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Conserved domains on  [gi|939619633|ref|NP_001303325|]
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yuri gagarin, isoform R [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Yuri_gagarin super family cl25777
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
 88-270 1.04e-90

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


The actual alignment was detected with superfamily member pfam15934:

Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 275.30  E-value: 1.04e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   88 ELEIQNGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVE 167
Cdd:pfam15934  52 EFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSDISENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  168 LCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQL 247
Cdd:pfam15934 132 LCDKYESLLGSFEEQCQELKRANRRVQSLQTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQT 211

                         170       180
                  ....*....|....*....|...
gi 939619633  248 EMEKMRTLVRKMQSHLQLDDIRH 270
Cdd:pfam15934 212 EIEKSRTLIRNMQSHLQLEDAHH 234
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-380 2.82e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 180 EDQCQELKDAKRKA---QSLQTRLDQVEQLQ-----DELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEK 251
Cdd:COG1196  199 ERQLEPLERQAEKAeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 252 MRTLVRKMQSHLQLddirHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSfrkWKDAQVRADE 331
Cdd:COG1196  279 LELELEEAQAEEYE----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---LEEELEEAEE 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 939619633 332 AMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVN 380
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
 
Name Accession Description Interval E-value
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
 88-270 1.04e-90

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 275.30  E-value: 1.04e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   88 ELEIQNGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVE 167
Cdd:pfam15934  52 EFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSDISENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  168 LCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQL 247
Cdd:pfam15934 132 LCDKYESLLGSFEEQCQELKRANRRVQSLQTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQT 211

                         170       180
                  ....*....|....*....|...
gi 939619633  248 EMEKMRTLVRKMQSHLQLDDIRH 270
Cdd:pfam15934 212 EIEKSRTLIRNMQSHLQLEDAHH 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-391 1.22e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633    99 QIKGLQENLKDRDNQISQLQSMINSYSDFSEN-----NRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYE 173
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   174 SLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---QKSAQLEME 250
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQletLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   251 KMRTLVRKMQSHL--QLDDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWK-DAQV 327
Cdd:TIGR02168  393 LQIASLNNEIERLeaRLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEElREEL 470

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939619633   328 RADEAMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSaISCPP 391
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE 533
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-380 2.82e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 180 EDQCQELKDAKRKA---QSLQTRLDQVEQLQ-----DELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEK 251
Cdd:COG1196  199 ERQLEPLERQAEKAeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 252 MRTLVRKMQSHLQLddirHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSfrkWKDAQVRADE 331
Cdd:COG1196  279 LELELEEAQAEEYE----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---LEEELEEAEE 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 939619633 332 AMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVN 380
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-356 4.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 171 KYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEME 250
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 251 KMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRAD 330
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180
                 ....*....|....*....|....*.
gi 939619633 331 EAMRLCAKRAEEHIHMLLDENRTLAE 356
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLER 418
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 170-308 9.04e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 43.88  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 170 TKYESLMASFEdQCQELKDAKRKAQSLQTRldQVEQLQDELRTERKILREEVVALKeKEAVSSGRERALQDQQKSAQLEM 249
Cdd:cd07680  102 AYHKQIMGGFK-ETKEAEDGFRKAQKPWAK--KMKELEAAKKAYHLACKEEKLAMT-REANSKAEQSVTPEQQKKLQDKV 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 250 EKMRTLVRKMQShlqlddiRHRESIQRMNETTESLREELRTISENCQQM-QIRLNQQTEV 308
Cdd:cd07680  178 DKCKQDVQKTQE-------KYEKVLDDVGKTTPQYMENMEQVFEQCQQFeEKRLVFLKEV 230
46 PHA02562
endonuclease subunit; Provisional
 99-364 1.85e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  99 QIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEemhvlKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMAS 178
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN-----GENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 179 FEDQCQELKDAKRKAQSLQTrldQVEQLQDELrterKILREEVVALKEKEAVSSGRERalqdqqksaqleMEKMRTLVRK 258
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKS---KIEQFQKVI----KMYEKGGVCPTCTQQISEGPDR------------ITKIKDKLKE 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 259 MQSHLQLDDIRHRESIQRMNETTEslreelrtisencQQMQIRLNqQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAK 338
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIMDEFNE-------------QSKKLLEL-KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376

                        250       260
                 ....*....|....*....|....*.
gi 939619633 339 RAEEhIHMLLDENRTLAEDYRNLFRD 364
Cdd:PHA02562 377 NAEE-LAKLQDELDKIVKTKSELVKE 401
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
181-376 2.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 181 DQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEK----EAVSSGRERALQDQQKSAQLEMEKMRTLV 256
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERaaelEAEAEEKREAAAEAEEEAEEAREEVAELN 578

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 257 RKMQ----SHLQLDDIRHR-ESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDsfrkwkDAQVradE 331
Cdd:PRK02224 579 SKLAelkeRIESLERIRTLlAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD------EARI---E 649

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 939619633 332 AMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVK 376
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 199-372 3.78e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.64  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  199 RLDQVEQLQDeLRTERKILREEVVALKEK-EAVSsgreralqdqqksaqlemEKMRTLVRKMQSHLQlddiRHRESIQRM 277
Cdd:pfam10168 570 KEQQLQELQS-LEEERKSLSERAEKLAEKyEEIK------------------DKQEKLMRRCKKVLQ----RLNSQLPVL 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  278 NETTESLREELRTISENCQQMQIRLNQQTE-VNQQQEQIIdsfrkwKDAQVRADEAMRLCAKRaEEHIHMLLDEnrtLAE 356
Cdd:pfam10168 627 SDAEREMKKELETINEQLKHLANAIKQAKKkMNYQRYQIA------KSQSIRKKSSLSLSEKQ-RKTIKEILKQ---LGS 696

                         170
                  ....*....|....*.
gi 939619633  357 DYRNLFRDYKLLETEI 372
Cdd:pfam10168 697 EIDELIKQVKDINKHV 712
 
Name Accession Description Interval E-value
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
 88-270 1.04e-90

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 275.30  E-value: 1.04e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   88 ELEIQNGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVE 167
Cdd:pfam15934  52 EFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSDISENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  168 LCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQL 247
Cdd:pfam15934 132 LCDKYESLLGSFEEQCQELKRANRRVQSLQTRLSQVEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQT 211

                         170       180
                  ....*....|....*....|...
gi 939619633  248 EMEKMRTLVRKMQSHLQLDDIRH 270
Cdd:pfam15934 212 EIEKSRTLIRNMQSHLQLEDAHH 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-391 1.22e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633    99 QIKGLQENLKDRDNQISQLQSMINSYSDFSEN-----NRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYE 173
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   174 SLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---QKSAQLEME 250
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQletLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   251 KMRTLVRKMQSHL--QLDDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWK-DAQV 327
Cdd:TIGR02168  393 LQIASLNNEIERLeaRLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEElREEL 470

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939619633   328 RADEAMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVNCASSSaISCPP 391
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL-ISVDE 533
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-380 2.82e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 180 EDQCQELKDAKRKA---QSLQTRLDQVEQLQ-----DELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEK 251
Cdd:COG1196  199 ERQLEPLERQAEKAeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 252 MRTLVRKMQSHLQLddirHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSfrkWKDAQVRADE 331
Cdd:COG1196  279 LELELEEAQAEEYE----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---LEEELEEAEE 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 939619633 332 AMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVKQAVN 380
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-356 4.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 171 KYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEME 250
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 251 KMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRAD 330
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180
                 ....*....|....*....|....*.
gi 939619633 331 EAMRLCAKRAEEHIHMLLDENRTLAE 356
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLER 418
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 170-308 9.04e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 43.88  E-value: 9.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 170 TKYESLMASFEdQCQELKDAKRKAQSLQTRldQVEQLQDELRTERKILREEVVALKeKEAVSSGRERALQDQQKSAQLEM 249
Cdd:cd07680  102 AYHKQIMGGFK-ETKEAEDGFRKAQKPWAK--KMKELEAAKKAYHLACKEEKLAMT-REANSKAEQSVTPEQQKKLQDKV 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 250 EKMRTLVRKMQShlqlddiRHRESIQRMNETTESLREELRTISENCQQM-QIRLNQQTEV 308
Cdd:cd07680  178 DKCKQDVQKTQE-------KYEKVLDDVGKTTPQYMENMEQVFEQCQQFeEKRLVFLKEV 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-356 1.19e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   184 QELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKmrtlVRKMQSHL 263
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   264 QLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAKRAEEH 343
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170
                   ....*....|...
gi 939619633   344 IHMLLDENRTLAE 356
Cdd:TIGR02168  833 IAATERRLEDLEE 845
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 88-299 1.50e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633    88 ELEIQNGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDF-------------SENNRLKEEMHVLKQKNCDLSRQLRDL 154
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   155 PSLLKNQENQSVEL---CTKYESLMASFEDQCQ-----------ELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREE 220
Cdd:TIGR02169  314 ERELEDAEERLAKLeaeIDKLLAEIEELEREIEeerkrrdklteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   221 VVALKEKEAVSSGRERALQDQQKSAQLEMEKMRT-LVRKMQSHLQLDdirhresiqrmnETTESLREELRTISENCQQMQ 299
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAaIAGIEAKINELE------------EEKEDKALEIKKQEWKLEQLA 461
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-313 1.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  28 DLLQATRDNYLSIIDEFKRDLEELTEQVEQqqqqlqqsslasqscpepelhfvDQSRINcELEIQNGQLSCQIKGLQENL 107
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAE-----------------------LEAELE-ELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 108 KDRDNQISQLQSMINSYSDfsENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELK 187
Cdd:COG1196  291 YELLAELARLEQDIARLEE--RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 188 DAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDD 267
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 939619633 268 IRHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQE 313
Cdd:COG1196  449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-366 2.65e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  186 LKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLvrkmQSHLQL 265
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD----ASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  266 DDIRHResIQRMNETTESLREELRTISENCQQMQIRLNQ----QTEVNQQQEQIIDSFRKWKD-------AQVRADEAMR 334
Cdd:COG4913   688 AALEEQ--LEELEAELEELEEELDELKGEIGRLEKELEQaeeeLDELQDRLEAAEDLARLELRalleerfAAALGDAVER 765

                         170       180       190
                  ....*....|....*....|....*....|..
gi 939619633  335 LCAKRAEEHIHMLLDENRTLAEDYRNLFRDYK 366
Cdd:COG4913   766 ELRENLEERIDALRARLNRAEEELERAMRAFN 797
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 140-356 2.71e-04

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: 43.21  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 140 LKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILRE 219
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 220 EVVALKeKEAVSSGRERALQ---DQQKSAQLE--MEKMRTLVRKMQShlQLDDIrhRESIQRMNETTESLREELRTISEN 294
Cdd:COG4942  105 ELAELL-RALYRLGRQPPLAlllSPEDFLDAVrrLQYLKYLAPARRE--QAEEL--RADLAELAALRAELEAERAELEAL 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939619633 295 CQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAKRAEEHIHMLLDENRTLAE 356
Cdd:COG4942  180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-331 3.09e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  166 VELCTKYESLMASFEDQcQELKDAkRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQ---- 241
Cdd:COG4913   258 RELAERYAAARERLAEL-EYLRAA-LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgn 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  242 --QKSAQLEME---KMRTLVRKMQSHLQLDdirhrESIQRMNETTESLREELRTISENCQQMQIRLNQQTEvnQQQEQII 316
Cdd:COG4913   336 ggDRLEQLEREierLERELEERERRRARLE-----ALLAALGLPLPASAEEFAALRAEAAALLEALEEELE--ALEEALA 408

                         170
                  ....*....|....*
gi 939619633  317 DSFRKWKDAQVRADE 331
Cdd:COG4913   409 EAEAALRDLRRELRE 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 41-307 3.20e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633    41 IDEFKRDLEELTEQVEQQQ-------------QQLQQSSLASQSCPEPELHFVDQSRINCELEIQngQLSCQIKGLQENL 107
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEkalaelrkeleelEEELEQLRKELEELSRQISALRKDLARLEAEVE--QLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   108 KDRDNQISQLQSMINSysdfsennrLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELK 187
Cdd:TIGR02168  757 TELEAEIEELEERLEE---------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   188 DAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQShlQLDD 267
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE--ELRE 905

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 939619633   268 IRHResIQRMNETTESLREELRTISENCQQMQIRLNQQTE 307
Cdd:TIGR02168  906 LESK--RSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
132-330 6.32e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  132 RLKEEMHVLKQKNCDLSRQLRDLPSLLknQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELR 211
Cdd:COG4913   621 ELEEELAEAEERLEALEAELDALQERR--EALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELE 698

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  212 TERKILREEVVALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKmQSHLQLDDIRHRESI-QRMNETTESLREELRT 290
Cdd:COG4913   699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALLEERFAAALGdAVERELRENLEERIDA 777

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 939619633  291 isencqqmqirlnQQTEVNQQQEQIIDSF----RKWKDAQVRAD 330
Cdd:COG4913   778 -------------LRARLNRAEEELERAMrafnREWPAETADLD 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-315 7.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 149 RQLRDLPSLLKNQENQSVELCTKYESLmASFEDQCQELKDAKRKAQSLQTRLDQVEQLQD------ELRTERKILREEVV 222
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyqeleALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 223 ALKEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISENCQQMQIRL 302
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|....*.
gi 939619633 303 NQ---QTEVNQQQEQI 315
Cdd:COG4717  230 EQlenELEAAALEERL 245
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 99-226 1.53e-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: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   99 QIKGLQENLKDRDNQISQLQSMINSYSDfsENNRLKEEMHVLKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMAS 178
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNE--QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 939619633  179 FEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKE 226
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
46 PHA02562
endonuclease subunit; Provisional
 99-364 1.85e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  99 QIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEemhvlKQKNCDLSRQLRDLPSLLKNQENQSVELCTKYESLMAS 178
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN-----GENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 179 FEDQCQELKDAKRKAQSLQTrldQVEQLQDELrterKILREEVVALKEKEAVSSGRERalqdqqksaqleMEKMRTLVRK 258
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKS---KIEQFQKVI----KMYEKGGVCPTCTQQISEGPDR------------ITKIKDKLKE 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 259 MQSHLQLDDIRHRESIQRMNETTEslreelrtisencQQMQIRLNqQTEVNQQQEQIIDSFRKWKDAQVRADEAMRLCAK 338
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIMDEFNE-------------QSKKLLEL-KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376

                        250       260
                 ....*....|....*....|....*.
gi 939619633 339 RAEEhIHMLLDENRTLAEDYRNLFRD 364
Cdd:PHA02562 377 NAEE-LAKLQDELDKIVKTKSELVKE 401
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
181-376 2.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 181 DQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEK----EAVSSGRERALQDQQKSAQLEMEKMRTLV 256
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERaaelEAEAEEKREAAAEAEEEAEEAREEVAELN 578

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 257 RKMQ----SHLQLDDIRHR-ESIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDsfrkwkDAQVradE 331
Cdd:PRK02224 579 SKLAelkeRIESLERIRTLlAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD------EARI---E 649

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 939619633 332 AMRLCAKRAEEHIHMLLDENRTLAEDYRNLFRDYKLLETEIKRVK 376
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 147-293 3.28e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 147 LSRQLRDLPSLLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTER--KILREEVVAL 224
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESL 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939619633 225 KEKEAVSSGRERALQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRESIQRMNETTESLREELRTISE 293
Cdd:COG1579  102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 199-372 3.78e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.64  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  199 RLDQVEQLQDeLRTERKILREEVVALKEK-EAVSsgreralqdqqksaqlemEKMRTLVRKMQSHLQlddiRHRESIQRM 277
Cdd:pfam10168 570 KEQQLQELQS-LEEERKSLSERAEKLAEKyEEIK------------------DKQEKLMRRCKKVLQ----RLNSQLPVL 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  278 NETTESLREELRTISENCQQMQIRLNQQTE-VNQQQEQIIdsfrkwKDAQVRADEAMRLCAKRaEEHIHMLLDEnrtLAE 356
Cdd:pfam10168 627 SDAEREMKKELETINEQLKHLANAIKQAKKkMNYQRYQIA------KSQSIRKKSSLSLSEKQ-RKTIKEILKQ---LGS 696

                         170
                  ....*....|....*.
gi 939619633  357 DYRNLFRDYKLLETEI 372
Cdd:pfam10168 697 EIDELIKQVKDINKHV 712
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 180-379 4.16e-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: 39.72  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  180 EDQCQELKDAKRKAQSLQ-TRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKsaqlEMEKMRTlvrk 258
Cdd:pfam17380 356 EERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV----EMEQIRA---- 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  259 mqshlQLDDIRHREsIQRMNETTESLREELRTISENCQQMQIRLNQQTEVNQQQEQIIDsfrKWKDAQVRADEAMR-LCA 337
Cdd:pfam17380 428 -----EQEEARQRE-VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRkILE 498

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 939619633  338 KRAEEHIHMLLDENRTlaedyrnlfrdYKLLETEIKRVKQAV 379
Cdd:pfam17380 499 KELEERKQAMIEEERK-----------RKLLEKEMEERQKAI 529
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 208-315 5.07e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.97  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633  208 DELRTERKILREEVVALKEKeaVSSGRERaLQDQQKSAQLEMEKMRTLVRKMQSHLQLDDIRHRES---IQRMNETTESL 284
Cdd:pfam09787  50 EELRQERDLLREEIQKLRGQ--IQQLRTE-LQELEAQQQEEAESSREQLQELEEQLATERSARREAeaeLERLQEELRYL 126

                          90       100       110
                  ....*....|....*....|....*....|.
gi 939619633  285 REELRTiSENCQQMQIRlNQQTEVNQQQEQI 315
Cdd:pfam09787 127 EEELRR-SKATLQSRIK-DREAEIEKLRNQL 155
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
157-343 7.54e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 157 LLKNQENQSVELCTKYESLMASFEDQCQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRER 236
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 237 ALQDQQKSAQLEMEkMRTLVRKMQSHLQlddirHRESIQRMNETTESLREELRTISENCQQMQIRLNQQTEvnQQQEQII 316
Cdd:COG4717  127 LLPLYQELEALEAE-LAELPERLEELEE-----RLEELRELEEELEELEAELAELQEELEELLEQLSLATE--EELQDLA 198

                        170       180
                 ....*....|....*....|....*..
gi 939619633 317 DSFRKWKDAQVRADEAMRLCAKRAEEH 343
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEEL 225
PLN02939 PLN02939
transferase, transferring glycosyl groups
 104-287 9.72e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 38.73  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 104 QENLKDRDNqISQLQSMINSYSDfsennrLKEEMHVLKQKNCDLSRQLRDLPS-LLKNQENQSVELCTKYESLMASFEDQ 182
Cdd:PLN02939 233 EENMLLKDD-IQFLKAELIEVAE------TEERVFKLEKERSLLDASLRELESkFIVAQEDVSKLSPLQYDCWWEKVENL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633 183 CQELKDAKRKAQSLQTRLDQVEQLQDELRTERKILREEVVAlkekeAVSSGRERALQDQQKSAQlemEKMRTLVRKMQSH 262
Cdd:PLN02939 306 QDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVS-----KFSSYKVELLQQKLKLLE---ERLQASDHEIHSY 377

                        170       180
                 ....*....|....*....|....*
gi 939619633 263 LQLddirHRESIQRMNETTESLREE 287
Cdd:PLN02939 378 IQL----YQESIKEFQDTLSKLKEE 398
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 92-376 9.95e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.56  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633    92 QNGQLSCQIKGLQENLKDRDNQISQLQSMINSYSDFSENNRLKEEmhvlkqkncDLSRQLRDlpsllKNQENQsvelctK 171
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITID---------HLRRELDD-----RNMEVQ------R 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   172 YESLMASFEDQCQELKDAKRKA-QSLQTRLDQVEQLQDELRTERKILREEVVALKEKEAVSSGRERALQDQQKSAQLE-- 248
Cdd:pfam15921  431 LEALLKAMKSECQGQMERQMAAiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKer 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939619633   249 -MEKMRTLVRKMQSHLqldDIRHRESIQRMNETteslrEELRTISENCQQMQIRLNQQTEVNQQQEQIIDSFRKWKDAQV 327
Cdd:pfam15921  511 aIEATNAEITKLRSRV---DLKLQELQHLKNEG-----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG 582

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 939619633   328 RADEAMRLCAKRAEEHIH---MLLDENRTLAEDYRNLFRDY--KLLETEIKRVK 376
Cdd:pfam15921  583 RTAGAMQVEKAQLEKEINdrrLELQEFKILKDKKDAKIRELeaRVSDLELEKVK 636
 
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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