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Conserved domains on  [gi|1622835410|ref|XP_028696663|]
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coiled-coil domain-containing protein 27 isoform X2 [Macaca mulatta]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-620 1.62e-09

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: 61.11  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKH-QEMMGLIEKDNQL 496
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARlEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 497 LRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRN 576
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622835410 577 KIIQAtfsitgtkslvnEISDNDILEALQRIISERSDYYNQLKQ 620
Cdd:COG1196   401 QLEEL------------EEAEEALLERLERLEEELEELEEALAE 432
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 264-304 1.44e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


:

Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 42.55  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622835410 264 PPLPGSCSSLEGGVLPGAPAVSIRVPHPGGAPQPCPAPALP 304
Cdd:pfam06346  61 PPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPPPPPLP 101
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-620 1.62e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKH-QEMMGLIEKDNQL 496
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARlEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 497 LRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRN 576
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622835410 577 KIIQAtfsitgtkslvnEISDNDILEALQRIISERSDYYNQLKQ 620
Cdd:COG1196   401 QLEEL------------EEAEEALLERLERLEEELEELEEALAE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 432-612 4.81e-08

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: 56.60  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMtdkfsNLREDKKHQEMMGLiEKDNQLLRQQVSKLERKLTKR 511
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISAL-RKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  512 DRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKIIQATFsitGTKSL 591
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE---RLESL 829

                          170       180
                   ....*....|....*....|..
gi 1622835410  592 VNEISDNDI-LEALQRIISERS 612
Cdd:TIGR02168  830 ERRIAATERrLEDLEEQIEELS 851
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 415-578 1.56e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  415 QFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINR-------ENETLQKELRERKQQLQAMtdkfsNLREDKKHQEMM 487
Cdd:pfam15921  547 QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtagamqvEKAQLEKEINDRRLELQEF-----KILKDKKDAKIR 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  488 GLIEKDNQLLRQQVsKLERKLTKRDRVISELDTKVSQLQEQVELDQNHL----QRWKQLQEDLQSKKEMIQESEQQVRVA 563
Cdd:pfam15921  622 ELEARVSDLELEKV-KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNKLKMQ 700

                          170
                   ....*....|....*
gi 1622835410  564 LESSQSRLERLRNKI 578
Cdd:pfam15921  701 LKSAQSELEQTRNTL 715
PRK12704 PRK12704
phosphodiesterase; Provisional
 424-610 6.55e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 424 RYSLATGVIASLQQQLdfqESQLRKINRENETLQKElrerkQQLQAmTDKFSNLREDkkhqemmglIEKDNQLLRQQVSK 503
Cdd:PRK12704   25 RKKIAEAKIKEAEEEA---KRILEEAKKEAEAIKKE-----ALLEA-KEEIHKLRNE---------FEKELRERRNELQK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 504 LERKLTKRDrviSELDTKVSQL-QEQVELDQnHLQRWKQLQEDLQSKKEMIQESEQQVRVALE------SSQSR---LER 573
Cdd:PRK12704   87 LEKRLLQKE---ENLDRKLELLeKREEELEK-KEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKeilLEK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622835410 574 LRNKIIQATFSI-----TGTKSLVNEISDNDILEALQRIISE 610
Cdd:PRK12704  163 VEEEARHEAAVLikeieEEAKEEADKKAKEILAQAIQRCAAD 204
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 264-304 1.44e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 42.55  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622835410 264 PPLPGSCSSLEGGVLPGAPAVSIRVPHPGGAPQPCPAPALP 304
Cdd:pfam06346  61 PPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPPPPPLP 101
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 432-560 7.98e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.97  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQEMMGLIEKDN-----------QLLRQQ 500
Cdd:cd22656   130 AKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIKDLQKELEKLNeeyaaklkakiDELKAL 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622835410 501 VSKLERKLTKRDRVISEL---DTKVSQLQEQVELDQNHLQR----WKQLQEDLQSKKEMIQESEQQV 560
Cdd:cd22656   210 IADDEAKLAAALRLIADLtaaDTDLDNLLALIGPAIPALEKlqgaWQAIATDLDSLKDLLEDDISKI 276
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-620 1.62e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKH-QEMMGLIEKDNQL 496
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARlEERRRELEERLEE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 497 LRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRN 576
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622835410 577 KIIQAtfsitgtkslvnEISDNDILEALQRIISERSDYYNQLKQ 620
Cdd:COG1196   401 QLEEL------------EEAEEALLERLERLEEELEELEEALAE 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 418-581 9.69e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 57.85  E-value: 9.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDK-FSNLREDK-----------KHQE 485
Cdd:COG4942    57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPlalllspedflDAVR 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 486 MMGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQE---QVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRV 562
Cdd:COG4942   137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                         170
                  ....*....|....*....
gi 1622835410 563 ALESSQSRLERLRNKIIQA 581
Cdd:COG4942   217 ELQQEAEELEALIARLEAE 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 408-581 3.99e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 408 EQVILDFQFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKH-QEM 486
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaEEE 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 487 MGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALES 566
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         170
                  ....*....|....*
gi 1622835410 567 SQSRLERLRNKIIQA 581
Cdd:COG1196   433 LEEEEEEEEEALEEA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 432-612 4.81e-08

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: 56.60  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMtdkfsNLREDKKHQEMMGLiEKDNQLLRQQVSKLERKLTKR 511
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISAL-RKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  512 DRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKIIQATFsitGTKSL 591
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE---RLESL 829

                          170       180
                   ....*....|....*....|..
gi 1622835410  592 VNEISDNDI-LEALQRIISERS 612
Cdd:TIGR02168  830 ERRIAATERrLEDLEEQIEELS 851
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
441-610 2.11e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 441 FQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDkkhqemmgLIEKDNQL--LRQQVSKLERKLTKRDRVISEL 518
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE--------LEQARSELeqLEEELEELNEQLQAAQAELAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 519 DTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKIIQATFSITGTKSLVNEISDN 598
Cdd:COG4372   100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                         170
                  ....*....|..
gi 1622835410 599 DILEALQRIISE 610
Cdd:COG4372   180 EAEQALDELLKE 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 411-620 2.34e-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: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  411 ILDFQFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDkkHQEMMGLI 490
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE--LESLEAEL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  491 EKDNQLLRQqvskLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQ--------------RWKQLQEDLQSKKEMIQES 556
Cdd:TIGR02168  361 EELEAELEE----LESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerledrreRLQQEIEELLKKLEEAELK 436

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622835410  557 EQQVRVA------------LESSQSRLERLRNKIIQATFSITGTKSLVNEISDNdiLEALQRIISERSDYYNQLKQ 620
Cdd:TIGR02168  437 ELQAELEeleeeleelqeeLERLEEALEELREELEEAEQALDAAERELAQLQAR--LDSLERLQENLEGFSEGVKA 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-580 5.04e-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: 53.14  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLRED---------------KK 482
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeleseleallnerAS 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  483 HQEMMGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVE-LDQNHLQRWKQLQEDLQSKKEMIQESEQQVR 561
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964

                          170
                   ....*....|....*....
gi 1622835410  562 VALESSQSRLERLRNKIIQ 580
Cdd:TIGR02168  965 DDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 417-581 6.34e-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: 52.75  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  417 NLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENEtLQKELRERKQQLQAMtdkfsNLREDKKHQEMMGLIEKDNQl 496
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLVL-----RLEELREELEELQEELKEAE- 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  497 lrQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRN 576
Cdd:TIGR02168  253 --EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330


                   ....*
gi 1622835410  577 KIIQA 581
Cdd:TIGR02168  331 KLDEL 335
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 418-578 7.47e-07

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: 51.69  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQ----EMMGLIEKD 493
Cdd:COG4942    43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 494 NQLLRQQ-VSKLERKLT-------KRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALE 565
Cdd:COG4942   123 ALLLSPEdFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202

                         170
                  ....*....|...
gi 1622835410 566 SSQSRLERLRNKI 578
Cdd:COG4942   203 RLEKELAELAAEL 215
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 444-641 1.28e-06

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: 51.56  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 444 SQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQemmgliEKDNQLLRQQVSKLERKLTKRDRVISELDTKVS 523
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS------ESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 524 QLQEQVELDQNHLQRWKQLQEDLQSKkemIQESEQQvrvaLESSQSRLERLRNKIIQATFSItgtKSLVNEISD------ 597
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQ---IKKLQQE----KELLEKEIERLKETIIKNNSEI---KDLTNQDSVkeliik 457

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622835410 598 --NDILEALQRIISERSDYYNQLKQKgvkvppLQQSETFLPSKTKK 641
Cdd:TIGR04523 458 nlDNTRESLETQLKVLSRSINKIKQN------LEQKQKELKSKEKE 497
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 434-574 1.47e-06

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: 51.56  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 434 SLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLredkkhqemmgliEKDNQLLRQQVSKLERKLTKRDR 513
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL-------------EEKVKDLTKKISSLKEKIEKLES 531

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622835410 514 VISELDTKVSQLQEQVELDQNHLqRWKQLQEDLQSKKEMIQESEQQVRvALESSQSRLERL 574
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQK-SLKKKQEEKQEL 590
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 417-645 2.26e-06

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: 50.84  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  417 NLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSN-----LREDKKHQEMMGLIE 491
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkekIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  492 KDNQL----LRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESS 567
Cdd:TIGR02169  311 AEKEReledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  568 QSRLERLRNKIiqatfsitgtkslvNEISDND--ILEALQRIISERSDYYNQLKQKGVKVPPLQQSETFLPSKTKKGTSK 645
Cdd:TIGR02169  391 REKLEKLKREI--------------NELKRELdrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
416-578 2.65e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  416 FNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAmtdkfsnlredkkhqemMGLIEKDNq 495
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----------------NGGDRLEQ- 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  496 lLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELD----QNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRL 571
Cdd:COG4913    343 -LEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421


                   ....*..
gi 1622835410  572 ERLRNKI 578
Cdd:COG4913    422 RELEAEI 428
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 443-620 2.70e-06

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: 50.79  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 443 ESQLRKINRENETLQKELRERKQQLqamtdkfsNLREDKKHQemmglIEKDNQLLRQQVSKLERKLTKRDRV-------- 514
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENEL--------NLLEKEKLN-----IQKNIDKIKNKLLKLELLLSNLKKKiqknksle 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 515 --ISELDTKVSQLQEQVEldqnhlqrwkQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKIIQatfsITGTKSLV 592
Cdd:TIGR04523 218 sqISELKKQNNQLKDNIE----------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKI 283

                         170       180
                  ....*....|....*....|....*...
gi 1622835410 593 NEISDNdileaLQRIISERSDYYNQLKQ 620
Cdd:TIGR04523 284 KELEKQ-----LNQLKSEISDLNNQKEQ 306
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 427-633 3.12e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 427 LATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLRED-KKHQEMMGLIEKDNQLLRQQVSKLE 505
Cdd:COG3883     6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAElEALQAEIDKLQAEIAEAEAEIEERR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 506 RKLTKRDRV-------------------ISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALES 566
Cdd:COG3883    86 EELGERARAlyrsggsvsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622835410 567 SQSRLERLRNKIIQAtfsitgtKSLVNEISDN--DILEALQRIISERSDYYNQLKQKGVKVPPLQQSET 633
Cdd:COG3883   166 LEAAKAELEAQQAEQ-------EALLAQLSAEeaAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
418-578 4.13e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAmtdkFSNLREDKKH-QEMMGLIEKDNQL 496
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL----LPLYQELEALeAELAELPERLEEL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 497 LRQ--QVSKLERKLTKRDRVISELDTKVSQLQEQVELDQnhLQRWKQLQEDLqskkEMIQESEQQVRVALESSQSRLERL 574
Cdd:COG4717   152 EERleELRELEEELEELEAELAELQEELEELLEQLSLAT--EEELQDLAEEL----EELQQRLAELEEELEEAQEELEEL 225


                  ....
gi 1622835410 575 RNKI 578
Cdd:COG4717   226 EEEL 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-608 5.84e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 402 AQLEEYEQVILDFQFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDK 481
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 482 KHQEMM--GLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRwKQLQEDLQSKKEMIQESEQQ 559
Cdd:COG1196   403 EELEEAeeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL-LELLAELLEEAALLEAALAE 481

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622835410 560 VRVALESSQSRLERLRNKIIQATFSITGTKSLVNEISDNDILEALQRII 608
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 437-578 7.61e-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: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 437 QQLDfqeSQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKK------------HQEMMGLIEKDNQLLRQ----- 499
Cdd:COG1579    13 QELD---SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEdlekeikrleleIEEVEARIKKYEEQLGNvrnnk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 500 -------QVSKLERKLTKRDRVISELDTKVSQLQEQVELDQnhlQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLE 572
Cdd:COG1579    90 eyealqkEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELEAERE 166


                  ....*.
gi 1622835410 573 RLRNKI 578
Cdd:COG1579   167 ELAAKI 172
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
432-581 7.91e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  432 IASLQQQLDFQESQLRKINRENETLQKE---LRERKQQLQAMTDKFSNLRE--------DKKHQEMMGLIEKDNQL--LR 498
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLAEYSWDEIDvasaereiAELEAELERLDASSDDLaaLE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  499 QQVSKLERKLTKRDRVISELDTKVSQLQEQVEldqNHLQRWKQLQEDLQS-----------------KKEMIQESEQQVR 561
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELE---QAEEELDELQDRLEAaedlarlelralleerfAAALGDAVERELR 768

                          170       180
                   ....*....|....*....|....
gi 1622835410  562 VALESS----QSRLERLRNKIIQA 581
Cdd:COG4913    769 ENLEERidalRARLNRAEEELERA 792
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 432-620 1.06e-05

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: 48.86  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMtdkfsnlreDKKHQEMMGLIEKDNqllrQQVSKLERKLTKR 511
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL---------EKEIERLKETIIKNN----SEIKDLTNQDSVK 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 512 DRVISELDTKVSQLQEQVELDQNHL----QRWKQLQEDLQSKKEMI-------QESEQQVRV---ALESSQSRLERLRNK 577
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKELkklneekKELEEKVKDltkKISSLKEKIEKLESE 532

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622835410 578 IIQATFSITGTKSLVNEISDNDILEALQRIISERSDYYNQLKQ 620
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQ 575
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 415-578 1.56e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  415 QFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINR-------ENETLQKELRERKQQLQAMtdkfsNLREDKKHQEMM 487
Cdd:pfam15921  547 QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtagamqvEKAQLEKEINDRRLELQEF-----KILKDKKDAKIR 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  488 GLIEKDNQLLRQQVsKLERKLTKRDRVISELDTKVSQLQEQVELDQNHL----QRWKQLQEDLQSKKEMIQESEQQVRVA 563
Cdd:pfam15921  622 ELEARVSDLELEKV-KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNKLKMQ 700

                          170
                   ....*....|....*
gi 1622835410  564 LESSQSRLERLRNKI 578
Cdd:pfam15921  701 LKSAQSELEQTRNTL 715
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 437-574 1.83e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.81  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 437 QQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQEmmgliEKDNQL---LRQQVSKLERKLTKRDR 513
Cdd:pfam05557  51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQL-----ADAREViscLKNELSELRRQIQRAEL 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622835410 514 VISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVR-------------VALESSQSRLERL 574
Cdd:pfam05557 126 ELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKelefeiqsqeqdsEIVKNSKSELARI 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-594 2.51e-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: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDkkhqemMGLIEKDNQLL 497
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR------IAATERRLEDL 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  498 RQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQN----HLQRWKQLQEDLQSKKEMIQESEQQV---RVALESSQSR 570
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasLEEALALLRSELEELSEELRELESKRselRRELEELREK 923

                          170       180
                   ....*....|....*....|....
gi 1622835410  571 LERLRNKIIQATFSITGTKSLVNE 594
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERLSE 947
PRK12704 PRK12704
phosphodiesterase; Provisional
 424-610 6.55e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 424 RYSLATGVIASLQQQLdfqESQLRKINRENETLQKElrerkQQLQAmTDKFSNLREDkkhqemmglIEKDNQLLRQQVSK 503
Cdd:PRK12704   25 RKKIAEAKIKEAEEEA---KRILEEAKKEAEAIKKE-----ALLEA-KEEIHKLRNE---------FEKELRERRNELQK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 504 LERKLTKRDrviSELDTKVSQL-QEQVELDQnHLQRWKQLQEDLQSKKEMIQESEQQVRVALE------SSQSR---LER 573
Cdd:PRK12704   87 LEKRLLQKE---ENLDRKLELLeKREEELEK-KEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKeilLEK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622835410 574 LRNKIIQATFSI-----TGTKSLVNEISDNDILEALQRIISE 610
Cdd:PRK12704  163 VEEEARHEAAVLikeieEEAKEEADKKAKEILAQAIQRCAAD 204
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 427-621 1.16e-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: 44.75  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 427 LATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMtdkfsnLREDKKHQEMMGLIEKDNQLLRQQVSKLER 506
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL------LKQLAALERRIAALARRIRALEQELAALEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 507 KLTKRDRVISELDTKVSQLQEQVELDQNHLQR---------------WKQLQEDLQSKKEMIQESEQQVRvALESSQSRL 571
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAE-ELRADLAEL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622835410 572 ERLRNKIIQATFSItgtKSLVNEISDNdiLEALQRIISERSDYYNQLKQK 621
Cdd:COG4942   163 AALRAELEAERAEL---EALLAELEEE--RAALEALKAERQKLLARLEKE 207
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 264-304 1.44e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 42.55  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622835410 264 PPLPGSCSSLEGGVLPGAPAVSIRVPHPGGAPQPCPAPALP 304
Cdd:pfam06346  61 PPLPGAASIPPPPPLPGSTGIPPPPPLPGGAGIPPPPPPLP 101
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 434-620 1.82e-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: 44.63  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 434 SLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHqEMMGLIEKDNQLlrQQVSKLERKLTKRdr 513
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKEL--EQNNKKIKELEKQ-- 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 514 vISELDTKVSQLQEQVELDQNhlqrwKQLQEDLQSKKEMIQESEQQvrvaLESSQSRLERLRNKIIQATFSITGTKSLVN 593
Cdd:TIGR04523 290 -LNQLKSEISDLNNQKEQDWN-----KELKSELKNQEKKLEEIQNQ----ISQNNKIISQLNEQISQLKKELTNSESENS 359

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622835410 594 EIsDNDILE---ALQRIISERSDYYNQLKQ 620
Cdd:TIGR04523 360 EK-QRELEEkqnEIEKLKKENQSYKQEIKN 388
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 418-569 1.87e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQL--------------------------QAMT 471
Cdd:COG3883    39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfSDFL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 472 DKFSNLREDKKHQ-EMMGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKK 550
Cdd:COG3883   119 DRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198

                         170
                  ....*....|....*....
gi 1622835410 551 EMIQESEQQVRVALESSQS 569
Cdd:COG3883   199 AELEAELAAAEAAAAAAAA 217
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
435-621 3.32e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 435 LQQQLDFQESQLRKINREnetLQKELRERKQQLQAMTDKFSNLREdkkhQEMMGLIEKDNQLLRQQVSKLERKLTKRDRV 514
Cdd:COG3206   162 LEQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQ----KNGLVDLSEEAKLLLQQLSELESQLAEARAE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 515 ISELDTKVSQLQEQVELD-------------QNHLQRWKQLQEDL--------------QSKKEMIQESEQQ----VRVA 563
Cdd:COG3206   235 LAEAEARLAALRAQLGSGpdalpellqspviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQlqqeAQRI 314

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622835410 564 LESSQSRLERLRNKIIQATFSITGTKSLVNEISDNDI-LEALQRIISERSDYYNQLKQK 621
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAeLRRLEREVEVARELYESLLQR 373
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
435-621 3.84e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 435 LQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTdkfSNLREDKKHQEMMGLIEKDNQLLRQQVSKLERKLTKRDRV 514
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEISSELPELREELEKLE---KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 515 ISELDTKVSQLQEQVEldqnhlqRWKQLQEDLQSKKEMIQESEQ--QVRVALESSQSRLERLRNKIIQATFSITGTKSLV 592
Cdd:PRK03918  268 IEELKKEIEELEEKVK-------ELKELKEKAEEYIKLSEFYEEylDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622835410 593 NEISDNdiLEALQR---IISERSDYYNQLKQK 621
Cdd:PRK03918  341 EELKKK--LKELEKrleELEERHELYEEAKAK 370
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
432-578 5.58e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKEL---RERKQQLQAMTDKFSNLREDKKHQEMmgliEKDNqllrqqvskLERKL 508
Cdd:PRK02224  215 LAELDEEIERYEEQREQARETRDEADEVLeehEERREELETLEAEIEDLRETIAETER----EREE---------LAEEV 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 509 TKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKI 578
Cdd:PRK02224  282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
PCRF pfam03462
PCRF domain; This domain is found in peptide chain release factors.
 497-578 5.62e-04

PCRF domain; This domain is found in peptide chain release factors.


Pssm-ID: 460929 [Multi-domain]  Cd Length: 192  Bit Score: 41.60  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 497 LRQQVSKLERKLTKRDrVIS------ELDTKVSQLQEQVELdqnhLQRWKQLQEDLQSKKEMIQESE--QQVRVALESSQ 568
Cdd:pfam03462   1 LEERYEELEALLSDPD-VWDdqkraqKLSKEYSELEPIVEA----YREYKQALEDLEEAKELLEDPElaELAEEELEELE 75

                          90
                  ....*....|
gi 1622835410 569 SRLERLRNKI 578
Cdd:pfam03462  76 KRLEELEEEL 85
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
418-570 6.31e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 418 LEATRTRYSLATGVIASLQQQLDFQESQLRKI--NRENETLQKELRERKQQLQAMTDKFSNlredkKHQEMMGL---IEK 492
Cdd:COG3206   228 LAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTP-----NHPDVIALraqIAA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 493 DNQLLRQQVSKLERKLTKRDRV----ISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKK---EMIQESEQQVRVALE 565
Cdd:COG3206   303 LRAQLQQEAQRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARelyESLLQRLEEARLAEA 382


                  ....*
gi 1622835410 566 SSQSR 570
Cdd:COG3206   383 LTVGN 387
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 429-569 6.77e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 429 TGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNL------------------------------- 477
Cdd:pfam10174 379 AGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLqtdssntdtalttleealsekeriierlkeq 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 478 --REDKKHQEMMGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLqrwKQLQEDLQSKKEMIQE 555
Cdd:pfam10174 459 reREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL---KSLEIAVEQKKEECSK 535

                         170
                  ....*....|....
gi 1622835410 556 SEQQVRVALESSQS 569
Cdd:pfam10174 536 LENQLKKAHNAEEA 549
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 432-560 7.98e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.97  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQEMMGLIEKDN-----------QLLRQQ 500
Cdd:cd22656   130 AKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEIKDLQKELEKLNeeyaaklkakiDELKAL 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622835410 501 VSKLERKLTKRDRVISEL---DTKVSQLQEQVELDQNHLQR----WKQLQEDLQSKKEMIQESEQQV 560
Cdd:cd22656   210 IADDEAKLAAALRLIADLtaaDTDLDNLLALIGPAIPALEKlqgaWQAIATDLDSLKDLLEDDISKI 276
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
498-581 8.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 8.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  498 RQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQE------DLQSKKEMIQESEQQVRvALESSQSRL 571
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELE-RLDASSDDL 687

                           90
                   ....*....|
gi 1622835410  572 ERLRNKIIQA 581
Cdd:COG4913    688 AALEEQLEEL 697
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 413-597 9.85e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 413 DFQFNLEATRTRyslatgvIASLQQQLDFQESQLRKINRENETLQKELRERK--------------QQLQAMTDKFSNLR 478
Cdd:pfam05483 258 DLTFLLEESRDK-------ANQLEEKTKLQDENLKELIEKKDHLTKELEDIKmslqrsmstqkaleEDLQIATKTICQLT 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 479 EDKKHQ----------------EMMGLIEKDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQL 542
Cdd:pfam05483 331 EEKEAQmeelnkakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622835410 543 QEDLQSKKEMIQESEQQVRVALESS----------QSRLERLRNKIIQATFSITGTKSLVNEISD 597
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 438-580 1.01e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  438 QLDFQESQLRKINRENETLQKE---LRERKQQLQAMTDKFSNLREDKKH---QEMMGLIEKDNQLlrqqVSKLERKLTKR 511
Cdd:COG3096    921 QLEPLVAVLQSDPEQFEQLQADylqAKEQQRRLKQQIFALSEVVQRRPHfsyEDAVGLLGENSDL----NEKLRARLEQA 996

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622835410  512 DRVISELDTKVSQLQEQVEldqNHLQRWKQLQEDLQSKKEMIQESEQQ-----VRV---ALESSQSRLERLRNKIIQ 580
Cdd:COG3096    997 EEARREAREQLRQAQAQYS---QYNQVLASLKSSRDAKQQTLQELEQEleelgVQAdaeAEERARIRRDELHEELSQ 1070
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 432-597 1.37e-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: 41.93  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTD--KFSNLRE--DKKHQEMMGLIEKDNQLLRQQ------V 501
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelKKENLEKeiDEKNKEIEELKQTQKSLKKKQeekqelI 591

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 502 SKLERKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVrvalessQSRLERLRNKIIQA 581
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI-------KETIKEIRNKWPEI 664

                         170
                  ....*....|....*.
gi 1622835410 582 TFSITGTKSLVNEISD 597
Cdd:TIGR04523 665 IKKIKESKTKIDDIIE 680
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 436-574 1.84e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 436 QQQLDFQESQLRKIN----RENETLQKELRERKQQLQAMTDKFSNLREDKKHQEMMgliEKDNQLLRQQVSK-LERKLTK 510
Cdd:pfam17380 427 AEQEEARQREVRRLEeeraREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE---KRDRKRAEEQRRKiLEKELEE 503

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622835410 511 RDRVISELDTKVSQLQEQVELDQNHL---QRWKQLQEDLQSKKEMIQES--EQQVRVALEsSQSRLERL 574
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIyeeERRREAEEERRKQQEMEERRriQEQMRKATE-ERSRLEAM 571
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 449-575 2.50e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.86  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 449 INRENETLQKELRERKQQLQAMTdkfsnlredkkhQEMMGLIEKDNQLLRQqvsklerkltkrdrviseLDTKVSQLQEQ 528
Cdd:PRK06975  344 LNRKVDRLDQELVQRQQANDAQT------------AELRVKTEQAQASVHQ------------------LDSQFAQLDGK 393

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622835410 529 VELDQNHLQRWKQLQEDLQSKKE--MIQESEQ-------------QVRVALESSQSRLERLR 575
Cdd:PRK06975  394 LADAQSAQQALEQQYQDLSRNRDdwMIAEVEQmlssasqqlqltgNVQLALIALQNADARLA 455
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 434-579 2.63e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 434 SLQQQLDFQESQLRKINRENETLQK---------------------ELRERKQQLQAMTDKFSNLREDKK--HQEMMGLI 490
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKkgsaenkqlnayeikvnklelELASAKQKFEEIIDNYQKEIEDKKisEEKLLEEV 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 491 EKDNQLLRQQVsKLERKLTKRDRviseldtkvSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSR 570
Cdd:pfam05483 678 EKAKAIADEAV-KLQKEIDKRCQ---------HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIE 747


                  ....*....
gi 1622835410 571 LERLRNKII 579
Cdd:pfam05483 748 LSNIKAELL 756
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 387-621 2.99e-03

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: 40.81  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  387 RSASSLAESFEEELLAQLEEYEQVILDFQFNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQ 466
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  467 LQAMTDKFSNLREdkkhqemmgliekDNQLLRQQVSKLERKLTkrdrvisELDTKVSQLQEQVELDQNHLQRWKQLQEDL 546
Cdd:TIGR02168  784 IEELEAQIEQLKE-------------ELKALREALDELRAELT-------LLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622835410  547 QSKKEMIQESEQQVRVALESSQSRLERLRNKIIQATFSITGTKSLVNEISDNdiLEALQRIISERSDYYNQLKQK 621
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE--LEELSEELRELESKRSELRRE 916
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 435-565 3.27e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 435 LQQQLDFQESQLRKINRENETLQKELRERKQQLQAmtdkfsNLREDKKHQEMMGLIEKDNQLLRQQVSKLERKLTKRDRV 514
Cdd:pfam15709 380 LEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQL------QAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQR 453

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622835410 515 ISELDTKVSQ----LQEQVELDQNHLQRWKQLQED--LQSKKEMIQESEQQVRVALE 565
Cdd:pfam15709 454 QKELEMQLAEeqkrLMEMAEEERLEYQRQKQEAEEkaRLEAEERRQKEEEAARLALE 510
mukB PRK04863
chromosome partition protein MukB;
432-560 3.42e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  432 IASLQQQ---LDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNlREDKKHQEMMGLIEKDNQLLRQQVSKLERKL 508
Cdd:PRK04863   920 LAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR-RAHFSYEDAAEMLAKNSDLNEKLRQRLEQAE 998

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622835410  509 TKRDRviseLDTKVSQLQEQveLDQNHlQRWKQLQEDLQSKKEMIQESEQQV 560
Cdd:PRK04863   999 QERTR----AREQLRQAQAQ--LAQYN-QVLASLKSSYDAKRQMLQELKQEL 1043
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 450-561 4.34e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.56  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 450 NRENETLqKELRERKQQLQAMTDKFSNLRED-KKHQEMMGLIEKDNQLLRQQVSKLER---KLTKRDRVISELDTKVSQL 525
Cdd:pfam18595   5 AEEKEEL-AELERKARELQAKIDALQVVEKDlRSCIKLLEEIEAELAKLEEAKKKLKElrdALEEKEIELRELERREERL 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622835410 526 QEQVELDQNHLQRwkqLQEDLQSKKEMIQESEQQVR 561
Cdd:pfam18595  84 QRQLENAQEKLER---LREQAEEKREAAQARLEELR 116
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 435-578 4.63e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  435 LQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKkhqemmgLIEKDNQLLRQQvskLERKLTKRDRV 514
Cdd:TIGR00606  827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK-------LQIGTNLQRRQQ---FEEQLVELSTE 896

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622835410  515 ISELDTKVSQLQEQVELDQnhlqrwKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKI 578
Cdd:TIGR00606  897 VQSLIREIKDAKEQDSPLE------TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 432-621 4.90e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 432 IASLQQQLDFQESQLRKINRENETLQKELRERKQQLqaMTDKfSNLREDKKhqEMMGLIEKDNQLL-RQQVSKLERKLTK 510
Cdd:cd22656   116 KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQT--EKDQ-TALETLEK--ALKDLLTDEGGAIaRKEIKDLQKELEK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 511 -RDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESsqsrLERLRN--KIIQATFSitG 587
Cdd:cd22656   191 lNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA----LEKLQGawQAIATDLD--S 264

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622835410 588 TKSLVNEISDNDILEALQRIISER-SDYYNQLKQK 621
Cdd:cd22656   265 LKDLLEDDISKIPAAILAKLELEKaIEKWNELAEK 299
mukB PRK04863
chromosome partition protein MukB;
437-574 5.89e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  437 QQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQEMM--GLIEKDNQL------LRQQVSKLE--- 505
Cdd:PRK04863   516 QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARleSLSESVSEArerrmaLRQQLEQLQari 595

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622835410  506 RKLTKRDRVISELDTKVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERL 574
Cdd:PRK04863   596 QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 416-621 7.93e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.57  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  416 FNLEATRTRYSLATGVIASLQQQLDFQESQLRKINRENETLQKELRERKQQLQAMTDKFSNLREDKKHQEMM----GLIE 491
Cdd:pfam02463  213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelKLLA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410  492 KDNQLLRQQVSKLERKLTKRDRVISELDTKVSQLQEQVELDQ---NHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQ 568
Cdd:pfam02463  293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622835410  569 SRLERLRNKIIQATFSITGTKSLVNEISDNDILEA-LQRIISERSDYYNQLKQK 621
Cdd:pfam02463  373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAqLLLELARQLEDLLKEEKK 426
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 441-578 8.63e-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: 39.23  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 441 FQESQLRKINRENETLQKELRERKQQLQAMtDKFSNLREDKKHQemmglIEKDNQLLRQQVSKLERKLTKRDRVISELDT 520
Cdd:TIGR04523  30 KQDTEEKQLEKKLKTIKNELKNKEKELKNL-DKNLNKDEEKINN-----SNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622835410 521 KVSQLQEQVELDQNHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNKI 578
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY 161
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 438-577 8.83e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 38.85  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835410 438 QLDFQESQLRKINRENETLqkelRERKQQLQAMTDKFsnlrEDKKHQEMMGLIEKDNQLlRQQVSKLERKLTKRD----- 512
Cdd:pfam04849 165 QLDALQEKLRGLEEENLKL----RSEASHLKTETDTY----EEKEQQLMSDCVEQLSEA-NQQMAELSEELARKMeenlr 235

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622835410 513 --RVISELDTKVSQLQ--------EQVELDQnHLQRWKQLQEDLQSKKEMIQESEQQVRVALESSQSRLERLRNK 577
Cdd:pfam04849 236 qqEEITSLLAQIVDLQhkckelgiENEELQQ-HLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
 
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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