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Conserved domains on  [gi|380808772|gb|AFE76261|]
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noelin isoform 1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
210-460 9.43e-155

Olfactomedin-like domains;


:

Pssm-ID: 128580  Cd Length: 255  Bit Score: 439.27  E-value: 9.43e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   210 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 286
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   287 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 366
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   367 VSLQTLQTWNTSYPKRSAGEAFMICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 445
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
                          250
                   ....*....|....*
gi 380808772   446 WNNGHQILYNVTLFH 460
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
Noelin-1 pfam12308
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ...
38-134 9.10e-54

Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.


:

Pssm-ID: 432468 [Multi-domain]  Cd Length: 100  Bit Score: 175.35  E-value: 9.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   38 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 117
Cdd:pfam12308   3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
                          90
                  ....*....|....*..
gi 380808772  118 FKQVEESHKQHLARQFK 134
Cdd:pfam12308  83 LKVAEANPQSLSARSFQ 99
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
74-200 2.46e-07

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 149
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 380808772 150 LEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 200
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
210-460 9.43e-155

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 439.27  E-value: 9.43e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   210 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 286
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   287 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 366
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   367 VSLQTLQTWNTSYPKRSAGEAFMICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 445
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
                          250
                   ....*....|....*
gi 380808772   446 WNNGHQILYNVTLFH 460
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
212-458 3.02e-136

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 391.90  E-value: 3.02e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  212 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 291
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  292 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 371
Cdd:pfam02191  79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  372 LQTWNTSYPKRSAGEAFMICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 450
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238

                  ....*...
gi 380808772  451 QILYNVTL 458
Cdd:pfam02191 239 QVTYPVTF 246
Noelin-1 pfam12308
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ...
38-134 9.10e-54

Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.


Pssm-ID: 432468 [Multi-domain]  Cd Length: 100  Bit Score: 175.35  E-value: 9.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   38 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 117
Cdd:pfam12308   3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
                          90
                  ....*....|....*..
gi 380808772  118 FKQVEESHKQHLARQFK 134
Cdd:pfam12308  83 LKVAEANPQSLSARSFQ 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-200 2.46e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 149
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 380808772 150 LEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 200
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-208 1.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  63 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLESKFKQVEEsHKQHLARQFKAIKAK 139
Cdd:COG4717   77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380808772 140 MDELRPLIPVLEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
74-217 9.77e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.93  E-value: 9.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   74 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 147
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  148 PVLEEYKADAKLVlqFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 217
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-200 1.25e-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: 47.74  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 136
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380808772   137 KAKMDELRplipvlEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 200
Cdd:TIGR02168  343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
70-198 7.94e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 147
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380808772 148 PVL-------EEYKADAKLVLQFKEEAQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 198
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
70-180 1.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 149
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
                         90       100       110
                 ....*....|....*....|....*....|.
gi 380808772 150 LEEYKADAKLVLQFKEEAQnLTSVLNELQEE 180
Cdd:COG4372  162 LQEELAALEQELQALSEAE-AEQALDELLKE 191
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
217-402 1.83e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 43.08  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 217 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 292
Cdd:COG4257   44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 293 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 368
Cdd:COG4257  116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380808772 369 LQTLQTwNTSYPKR-SAGEAfmicGTLYVTNGYSG 402
Cdd:COG4257  180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
75-208 4.74e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.58  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  75 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 154
Cdd:cd00176   34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380808772 155 aDAKLVLQFKEEAQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 208
Cdd:cd00176  104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
210-460 9.43e-155

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 439.27  E-value: 9.43e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   210 GKLTGISDPVTVKTSG-SRFGSWMTDPLAPEG-DNRVWYMDGY-HNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQV 286
Cdd:smart00284   1 GGLAGISKPVTLQTSWkGKSGAWMKDPLWNTTkKSLYWYMPLNtRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGTGVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   287 VYNGSIYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDP 366
Cdd:smart00284  81 VYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISKLNP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   367 VSLQTLQTWNTSYPKRSAGEAFMICGTLYVTN-GYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYA 445
Cdd:smart00284 161 ATLTIENTWITTYNKRSASNAFMICGILYVTRsLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRKLYA 240
                          250
                   ....*....|....*
gi 380808772   446 WNNGHQILYNVTLFH 460
Cdd:smart00284 241 WNNGHLVHYDIALKP 255
OLF pfam02191
Olfactomedin-like domain;
212-458 3.02e-136

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 391.90  E-value: 3.02e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  212 LTGISDPVTVKTSGSRFGSWMTDPLAPEgdNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGS 291
Cdd:pfam02191   1 LVSVSKPVTVKLSGGKYGAWMKDPLPPS--DKIYVTDRGTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGHVVYNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  292 IYFNKFQSHIIIRFDLKTETILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDESGLWAVYATNQNAGNIVVSRLDPVSLQT 371
Cdd:pfam02191  79 LYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLDPETLEV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  372 LQTWNTSYPKRSAGEAFMICGTLYVTNGYSGG-TKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGH 450
Cdd:pfam02191 159 EQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRrEEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLYAWDDGY 238

                  ....*...
gi 380808772  451 QILYNVTL 458
Cdd:pfam02191 239 QVTYPVTF 246
Noelin-1 pfam12308
Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 ...
38-134 9.10e-54

Neurogenesis glycoprotein; This domain family is found in eukaryotes, and is approximately 100 amino acids in length. The family is found in association with pfam02191. There are two conserved sequence motifs: SAQ and VQN. Noelin-1 is a glycoprotein which is secreted mainly by postmitotic neurogenic tissues in the developing central and peripheral nervous systems, first appearing after neural tube closure. It is likely that it forms large multimeric complexes.It has a divergent function in neurogenesis. In animal caps neuralized by expression of noggin, co-expression of Noelin-1 causes expression of neuronal differentiation markers several stages before neurogenesis normally occurs in this tissue. Finally, only secreted forms of the protein can activate sensory marker expression, while all forms of the protein can induce early neurogenesis.


Pssm-ID: 432468 [Multi-domain]  Cd Length: 100  Bit Score: 175.35  E-value: 9.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   38 PEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESK 117
Cdd:pfam12308   3 PEEGWQVYSSAQDPDGRCVCTVVAPAQDVCSRDPRSRQLRQLMEKVQNVSQSMEVLDLRTSRDLQYVRTTETLLKTLDSK 82
                          90
                  ....*....|....*..
gi 380808772  118 FKQVEESHKQHLARQFK 134
Cdd:pfam12308  83 LKVAEANPQSLSARSFQ 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-200 2.46e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVLDRR----TQRDLQyVEKMENQMKGLESKFKQVEEshkqhlarQFKAIKAKMDELRPLIPV 149
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELkeeiEELEKE-LESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKE 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 380808772 150 LEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAYdydelQSRVSNLEERL 200
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL-----EEEINGIEERI 330
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-208 1.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  63 QQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRR---TQRDLQYVEKMEnQMKGLESKFKQVEEsHKQHLARQFKAIKAK 139
Cdd:COG4717   77 EEELKEAEEKEEEYAELQEELEELEEELEELEAEleeLREELEKLEKLL-QLLPLYQELEALEA-ELAELPERLEELEER 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380808772 140 MDELRPLIPVLEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
70-143 1.97e-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: 1.97e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380808772    70 DARTKQLRQLLEKVQNmsqSIEVLDRRTQRDLQYVEKMENQMKGlESKFKQVEESHKQHLARQFKAIKAKMDEL 143
Cdd:pfam01576  888 EARIAQLEEELEEEQS---NTELLNDRLRKSTLQVEQLTTELAA-ERSTSQKSESARQQLERQNKELKAKLQEM 957
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
39-207 2.12e-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: 50.11  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   39 EESWQVYSSAQDSEGRCICTVVAPQ-QTMCSRDARTKQLRQLLEKVQNMSQSI--EVLDRRTQRDL---QYVEKmENQMK 112
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYkkEINDKEKQVSLlliQITEK-ENKMK 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  113 GL-----ESKFK--QVEESHK-------------QHLARQFKAIKAKMDELRPLIPVLEE-YKADAKLVLQFKEEAQnlt 171
Cdd:pfam05483 258 DLtflleESRDKanQLEEKTKlqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEdLQIATKTICQLTEEKE--- 334
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 380808772  172 SVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 207
Cdd:pfam05483 335 AQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRL 372
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
63-207 2.93e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  63 QQTMCSRDARTKQLRQLLEKVQNMSQSIEvldrRTQRDLQY----VEKMENQMKGLESKFKQVEESHKQhLARQFKAIKA 138
Cdd:COG4372   34 RKALFELDKLQEELEQLREELEQAREELE----QLEEELEQarseLEQLEEELEELNEQLQAAQAELAQ-AQEELESLQE 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380808772 139 KMDELRPLIpvlEEYKADAKlvlQFKEEAQNLTSVLNELQEEIGAYDY--DELQSRVSNLEERLRACMQKL 207
Cdd:COG4372  109 EAEELQEEL---EELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEelKELEEQLESLQEELAALEQEL 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
70-202 4.92e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.61  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEK----VQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVE---ESHKQHL-----ARQFKAIK 137
Cdd:COG1579   16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLgnvrnNKEYEALQ 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380808772 138 AKMDELRPLIPVLEEykadakLVLQFKEEAQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRA 202
Cdd:COG1579   96 KEIESLKRRISDLED------EILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDE 149
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
74-217 9.77e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.93  E-value: 9.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   74 KQLRQLLEKVQNMSQSIevldrRTQRDL--QYVEKMENQMKGLESKFKQVEE--SHKQHLA--RQFKAIKAKMDELRPLI 147
Cdd:pfam06160 121 EEVEELKDKYRELRKTL-----LANRFSygPAIDELEKQLAEIEEEFSQFEEltESGDYLEarEVLEKLEEETDALEELM 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  148 PVLEEYKADAKLVlqFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISD 217
Cdd:pfam06160 196 EDIPPLYEELKTE--LPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEE 263
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-200 1.25e-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: 47.74  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ-------MKGLESKFKQVE------ESHKQHLARQFKAI 136
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEaqleelESKLDELAEELAEL 342
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380808772   137 KAKMDELRplipvlEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAY--DYDELQ-------SRVSNLEERL 200
Cdd:TIGR02168  343 EEKLEELK------EELESLEAELEELEAELEELESRLEELEEQLETLrsKVAQLElqiaslnNEIERLEARL 409
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
68-201 3.05e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  68 SRDARTKQLRQLL-----EKV-QNMSQSIEVLDRRTQRDLQYVEKMENqmkgLESKFKQVEEShkqhLARQFKAIKAKMD 141
Cdd:PRK03918 143 SDESREKVVRQILglddyENAyKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKE----LEEVLREINEISS 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 142 ELRPLIPVLEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAydydeLQSRVSNLEERLR 201
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIE 269
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
63-213 6.40e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  63 QQTmcsRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENqmkgLESKFKQVEESHKQ--HLARQFKAIKAKM 140
Cdd:COG1340  125 QQT---EVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEEIHKKikELAEEAQELHEEM 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 141 DELRPLIpvlEEYKADA----KLVLQFKEEAQNLTSVLNELQEEIGAYDyDEL------------QSRVSNLEERLRACM 204
Cdd:COG1340  198 IELYKEA---DELRKEAdelhKEIVEAQEKADELHEEIIELQKELRELR-KELkklrkkqralkrEKEKEELEEKAEEIF 273
                        170
                 ....*....|
gi 380808772 205 QKLACG-KLT 213
Cdd:COG1340  274 EKLKKGeKLT 283
PLN02939 PLN02939
transferase, transferring glycosyl groups
76-207 7.20e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 45.28  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  76 LRQLLEKVQNMSQSIEVLDRrtQRDLqyvekMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKA 155
Cdd:PLN02939 245 LKAELIEVAETEERVFKLEK--ERSL-----LDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVE 317
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380808772 156 DAKLVLQFKEEAQNLTSVLNELQEEIGAYDY-----DELQSRVSNLEERLRACMQKL 207
Cdd:PLN02939 318 KAALVLDQNQDLRDKVDKLEASLKEANVSKFssykvELLQQKLKLLEERLQASDHEI 374
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
70-198 7.94e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 7.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEKVQNMsqsievldRRTQRDLQYVEKMENQMKGLESKFKQ--VEESHKQhlARQFKAIKAKMDELRPLI 147
Cdd:PRK03918 472 EEKERKLRKELRELEKV--------LKKESELIKLKELAEQLKELEEKLKKynLEELEKK--AEEYEKLKEKLIKLKGEI 541
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380808772 148 PVL-------EEYKADAKLVLQFKEEAQN-LTSVLNELqEEIGAYDYDELQSRVSNLEE 198
Cdd:PRK03918 542 KSLkkeleklEELKKKLAELEKKLDELEEeLAELLKEL-EELGFESVEELEERLKELEP 599
PRK12704 PRK12704
phosphodiesterase; Provisional
74-168 8.21e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLAR-----QFKAIKAK---MDELRp 145
Cdd:PRK12704  86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisGLTAEEAKeilLEKVE- 164
                         90       100
                 ....*....|....*....|....
gi 380808772 146 lipvlEEYKAD-AKLVLQFKEEAQ 168
Cdd:PRK12704 165 -----EEARHEaAVLIKEIEEEAK 183
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
70-208 1.18e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEKVQNmsqsiEVLDRRTQrdlqY---VEKMENQMKGLESKFKQVEE-----------SHKQHLARQFKA 135
Cdd:PRK04778 139 REEVEQLKDLYRELRK-----SLLANRFS----FgpaLDELEKQLENLEEEFSQFVEltesgdyvearEILDQLEEELAA 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380808772 136 IKAKMDELRPLIpvleeykadAKLVLQFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK04778 210 LEQIMEEIPELL---------KELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
70-180 1.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  70 DARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELRPLIPV 149
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLES 161
                         90       100       110
                 ....*....|....*....|....*....|.
gi 380808772 150 LEEYKADAKLVLQFKEEAQnLTSVLNELQEE 180
Cdd:COG4372  162 LQEELAALEQELQALSEAE-AEQALDELLKE 191
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
69-207 1.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  69 RDARTKQLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQV-------EESHKqhlarQFKAIKAKMD 141
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELekrleelEERHE-----LYEEAKAKKE 372
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380808772 142 ELRPLIPVLEEYKADaklvlQFKEEAQNLTSVLNELQEEIgaydyDELQSRVSNLE---ERLRACMQKL 207
Cdd:PRK03918 373 ELERLKKRLTGLTPE-----KLEKELEELEKAKEEIEEEI-----SKITARIGELKkeiKELKKAIEEL 431
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
217-402 1.83e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 43.08  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 217 DPVT--VKTSGSRFGSWMTDpLAPEGDNRVWYMDGYhNNRFVReyksmVDfMNTDNFTSHRLPHPWSGTGQVVY--NGSI 292
Cdd:COG4257   44 DPATgeFTEYPLGGGSGPHG-IAVDPDGNLWFTDNG-NNRIGR-----ID-PKTGEITTFALPGGGSNPHGIAFdpDGNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 293 YFNKFQSHIIIRFDLKTETILKTRSldYAGYNNMYhyawgghsdiDLMVDESGlwAVYATNQNAGNIVvsRLDP----VS 368
Cdd:COG4257  116 WFTDQGGNRIGRLDPATGEVTEFPL--PTGGAGPY----------GIAVDPDG--NLWVTDFGANAIG--RIDPdtgtLT 179
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380808772 369 LQTLQTwNTSYPKR-SAGEAfmicGTLYVTNGYSG 402
Cdd:COG4257  180 EYALPT-PGAGPRGlAVDPD----GNLWVADTGSG 209
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
68-208 1.85e-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: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    68 SRDARTKQL--RQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKfkqVEESHKQHlarqfkaikakmDELRP 145
Cdd:TIGR02169  659 SRAPRGGILfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKI------------GEIEK 723
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380808772   146 LIPVLEEYKAdaklvlQFKEEAQNLTSVLNELQEEIGAYD--YDELQSRVSNLEERLRACMQKLA 208
Cdd:TIGR02169  724 EIEQLEQEEE------KLKERLEELEEDLSSLEQEIENVKseLKELEARIEELEEDLHKLEEALN 782
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-206 1.85e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   70 DARTKQLRQLLE---KVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPL 146
Cdd:COG4913   671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  147 ipvLEEYKADAKLVLQFKEEAQNLTSvlnelqeeigayDYDELQSRVSNLEERLRACMQK 206
Cdd:COG4913   751 ---LEERFAAALGDAVERELRENLEE------------RIDALRARLNRAEEELERAMRA 795
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
75-208 3.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  75 QLRQLLEKVQNMSQSIEVLDRRTQRdlqYVEKMENQMKGLESKFKQVEEshkqhlarqfkaIKAKMDELRPLIPVLEEYK 154
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEE---RIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYL 306
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 380808772 155 adaKLVLQFKEEAQNLTSVLNELQEEIGayDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK03918 307 ---DELREIEKRLSRLEEEINGIEERIK--ELEEKEERLEELKKKLKELEKRLE 355
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
73-208 5.17e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 5.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    73 TKQLRQLLEKVQNmSQsiEVLDRRTQRDLQY---VEKMENQMKGLESKFKQVEES------HKQHLARQFKAIKAKMDEL 143
Cdd:pfam01576  460 SKDVSSLESQLQD-TQ--ELLQEETRQKLNLstrLRQLEDERNSLQEQLEEEEEAkrnverQLSTLQAQLSDMKKKLEED 536
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380808772   144 RPLIPVLEEYKADAK-----LVLQFKEEAQ---NLTSVLNELQEEIG--AYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:pfam01576  537 AGTLEALEEGKKRLQreleaLTQQLEEKAAaydKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKKQKKFDQMLA 611
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
77-202 6.23e-04

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: 42.31  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   77 RQLLEKVQnmsqSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQVEESHKQhLARQFKAIKAKMDELrplipvLEEYKAD 156
Cdd:TIGR04523 363 RELEEKQN----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELL------EKEIERL 431
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 380808772  157 AKLVLQFKEEAQNLTSVLNELQEEigaydYDELQSRVSNLEERLRA 202
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELI-----IKNLDNTRESLETQLKV 472
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
77-208 1.17e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 40.83  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   77 RQLLEKVQNMSQSIEVLDRRTQRDLQYVEK----MENQMKGLESKFKQVEESHKQHLARQfkaiKAKMDELR--PLIPVL 150
Cdd:pfam04108  20 RSLLEELVVLLAKIAFLRRGLSVQLANLEKvregLEKVLNELKKDFKQLLKDLDAALERL----EETLDKLRntPVEPAL 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  151 EEYKADAKLVLQF--KEEAQNLTSVLNELQEEIGAyDYDELQSRVSNLEERLRACMQKLA 208
Cdd:pfam04108  96 PPGEEKQKTLLDFidEDSVEILRDALKELIDELQA-AQESLDSDLKRFDDDLRDLQKELE 154
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
61-203 1.45e-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: 41.31  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    61 APQQTMCSRDARTKQlrQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLESKFKQvEESHKQHLARQFKAIKAKM 140
Cdd:pfam01576   57 AEAEEMRARLAARKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKI 133
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   141 DELRPLIPVLEEykADAKLVLQFK---EEAQNLTSVLNElqEEIGAYDYDEL----QSRVSNLEERLRAC 203
Cdd:pfam01576  134 KKLEEDILLLED--QNSKLSKERKlleERISEFTSNLAE--EEEKAKSLSKLknkhEAMISDLEERLKKE 199
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
68-200 1.76e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.28  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  68 SRDARTKQLRQLLEKVQNMSQSIEVLdrRTQRDlqyveKMENQMKGLESKfkqveeshKQHLARQFKAIKAKMDELRpli 147
Cdd:COG1340    2 KTDELSSSLEELEEKIEELREEIEEL--KEKRD-----ELNEELKELAEK--------RDELNAQVKELREEAQELR--- 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380808772 148 pvlEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAY------------DYDELQSRVSNLEERL 200
Cdd:COG1340   64 ---EKRDELNEKVKELKEERDELNEKLNELREELDELrkelaelnkaggSIDKLRKEIERLEWRQ 125
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-198 1.80e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVLDRRTQRD--LQYVeKMENqMKGLESKFKQVEESHKqhLARQFKAIKAKMDELRPLIPVLE 151
Cdd:COG4717  347 EELQELLREAEELEEELQLEELEQEIAalLAEA-GVED-EEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELL 422
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 380808772 152 EYKADAKL---VLQFKEEAQNLTSVLNELQEEIGaydydELQSRVSNLEE 198
Cdd:COG4717  423 EALDEEELeeeLEELEEELEELEEELEELREELA-----ELEAELEQLEE 467
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
71-200 2.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  71 ARTKQLRQLLEKVQNMSQSIEVLdrrtQRDLQYVEKMENQMKGLESKFKQVEES----HKQHLARQFKAIKAKMDELRPL 146
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKEL 597
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380808772 147 IPVLEEYKA--DAKLVLQFKEEAQN-LTSVLNELQEEIgaydyDELQSRVSNLEERL 200
Cdd:PRK03918 598 EPFYNEYLElkDAEKELEREEKELKkLEEELDKAFEEL-----AETEKRLEELRKEL 649
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
76-208 2.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  76 LRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKmenQMKGLESKFKQVEEshkqhLARQFKAIKAKMDELRPLIPVLEEyka 155
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEE---RIKELEEKEERLEE-----LKKKLKELEKRLEELEERHELYEE--- 366
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 380808772 156 daklVLQFKEEAQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLA 208
Cdd:PRK03918 367 ----AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
75-208 4.74e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.58  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  75 QLRQLLEKVQNMSQSIEVLDRRtqrdLQYVEKMENQMKGLESKFKQVEESHKQHLARQFKAIKAKMDELRPLipvLEeyk 154
Cdd:cd00176   34 SVEALLKKHEALEAELAAHEER----VEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQR---LE--- 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380808772 155 aDAKLVLQFKEEAQNLTSVLNELQEEIGAYDYD-------ELQSRVSNLEERLRACMQKLA 208
Cdd:cd00176  104 -EALDLQQFFRDADDLEQWLEEKEAALASEDLGkdlesveELLKKHKELEEELEAHEPRLK 163
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
66-206 6.26e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.26  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772    66 MCSRDARTK-QLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKG--------LESKFKQVEE--SHKQHLARQFK 134
Cdd:TIGR00606  682 VCQRVFQTEaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGlapgrqsiIDLKEKEIPElrNKLQKVNRDIQ 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   135 AIKAKMDE----LRPLIPVLEEYK---ADAKLVLQFKEEAQN----LTSVLNELQEEIGAYDYDELQSRVSNLEERLRAC 203
Cdd:TIGR00606  762 RLKNDIEEqetlLGTIMPEEESAKvclTDVTIMERFQMELKDverkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841

                   ...
gi 380808772   204 MQK 206
Cdd:TIGR00606  842 VSK 844
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
77-208 6.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   77 RQLLEKVQNMSQSIEVLDRrTQRDlqyVEKMENQMKGLEskfkQVEESHkqhlaRQFKAIKAKMDELRPLIPVLEEYKAD 156
Cdd:COG4913   221 PDTFEAADALVEHFDDLER-AHEA---LEDAREQIELLE----PIRELA-----ERYAAARERLAELEYLRAALRLWFAQ 287
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 380808772  157 AKLVLQfKEEAQNLTSVLNELQEEIgaydyDELQSRVSNLEERLRACMQKLA 208
Cdd:COG4913   288 RRLELL-EAELEELRAELARLEAEL-----ERLEARLDALREELDELEAQIR 333
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
68-207 7.32e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  68 SRDARTKQLRQLLEKVQNMSQSIEVLDRRTqRDLQYVEKMENQmkgLEskFKQVEESHKQHLARQF----KAIKAKMDEL 143
Cdd:COG1340   79 ERDELNEKLNELREELDELRKELAELNKAG-GSIDKLRKEIER---LE--WRQQTEVLSPEEEKELvekiKELEKELEKA 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772 144 RPLIPVLEEYKADAKLVLQFKEEAQNLTSVLNELQEEIGAY-----------------------DYDELQSRVSNLEERL 200
Cdd:COG1340  153 KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheemielykeadelrkeadelhkEIVEAQEKADELHEEI 232

                 ....*..
gi 380808772 201 RACMQKL 207
Cdd:COG1340  233 IELQKEL 239
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
74-198 8.17e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 38.66  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772  74 KQLRQLLEKVQNMSQSIEVldrrTQRDLQYVEKMENQMKGLESKFKQ-VEESHKQHLA------------RQFKAIKAKM 140
Cdd:PRK04778 324 EQNKELKEEIDRVKQSYTL----NESELESVRQLEKQLESLEKQYDEiTERIAEQEIAyselqeeleeilKQLEEIEKEQ 399
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380808772 141 DELRPLIPVLEEYKADAK-LVLQFKE---------EAQNLTSV-------LNELQEEIGAYDyDELQSRVSNLEE 198
Cdd:PRK04778 400 EKLSEMLQGLRKDELEAReKLERYRNklheikrylEKSNLPGLpedylemFFEVSDEIEALA-EELEEKPINMEA 473
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
73-201 8.72e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 36.51  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380808772   73 TKQLRQLLEKVqnmsqsievldRRTQRDlqyVEKMENQMKGLESKFKQVEEShKQHLARQFKAIKAKMDELRPLIPVLEE 152
Cdd:pfam10473   2 EKKQLHVLEKL-----------KESERK---ADSLKDKVENLERELEMSEEN-QELAILEAENSKAEVETLKAEIEEMAQ 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 380808772  153 YKADAKLVLQ-FKEEAQNLTSVLNELQEEIgaydyDELQSRVSNLEERLR 201
Cdd:pfam10473  67 NLRDLELDLVtLRSEKENLTKELQKKQERV-----SELESLNSSLENLLE 111
 
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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