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Conserved domains on  [gi|755515061|ref|XP_011239320|]
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microtubule-associated tumor suppressor candidate 2 homolog isoform X1 [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
973-1280 1.96e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   973 QAREAERQLaQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKC 1052
Cdd:TIGR02168  692 KIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1053 EKLQKEKETLERRFEEELRRLgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRcQHQEQVEDITASHEAALLEM 1132
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1133 ENNhtvaitilqddhdhKVQELMSTHEFEkkELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKII 1212
Cdd:TIGR02168  848 EEL--------------SEDIESLAAEIE--ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061  1213 ELE----KLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK-KRLSRTNEEL 1280
Cdd:TIGR02168  912 ELRreleELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKEL 984
PHA03247 super family cl33720
large tegument protein UL36; Provisional
516-974 2.92e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  516 STPAPLLHPETTVNSSHHPTPPG--SSSQELGvfSGDTGSPSVASPPTdggqvlnTSPKVPDRTTcssgipkPPTHPKDT 593
Cdd:PHA03247 2513 SRLAPAILPDEPVGEPVHPRMLTwiRGLEELA--SDDAGDPPPPLPPA-------APPAAPDRSV-------PPPRPAPR 2576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  594 PSSQEAREKletekmeeraEAKPILMPKPkhVRPKIITYIRRNPQALSQgdaslvPVGLPYAPPTCGMPLPQEEKAASRD 673
Cdd:PHA03247 2577 PSEPAVTSR----------ARRPDAPPQS--ARPRAPVDDRGDPRGPAP------PSPLPPDTHAPDPPPPSPSPAANEP 2638
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  674 LQPSAnmyeKLKPDLQKPRVFPSGLMVS-------------------GIKPPAHHFSQMSEKFLQEVADHPGKEEFCSPP 734
Cdd:PHA03247 2639 DPHPP----PTVPPPERPRDDPAPGRVSrprrarrlgraaqassppqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  735 YTHYEVPPTFYRSAMLLKPQLGLGAMSRlPSTKSRILIASQRSSASaihPPGSLTTAASFYGSDPSDLKKASNSNAAKAS 814
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPAR---PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  815 LPKSGLRPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSVQPEQSRPVTRSTFGNEEQAPLKQALPSKD-TPKGAGRA 893
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRS 2870
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  894 APASSSNATTPRRSLLPAPK-STSTPAGAKKELQKDPEaKKPAVSSPKRTASAATKPHSPGYPKQRTSAPRNEFPPKPDL 972
Cdd:PHA03247 2871 PAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERP-PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949

                  ..
gi 755515061  973 QA 974
Cdd:PHA03247 2950 AG 2951
PHA03247 super family cl33720
large tegument protein UL36; Provisional
309-677 1.94e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  309 PRNEEGLTSAQAQGPGCHEERSMSPVERQELLEKAYREATSQGNSSHRQlGVRRGSSLEEMTGVSAGVEGSQQATPTLSA 388
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ-RPRRRAARPTVGSLTSLADPPPPPPTPEPA 2711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  389 APAGEAGTRL-TGKMSAGVGRMARETASGQTAPDVGQAAPVRRDPTESVPSEvsgeerrlgSGNSGSTKllASGPSAGGS 467
Cdd:PHA03247 2712 PHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---------AGPPAPAP--PAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  468 RTDTSGLLSPRGSNLEARKGKEMVAEnrnllenAAQTDNTPAGVDSAFSTPAPLLHPETTVNSSHHPTPPGSSSQELGVF 547
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPAD-------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  548 SG-DTGSPSVASPPTDGGQVLNTSPKVPDRTTCSSGIPKPPTHPKDTPSSQEAREKLETEKMEERAEAKPILMPKPKhvr 626
Cdd:PHA03247 2854 GSvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ--- 2930
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755515061  627 PKIITYIRRNPQALSQGDASLVPVGLPYAPPTCGMPLPQEEKAASRDLQPS 677
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQ 2981
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
973-1280 1.96e-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: 58.91  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   973 QAREAERQLaQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKC 1052
Cdd:TIGR02168  692 KIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1053 EKLQKEKETLERRFEEELRRLgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRcQHQEQVEDITASHEAALLEM 1132
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1133 ENNhtvaitilqddhdhKVQELMSTHEFEkkELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKII 1212
Cdd:TIGR02168  848 EEL--------------SEDIESLAAEIE--ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061  1213 ELE----KLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK-KRLSRTNEEL 1280
Cdd:TIGR02168  912 ELRreleELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
975-1288 2.49e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  975 REAERQLAQ------RLRDRCEWQARQLG-LAR--------RELKKAIQGFDAlavstkhffgksERALAKEKELSIELA 1039
Cdd:COG1196   175 EEAERKLEAteenleRLEDILGELERQLEpLERqaekaeryRELKEELKELEA------------ELLLLKLRELEAELE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1040 NIRDEVAFNTAKCEKLQKEKETLERRFEEELRrlgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRCQHQEQVE 1119
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1120 DITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEM 1199
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1200 KNQQIHLQEkkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEE 1279
Cdd:COG1196   399 AAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLEEA 472

                  ....*....
gi 755515061 1280 LLWKLQTGD 1288
Cdd:COG1196   473 ALLEAALAE 481
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1093-1283 3.72e-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: 51.65  E-value: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1093 QAESARLQ-----AEHQDQLLRMRCQHQEQVEDITASHEAALLEM--ENNHTVAITILQDDHDHKVQELMSTHEFEKKEL 1165
Cdd:pfam05483  205 QAENARLEmhfklKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIteKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1166 EENFEK----------LRLTLQIALAPYQHLEEDMQ----SLKQVLEMKNQQIHLQEKK-------IIELEKLVeknIIL 1224
Cdd:pfam05483  285 KELIEKkdhltkeledIKMSLQRSMSTQKALEEDLQiatkTICQLTEEKEAQMEELNKAkaahsfvVTEFEATT---CSL 361
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755515061  1225 EERIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELLWK 1283
Cdd:pfam05483  362 EELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDE 423
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1101-1278 1.91e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1101 AEHQDQLLRMRCQHQEQVEDITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIA- 1179
Cdd:PTZ00341  408 ALYTDEDLLFDLEKQKYMDMLDGSEDESVEDNEEEHSGDANEEELSVDEHVEEHNADDSGEQQSDDESGEHQSVNEIVEe 487
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1180 LAPYQHLEEdmQSLKQVLEMKNQQIHLQEKKIIELEklvekniileeriqvlQQQNEDlkARIDQNTVVTRQLSEENANL 1259
Cdd:PTZ00341  488 QSVNEHVEE--PTVADIVEQETVDEHVEEPAVDENE----------------EQQTAD--EHVEEPTIAEEHVEEEISTA 547
                         170       180
                  ....*....|....*....|..
gi 755515061 1260 QEYVEK---ETQEKKRLSRTNE 1278
Cdd:PTZ00341  548 EEHIEEpasDVQQDSEAAPTIE 569
PHA03247 PHA03247
large tegument protein UL36; Provisional
516-974 2.92e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  516 STPAPLLHPETTVNSSHHPTPPG--SSSQELGvfSGDTGSPSVASPPTdggqvlnTSPKVPDRTTcssgipkPPTHPKDT 593
Cdd:PHA03247 2513 SRLAPAILPDEPVGEPVHPRMLTwiRGLEELA--SDDAGDPPPPLPPA-------APPAAPDRSV-------PPPRPAPR 2576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  594 PSSQEAREKletekmeeraEAKPILMPKPkhVRPKIITYIRRNPQALSQgdaslvPVGLPYAPPTCGMPLPQEEKAASRD 673
Cdd:PHA03247 2577 PSEPAVTSR----------ARRPDAPPQS--ARPRAPVDDRGDPRGPAP------PSPLPPDTHAPDPPPPSPSPAANEP 2638
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  674 LQPSAnmyeKLKPDLQKPRVFPSGLMVS-------------------GIKPPAHHFSQMSEKFLQEVADHPGKEEFCSPP 734
Cdd:PHA03247 2639 DPHPP----PTVPPPERPRDDPAPGRVSrprrarrlgraaqassppqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  735 YTHYEVPPTFYRSAMLLKPQLGLGAMSRlPSTKSRILIASQRSSASaihPPGSLTTAASFYGSDPSDLKKASNSNAAKAS 814
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPAR---PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  815 LPKSGLRPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSVQPEQSRPVTRSTFGNEEQAPLKQALPSKD-TPKGAGRA 893
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRS 2870
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  894 APASSSNATTPRRSLLPAPK-STSTPAGAKKELQKDPEaKKPAVSSPKRTASAATKPHSPGYPKQRTSAPRNEFPPKPDL 972
Cdd:PHA03247 2871 PAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERP-PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949

                  ..
gi 755515061  973 QA 974
Cdd:PHA03247 2950 AG 2951
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
553-1060 1.73e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   553 SPSVASPPTDGG--------QVLNTSPKVpdrTTCSSGIPKPPTHPKDTPSSqearekLETEKMEERAEAKPIlMPKPKH 624
Cdd:pfam03154  145 SPSIPSPQDNESdsdssaqqQILQTQPPV---LQAQSGAASPPSPPPPGTTQ------AATAGPTPSAPSVPP-QGSPAT 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   625 VRPKIITYIRRNPQALSQGDASLVPVGLPYA-PPTCGMPLPQEEKAASRDLQPSANMYEKLKPDLQKPRVFPSGLMVSGI 703
Cdd:pfam03154  215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPhPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVP 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   704 KPPAHHFSQMSEKFL----QEVADHPGKEEFCSPPYTHYEVPPTFYRSAMLLKPQLGLGAMSRLPSTKSRILIASQrssa 779
Cdd:pfam03154  295 PQPFPLTPQSSQSQVppgpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQ---- 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   780 SAIHPPgslttaasfYGSDPSDLKKASNSNAAKASLPKSGL---RPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSV 856
Cdd:pfam03154  371 SHKHPP---------HLSGPSPFQMNSNLPPPPALKPLSSLsthHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLP 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   857 QPEQSRPVTRSTFGNEEQAPLKQA--LPSKDTPKGAGRAAPASSSNATTPRRSLLPAPKSTSTPagakkeLQKDPEAKKP 934
Cdd:pfam03154  442 PPAASHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP------VPAAVSCPLP 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   935 AVSSPKRTASAATKPHSPGyPKQRTSAPRNEFPPKPDLQAREAerqlaqrlrdrcewqarqlglarRELKKAIQGFDALA 1014
Cdd:pfam03154  516 PVQIKEEALDEAEEPESPP-PPPRSPSPEPTVVNTPSHASQSA-----------------------RFYKHLDRGYNSCA 571
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 755515061  1015 VSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKCEKLQKEKE 1060
Cdd:pfam03154  572 RTDLYFMPLAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKE 617
PHA03247 PHA03247
large tegument protein UL36; Provisional
309-677 1.94e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  309 PRNEEGLTSAQAQGPGCHEERSMSPVERQELLEKAYREATSQGNSSHRQlGVRRGSSLEEMTGVSAGVEGSQQATPTLSA 388
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ-RPRRRAARPTVGSLTSLADPPPPPPTPEPA 2711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  389 APAGEAGTRL-TGKMSAGVGRMARETASGQTAPDVGQAAPVRRDPTESVPSEvsgeerrlgSGNSGSTKllASGPSAGGS 467
Cdd:PHA03247 2712 PHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---------AGPPAPAP--PAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  468 RTDTSGLLSPRGSNLEARKGKEMVAEnrnllenAAQTDNTPAGVDSAFSTPAPLLHPETTVNSSHHPTPPGSSSQELGVF 547
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPAD-------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  548 SG-DTGSPSVASPPTDGGQVLNTSPKVPDRTTCSSGIPKPPTHPKDTPSSQEAREKLETEKMEERAEAKPILMPKPKhvr 626
Cdd:PHA03247 2854 GSvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ--- 2930
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755515061  627 PKIITYIRRNPQALSQGDASLVPVGLPYAPPTCGMPLPQEEKAASRDLQPS 677
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQ 2981
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1097-1234 3.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.22e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   1097 ARLQAEhqdqllRM----RCQHQEQVEDITASHeAALLEMENNHTVAITILQDDHDHKVQELMST--HEFEK-KELEENF 1169
Cdd:smart00787  126 ARLEAK------KMwyewRMKLLEGLKEGLDEN-LEGLKEDYKLLMKELELLNSIKPKLRDRKDAleEELRQlKQLEDEL 198
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   1170 ------------EKLRLTL-QIALAPYQH--LEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKN--------IILEE 1226
Cdd:smart00787  199 edcdpteldrakEKLKKLLqEIMIKVKKLeeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKE 278

                    ....*...
gi 755515061   1227 RIQVLQQQ 1234
Cdd:smart00787  279 QLKLLQSL 286
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
1200-1277 9.66e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.77  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1200 KNQQIHLQEKKIIELEKLV----EKNIILEERIQVLQQQNEDLKARID----QNTVVT---RQLSEENANL-QEYVEKET 1267
Cdd:cd22887     2 LESELQELEKRLAELEAELasleEEIKDLEEELKEKNKANEILNDELIalqiENNLLEeklRKLQEENDELvERWMAKKQ 81
                          90
                  ....*....|
gi 755515061 1268 QEKKRLSRTN 1277
Cdd:cd22887    82 QEADKMNEAN 91
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
973-1280 1.96e-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: 58.91  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   973 QAREAERQLaQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKC 1052
Cdd:TIGR02168  692 KIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1053 EKLQKEKETLERRFEEELRRLgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRcQHQEQVEDITASHEAALLEM 1132
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1133 ENNhtvaitilqddhdhKVQELMSTHEFEkkELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKII 1212
Cdd:TIGR02168  848 EEL--------------SEDIESLAAEIE--ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061  1213 ELE----KLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK-KRLSRTNEEL 1280
Cdd:TIGR02168  912 ELRreleELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
975-1288 2.49e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  975 REAERQLAQ------RLRDRCEWQARQLG-LAR--------RELKKAIQGFDAlavstkhffgksERALAKEKELSIELA 1039
Cdd:COG1196   175 EEAERKLEAteenleRLEDILGELERQLEpLERqaekaeryRELKEELKELEA------------ELLLLKLRELEAELE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1040 NIRDEVAFNTAKCEKLQKEKETLERRFEEELRrlgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRCQHQEQVE 1119
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1120 DITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEM 1199
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1200 KNQQIHLQEkkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRLSRTNEE 1279
Cdd:COG1196   399 AAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE--EEEALLELLAELLEEA 472

                  ....*....
gi 755515061 1280 LLWKLQTGD 1288
Cdd:COG1196   473 ALLEAALAE 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
975-1280 2.07e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 2.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   975 REAERQLA------QRLRDrcewqarqlglARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSI--------ELAN 1040
Cdd:TIGR02168  175 KETERKLErtrenlDRLED-----------ILNELERQLKSLERQAEKAERYKELKAELRELELALLVlrleelreELEE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1041 IRDEVAFNTAKCEKLQKEKETLERRFEEELRrlgwqQQAEVQELQERLQQQFQAESARLQA-EHQDQLLRMRcqhQEQVE 1119
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRL-----EVSELEEEIEELQKELYALANEISRlEQQKQILRER---LANLE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1120 DITASHEAALLEMENNHTVAITILqddhdHKVQELMSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEM 1199
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1200 KNQQIHLQEKKIIELEKLVEkniILEERIQVLQQQNEDLKARIDQNTV--VTRQLSEENANLQEYVEKETQEKKRLSRTN 1277
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELR 467

                   ...
gi 755515061  1278 EEL 1280
Cdd:TIGR02168  468 EEL 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1155-1280 5.21e-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: 5.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1155 MSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQ 1234
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKE 755
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 755515061  1235 NEDLKARIdqnTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1280
Cdd:TIGR02168  756 LTELEAEI---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1022-1285 6.12e-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: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1022 GKSERALAKEKELSIELANIRDEVAFNTAKCEKLQKE-KETLERRFEEELRRLGWQQQAEvqeLQERLQQQFQAESARLQ 1100
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLE 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1101 AEHQdQLLRMRCQHQEQVEDITASHEAALLEMENNHTVAITILQddhdhKVQELmsthEFEKKELEENFEKLRLTLQIAL 1180
Cdd:TIGR02168  740 AEVE-QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEEL----EAQIEQLKEELKALREALDELR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1181 APYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKN----IILEERIQVLQQQNEDLKARIDQNTVVTRQLSEEN 1256
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsediESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          250       260
                   ....*....|....*....|....*....
gi 755515061  1257 ANLQEYVEKETQEKKRLSRTNEELLWKLQ 1285
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELE 918
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1093-1283 3.72e-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: 51.65  E-value: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1093 QAESARLQ-----AEHQDQLLRMRCQHQEQVEDITASHEAALLEM--ENNHTVAITILQDDHDHKVQELMSTHEFEKKEL 1165
Cdd:pfam05483  205 QAENARLEmhfklKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQIteKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1166 EENFEK----------LRLTLQIALAPYQHLEEDMQ----SLKQVLEMKNQQIHLQEKK-------IIELEKLVeknIIL 1224
Cdd:pfam05483  285 KELIEKkdhltkeledIKMSLQRSMSTQKALEEDLQiatkTICQLTEEKEAQMEELNKAkaahsfvVTEFEATT---CSL 361
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755515061  1225 EERIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELLWK 1283
Cdd:pfam05483  362 EELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLLDE 423
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1022-1286 2.25e-05

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: 49.20  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1022 GKSERALAKEKElsiELANIRDEVA---FNTAKCEKLQKEKETLERRFEEELRRLGWQQQAEVQELQERLQQQFQAESAR 1098
Cdd:pfam02463  142 GKIEIIAMMKPE---RRLEIEEEAAgsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1099 LQAEHQDQLLRMRCQHQEQVED----ITASHEAALLEMENNHTVAITILQDDH-----DHKVQELM----STHEFEKKEL 1165
Cdd:pfam02463  219 LELEEEYLLYLDYLKLNEERIDllqeLLRDEQEEIESSKQEIEKEEEKLAQVLkenkeEEKEKKLQeeelKLLAKEEEEL 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1166 EENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKNiiLEERIQVLQQQNEDLKARIDQN 1245
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE--EEEEEELEKLQEKLEQLEEELL 376
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 755515061  1246 TVVTRQ---------LSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1286
Cdd:pfam02463  377 AKKKLEserlssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1022-1280 2.38e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1022 GKSERALAKEKELSIELANIRDEVA-FNTAKCEKLQKEKETLERRFEEELRRLGWQQQAEVQELQERLQQQFQAESARLQ 1100
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRrIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1101 AEHQDQLLRMRCQHQEQVEDITASHEA-ALLEMENNHTVAITIlqDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIA 1179
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1180 LAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQntvVTRQLSEENANL 1259
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE---LEAALRDLESRLGDLKKERDE---LEAQLRELERKI 905
                          250       260
                   ....*....|....*....|.
gi 755515061  1260 QEYVEKETQEKKRLSRTNEEL 1280
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKL 926
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1143-1280 2.70e-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: 48.48  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1143 LQDDHDHKVQELMSThefEKKELEENFEKLR-LTLQIALAPYQ--HLEEDMQSLKQV---LEMKNQQIHLQ-EKKIIELE 1215
Cdd:TIGR04523  297 ISDLNNQKEQDWNKE---LKSELKNQEKKLEeIQNQISQNNKIisQLNEQISQLKKEltnSESENSEKQRElEEKQNEIE 373
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755515061  1216 KLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1280
Cdd:TIGR04523  374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
1120-1259 4.52e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1120 DITASHEAALLEMEN--NHTVA-----ITILQDD-HDHKVQE-----LMSTHEFEKKELEE-----------------NF 1169
Cdd:pfam13851    1 ELMKNHEKAFNEIKNyyNDITRnnlelIKSLKEEiAELKKKEernekLMSEIQQENKRLTEplqkaqeeveelrkqleNY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1170 EKLRLTLQIALAPYQHLEEDMQSLK---QVLEMKNQQIHL--------QEKKIIEL-EKLVEKNIILEERIQVLQqqnED 1237
Cdd:pfam13851   81 EKDKQSLKNLKARLKVLEKELKDLKwehEVLEQRFEKVERerdelydkFEAAIQDVqQKTGLKNLLLEKKLQALG---ET 157
                          170       180
                   ....*....|....*....|....
gi 755515061  1238 LKARidqntvvTRQLSE--ENANL 1259
Cdd:pfam13851  158 LEKK-------EAQLNEvlAAANL 174
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1101-1278 1.91e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1101 AEHQDQLLRMRCQHQEQVEDITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIA- 1179
Cdd:PTZ00341  408 ALYTDEDLLFDLEKQKYMDMLDGSEDESVEDNEEEHSGDANEEELSVDEHVEEHNADDSGEQQSDDESGEHQSVNEIVEe 487
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1180 LAPYQHLEEdmQSLKQVLEMKNQQIHLQEKKIIELEklvekniileeriqvlQQQNEDlkARIDQNTVVTRQLSEENANL 1259
Cdd:PTZ00341  488 QSVNEHVEE--PTVADIVEQETVDEHVEEPAVDENE----------------EQQTAD--EHVEEPTIAEEHVEEEISTA 547
                         170       180
                  ....*....|....*....|..
gi 755515061 1260 QEYVEK---ETQEKKRLSRTNE 1278
Cdd:PTZ00341  548 EEHIEEpasDVQQDSEAAPTIE 569
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
975-1251 2.37e-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: 45.48  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   975 REAERQLAQ---------RLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALakeKELSIELANIRDEV 1045
Cdd:pfam05483  527 KQEERMLKQienleekemNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQI 603
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1046 AFNTAKCEKLQKEKETLERRFEEElrrlgwQQQAEVQELQERLQQqFQAESARLQAEHqdqllrMRCQHQEQVEDITASH 1125
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGSAE------NKQLNAYEIKVNKLE-LELASAKQKFEE------IIDNYQKEIEDKKISE 670
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1126 EAALLEMENNHTVA--ITILQDDHD----HKVQELMSTHEFEKKELEENFEKLRLTLQIalapYQHLEEDMQSLKQVLEm 1199
Cdd:pfam05483  671 EKLLEEVEKAKAIAdeAVKLQKEIDkrcqHKIAEMVALMEKHKHQYDKIIEERDSELGL----YKNKEQEQSSAKAALE- 745
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755515061  1200 knqqihlqekkiIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQ 1251
Cdd:pfam05483  746 ------------IELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1150-1280 2.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1150 KVQELMSTHEfEKKELEENFEKLR---LTLQIALAPYQHLEEdMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKNIILEE 1226
Cdd:COG4717    93 LQEELEELEE-ELEELEAELEELReelEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEA 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755515061 1227 RIQVLQQQNEDLKARIDQNTVVT-RQLSEENANLQEYVEKETQEKKRLSRTNEEL 1280
Cdd:COG4717   171 ELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEEL 225
PHA03247 PHA03247
large tegument protein UL36; Provisional
516-974 2.92e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  516 STPAPLLHPETTVNSSHHPTPPG--SSSQELGvfSGDTGSPSVASPPTdggqvlnTSPKVPDRTTcssgipkPPTHPKDT 593
Cdd:PHA03247 2513 SRLAPAILPDEPVGEPVHPRMLTwiRGLEELA--SDDAGDPPPPLPPA-------APPAAPDRSV-------PPPRPAPR 2576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  594 PSSQEAREKletekmeeraEAKPILMPKPkhVRPKIITYIRRNPQALSQgdaslvPVGLPYAPPTCGMPLPQEEKAASRD 673
Cdd:PHA03247 2577 PSEPAVTSR----------ARRPDAPPQS--ARPRAPVDDRGDPRGPAP------PSPLPPDTHAPDPPPPSPSPAANEP 2638
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  674 LQPSAnmyeKLKPDLQKPRVFPSGLMVS-------------------GIKPPAHHFSQMSEKFLQEVADHPGKEEFCSPP 734
Cdd:PHA03247 2639 DPHPP----PTVPPPERPRDDPAPGRVSrprrarrlgraaqassppqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  735 YTHYEVPPTFYRSAMLLKPQLGLGAMSRlPSTKSRILIASQRSSASaihPPGSLTTAASFYGSDPSDLKKASNSNAAKAS 814
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPAR---PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  815 LPKSGLRPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSVQPEQSRPVTRSTFGNEEQAPLKQALPSKD-TPKGAGRA 893
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRS 2870
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  894 APASSSNATTPRRSLLPAPK-STSTPAGAKKELQKDPEaKKPAVSSPKRTASAATKPHSPGYPKQRTSAPRNEFPPKPDL 972
Cdd:PHA03247 2871 PAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERP-PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949

                  ..
gi 755515061  973 QA 974
Cdd:PHA03247 2950 AG 2951
PRK11281 PRK11281
mechanosensitive channel MscK;
1190-1277 3.08e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1190 MQSLKQV-LEMKNQQIHLQEKKIIELEKLV-EKNIILEERiQVLQQQNEDLKARIDQNTVVTRQLsEENANLQEYVEKET 1267
Cdd:PRK11281  221 LQDLLQKqRDYLTARIQRLEHQLQLLQEAInSKRLTLSEK-TVQEAQSQDEAARIQANPLVAQEL-EINLQLSQRLLKAT 298
                          90
                  ....*....|
gi 755515061 1268 QEKKRLSRTN 1277
Cdd:PRK11281  299 EKLNTLTQQN 308
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1158-1286 3.83e-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: 45.01  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1158 HEFEKKELEENFEKLRLTLQIALAPYQHLEedMQSLKQVLEMKNQQIHLQEKKIIELEKlveKNIILEERIQVLQQQNED 1237
Cdd:TIGR04523  169 EELENELNLLEKEKLNIQKNIDKIKNKLLK--LELLLSNLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINE 243
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 755515061  1238 LKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1286
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1118-1275 4.03e-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: 44.78  E-value: 4.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1118 VEDITASHEAALLEMENNHTVAITILQDDHDH---------------------------KVQELMSTHEFEKKELEENFE 1170
Cdd:pfam01576  336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrnkanlekakqalesenaelqaelrTLQQAKQDSEHKRKKLEGQLQ 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1171 KLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQ-NEDLKARIDQNTVVt 1249
Cdd:pfam01576  416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS---LESQLQDTQELlQEETRQKLNLSTRL- 491
                          170       180
                   ....*....|....*....|....*.
gi 755515061  1250 RQLSEENANLQEYVEKETQEKKRLSR 1275
Cdd:pfam01576  492 RQLEDERNSLQEQLEEEEEAKRNVER 517
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
1116-1270 4.97e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1116 EQVEDITASHEAALLEMEN----NHTVAITILQDDHDHkVQELMsTHEFE-KKELEENFEKLRLTLqialapyQHLEEDM 1190
Cdd:PRK04778  256 KEIQDLKEQIDENLALLEEldldEAEEKNEEIQERIDQ-LYDIL-EREVKaRKYVEKNSDTLPDFL-------EHAKEQN 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1191 QSLKQVLEMKNQQIHLQEKkiiELEKlVEKniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE--KETQ 1268
Cdd:PRK04778  327 KELKEEIDRVKQSYTLNES---ELES-VRQ---LEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQ 399

                  ..
gi 755515061 1269 EK 1270
Cdd:PRK04778  400 EK 401
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1113-1281 5.15e-04

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: 44.35  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1113 QHQEQVEDITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELE------ENFEKLRLTLQIALAPYQHL 1186
Cdd:pfam05557   13 QLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEaeealrEQAELNRLKKKYLEALNKKL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1187 EEDMQSLKQVLEMK---------------NQQIHLQEkKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQ 1251
Cdd:pfam05557   93 NEKESQLADAREVIsclknelselrrqiqRAELELQS-TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171
                          170       180       190
                   ....*....|....*....|....*....|
gi 755515061  1252 LSEenanLQEYVEKETQEKKRLSRTNEELL 1281
Cdd:pfam05557  172 IKE----LEFEIQSQEQDSEIVKNSKSELA 197
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
972-1288 5.30e-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: 44.33  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   972 LQAREAERQ------LAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELanirdEV 1045
Cdd:pfam05483  247 IQITEKENKmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL-----QI 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1046 AfnTAKCEKLQKEKETLERRFEEELRRLGWQQqAEVQELQERLQQQFQAESARLQA-EHQDQLLRMRCQHQ----EQVED 1120
Cdd:pfam05483  322 A--TKTICQLTEEKEAQMEELNKAKAAHSFVV-TEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKsselEEMTK 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1121 ITASHEAALLEMEnnhtvaiTILQDDhdhkvQELMstheFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLK-QVLEM 1199
Cdd:pfam05483  399 FKNNKEVELEELK-------KILAED-----EKLL----DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiQLTAI 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1200 K-NQQIHLQEKKII--ELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENAN-----------LQEYVEK 1265
Cdd:pfam05483  463 KtSEEHYLKEVEDLktELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINckkqeermlkqIENLEEK 542
                          330       340
                   ....*....|....*....|...
gi 755515061  1266 ETQEKKRLSRTNEELlwkLQTGD 1288
Cdd:pfam05483  543 EMNLRDELESVREEF---IQKGD 562
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
971-1273 7.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  971 DLQAREAERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDAlavstkhffgKSERALAKEKELSIELANIRDEVAFNTA 1050
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL----------ELEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1051 KCEKLQKEKETLERRFEEELRrlgwQQQAEVQelqerlqqqfQAESARLQAEHQDQLLRMRCQHQEQVEDITASHEAALL 1130
Cdd:COG1196   310 RRRELEERLEELEEELAELEE----ELEELEE----------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1131 EmennhtvaitiLQDDHDHKVQElmsthEFEKKELEENFEKLRLTLQIALapyQHLEEDMQSLKQVLEMKNQQIHLQEKK 1210
Cdd:COG1196   376 E-----------AEEELEELAEE-----LLEALRAAAELAAQLEELEEAE---EALLERLERLEEELEELEEALAELEEE 436
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061 1211 IIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRL 1273
Cdd:COG1196   437 EEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
1214-1285 7.72e-04

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 39.17  E-value: 7.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755515061  1214 LEKLVEKNIILEERIQVLQQQNEDLKARidqntvvTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1285
Cdd:pfam06005    6 LEQLETKIQAAVDTIALLQMENEELKEE-------NEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
977-1281 8.15e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 8.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   977 AERQLAQRLRDRCEWQARQLGLA---RRELKKAI-QGFDALAVSTK---------HFFGKSERALAKE--------KELS 1035
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLqseLRRIENRLdELSQELSDASRkigeiekeiEQLEQEEEKLKERleeleedlSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1036 IELANIRDEVAFNTAKCEKLQKEKETLERRFEEELRRLGWQQQAEVqelqerlqqqfQAESARLQAEHQDqlLRMRCQHQ 1115
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI-----------QAELSKLEEEVSR--IEARLREI 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1116 EQveDITASH-EAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLK 1194
Cdd:TIGR02169  818 EQ--KLNRLTlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1195 QvlEMKNQQIHLQEKKiIELEKLVEKNIILEERIQVLQQQN--------------------EDLKARIDQNTVVTRQLSE 1254
Cdd:TIGR02169  896 A--QLRELERKIEELE-AQIEKKRKRLSELKAKLEALEEELseiedpkgedeeipeeelslEDVQAELQRVEEEIRALEP 972
                          330       340       350
                   ....*....|....*....|....*....|....
gi 755515061  1255 EN-ANLQEYVE-----KETQEKK-RLSRTNEELL 1281
Cdd:TIGR02169  973 VNmLAIQEYEEvlkrlDELKEKRaKLEEERKAIL 1006
PHA03247 PHA03247
large tegument protein UL36; Provisional
625-977 8.86e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  625 VRPKIITYIRrNPQALSQGDAS-----LVPVGLPYA-----PPTCGMPLPQEEKAASRDLQPSAnmyeklKPDLQKPRVf 694
Cdd:PHA03247 2529 VHPRMLTWIR-GLEELASDDAGdppppLPPAAPPAApdrsvPPPRPAPRPSEPAVTSRARRPDA------PPQSARPRA- 2600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  695 PSGLMVSGIKPPAHHfsqmsekflqevadhpgkeefCSPPYTHYEVPPTFYRSAMLLKPQLGlGAMSRLPSTKSRILIAS 774
Cdd:PHA03247 2601 PVDDRGDPRGPAPPS---------------------PLPPDTHAPDPPPPSPSPAANEPDPH-PPPTVPPPERPRDDPAP 2658
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  775 QRSSASAihppgslttaasfygsdpsdlKKASNSNAAKASLPKSGLRPPGySRLPAAKLAAFGFVRSSSISAVPSSQSLD 854
Cdd:PHA03247 2659 GRVSRPR---------------------RARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPEPAPHALV 2716
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  855 SVQPeqSRPVTRSTFGNEEQAPLKQ---------ALPSKDTPKG-----AGRAAPASSSN-ATTPRRSLLPAPKSTSTPA 919
Cdd:PHA03247 2717 SATP--LPPGPAAARQASPALPAAPappavpagpATPGGPARPArppttAGPPAPAPPAApAAGPPRRLTRPAVASLSES 2794
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755515061  920 GAKKELQKDPEAKKPAVSSPKRTASAATKPhSPGYPKQRTSAPRNEFPPKPDLQAREA 977
Cdd:PHA03247 2795 RESLPSPWDPADPPAAVLAPAAALPPAASP-AGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
1102-1285 9.03e-04

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 42.34  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1102 EHQDQLLRMRCQHQEQVEDITASHEAALLEMENNHTVAItilqdDHDHKVQELMST---HEFEKKELEENFE--KLRLTL 1176
Cdd:pfam15665   11 EHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEEL-----DLKRRIQTLEESleqHERMKRQALTEFEqyKRRVEE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1177 QIALAPYQHLEEDMQSLKQVLEMKN---QQIHLQEKKIIELEKlvEKNIILEERIQVLQQQNEDL--KARIDQNTVVTRQ 1251
Cdd:pfam15665   86 RELKAEAEHRQRVVELSREVEEAKRafeEKLESFEQLQAQFEQ--EKRKALEELRAKHRQEIQELltTQRAQSASSLAEQ 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 755515061  1252 LSEENA------NLQEYVEKETQEKKRLSRTNEELLWKLQ 1285
Cdd:pfam15665  164 EKLEELhkaeleSLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
1175-1285 9.22e-04

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 41.06  E-value: 9.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1175 TLQIALAPYQHLEEDMQSLKQvlemKNQQIHLQEKKIIELEKLVEKNIILEEriQVLQQQNEDLKARIDQNTVVTRQLSE 1254
Cdd:pfam09744   37 LLESLASRNQEHNVELEELRE----DNEQLETQYEREKALRKRAEEELEEIE--DQWEQETKDLLSQVESLEEENRRLEA 110
                           90       100       110
                   ....*....|....*....|....*....|....
gi 755515061  1255 ENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 1285
Cdd:pfam09744  111 DHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
997-1285 9.81e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   997 GLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVafntakcEKLQKEKETL---ERRFEEELRRL 1073
Cdd:TIGR02169  152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-------ERLRREREKAeryQALLKEKREYE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1074 GWQQQAEVQELqerlqqqfQAESARLQAEHQDQllrmrcqhQEQVEDITASHEAALLEMEnnhtvAITILQDDHDHKVQE 1153
Cdd:TIGR02169  225 GYELLKEKEAL--------ERQKEAIERQLASL--------EEELEKLTEEISELEKRLE-----EIEQLLEELNKKIKD 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1154 LMSTHEFE-KKELEE---NFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQ 1229
Cdd:TIGR02169  284 LGEEEQLRvKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---LTEEYA 360
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755515061  1230 VLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1285
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1093-1262 1.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1093 QAESARLQAEHQDQLLRmrcQHQEQVEDITASHEAALLEMENnhtvaITILQDDHDHKVQELMSTHEFE--KKELEENFE 1170
Cdd:COG4717    75 ELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAELEE-----LREELEKLEKLLQLLPLYQELEalEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1171 KLRlTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKK------------IIELEKLVEKNIILEERIQVLQQQNEDL 1238
Cdd:COG4717   147 RLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQRLAELEEELEEAQEELEEL 225
                         170       180
                  ....*....|....*....|....
gi 755515061 1239 KARIDQnTVVTRQLSEENANLQEY 1262
Cdd:COG4717   226 EEELEQ-LENELEAAALEERLKEA 248
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1161-1277 1.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1161 EKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKII-----------ELEKLVEKNIILEERIQ 1229
Cdd:COG4372    53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELEslqeeaeelqeELEELQKERQDLEQQRK 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755515061 1230 VLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1277
Cdd:COG4372   133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
553-1060 1.73e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   553 SPSVASPPTDGG--------QVLNTSPKVpdrTTCSSGIPKPPTHPKDTPSSqearekLETEKMEERAEAKPIlMPKPKH 624
Cdd:pfam03154  145 SPSIPSPQDNESdsdssaqqQILQTQPPV---LQAQSGAASPPSPPPPGTTQ------AATAGPTPSAPSVPP-QGSPAT 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   625 VRPKIITYIRRNPQALSQGDASLVPVGLPYA-PPTCGMPLPQEEKAASRDLQPSANMYEKLKPDLQKPRVFPSGLMVSGI 703
Cdd:pfam03154  215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPhPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVP 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   704 KPPAHHFSQMSEKFL----QEVADHPGKEEFCSPPYTHYEVPPTFYRSAMLLKPQLGLGAMSRLPSTKSRILIASQrssa 779
Cdd:pfam03154  295 PQPFPLTPQSSQSQVppgpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQ---- 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   780 SAIHPPgslttaasfYGSDPSDLKKASNSNAAKASLPKSGL---RPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSV 856
Cdd:pfam03154  371 SHKHPP---------HLSGPSPFQMNSNLPPPPALKPLSSLsthHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLP 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   857 QPEQSRPVTRSTFGNEEQAPLKQA--LPSKDTPKGAGRAAPASSSNATTPRRSLLPAPKSTSTPagakkeLQKDPEAKKP 934
Cdd:pfam03154  442 PPAASHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP------VPAAVSCPLP 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   935 AVSSPKRTASAATKPHSPGyPKQRTSAPRNEFPPKPDLQAREAerqlaqrlrdrcewqarqlglarRELKKAIQGFDALA 1014
Cdd:pfam03154  516 PVQIKEEALDEAEEPESPP-PPPRSPSPEPTVVNTPSHASQSA-----------------------RFYKHLDRGYNSCA 571
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 755515061  1015 VSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKCEKLQKEKE 1060
Cdd:pfam03154  572 RTDLYFMPLAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKE 617
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1105-1280 1.81e-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: 42.70  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1105 DQLLRMRCQHQEQVEDITASHEAALLEMENNhtvaitilQDDHDHKVQELMSTHEfEKKELEENF--------------- 1169
Cdd:TIGR04523  457 KNLDNTRESLETQLKVLSRSINKIKQNLEQK--------QKELKSKEKELKKLNE-EKKELEEKVkdltkkisslkekie 527
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1170 ----EKLRLTLQIAlapyqHLEEDMQSLKQVLEMKNQQIHLQE--KKIIEL----EKLVEKNIILEERIQVLQQQNEDLK 1239
Cdd:TIGR04523  528 klesEKKEKESKIS-----DLEDELNKDDFELKKENLEKEIDEknKEIEELkqtqKSLKKKQEEKQELIDQKEKEKKDLI 602
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 755515061  1240 ARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1280
Cdd:TIGR04523  603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1161-1281 1.84e-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: 42.70  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1161 EKKELEENFEKLR---LTLQIALAPYQHLEEDMQSL-KQVLEMKNQQIHLQEKKIIELEKLVEKNIILEERiqvlQQQNE 1236
Cdd:TIGR04523  181 EKLNIQKNIDKIKnklLKLELLLSNLKKKIQKNKSLeSQISELKKQNNQLKDNIEKKQQEINEKTTEISNT----QTQLN 256
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755515061  1237 DLKariDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELL 1281
Cdd:TIGR04523  257 QLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
973-1195 1.85e-03

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: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  973 QAREAERQLAQrLRdrcewQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEkelsiELANIRDEVAFNTAKC 1052
Cdd:COG4913   243 ALEDAREQIEL-LE-----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELRAELARLEAEL 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1053 EKLQKEKETLERRFEEElrrlgwqqQAEVQELQERLQQQFQAESARLQAEhQDQLLRMRCQHQEQVEDITASHEAALLEM 1132
Cdd:COG4913   312 ERLEARLDALREELDEL--------EAQIRGNGGDRLEQLEREIERLERE-LEERERRRARLEALLAALGLPLPASAEEF 382
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061 1133 ENNHtvaitilqddhdHKVQELMSTHEFEKKELEENFEKLRLTLQIALAPYQHLEEDMQSLKQ 1195
Cdd:COG4913   383 AALR------------AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1103-1280 1.91e-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: 42.85  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1103 HQDQLLRMRCQHQEQVEDITASHEAA------------LLEMENNHTVA-ITILQD---DHDHK-------VQELMSTH- 1158
Cdd:pfam01576  343 HEAQLQEMRQKHTQALEELTEQLEQAkrnkanlekakqALESENAELQAeLRTLQQakqDSEHKrkklegqLQELQARLs 422
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1159 --EFEKKELEENFEKLRLTLQIALAPYQHLE-----------------EDMQSLKQ------------VLEMKNQQIHLQ 1207
Cdd:pfam01576  423 esERQRAELAEKLSKLQSELESVSSLLNEAEgkniklskdvsslesqlQDTQELLQeetrqklnlstrLRQLEDERNSLQ 502
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1208 EkkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKKRLSRTNEEL 1280
Cdd:pfam01576  503 E----QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYDKLEKTKNRL 578
PHA03247 PHA03247
large tegument protein UL36; Provisional
309-677 1.94e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  309 PRNEEGLTSAQAQGPGCHEERSMSPVERQELLEKAYREATSQGNSSHRQlGVRRGSSLEEMTGVSAGVEGSQQATPTLSA 388
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ-RPRRRAARPTVGSLTSLADPPPPPPTPEPA 2711
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  389 APAGEAGTRL-TGKMSAGVGRMARETASGQTAPDVGQAAPVRRDPTESVPSEvsgeerrlgSGNSGSTKllASGPSAGGS 467
Cdd:PHA03247 2712 PHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---------AGPPAPAP--PAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  468 RTDTSGLLSPRGSNLEARKGKEMVAEnrnllenAAQTDNTPAGVDSAFSTPAPLLHPETTVNSSHHPTPPGSSSQELGVF 547
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPAD-------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  548 SG-DTGSPSVASPPTDGGQVLNTSPKVPDRTTCSSGIPKPPTHPKDTPSSQEAREKLETEKMEERAEAKPILMPKPKhvr 626
Cdd:PHA03247 2854 GSvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ--- 2930
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755515061  627 PKIITYIRRNPQALSQGDASLVPVGLPYAPPTCGMPLPQEEKAASRDLQPS 677
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQ 2981
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
1115-1270 2.16e-03

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: 42.15  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1115 QEQVEDITASHEAALLEMENNHT----VAITILQDDHDHkVQELMsTHEFE-KKELEENFEKLRLTLqialapyQHLEED 1189
Cdd:pfam06160  236 DKEIQQLEEQLEENLALLENLELdeaeEALEEIEERIDQ-LYDLL-EKEVDaKKYVEKNLPEIEDYL-------EHAEEQ 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1190 MQSLKQVLEMKNQQIHLQEKkiiELEKLVEkniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE--KET 1267
Cdd:pfam06160  307 NKELKEELERVQQSYTLNEN---ELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEeiEEE 379

                   ...
gi 755515061  1268 QEK 1270
Cdd:pfam06160  380 QEE 382
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1097-1234 3.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.22e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   1097 ARLQAEhqdqllRM----RCQHQEQVEDITASHeAALLEMENNHTVAITILQDDHDHKVQELMST--HEFEK-KELEENF 1169
Cdd:smart00787  126 ARLEAK------KMwyewRMKLLEGLKEGLDEN-LEGLKEDYKLLMKELELLNSIKPKLRDRKDAleEELRQlKQLEDEL 198
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   1170 ------------EKLRLTL-QIALAPYQH--LEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKN--------IILEE 1226
Cdd:smart00787  199 edcdpteldrakEKLKKLLqEIMIKVKKLeeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeiEKLKE 278

                    ....*...
gi 755515061   1227 RIQVLQQQ 1234
Cdd:smart00787  279 QLKLLQSL 286
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
1092-1280 3.37e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1092 FQAESARlqaehQDqlLRMRCQHQE--------QVEDIT-ASHEAALLEMEnnhtvaITILQDDHDhKVQELMSTHEFEK 1162
Cdd:pfam05622   76 FRLETAR-----DD--YRIKCEELEkevlelqhRNEELTsLAEEAQALKDE------MDILRESSD-KVKKLEATVETYK 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1163 KELEenfeklrltlqialapyqhleeDMQSLK-QV--LEMKNQqIHLQEKkiIELEKLVEKNIILEERIQVLQQQNEDLK 1239
Cdd:pfam05622  142 KKLE----------------------DLGDLRrQVklLEERNA-EYMQRT--LQLEEELKKANALRGQLETYKRQVQELH 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 755515061  1240 ARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLS-------RTNEEL 1280
Cdd:pfam05622  197 GKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIierdtlrETNEEL 244
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
1170-1272 4.33e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.82  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1170 EKLRLTLQIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNTVVT 1249
Cdd:pfam12718    3 NSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEK---LEEQLKEAKEKAEESEKLKTNNENLT 79
                           90       100
                   ....*....|....*....|....*
gi 755515061  1250 R--QLSEENANLQEYVEKETQEKKR 1272
Cdd:pfam12718   80 RkiQLLEEELEESDKRLKETTEKLR 104
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
1001-1278 4.64e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 40.71  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1001 RELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRdevafntAKCEKLQKEKEtlerrfeeelrrlgwQQQAE 1080
Cdd:pfam09728    4 RELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLK-------KKQDQLQKEKD---------------QLQSE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1081 VQelqerlqqqfQAESAR---------LQAEH---QDQLLRMRCQHQEQVEDITASHEAALLEmennhtvaITILQDDHD 1148
Cdd:pfam09728   62 LS----------KAILAKskleklcreLQKQNkklKEESKKLAKEEEEKRKELSEKFQSTLKD--------IQDKMEEKS 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1149 HKvqelmsthefEKKELEENfEKLRLTLQIALAPYQHLEEDMQSL-------KQVLEMKNQQIHLQEKKIIElEKLVEKN 1221
Cdd:pfam09728  124 EK----------NNKLREEN-EELREKLKSLIEQYELRELHFEKLlktkeleVQLAEAKLQQATEEEEKKAQ-EKEVAKA 191
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 755515061  1222 IILEERIQVLQQQNEDLKARidqntvvtrqlseenanLQEYVEKETQEKKRLSRTNE 1278
Cdd:pfam09728  192 RELKAQVQTLSETEKELREQ-----------------LNLYVEKFEEFQDTLNKSNE 231
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
1153-1280 4.98e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1153 ELMSTHEFEK--KELEENFEKLRLTLQIALAPYQHLEED-MQSLKQVLEMKNQQIHLQEkkiiELEKLVEKNIILEERIQ 1229
Cdd:PRK04778  346 ELESVRQLEKqlESLEKQYDEITERIAEQEIAYSELQEElEEILKQLEEIEKEQEKLSE----MLQGLRKDELEAREKLE 421
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755515061 1230 VLQQQNEDLKaridqntvvtRQLseENANL----QEYVEKETQEKKRLSRTNEEL 1280
Cdd:PRK04778  422 RYRNKLHEIK----------RYL--EKSNLpglpEDYLEMFFEVSDEIEALAEEL 464
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1033-1280 6.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1033 ELSIELANIRDEVAFNTAKCEKLQKEKETlerrfeeelrrlgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRC 1112
Cdd:PRK02224  479 ELEAELEDLEEEVEEVEERLERAEDLVEA--------------EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1113 QHQEQVEDITASHEAALLEMENNHTVAITIlqDDHDHKVQELmsthefekKELEENFEKLRlTLQIALAPY-QHLEEDMQ 1191
Cdd:PRK02224  545 RAAELEAEAEEKREAAAEAEEEAEEAREEV--AELNSKLAEL--------KERIESLERIR-TLLAAIADAeDEIERLRE 613
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1192 SLKQVLEMKNQQI-HLQEK--KIIELEKLVEkniilEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ 1268
Cdd:PRK02224  614 KREALAELNDERReRLAEKreRKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
                         250
                  ....*....|..
gi 755515061 1269 EKKRLSRTNEEL 1280
Cdd:PRK02224  689 ELEELEELRERR 700
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
973-1279 7.07e-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: 40.88  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   973 QAREAERQLAQRLRDRCEWQARQLGlARRELKKAIQGFDALAVSTKHFFGKSERaLAKEKELsiELANIRDEvafntakc 1052
Cdd:pfam17380  289 QQEKFEKMEQERLRQEKEEKAREVE-RRRKLEEAEKARQAEMDRQAAIYAEQER-MAMERER--ELERIRQE-------- 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1053 eklQKEKETLERrfeeelrrlgwqQQAEVQELQERLQqqfqaESARLQAEHQDQLLRMRcqhqeqvEDITASHEAALLEM 1132
Cdd:pfam17380  357 ---ERKRELERI------------RQEEIAMEISRMR-----ELERLQMERQQKNERVR-------QELEAARKVKILEE 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1133 ENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTL-----QIALAPYQHLEEDMQSLKQVLEM---KNQQI 1204
Cdd:pfam17380  410 ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLeeqerQQQVERLRQQEEERKRKKLELEKekrDRKRA 489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1205 HLQEKKIIELEKLVEKNIILEE--RIQVLQQQNEDLKA--------RIDQNTVVTRQLSEENANLQEYVEKETQEKKRLS 1274
Cdd:pfam17380  490 EEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKaiyeeerrREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569

                   ....*
gi 755515061  1275 RTNEE 1279
Cdd:pfam17380  570 AMERE 574
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1157-1281 8.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1157 THEFEKKELEENFEKLRlTLQIALAPYQHLEEDMQSLKQVLE-MKNQQIHLQEK-----KIIELEKLVEKNIILEERIQV 1230
Cdd:COG4717    65 KPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEeLEAELEELREElekleKLLQLLPLYQELEALEAELAE 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755515061 1231 LQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELL 1281
Cdd:COG4717   144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
973-1271 9.02e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 9.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061   973 QAREAERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALA----KEKELSIEL-ANIR--DEV 1045
Cdd:pfam15921  328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKeQNKRlwDRD 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1046 AFNTAKCEKLQKEKEtlerrfeeelrrlgwQQQAEVqelqERLQQQFQAESARLQAEHQDQLLRMRCQHQ--EQVEDITA 1123
Cdd:pfam15921  408 TGNSITIDHLRRELD---------------DRNMEV----QRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTA 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061  1124 SHEAA--LLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELE---ENFEKLRLTLQIALAPYQHLEEDMQSLKQVlE 1198
Cdd:pfam15921  469 QLESTkeMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGDHLRNV-Q 547
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755515061  1199 MKNQQIHLQekkiielekLVEKNIILEeriqVLQQQNEDLKARIDQNTVVTRQLSEENANLqeyvEKETQEKK 1271
Cdd:pfam15921  548 TECEALKLQ---------MAEKDKVIE----ILRQQIENMTQLVGQHGRTAGAMQVEKAQL----EKEINDRR 603
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
1200-1277 9.66e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.77  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515061 1200 KNQQIHLQEKKIIELEKLV----EKNIILEERIQVLQQQNEDLKARID----QNTVVT---RQLSEENANL-QEYVEKET 1267
Cdd:cd22887     2 LESELQELEKRLAELEAELasleEEIKDLEEELKEKNKANEILNDELIalqiENNLLEeklRKLQEENDELvERWMAKKQ 81
                          90
                  ....*....|
gi 755515061 1268 QEKKRLSRTN 1277
Cdd:cd22887    82 QEADKMNEAN 91
 
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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