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Conserved domains on  [gi|568938795|ref|XP_006504802|]
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IQ domain-containing protein E 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

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-557 1.25e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 557
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-476 3.69e-06

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 273
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   274 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 352
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   353 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 424
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938795   425 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 476
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 493-810 6.39e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  493 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 572
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  573 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 652
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  653 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 732
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795  733 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 810
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-557 1.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 557
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-476 3.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 273
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   274 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 352
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   353 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 424
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938795   425 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 476
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
PHA03247 PHA03247
large tegument protein UL36; Provisional
 493-810 6.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  493 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 572
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  573 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 652
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  653 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 732
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795  733 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 810
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 141-466 7.85e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  221 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  292 SALLNLTRSVQELTEENQSLKEDLDRML-----SNSPTISKIKGYGDWSKpRLLRRIAELEKKVSS-----SESPKQSTS 361
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLgilreVENEKNDKDKKIAELES-LTLRQMKEQNKKVANikhgqQEMKKKGAQ 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  362 ELVNPNPLVRSPSNISVQKQPkgdqspEDLPKVAPCEEQE------HLQGTVKSLREELGAL------QEQLLEKDLEMK 429
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQL------EELMGALEKTRQEldatkaRLSSTQQSLAEKDGHLtnlraeRRKQLEEILEMK 710

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 568938795  430 Q-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 466
Cdd:pfam10174 711 QeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 546-577 2.58e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 2.58e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938795 546 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 577
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
143-479 8.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 143 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 211
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 212 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLA--SSEATG-KKPMVEKKLGVKRQK 288
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSrlEEEINGiEERIKELEEKEERLE 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 289 KMSSALLNLTRSVQELtEENQSLKEDLDRMLSNSPTISKIKgyGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNPN 367
Cdd:PRK03918 342 ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKaKEEIEEEISKITARIGELK 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 368 PLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELE 443
Cdd:PRK03918 419 KEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568938795 444 TAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 479
Cdd:PRK03918 491 KESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
279-479 1.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 279 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 358
Cdd:COG3206  213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 359 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 438
Cdd:COG3206  277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568938795 439 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 479
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 553-573 2.97e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.97e-03
                           10        20
                   ....*....|....*....|.
gi 568938795   553 LDEAATVLQAAFRGHLARSKL 573
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 555-573 5.68e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.68e-03
                          10
                  ....*....|....*....
gi 568938795  555 EAATVLQAAFRGHLARSKL 573
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 440-582 7.49e-03

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 39.46  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 440 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 514
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795 515 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 582
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 336-481 8.05e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  336 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 413
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795  414 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 481
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-557 1.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 557
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-476 3.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 273
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   274 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 352
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   353 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 424
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938795   425 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 476
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-481 7.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   149 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 228
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   229 KDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 308
Cdd:TIGR02168  745 LEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   309 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 380
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   381 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 452
Cdd:TIGR02168  886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568938795   453 QEQEQALREEVEALTKKCQEL--------EEAKREEK 481
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELgpvnlaaiEEYEELKE 1000
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
381-479 1.38e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 381 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 452
Cdd:COG2433  390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462

                         90       100
                 ....*....|....*....|....*...
gi 568938795 453 QEQE-QALREEVEALTKKCQELEEAKRE 479
Cdd:COG2433  463 KDREiSRLDREIERLERELEEERERIEE 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-577 2.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKNSFVAVTHEAHPELHApspcsRHSEPDSDNSAGEEGSSQppapcsEERREAAIRTLQAQwkAHRRKKREAALDEAA 557
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAEL------AAQLEELEEAEEAL--LERLERLEEELEELE 427

                        170       180
                 ....*....|....*....|
gi 568938795 558 TVLQAAFRGHLARSKLVRSK 577
Cdd:COG1196  428 EALAELEEEEEEEEEALEEA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 215-565 2.86e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   215 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 288
Cdd:TIGR02168  198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   289 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 368
Cdd:TIGR02168  274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   369 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 448
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   449 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 528
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568938795   529 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 565
Cdd:TIGR02168  458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-573 2.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 557
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                        170
                 ....*....|....*.
gi 568938795 558 TVLQAAFRGHLARSKL 573
Cdd:COG1196  501 ADYEGFLEGVKAALLL 516
PHA03247 PHA03247
large tegument protein UL36; Provisional
 493-810 6.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  493 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 572
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  573 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 652
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  653 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 732
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795  733 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 810
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-563 6.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 478 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 557
Cdd:COG1196  333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397


                 ....*.
gi 568938795 558 TVLQAA 563
Cdd:COG1196  398 LAAQLE 403
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 141-466 7.85e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  221 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  292 SALLNLTRSVQELTEENQSLKEDLDRML-----SNSPTISKIKGYGDWSKpRLLRRIAELEKKVSS-----SESPKQSTS 361
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLgilreVENEKNDKDKKIAELES-LTLRQMKEQNKKVANikhgqQEMKKKGAQ 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  362 ELVNPNPLVRSPSNISVQKQPkgdqspEDLPKVAPCEEQE------HLQGTVKSLREELGAL------QEQLLEKDLEMK 429
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQL------EELMGALEKTRQEldatkaRLSSTQQSLAEKDGHLtnlraeRRKQLEEILEMK 710

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 568938795  430 Q-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 466
Cdd:pfam10174 711 QeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
398-484 8.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG4372   59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                 ....*..
gi 568938795 478 REEKNSF 484
Cdd:COG4372  139 AELQSEI 145
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-481 9.25e-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: 46.17  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 220
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  221 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGK---KPMVEKKLGVKRqkkmssalLNL 297
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKdltNQDSVKELIIKN--------LDN 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  298 TRSVQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNIS 377
Cdd:TIGR04523 462 TRESLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  378 VQKQpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQ 453
Cdd:TIGR04523 523 KEKI-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595

                         330       340       350
                  ....*....|....*....|....*....|..
gi 568938795  454 EQEQALREEVEALTKKC----QELEEAKREEK 481
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKIssleKELEKAKKENE 627
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-482 1.04e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   147 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 226
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   227 KEKDNTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEatgkkpmVEKKLGVKRQKKMSSALLNLTRSVQEL 304
Cdd:TIGR02168  305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   305 TEENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKG 384
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   385 DQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVE 464
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLD 492

                          330
                   ....*....|....*...
gi 568938795   465 ALTKKCQELEEAKREEKN 482
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKA 510
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 212-483 1.28e-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: 45.78  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  212 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 291
Cdd:TIGR04523  77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  292 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 370
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  371 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 449
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568938795  450 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 483
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
338-487 1.51e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 338 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 413
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938795 414 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 487
Cdd:COG4717  179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 134-479 1.61e-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: 45.44  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   134 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 205
Cdd:TIGR02169  162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   206 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 279
Cdd:TIGR02169  241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   280 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 355
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   356 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQllqs 434
Cdd:TIGR02169  390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKK---- 452

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 568938795   435 kidLEKELETAREGEKGRQEQEQALREEVEALTKkcqELEEAKRE 479
Cdd:TIGR02169  453 ---QEWKLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRE 491
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 138-482 1.78e-04

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: 45.11  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   138 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 215
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   216 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 289
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   290 MS-----SALLNLTRSVQELT---------------------EENQSLKEDLDRmLSNSPT------------------- 324
Cdd:pfam15921  489 MTlesseRTVSDLTASLQEKEraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvieil 567

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   325 ------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDLPK 393
Cdd:pfam15921  568 rqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERLRA 647

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   394 VAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK------- 450
Cdd:pfam15921  648 VKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdghamk 727

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 568938795   451 ---GRQEQEQALREEVEALTKKCQELEEAK----------REEKN 482
Cdd:pfam15921  728 vamGMQKQITAKRGQIDALQSKIQFLEEAMtnankekhflKEEKN 772
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 546-577 2.58e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 2.58e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938795 546 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 577
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
398-479 2.93e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                 ..
gi 568938795 478 RE 479
Cdd:COG4372  125 QD 126
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-484 4.41e-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: 43.86  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  141 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 220
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  221 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRlqtllasSEATGKKPMVEKKLGVKRQKKMssaLLNLTRS 300
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKE---LKKLNEE 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  301 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 380
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  381 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 460
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637

                         330       340
                  ....*....|....*....|....
gi 568938795  461 EEVEALTKKCQELEEAKREEKNSF 484
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
143-479 8.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 143 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 211
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 212 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLA--SSEATG-KKPMVEKKLGVKRQK 288
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSrlEEEINGiEERIKELEEKEERLE 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 289 KMSSALLNLTRSVQELtEENQSLKEDLDRMLSNSPTISKIKgyGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNPN 367
Cdd:PRK03918 342 ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKaKEEIEEEISKITARIGELK 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 368 PLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELE 443
Cdd:PRK03918 419 KEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568938795 444 TAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 479
Cdd:PRK03918 491 KESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
141-479 9.37e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 9.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 217
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 218 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 297
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 298 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 377
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 378 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 444
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 568938795 445 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 479
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 220-428 1.72e-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: 41.76  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  220 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 298
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  299 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 373
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568938795  374 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 428
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
407-570 1.83e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  407 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKreekns 483
Cdd:COG4913   663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL------ 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  484 fvavtheahpelhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERREAAIRTLQ----AQWKAHRRKKREAALDEAATV 559
Cdd:COG4913   737 ----------------------------EAAEDLARLELRALLEERFAAALGDAVerelRENLEERIDALRARLNRAEEE 788

                         170
                  ....*....|.
gi 568938795  560 LQAAFRGHLAR 570
Cdd:COG4913   789 LERAMRAFNRE 799
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
279-479 1.86e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 279 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 358
Cdd:COG3206  213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 359 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 438
Cdd:COG3206  277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568938795 439 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 479
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 497-810 2.64e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  497 APSPCSRHSEPDSDNSAGEEGSSQPPAPCSEERREAAIR-TLQAQWKAHRRKKREAALDEAATVLQAAFR---GHLARSK 572
Cdd:PHA03307   70 GPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPpGPSSPDPPPPTPPPASPPPSPAPDLSEMLRpvgSPGPPPA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  573 LVRSKVPDSRSPSLPGLLSP----LNQSSPAPRVLSPISPAEENPTQEEAviviqsilrgylaqarfiasccREIAASSQ 648
Cdd:PHA03307  150 ASPPAAGASPAAVASDAASSrqaaLPLSSPEETARAPSSPPAEPPPSTPP----------------------AAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  649 RETVSLTPSGSASPPSLRASPEWGPSGKNSEASSGEAA-KDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSV 727
Cdd:PHA03307  208 RRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASS 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  728 PYSAQGGHGD-CPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKK 806
Cdd:PHA03307  288 SSSPRERSPSpSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367


                  ....
gi 568938795  807 SPSP 810
Cdd:PHA03307  368 RPRP 371
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 398-488 2.79e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 454
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938795 455 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 488
Cdd:COG1579  111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 553-573 2.97e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 2.97e-03
                           10        20
                   ....*....|....*....|.
gi 568938795   553 LDEAATVLQAAFRGHLARSKL 573
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 571-810 3.29e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.07  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 571 SKLVRSKVPDSRSPSLPGLLSPLNQSSPAPrvlspisPAEENPTQEEAVIviQSILRGYLAQarfiasccreiaassqre 650
Cdd:PLN03209 325 SQRVPPKESDAADGPKPVPTKPVTPEAPSP-------PIEEEPPQPKAVV--PRPLSPYTAY------------------ 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 651 tVSLTPSGSASPPSlraspewgPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPA------ 724
Cdd:PLN03209 378 -EDLKPPTSPIPTP--------PSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlk 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 725 -PSVPySAQGGHGDCPSSSSLEAVPSMKDamceersSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLP 803
Cdd:PLN03209 449 pPTSP-SPTAPTGVSPSVSSTSSVPAVPD-------TAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGK 520


                 ....*..
gi 568938795 804 RKKSPSP 810
Cdd:PLN03209 521 VAPSSTN 527
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-481 3.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318


                 ....
gi 568938795 478 REEK 481
Cdd:COG1196  319 EELE 322
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
141-496 3.57e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 141 REKEDMYDEIIELKKsLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrgpdfvrTLAEKKPdtgwviTGLKQRIF 220
Cdd:PRK02224 149 SDRQDMIDDLLQLGK-LEEYRERASDARLGVERVLSDQRGSLDQLKA------------QIEEKEE------KDLHERLN 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 221 RLEQQCKEKDNTINKL--QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATgkkpmVEKKLGVKRQKKmssallNLT 298
Cdd:PRK02224 210 GLESELAELDEEIERYeeQREQARETRDEADEVLEEHEERREELETLEAEIEDL-----RETIAETERERE------ELA 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 299 RSVQELTEENQSLKEDLDRMLSNSptiskikGYGDWSKPRLLRRIAELEKKVSSSEspkqstselvnpnplvrspsnisv 378
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEA-------GLDDADAEAVEARREELEDRDEELR------------------------ 327

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 379 qkqpkgdqspEDLPKVAPceEQEHLQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAREGEKGRQEQEQA 458
Cdd:PRK02224 328 ----------DRLEECRV--AAQAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEE 388

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568938795 459 LREEVEALTKKCQELEEAkREEKNSFVAVTHEAHPELH 496
Cdd:PRK02224 389 LEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELR 425
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 398-479 3.60e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 468
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103

                         90
                 ....*....|.
gi 568938795 469 KCQELEEAKRE 479
Cdd:COG1579  104 RISDLEDEILE 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 398-481 4.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 398 EEQEHLQGTV-----KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQE 472
Cdd:COG1196  220 EELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299


                 ....*....
gi 568938795 473 LEEAKREEK 481
Cdd:COG1196  300 LEQDIARLE 308
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 555-573 5.68e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.68e-03
                          10
                  ....*....|....*....
gi 568938795  555 EAATVLQAAFRGHLARSKL 573
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
140-478 5.73e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 140 YREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD--PSRGPDFVRTLAEKkpdtgwvITGLKQ 217
Cdd:COG4717  134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEE-------LEELQQ 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 218 RIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLA-----SSEATGKKPMVEKKLGV-------- 284
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVlflvlgll 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 285 -------KRQKKMSSALLNLTRSVQELTE-ENQSLKEDLDR-MLSNSPTISKIKGYGDW--SKPRLLRRIAELEKKVSSS 353
Cdd:COG4717  287 allflllAREKASLGKEAEELQALPALEElEEEELEELLAAlGLPPDLSPEELLELLDRieELQELLREAEELEEELQLE 366

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 354 ESPKQSTSELvnpnplvrspsnisvqkQPKGDQSPEDLPKVApcEEQEHLQgtvkSLREELGALQEQLLEKDLEMKQLLQ 433
Cdd:COG4717  367 ELEQEIAALL-----------------AEAGVEDEEELRAAL--EQAEEYQ----ELKEELEELEEQLEELLGELEELLE 423

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 568938795 434 --SKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKR 478
Cdd:COG4717  424 alDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 142-477 5.88e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  142 EKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL--------LDPSRGPDFVRTLAEKKPDTGWVIT 213
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLkervkslqTDSSNTDTALTTLEEALSEKERIIE 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  214 GLKQRIFRLEQQCKEKDNTINKLQTDMKTTnLEEMRIAMETYYEEIHRLQTLlASSEATGkkpmvekklGVKRQKKMSSA 293
Cdd:pfam10174 454 RLKEQREREDRERLEELESLKKENKDLKEK-VSALQPELTEKESSLIDLKEH-ASSLASS---------GLKKDSKLKSL 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  294 LLNLTRSVQELTE-ENQSLK----EDLDRMlsnsptiskikgygdwsKPRLLRRIAELEKKVSS-SESPKQSTSELVNPN 367
Cdd:pfam10174 523 EIAVEQKKEECSKlENQLKKahnaEEAVRT-----------------NPEINDRIRLLEQEVARyKEESGKAQAEVERLL 585

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  368 PLVRSPSNisvQKQPKgDQSPEDLPKVAP--CEEQEHLQGTVKSLREELGALQEQLLEKDLEmkqllqskidlekeleta 445
Cdd:pfam10174 586 GILREVEN---EKNDK-DKKIAELESLTLrqMKEQNKKVANIKHGQQEMKKKGAQLLEEARR------------------ 643

                         330       340       350
                  ....*....|....*....|....*....|..
gi 568938795  446 REGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATK 675
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 440-582 7.49e-03

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 39.46  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795 440 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 514
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795 515 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 582
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 148-483 7.95e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  148 DEIIELKKSLHMQKSDVDLMRTKLRRLEEE-------NSRKDRQIEQLldpsrgPDFVRTLAEKKPDTGWVITGLKQRIF 220
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkYNDLKKQKEEL------ENELNLLEKEKLNIQKNIDKIKNKLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  221 RLEQQ---CKEKDNTINKLQTdmKTTNLEEMRIAMETYYE----EIHRLQTLLASSE-----ATGKKPMVEKKLGVKRQK 288
Cdd:TIGR04523 198 KLELLlsnLKKKIQKNKSLES--QISELKKQNNQLKDNIEkkqqEINEKTTEISNTQtqlnqLKDEQNKIKKQLSEKQKE 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  289 --KMSSALLNLTRSVQELTEE------------NQSLKEDL---DRMLSNSPT-ISKIKGygdwSKPRLLRRIAELEKKV 350
Cdd:TIGR04523 276 leQNNKKIKELEKQLNQLKSEisdlnnqkeqdwNKELKSELknqEKKLEEIQNqISQNNK----IISQLNEQISQLKKEL 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  351 SSSESPKQS-TSELVNPNPLVRS---------------PSNIS-----VQKQPKGDQSPEDLPKVAPCE------EQEHL 403
Cdd:TIGR04523 352 TNSESENSEkQRELEEKQNEIEKlkkenqsykqeiknlESQINdleskIQNQEKLNQQKDEQIKKLQQEkellekEIERL 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  404 QGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQALREeveaLTKKCQELEEAKREEKN 482
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlSRSINKIKQNLEQKQKE----LKSKEKELKKLNEEKKE 507


                  .
gi 568938795  483 S 483
Cdd:TIGR04523 508 L 508
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 336-481 8.05e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  336 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 413
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938795  414 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 481
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 296-477 8.16e-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: 39.77  E-value: 8.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   296 NLTRSVQELTEENQSLKEDLDrmlsnspTISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPL-VRSPS 374
Cdd:pfam01576  374 NLEKAKQALESENAELQAELR-------TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSeLESVS 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795   375 NISVQKQPKGDQSPEDLPKVAPC--EEQEHLQ----------GTVKSLREELGALQEQL---------LEKDLEM--KQL 431
Cdd:pfam01576  447 SLLNEAEGKNIKLSKDVSSLESQlqDTQELLQeetrqklnlsTRLRQLEDERNSLQEQLeeeeeakrnVERQLSTlqAQL 526

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 568938795   432 LQSKIDLEKELETAREGEKGRQEqeqaLREEVEALTKKCQELEEAK 477
Cdd:pfam01576  527 SDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQQLEEKAAAY 568
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 478-784 8.22e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  478 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 555
Cdd:PHA03307   80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  556 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 632
Cdd:PHA03307  160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  633 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPEWGP--SGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELC 710
Cdd:PHA03307  240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGpsSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS 316

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938795  711 ASEELRETSASEPAPSVPYSAQGGHGDCPSSSsleavpsmkdamceeRSSSPRSAGPSLAEPSPPELQPLSPPP 784
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPS---------------RSPSPSRPPPPADPSSPRKRPRPSRAP 375
PHA03247 PHA03247
large tegument protein UL36; Provisional
 493-810 9.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  493 PELHAPSPCSRHSEPDSDNSAGEEGSSQP---PAPCSEERREAAIRTLQAQWKAH--RRKKREAALDEAATVLQAAF--- 564
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPrddPAPGRVSRPRRARRLGRAAQASSppQRPRRRAARPTVGSLTSLADppp 2703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  565 --RGHLARSKLVRSKVPDSRSPSLPGLLSPLNQSSPAPRVL--SPISPAEENPTQEEAviviqsilrgylAQARFIASCC 640
Cdd:PHA03247 2704 ppPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVpaGPATPGGPARPARPP------------TTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  641 REIAASSQRETVSLTPSGSASPPSLRASPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVirkelcaseelRETSA 720
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-----------PTAPP 2840

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938795  721 SEPAPSVPYSAQGGH----GDC---PSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPvEDICSDDS 793
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSvapgGDVrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP-QAPPPPQP 2919

                         330
                  ....*....|....*..
gi 568938795  794 DDIIFSPFLPRKKSPSP 810
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPP 2936
 
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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