---KADMKV 545
Cdd:TIGR02168  319 -EELEAQLEELESKLDELAEELAELEEKLEELKEELES-------LEAELEELEAELEELESRLEELEEQLetlRSKVAQ 390

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 7270120     546 LVKEVKSLRRSHVELEKELTHSltdKTNAEKLLQEERKLLENTVAARKKLLS 597
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAELKELQ 439
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 114-184 6.85e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 45.83  E-value: 6.85e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7270120  114 VLRRFNDFLKL---LTDLKRTFPrkgFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFL 184
Cdd:cd06877  46 VLRRYNEFYVLeskLTEFHGEFP---DAPLPSRRIFGPKSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFL 116
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 114-187 1.09e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 45.43  E-value: 1.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPP--KGLLRM----------KSRAVLEERRCSLEEWITKLLSDIELARSVVVA 181
Cdd:cd07281  39 VKRRFSDFLGLYEKLSEKHSQNGFIVPPPpeKSLIGMtkvkvgkedsSSAEFLERRRAALERYLQRIVSHPSLLQDPDVR 118


                ....*.
gi 7270120  182 SFLELE 187
Cdd:cd07281 119 EFLEKE 124
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 100-184 1.11e-05

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 45.38  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  100 VSVQSPEGITTMRG--VLRRFNDFLKLLTDLKRTFPRK---GFPSAPPKGLLRMKsRAVLEERRCSLEEWITKLLSDIEL 174
Cdd:cd06876  43 IEVQRLNNDDQSSGwvVARRYSEFLELHKYLKKRYPGVlklDFPQKRKISLKYSK-TLLVEERRKALEKYLQELLKIPEV 121

                        90
                ....*....|
gi 7270120  175 ARSVVVASFL 184
Cdd:cd06876 122 CEDEEFRKFL 131
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 437-598 1.18e-05

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: 48.22  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  437 NKKVNDLEGELETTKQRSKEnLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSK 516
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAE-LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  517 ELDARKQQL-------------------------EDLSRRYEELEAKSKADMKvLVKEVKSLRRSHVELEKELTHSLTDK 571
Cdd:COG4942  98 ELEAQKEELaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALRAELEAERAEL 176

                       170       180
                ....*....|....*....|....*..
gi 7270120  572 TNAEKLLQEERKLLENTVAARKKLLSD 598
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLAR 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 420-614 1.20e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     420 EDLIARLNQEIAVKDYLNKKVNDL-EGELETTKQRSKE---NLEQAIMSERERFNQMQwDMEELRQKSYEMEMKLKSRED 495
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGEleaEIASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIE 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     496 GSSHAEPTVQStisEKHVLSKELDARKQQLEDLSRRYEELEAKSKA---DMKVLVKEVKSLRRSHVELEKELTHSLTDKT 572
Cdd:TIGR02169  340 ELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEKLKREINELKRELDRLQEELQ 416

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 7270120     573 NAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKEYNLNLS 614
Cdd:TIGR02169  417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 389-592 1.28e-05

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: 48.90  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     389 AQIVLPLELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELeTTKQRSKENLEQAIMSERER 468
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAATERR 839

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     469 FNQMQwdmEELRQKSYEMEMKLKSREDGSSHAEptvqsTISEKHV-LSKELDARKQQLEDLSRRYEELEAkskadmkvlv 547
Cdd:TIGR02168  840 LEDLE---EQIEELSEDIESLAAEIEELEELIE-----ELESELEaLLNERASLEEALALLRSELEELSE---------- 901

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 7270120     548 kEVKSLRRSHVELEKELTHsLTDKTNAEKLLQEERKLLENTVAAR 592
Cdd:TIGR02168  902 -ELRELESKRSELRRELEE-LREKLAQLELRLEGLEVRIDNLQER 944
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 395-595 1.87e-05

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: 47.45  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  395 LELRNKLNRILLATNERLVNAKTDMEDLIARLNQeiavkdyLNKKVNDLEGELETTKQRSKENLEQAIMSER-------- 466
Cdd:COG4942  54 LKQLAALERRIAALARRIRALEQELAALEAELAE-------LEKEIAELRAELEAQKEELAELLRALYRLGRqpplalll 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  467 --ERFNQMQWDMEELRQKSYEME---MKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKA 541
Cdd:COG4942 127 spEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7270120  542 DMKVLVKEVKSLRRSHVELEKELthsltDKTNAEKLLQEERKLLENTVAARKKL 595
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALI-----ARLEAEAAAAAERTPAAGFAALKGKL 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 407-608 2.34e-05

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: 47.45  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  407 ATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKEnLEQAIMSERERFNQMQWDMEELRQKSYEM 486
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAELRAELEAQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  487 EMKLKSREDG----SSHAEPTV-------QSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKAdmkvLVKEVKSLRR 555
Cdd:COG4942 103 KEELAELLRAlyrlGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEA 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7270120  556 SHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 114-187 2.46e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 44.11  E-value: 2.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPK---GLLRMKSRAVlEERRCSLEEWITKLLSDIELARSVVVASFLELE 187
Cdd:cd06859  39 VLRRYSDFLWLYERLVEKYPGRIVPPPPEKqavGRFKVKFEFI-EKRRAALERFLRRIAAHPVLRKDPDFRLFLESD 114
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
 114-184 2.47e-05

The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132779  Cd Length: 119  Bit Score: 44.20  E-value: 2.47e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMksravlEERRCSLEEWITKLLSDIELARSVVVASFL 184
Cdd:cd06869  52 VARRYSDFKKLHHDLKKEFPGKKLPKLPHKDKLPR------EKLRLSLRQYLRSLLKDPEVAHSSILQEFL 116
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 114-187 2.54e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 43.94  E-value: 2.54e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPrkGFP-SAPPKGLLRMKSRAV-LEERRCSLEEWITKLLSDIELARSVVVASFLELE 187
Cdd:cd07276  37 VFRRYTDFVRLNDKLKQMFP--GFRlSLPPKRWFKDNFDPDfLEERQLGLQAFVNNIMAHKDIAKCKLVREFFCLD 110
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 116-184 2.76e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 43.55  E-value: 2.76e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7270120  116 RRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMkSRAVLEERRCSLEEWITKLLSDIELARSVVVASFL 184
Cdd:cd06886  36 RRYREFANLHQNLKKEFPDFQFPKLPGKWPFSL-SEQQLDARRRGLEQYLEKVCSIRVIGESDIMQDFL 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
422-608 3.41e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  422 LIARLNQEiavKDYLNKKvNDLEGELETTKQRSKENLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSREDGSSHAE 501
Cdd:COG4717  47 LLERLEKE---ADELFKP-QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  502 ptvqsTISEKHVLSKELDARKQQLEDLSRRYEELEAKsKADMKVLVKEVKSLRRSHVELEKELTHSLTDKTNAEKL---- 577
Cdd:COG4717 123 -----KLLQLLPLYQELEALEAELAELPERLEELEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqd 196

                       170       180       190
                ....*....|....*....|....*....|.
gi 7270120  578 LQEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEE 227
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 399-564 4.13e-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: 4.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  399 NKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQ--AIMSERErFNQMQWDM 476
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKE-YEALQKEI 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  477 EELRQKSYEMEMKLKSREDgsshaeptvqstisEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVKSLRRS 556
Cdd:COG1579  99 ESLKRRISDLEDEILELME--------------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164


                ....*...
gi 7270120  557 HVELEKEL 564
Cdd:COG1579 165 REELAAKI 172
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-614 4.63e-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: 46.98  E-value: 4.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     415 AKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELEtTKQRSKENLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSRE 494
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     495 DGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAK---SKADMKVLVKEVKslrrshvELEKELthsltdK 571
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIK-------KQEWKL------E 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 7270120     572 TNAEKLLQEERKLLentvaarkKLLSDCRILHDRLKEYNLNLS 614
Cdd:TIGR02169  459 QLAADLSKYEQELY--------DLKEEYDRVEKELSKLQRELA 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 396-657 4.70e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  396 ELRNKLNRIllatNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQAIMSERERfnqmqwd 475
Cdd:COG1196 271 ELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL------- 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  476 mEELRQKSYEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVKSLRR 555
Cdd:COG1196 340 -EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  556 SHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKEYNLNLSmdgngnfvDDSTTISDVLRLL 635
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA--------ALAELLEELAEAA 490

                       250       260
                ....*....|....*....|..
gi 7270120  636 SISDDQIEEAQLLSGFDENAAA 657
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKA 512
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
 93-184 5.48e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 43.52  E-value: 5.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   93 EQFYRVQVSVQS-----PEGITTMRGVLRRFNDFLKLLTDLKRTFP---RKGFPSaPPKGLLRMKSRAVLEERRCSLEEW 164
Cdd:cd06878  26 VPLYVIVVHVSEvglneDESISSGWVVTRKLSEFHDLHRKLKECSSwlkKVELPS-LSKKWFKSIDKKFLDKSKNQLQKY 104

                        90       100
                ....*....|....*....|
gi 7270120  165 ITKLLSDIELARSVVVASFL 184
Cdd:cd06878 105 LQFILEDETLCQSEALYSFL 124
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 423-592 1.74e-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: 43.76  E-value: 1.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  423 IARLNQEIAVkdyLNKKVNDLEGELETTKQRsKENLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSredgsshaep 502
Cdd:COG1579  19 LDRLEHRLKE---LPAELAELEDELAALEAR-LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  503 tvQSTISEKHVLSKELDA---RKQQLEDLSRRYEELEAKSKADMKVLVKEVKSLRRSHVELEKELTHSLTDKTNAEKLLQ 579
Cdd:COG1579  85 --VRNNKEYEALQKEIESlkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162

                       170
                ....*....|...
gi 7270120  580 EERKLLENTVAAR 592
Cdd:COG1579 163 AEREELAAKIPPE 175
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 407-594 2.14e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  407 ATNERLVNAKTDMEDL---IARLNQEIAVkdyLNKKVNDLEGELETTKQRSKEnLEQAIMSERERFNQMQWDMEELRQKS 483
Cdd:COG3883  20 AKQKELSELQAELEAAqaeLDALQAELEE---LNEEYNELQAELEALQAEIDK-LQAEIAEAEAEIEERREELGERARAL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  484 YE-------MEMKLKS--------REDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVK 548
Cdd:COG3883  96 YRsggsvsyLDVLLGSesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7270120  549 EVKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENTVAARKK 594
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-611 3.98e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   395 LELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKEnleqaIMSERERFNQMQW 474
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-----LEKRLEELEERHE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   475 DMEELRQKSYEMEmKLKSREDGSS--HAEPTVQSTISEKHVLSKELD---ARKQQLE----DLSRRYEELE-AKSKAD-- 542
Cdd:PRK03918 363 LYEEAKAKKEELE-RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISkitARIGELKkeikELKKAIEELKkAKGKCPvc 441

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   543 ------------MKVLVKEVKSLRRSHVELEKELTHSLTDKTNAEKLLQEERKLLENtvaarKKLLSDCRILHDRLKEYN 610
Cdd:PRK03918 442 grelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN 516


                 .
gi 7270120   611 L 611
Cdd:PRK03918 517 L 517
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 410-541 4.76e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     410 ERLVNAKTDMEDLIARLnQEIAVK---------------DYLNKKVNDLEGEL----ETTKQRSKE--NLEQAIMSERER 468
Cdd:TIGR02169  357 EEYAELKEELEDLRAEL-EEVDKEfaetrdelkdyreklEKLKREINELKRELdrlqEELQRLSEElaDLNAAIAGIEAK 435

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7270120     469 FNQMQWDMEELRQKSYEMEMKLKSREDGSSHAEptvqstiSEKHVLSKELDARKQQLEDLSRRYEELEAKSKA 541
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYE-------QELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
425-731 5.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 5.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  425 RLNQEIAVKDYLNKKVNDLEGELETTKQRsKENLEQAIMSERErfnqmqwDMEELRQKSYEMEMKLKSREDGSSHAEPTV 504
Cdd:COG4372  32 QLRKALFELDKLQEELEQLREELEQAREE-LEQLEEELEQARS-------ELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  505 QSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSK---ADMKVLVKEVKSLRRSHVELEKEL-----THSLTDKTNAEK 576
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAelqSEIAEREEELKELEEQLESLQEELaaleqELQALSEAEAEQ 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  577 LLQEERKLLENTVAARKKLLSDCRILH---DRLKEYNLNLSMDGNGNFVDDSTTISDVLRLLSISDDQIEEAQLLSGFDE 653
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIEslpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7270120  654 NAAAEDIDKTLSMDTETRIMEDELRKILANIFVENAKLRKQVNSAMLRALQKDVKTTEDVNEENSDEKDEASRETLKR 731
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
410-608 6.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   410 ERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQR--SKENLEQAIMSERERFNQMQWDMEELRQKSYEME 487
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   488 MKLKSRedgsshaeptvqstisEKHVlsKELDARKQQLEDlsrRYEELEAKSKaDMKVLVKEVKSLRRS---HVELEKEL 564
Cdd:PRK03918 245 KELESL----------------EGSK--RKLEEKIRELEE---RIEELKKEIE-ELEEKVKELKELKEKaeeYIKLSEFY 302

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 7270120   565 THSLTDKTNAEKLL---QEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:PRK03918 303 EEYLDELREIEKRLsrlEEEINGIEERIKELEEKEERLEELKKKLKE 349
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 445-596 6.34e-04

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: 43.02  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    445 GELETTKQRSKENLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSRE---------DGSSHAEPTVQSTISEKHVLS 515
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREqeeqrrlqqEQLERAEKMREELELEQQRRF 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    516 KELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVK----SLRRSHVELEKELTHSLTDKTNAEKllqEERKLLENTVAA 591
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARqqqeEFRRKLQELQRKKQQEEAERAEAEK---QRQKELEMQLAE 463


                  ....*
gi 7270120    592 RKKLL 596
Cdd:pfam15709 464 EQKRL 468
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
410-608 6.93e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   410 ERLVNAKTDMEDLIARLNQ-EIAVKdylnkkvndLEGELETTKQRsKENLEQAIMSERERFNQMQWDMEELRQKSYEMEM 488
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERaEDLVE---------AEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEA 551

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   489 KLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEA---------------KSKADMKVLVKE-VKS 552
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiadaedeierlrekrEALAELNDERRErLAE 631

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7270120   553 LRRSHVELEKE-----LTHSLTDKTNAEKLLQ----------EERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:PRK02224 632 KRERKRELEAEfdearIEEAREDKERAEEYLEqveekldelrEERDDLQAEIGAVENELEELEELRERREA 702
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
438-721 7.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   438 KKVNDLEGELETTKQRSKE------NLEQAIMSERERFNQMQ--------------WDMEELRQKSYEMEmKLKSREDGS 497
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKlrkelrELEKVLKKESELIKLKElaeqlkeleeklkkYNLEELEKKAEEYE-KLKEKLIKL 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   498 SHAEPTVQSTI-------SEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVKSLRRSHVELeKELTHSLTD 570
Cdd:PRK03918 538 KGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLEL-KDAEKELER 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   571 KTNAEKLLQEErklLENTVAARKKLLSDCRILHDRLKEYNLNLSMDGNGNFVDDSTTISdvlRLLSISDDQIEEaqLLSG 650
Cdd:PRK03918 617 EEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS---RELAGLRAELEE--LEKR 688

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7270120   651 FDEnaAAEDIDKtLSMDTETR---IMEDE-LRKILANIFVENAKLRKQVNSAMLRALQKDVKTTEDVNEENSDEK 721
Cdd:PRK03918 689 REE--IKKTLEK-LKEELEERekaKKELEkLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGK 760
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 114-169 7.97e-04

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 39.64  E-value: 7.97e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLL 169
Cdd:cd07277  34 VYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKRLQVYLRRVV 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
396-614 8.29e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   396 ELRNKLNRIllatnERLVNAKTDMEDLIARLNQEIAVK----DYLNKKVNDLEGELE----------------TTKQRSK 455
Cdd:PRK03918 173 EIKRRIERL-----EKFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEklekevkeleelkeeiEELEKEL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   456 ENLEQAIMSERERFNQMQWDMEELRQKSYEMEMKLKSRE--------------------DGSSHAEPT----------VQ 505
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaeeyiklsefyeeylDELREIEKRlsrleeeingIE 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   506 STISEKHVLSKELDARKQQLEDLSRRYEELEAKSKA--DMKVLVKEVKSLRRSHVELEKElthsltdktNAEKLLQEERK 583
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPE---------KLEKELEELEK 398

                        250       260       270
                 ....*....|....*....|....*....|.
gi 7270120   584 LLENTVAARKKLLSDCRILHDRLKEYNLNLS 614
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIE 429
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
 393-556 1.10e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 42.45  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    393 LPLELRNKLNRILLATNERLVNAKTDMEDLIARLnQEIAVKDYLNKKVNDLEGELETTKQRSKEnLEQAIMSERERFNQM 472
Cdd:pfam18971 570 LSLQEANKLIKDFLSSNKELAGKALNFNKAVAEA-KSTGNYDEVKKAQKDLEKSLRKREHLEKE-VEKKLESKSGNKNKM 647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    473 QWDMEELRQKSyEMEMKLKSREDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKEVKS 552
Cdd:pfam18971 648 EAKAQANSQKD-EIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKA 726


                  ....
gi 7270120    553 LRRS 556
Cdd:pfam18971 727 LKGS 730
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 395-707 1.24e-03

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: 42.04  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    395 LELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLE--QAIMSERERFNQM 472
Cdd:pfam05557  12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnRLKKKYLEALNKK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    473 QWDMEELRQKSYEMEMKLKSR----EDGSSHAEPTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAKSK-------- 540
Cdd:pfam05557  92 LNEKESQLADAREVISCLKNElselRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaeaeqr 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    541 -----------ADMKVLVKEVKSLRRSHVELEKELTHSLTD-----KTNAEKLLQEE------RKL--LENTVAARKKLL 596
Cdd:pfam05557 172 ikelefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHnkhlnENIENKLLLKEevedlkRKLerEEKYREEAATLE 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    597 SDCRILHDRLKEYNlNLSMDGNGNFVDDSTTISDVLRLLSisddqiEEAQLLsgfDENAAAEdiDKTLSMDTETRIMEDE 676
Cdd:pfam05557 252 LEKEKLEQELQSWV-KLAQDTGLNLRSPEDLSRRIEQLQQ------REIVLK---EENSSLT--SSARQLEKARRELEQE 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 7270120    677 LRKILANIFVENAKLRKQvnSAMLRALQKDV 707
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRH--KALVRRLQRRV 348
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 99-186 1.81e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 39.06  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   99 QVSVQSPEGITTMRGVLRRFNDFLKLLT------DLKRTFPRKGFPS-APPKGLLRMKSRAVlEERRCSLEEWITKLLSD 171
Cdd:cd06893  38 QNPNAASEQPLATHTVNRRFREFLTLQTrleenpKFRKIMNVKGPPKrLFDLPFGNMDKDKI-EARRGLLETFLRQLCSI 116

                        90
                ....*....|....*
gi 7270120  172 IELARSVVVASFLEL 186
Cdd:cd06893 117 PEISNSEEVQEFLAY 131
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 438-594 1.84e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    438 KKVNDLEGELETTKQRSKENLEQAIMSERERFNQ----MQWDMEELRQKSYEMEMKLKSREdgsshAEPTVQSTISE--K 511
Cdd:pfam17380 420 VEMEQIRAEQEEARQREVRRLEEERAREMERVRLeeqeRQQQVERLRQQEEERKRKKLELE-----KEKRDRKRAEEqrR 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    512 HVLSKELDARKQQLEDLSRRYEELEAKSKADMKVLVKE-----VKSLRRSHVELE-----KELTHSLTDKTNAEKLLQEE 581
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEerrreAEEERRKQQEMEerrriQEQMRKATEERSRLEAMERE 574

                         170
                  ....*....|...
gi 7270120    582 RKLLENTVAARKK 594
Cdd:pfam17380 575 REMMRQIVESEKA 587
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 96-186 2.18e-03

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 38.16  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   96 YRVQVSVQSPEGIttmrgVLRRFNDFLKLLTDLKRTFPRKGFpSAPPKGLLRMK-SRAVLEERRCSLEEWITKLLSDIEL 174
Cdd:cd06870  23 YKVVVSVGRSSWF-----VFRRYAEFDKLYESLKKQFPASNL-KIPGKRLFGNNfDPDFIKQRRAGLDEFIQRLVSDPKL 96

                        90
                ....*....|..
gi 7270120  175 ARSVVVASFLEL 186
Cdd:cd06870  97 LNHPDVRAFLQM 108
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 396-565 2.43e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    396 ELRNKLNRI--LLATNERLVNAKTDMEDLIARLNQEIAVKDYLNKKvndLEGELETtKQRSKENLEQAIMSERERFNQMQ 473
Cdd:TIGR04523 364 ELEEKQNEIekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ---KDEQIKK-LQQEKELLEKEIERLKETIIKNN 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    474 WDMEELRQKSYEMEMKLKSREDGSSHAEPTVQSTI----SEKHVL---SKELDARKQQLEDLSRRYEELEAKskadMKVL 546
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinKIKQNLeqkQKELKSKEKELKKLNEEKKELEEK----VKDL 515

                         170
                  ....*....|....*....
gi 7270120    547 VKEVKSLRRSHVELEKELT 565
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKK 534
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 114-185 2.67e-03

The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.


Pssm-ID: 132828  Cd Length: 116  Bit Score: 38.25  E-value: 2.67e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7270120  114 VLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWItKLLSDIELAR--SVVVASFLE 185
Cdd:cd07295  40 VRRRYSDFEYFRDILERESPRVMIPPLPGKIFTNRFSDEVIEERRQGLETFL-QSVAGHPLLQtgSKVLAAFLQ 112
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
410-538 3.20e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120  410 ERLVNAKTDMEDLIARLNQEIAVKDYLNKKvNDLEGELETTKQRsKENLEQAIMSERERFNQMQWDMEELRQKSYEMEMK 489
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQEL-EALEAELAELPER-LEELEERLEELRELEEELEELEAELAELQEELEEL 182

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 7270120  490 LKS-----REDGSSHAEpTVQSTISEKHVLSKELDARKQQLEDLSRRYEELEAK 538
Cdd:COG4717 183 LEQlslatEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 396-608 4.09e-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: 40.54  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     396 ELRNKLNRILLATNERLVNAKTdmedliARLNQEIAvKDYLNKKVNDLEGELETTKQ------RSKENLEQAIMSERERF 469
Cdd:pfam01576  349 EMRQKHTQALEELTEQLEQAKR------NKANLEKA-KQALESENAELQAELRTLQQakqdseHKRKKLEGQLQELQARL 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     470 NQMQWDMEELRQKSYEMEMKLKSREDGSSHAEptvqstiSEKHVLSKELDARKQQLED--------------LSRRYEEL 535
Cdd:pfam01576  422 SESERQRAELAEKLSKLQSELESVSSLLNEAE-------GKNIKLSKDVSSLESQLQDtqellqeetrqklnLSTRLRQL 494

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7270120     536 EAKSKADMKVLVKEVKSLRRshveLEKELTHSLTDKTNAEKLLQEERKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:pfam01576  495 EDERNSLQEQLEEEEEAKRN----VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 96-187 4.73e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 37.31  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120   96 YRVQVsVQSPEGITTMRGVLRRFNDFLKLLTDLKRTFP----RKGFPSappKGLLRMKSRAVLEERRCSLEEWITKLLSD 171
Cdd:cd07279  21 YQLAV-VQTGDPDTQPAFIERRYSDFLKLYKALRKQHPqlmaKVSFPR---KVLMGNFSSELIAERSRAFEQFLGHILSI 96

                        90
                ....*....|....*.
gi 7270120  172 IELARSVVVASFLELE 187
Cdd:cd07279  97 PNLRDSKAFLDFLQGP 112
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 410-586 5.02e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 40.05  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    410 ERLVNAKTDMEDLIARLNQEIAVKDYLNKKVNDLEGELETTkqRSKENLEQAIMSERERFNQMQwdmeELRQKSYEMEmK 489
Cdd:pfam15742 158 ERIKEASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSL--QDKEAQLEMTNSQQQLRIQQQ----EAQLKQLENE-K 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    490 LKSREDGSSHAEPTVQ--STISEKHVLSKELDARKQQLEDLSRRYEELEAKSKADMK----VLVKEVkSLRRSHVE-LEK 562
Cdd:pfam15742 231 RKSDEHLKSNQELSEKlsSLQQEKEALQEELQQVLKQLDVHVRKYNEKHHHHKAKLRrakdRLVHEV-EQRDERIKqLEN 309

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 7270120    563 E--LTHSLTDKTNA---------EKLLQEERKLLE 586
Cdd:pfam15742 310 EigILQQQSEKEKAfqkqvtaqnEILLLEKRKLLE 344
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 384-563 5.37e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.13  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    384 ERQGSAQIVLPLELRNKLNRILLATNERLVNAKTDMEDLIARLNQEIavkDYLNKKVNDLEGELETTKQRS----KENLE 459
Cdd:pfam09731 250 ELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI---DQLSKKLAELKKREEKHIERAlekqKEELD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    460 QAIMSERERF-NQMQWDMEELR----------QKSYEMEMKLKSREdgsshaeptvQSTISEKHvLSKELDARKQQL--- 525
Cdd:pfam09731 327 KLAEELSARLeEVRAADEAQLRleferereeiRESYEEKLRTELER----------QAEAHEEH-LKDVLVEQEIELqre 395

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 7270120    526 --EDLSRRYEELEAKSKADMKVLVKEVKSLRR---SHVELEKE 563
Cdd:pfam09731 396 flQDIKEKVEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 429-731 6.65e-03

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: 40.05  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     429 EIA-VKDYLNKKVNDLEgELETTKQRSKENleQAIMSE-RERFNQMQWDME------ELRQKSYEMEMKLKSREDGSSHA 500
Cdd:TIGR02169  161 EIAgVAEFDRKKEKALE-ELEEVEENIERL--DLIIDEkRQQLERLRREREkaeryqALLKEKREYEGYELLKEKEALER 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     501 E-PTVQSTISEkhvLSKELDARKQQLEDLSRRYEELEAK----SKADMKVLVKEVKSLRRSHVELEKELthSLTDKTNAE 575
Cdd:TIGR02169  238 QkEAIERQLAS---LEEELEKLTEEISELEKRLEEIEQLleelNKKIKDLGEEEQLRVKEKIGELEAEI--ASLERSIAE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     576 KLLQEER--KLLENTVAARKKLLSDCRILHDRLKEYNLNLsmDGNGNFVDDSTTISDVLRllsiSDDQIEEAQLLSGFDE 653
Cdd:TIGR02169  313 KERELEDaeERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDLR----AELEEVDKEFAETRDE 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120     654 NAAA-EDIDKTL----SMDTETRIMEDELRKI---LANIFVENAKLRKQVNS--AMLRALQKDVKTTEDVNEENSDEKDE 723
Cdd:TIGR02169  387 LKDYrEKLEKLKreinELKRELDRLQEELQRLseeLADLNAAIAGIEAKINEleEEKEDKALEIKKQEWKLEQLAADLSK 466


                   ....*...
gi 7270120     724 ASRETLKR 731
Cdd:TIGR02169  467 YEQELYDL 474
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 405-608 7.46e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.63  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    405 LLATNERLVNAKTDMED------LIARLNQEIAVKDYLNKKVNDLEGELETTKQRSKENLEQAIMSERERFNQ-MQWDME 477
Cdd:pfam05667 208 LLERNAAELAAAQEWEEewnsqgLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELlSSFSGS 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7270120    478 ELRQKSYEMEMKLKSRED--------GSSHAEPTVQSTISE-KHVLSKELDARKQQLEDLSRRYEELEAKSK---ADMKV 545
Cdd:pfam05667 288 STTDTGLTKGSRFTHTEKlqftneapAATSSPPTKVETEEElQQQREEELEELQEQLEDLESSIQELEKEIKkleSSIKQ 367

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7270120    546 LVKEVKSLRRSHVELEKELthsltdkTNAEKLLqeerKLLENTVAARKKLLSDCRILHDRLKE 608
Cdd:pfam05667 368 VEEELEELKEQNEELEKQY-------KVKKKTL----DLLPDAEENIAKLQALVDASAQRLVE 419
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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