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Conserved domains on  [gi|568938801|ref|XP_006504805|]
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IQ domain-containing protein E isoform X4 [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]; ...
 353-512 1.77e-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: 51.48  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
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 ...
 149-431 8.34e-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: 49.67  E-value: 8.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 228
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   229 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 307
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   308 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 379
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938801   380 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 431
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 448-765 3.20e-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: 47.63  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  448 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 527
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  528 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 607
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  608 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 687
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938801  688 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 765
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-512 1.77e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-431 8.34e-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: 8.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 228
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   229 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 307
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   308 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 379
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938801   380 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 431
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
PHA03247 PHA03247
large tegument protein UL36; Provisional
 448-765 3.20e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  448 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 527
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  528 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 607
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  608 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 687
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938801  688 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 765
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 96-421 2.27e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  176 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprllRRIAELEKKVSSSESPKQSTSELVNPNPLVR 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  327 SPSNISVQKQPKgdqSPEDLPKVAPCEEQ-EHLQGTVKSLREELGAL-------QEQLLEKD-----------------L 381
Cdd:pfam10174 631 KKKGAQLLEEAR---RREDNLADNSQQLQlEELMGALEKTRQELDATkarlsstQQSLAEKDghltnlraerrkqleeiL 707

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 568938801  382 EMKQ-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 421
Cdd:pfam10174 708 EMKQeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 501-532 3.17e-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: 38.68  E-value: 3.17e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938801 501 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 532
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-434 1.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 172
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 173 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 252
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 253 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 332
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 333 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 399
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 568938801 400 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
234-434 2.54e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 234 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 313
Cdd:COG3206  213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 314 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 393
Cdd:COG3206  277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568938801 394 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 508-528 2.81e-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: 2.81e-03
                           10        20
                   ....*....|....*....|.
gi 568938801   508 LDEAATVLQAAFRGHLARSKL 528
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 510-528 5.37e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.37e-03
                          10
                  ....*....|....*....
gi 568938801  510 EAATVLQAAFRGHLARSKL 528
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 395-537 6.99e-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: 6.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 395 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 469
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938801 470 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 537
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-512 1.77e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196  340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-431 8.34e-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: 8.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 228
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   229 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 307
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   308 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 379
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568938801   380 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 431
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
336-434 1.65e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.32  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 336 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 407
Cdd:COG2433  390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462

                         90       100
                 ....*....|....*....|....*...
gi 568938801 408 QEQE-QALREEVEALTKKCQELEEAKRE 434
Cdd:COG2433  463 KDREiSRLDREIERLERELEEERERIEE 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-436 1.90e-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: 48.51  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   104 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 183
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   184 KDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 263
Cdd:TIGR02168  745 LEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   264 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 335
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   336 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 407
Cdd:TIGR02168  886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568938801   408 QEQEQALREEVEALTKKCQEL--------EEAKREEK 436
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELgpvnlaaiEEYEELKE 1000
PHA03247 PHA03247
large tegument protein UL36; Provisional
 448-765 3.20e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  448 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 527
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  528 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 607
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  608 SLTPSGSASPPSLRAsPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSVPYSAQ 687
Cdd:PHA03247 2760 PPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA 2838

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938801  688 GGHGDCPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 765
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-532 3.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKNSFVAVTHEAHPELHApspcsRHSEPDSDNSAGEEGSSQppapcsEERREAAIRTLQAQwkAHRRKKREAALDEAA 512
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAEL------AAQLEELEEAEEAL--LERLERLEEELEELE 427

                        170       180
                 ....*....|....*....|
gi 568938801 513 TVLQAAFRGHLARSKLVRSK 532
Cdd:COG1196  428 EALAELEEEEEEEEEALEEA 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-528 4.25e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                        170
                 ....*....|....*.
gi 568938801 513 TVLQAAFRGHLARSKL 528
Cdd:COG1196  501 ADYEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-520 7.36e-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: 46.59  E-value: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   170 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 243
Cdd:TIGR02168  198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   244 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 323
Cdd:TIGR02168  274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   324 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 403
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   404 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 483
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568938801   484 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 520
Cdd:TIGR02168  458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-518 9.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 433 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196  333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397


                 ....*.
gi 568938801 513 TVLQAA 518
Cdd:COG1196  398 LAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-437 2.17e-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: 45.05  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   102 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 181
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   182 KEKDNTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEatgkkpmVEKKLGVKRQKKMSSALLNLTRSVQEL 259
Cdd:TIGR02168  305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   260 TEENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKG 339
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   340 DQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVE 419
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLD 492

                          330
                   ....*....|....*...
gi 568938801   420 ALTKKCQELEEAKREEKN 437
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKA 510
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
353-439 2.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG4372   59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                 ....*..
gi 568938801 433 REEKNSF 439
Cdd:COG4372  139 AELQSEI 145
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 96-421 2.27e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  176 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprllRRIAELEKKVSSSESPKQSTSELVNPNPLVR 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  327 SPSNISVQKQPKgdqSPEDLPKVAPCEEQ-EHLQGTVKSLREELGAL-------QEQLLEKD-----------------L 381
Cdd:pfam10174 631 KKKGAQLLEEAR---RREDNLADNSQQLQlEELMGALEKTRQELDATkarlsstQQSLAEKDghltnlraerrkqleeiL 707

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 568938801  382 EMKQ-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 421
Cdd:pfam10174 708 EMKQeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
293-442 2.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 293 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 368
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568938801 369 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 442
Cdd:COG4717  179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 93-288 2.83e-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: 44.34  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801    93 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 170
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   171 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 244
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 568938801   245 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTISKIKGYGD 288
Cdd:pfam15921  489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVD 527
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 501-532 3.17e-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: 38.68  E-value: 3.17e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568938801 501 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 532
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-434 4.81e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801    89 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 160
Cdd:TIGR02169  162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   161 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 234
Cdd:TIGR02169  241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   235 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 310
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   311 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQllqs 389
Cdd:TIGR02169  390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKK---- 452

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 568938801   390 kidLEKELETAREGEKGRQEQEQALREEVEALTKkcqELEEAKRE 434
Cdd:TIGR02169  453 ---QEWKLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRE 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-438 6.74e-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: 43.09  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  167 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 246
Cdd:TIGR04523  77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  247 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 325
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  326 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 404
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568938801  405 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 438
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
353-434 7.76e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                 ..
gi 568938801 433 RE 434
Cdd:COG4372  125 QD 126
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 96-436 8.63e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 175
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  176 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKpmVEKKLGVKRQKKMSsalLNLTRS 255
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELIIKN---LDNTRE 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  256 VQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQK 335
Cdd:TIGR04523 465 SLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  336 QpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQE 411
Cdd:TIGR04523 526 I-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598

                         330       340
                  ....*....|....*....|....*....
gi 568938801  412 QALREEVEALTKKC----QELEEAKREEK 436
Cdd:TIGR04523 599 KDLIKEIEEKEKKIssleKELEKAKKENE 627
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 452-765 1.36e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  452 APSPCSRHSEPDSDNSAGEEGSSQPPAPCSEERREAAIR-TLQAQWKAHRRKKREAALDEAATVLQAAFR---GHLARSK 527
Cdd:PHA03307   70 GPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPpGPSSPDPPPPTPPPASPPPSPAPDLSEMLRpvgSPGPPPA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  528 LVRSKVPDSRSPSLPGLLSP----LNQSSPAPRVLSPISPAEENPTQEEAviviqsilrgylaqarfiasccREIAASSQ 603
Cdd:PHA03307  150 ASPPAAGASPAAVASDAASSrqaaLPLSSPEETARAPSSPPAEPPPSTPP----------------------AAASPRPP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  604 RETVSLTPSGSASPPSLRASPEWGPSGKNSEASSGEAA-KDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPAPSV 682
Cdd:PHA03307  208 RRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASS 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  683 PYSAQGGHGD-CPSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLPRKK 761
Cdd:PHA03307  288 SSSPRERSPSpSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367


                  ....
gi 568938801  762 SPSP 765
Cdd:PHA03307  368 RPRP 371
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-434 1.89e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 172
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 173 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 252
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 253 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 332
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 333 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 399
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 568938801 400 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
362-525 2.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  362 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKreekns 438
Cdd:COG4913   663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL------ 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  439 fvavtheahpelhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERREAAIRTLQ----AQWKAHRRKKREAALDEAATV 514
Cdd:COG4913   737 ----------------------------EAAEDLARLELRALLEERFAAALGDAVerelRENLEERIDALRARLNRAEEE 788

                         170
                  ....*....|.
gi 568938801  515 LQAAFRGHLAR 525
Cdd:COG4913   789 LERAMRAFNRE 799
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 526-765 2.35e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.45  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 526 SKLVRSKVPDSRSPSLPGLLSPLNQSSPAPrvlspisPAEENPTQEEAVIviQSILRGYLAQarfiasccreiaassqre 605
Cdd:PLN03209 325 SQRVPPKESDAADGPKPVPTKPVTPEAPSP-------PIEEEPPQPKAVV--PRPLSPYTAY------------------ 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 606 tVSLTPSGSASPPSlraspewgPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELCASEELRETSASEPA------ 679
Cdd:PLN03209 378 -EDLKPPTSPIPTP--------PSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlk 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 680 -PSVPySAQGGHGDCPSSSSLEAVPSMKDamceersSSPRSAGPSLAEPSPPELQPLSPPPVEDICSDDSDDIIFSPFLP 758
Cdd:PLN03209 449 pPTSP-SPTAPTGVSPSVSSTSSVPAVPD-------TAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGK 520


                 ....*..
gi 568938801 759 RKKSPSP 765
Cdd:PLN03209 521 VAPSSTN 527
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
234-434 2.54e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 234 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 313
Cdd:COG3206  213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 314 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 393
Cdd:COG3206  277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568938801 394 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 508-528 2.81e-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: 2.81e-03
                           10        20
                   ....*....|....*....|.
gi 568938801   508 LDEAATVLQAAFRGHLARSKL 528
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 96-439 3.65e-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: 40.77  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801   96 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 175
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  176 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKlgvkrqkkmsSALLNLTRS 255
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE----------KELKKLNEE 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  256 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 335
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  336 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 415
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637

                         330       340
                  ....*....|....*....|....
gi 568938801  416 EEVEALTKKCQELEEAKREEKNSF 439
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 433-739 3.82e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  433 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 510
Cdd:PHA03307   80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  511 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 587
Cdd:PHA03307  160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  588 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPEWGP--SGKNSEASSGEAAKDEDEAEEPPDLQPYSGVIRKELC 665
Cdd:PHA03307  240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGpsSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS 316

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938801  666 ASEELRETSASEPAPSvpysaqgghgdcPSSSSLEAVPSMKDamcEERSSSPRSAGPSLAEPSPPELQPLSPPP 739
Cdd:PHA03307  317 SSSSSRESSSSSTSSS------------SESSRGAAVSPGPS---PSRSPSPSRPPPPADPSSPRKRPRPSRAP 375
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-434 4.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  98 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 166
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 167 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLA--SSEATG-KKPMVEKKLGVKRQK 243
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSrlEEEINGiEERIKELEEKEERLE 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 244 KMSSALLNLTRSVQELtEENQSLKEDLDRMLSNSPTISKIKgyGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNPN 322
Cdd:PRK03918 342 ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKaKEEIEEEISKITARIGELK 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 323 PLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELE 398
Cdd:PRK03918 419 KEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568938801 399 TAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 434
Cdd:PRK03918 491 KESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-436 4.07e-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: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196  239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318


                 ....
gi 568938801 433 REEK 436
Cdd:COG1196  319 EELE 322
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 175-383 4.52e-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: 40.22  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  175 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 253
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  254 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 328
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568938801  329 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 383
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
PHA03247 PHA03247
large tegument protein UL36; Provisional
 448-765 4.79e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  448 PELHAPSPCSRHSEPDSDNSAGEEGSSQP---PAPCSEERREAAIRTLQAQWKAH--RRKKREAALDEAATVLQAAF--- 519
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPrddPAPGRVSRPRRARRLGRAAQASSppQRPRRRAARPTVGSLTSLADppp 2703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  520 --RGHLARSKLVRSKVPDSRSPSLPGLLSPLNQSSPAPRVL--SPISPAEENPTQEEAviviqsilrgylAQARFIASCC 595
Cdd:PHA03247 2704 ppPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVpaGPATPGGPARPARPP------------TTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  596 REIAASSQRETVSLTPSGSASPPSLRASPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPYSGVirkelcaseelRETSA 675
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-----------PTAPP 2840

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  676 SEPAPSVPYSAQGGH----GDC---PSSSSLEAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPPvEDICSDDS 748
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSvapgGDVrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP-QAPPPPQP 2919

                         330
                  ....*....|....*..
gi 568938801  749 DDIIFSPFLPRKKSPSP 765
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPP 2936
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 353-436 4.91e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTV-----KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQE 427
Cdd:COG1196  220 EELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299


                 ....*....
gi 568938801 428 LEEAKREEK 436
Cdd:COG1196  300 LEQDIARLE 308
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 353-443 5.28e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 409
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938801 410 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 443
Cdd:COG1579  111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 510-528 5.37e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.37e-03
                          10
                  ....*....|....*....
gi 568938801  510 EAATVLQAAFRGHLARSKL 528
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 353-434 6.15e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 423
Cdd:COG1579   24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103

                         90
                 ....*....|.
gi 568938801 424 KCQELEEAKRE 434
Cdd:COG1579  104 RISDLEDEILE 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 530-739 6.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  530 RSKVPDSRSPSLPGLLSPLNQSSPAPR--VLSPISPAEENPTQEEAVIVIQSILRGYLAQARfiASCCREIAASSQRETV 607
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPPSPLPPDTHAPDppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR--VSRPRRARRLGRAAQA 2676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  608 SLTPSG---------------SASPPSLRASPEWGPSGKNSEASSGEAAKDEDEAEEPPDLQPY-----SGVIRKELCAS 667
Cdd:PHA03247 2677 SSPPQRprrraarptvgsltsLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAppavpAGPATPGGPAR 2756

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  668 EELRETSASEPAPSVPYSAQGG-------HGDCPSSSSLEAVPSMKD------AMCEERSSSPRSAGPSLAEPSPPELQP 734
Cdd:PHA03247 2757 PARPPTTAGPPAPAPPAAPAAGpprrltrPAVASLSESRESLPSPWDpadppaAVLAPAAALPPAASPAGPLPPPTSAQP 2836


                  ....*
gi 568938801  735 LSPPP 739
Cdd:PHA03247 2837 TAPPP 2841
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-451 6.79e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801  96 REKEDMYDEIIELKKsLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrgpdfvrTLAEKKPdtgwviTGLKQRIF 175
Cdd:PRK02224 149 SDRQDMIDDLLQLGK-LEEYRERASDARLGVERVLSDQRGSLDQLKA------------QIEEKEE------KDLHERLN 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 176 RLEQQCKEKDNTINKL--QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATgkkpmVEKKLGVKRQKKmssallNLT 253
Cdd:PRK02224 210 GLESELAELDEEIERYeeQREQARETRDEADEVLEEHEERREELETLEAEIEDL-----RETIAETERERE------ELA 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 254 RSVQELTEENQSLKEDLDRMLSNSptiskikGYGDWSKPRLLRRIAELEKKVSSSEspkqstselvnpnplvrspsnisv 333
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEA-------GLDDADAEAVEARREELEDRDEELR------------------------ 327

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 334 qkqpkgdqspEDLPKVAPceEQEHLQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAREGEKGRQEQEQA 413
Cdd:PRK02224 328 ----------DRLEECRV--AAQAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEE 388

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568938801 414 LREEVEALTKKCQELEEAkREEKNSFVAVTHEAHPELH 451
Cdd:PRK02224 389 LEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELR 425
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 395-537 6.99e-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: 6.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 395 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 469
Cdd:cd22307   57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938801 470 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 537
Cdd:cd22307  129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
553-730 9.37e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 553 PAPRVLSPISPAEENPTQEEAVIVIqsilrgylaqarfIASCCREIAASSQRETVSLTPSGSASPPSLRASPEWGPSGKN 632
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGA-------------AGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938801 633 SEASSGEAAKDEDEAEEPPDLQPYSGViRKELCASEELRETSASEPAPSVPYSAQGGHGDCPSSSSLeAVPSMKDAMCEE 712
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADS-GSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAP-AAASREDAPAAA 525

                        170
                 ....*....|....*...
gi 568938801 713 RSSSPRSAGPSLAEPSPP 730
Cdd:PRK07003 526 APPAPEARPPTPAAAAPA 543
 
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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