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Conserved domains on  [gi|1720415016|ref|XP_030110714|]
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IQ domain-containing protein E isoform X11 [Mus musculus]

Protein Classification

IQ calmodulin-binding motif-containing protein( domain architecture ID 10635649)

IQ calmodulin-binding motif-containing protein may be involved in cooperative interactions with calmodulins or calmodulin-like proteins

Gene Ontology:  GO:0005516
PubMed:  9141499

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]; ...
 333-492 2.09e-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: 51.09  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 492
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 ...
 129-411 7.38e-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: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  129 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 208
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  209 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 287
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  288 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 359
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720415016  360 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 411
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 481-512 2.70e-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: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415016 481 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 512
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 413-686 2.85e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  413 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 490
Cdd:PHA03307    80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  491 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 567
Cdd:PHA03307   160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  568 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSV-PYSAQGGHGDCPSSSSL 646
Cdd:PHA03307   240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASS 316

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720415016  647 EAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPP 686
Cdd:PHA03307   317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-492 2.09e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 492
Cdd:COG1196   340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 129-411 7.38e-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: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  129 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 208
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  209 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 287
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  288 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 359
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720415016  360 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 411
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 73-673 2.05e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016   73 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 150
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  151 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 224
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  225 MSsaLLNLTRSVQELT----------------------------EENQSLKEDLDRmLSNSPT----------------- 259
Cdd:pfam15921  489 MT--LESSERTVSDLTaslqekeraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvie 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  260 --------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDL 326
Cdd:pfam15921  566 ilrqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERL 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  327 PKVAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK----- 385
Cdd:pfam15921  646 RAVKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdgha 725

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  386 -----GRQEQEQALREEVEALTKKCQELEEAkreeknsfvavTHEAHPElhapspcsRHSEPDSDNSAGEEGSSqppAPC 460
Cdd:pfam15921  726 mkvamGMQKQITAKRGQIDALQSKIQFLEEA-----------MTNANKE--------KHFLKEEKNKLSQELST---VAT 783

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  461 SEERREAAIRTLQAQWKAHRRK--KREAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSS 532
Cdd:pfam15921  784 EKNKMAGELEVLRSQERRLKEKvaNMEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSS 858

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  533 PAPRVLSPISPAEENPTqeeaviviqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELC 612
Cdd:pfam15921  859 MKPRLLQPASFTRTHSN------------------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL 908

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415016  613 asEELRETSASEPAPSVPYSAQGGHG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 673
Cdd:pfam15921  909 --QELRSVINEEPTVQLSKAEDKGRApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 76-401 1.92e-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: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 155
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 226
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 227 SALLNLTRSVQELTEENQSLKEDLDRML-----SNSPTISKIKGYGDWSKpRLLRRIAELEKKVSS-----SESPKQSTS 296
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLgilreVENEKNDKDKKIAELES-LTLRQMKEQNKKVANikhgqQEMKKKGAQ 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 297 ELVNPNPLVRSPSNISVQKQPkgdqspEDLPKVAPCEEQE------HLQGTVKSLREELGAL------QEQLLEKDLEMK 364
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQL------EELMGALEKTRQEldatkaRLSSTQQSLAEKDGHLtnlraeRRKQLEEILEMK 710

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1720415016 365 Q-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 401
Cdd:pfam10174 711 QeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 481-512 2.70e-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: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415016 481 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 512
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-414 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  78 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 146
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 147 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLASSEATGKKpmVEKKLgvKRQKKMS 226
Cdd:PRK03918  268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERI--KELEEKE 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 227 SALLNLTRSVQELTEENQSLKED---LDRMLSNSPTISKIKG-YGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNP 301
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKrLTGLTPEKLEKELEELEKaKEEIEEEISKITARIGEL 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 302 NPLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKEL 377
Cdd:PRK03918  418 KKEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1720415016 378 ETAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 414
Cdd:PRK03918  490 KKESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 488-508 2.62e-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: 2.62e-03
                           10        20
                   ....*....|....*....|.
gi 1720415016  488 LDEAATVLQAAFRGHLARSKL 508
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 413-686 2.85e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  413 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 490
Cdd:PHA03307    80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  491 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 567
Cdd:PHA03307   160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  568 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSV-PYSAQGGHGDCPSSSSL 646
Cdd:PHA03307   240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASS 316

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720415016  647 EAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPP 686
Cdd:PHA03307   317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
214-414 5.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 214 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 293
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 294 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 373
Cdd:COG3206   277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720415016 374 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 414
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 490-508 5.15e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.15e-03
                          10
                  ....*....|....*....
gi 1720415016 490 EAATVLQAAFRGHLARSKL 508
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 375-517 6.40e-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: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 375 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 449
Cdd:cd22307    57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415016 450 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 517
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]; ...
 333-492 2.09e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 492
Cdd:COG1196   340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 129-411 7.38e-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: 7.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  129 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 208
Cdd:TIGR02168  656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  209 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 287
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  288 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 359
Cdd:TIGR02168  795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720415016  360 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 411
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
316-414 1.50e-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: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 316 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 387
Cdd:COG2433   390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462

                          90       100
                  ....*....|....*....|....*...
gi 1720415016 388 QEQE-QALREEVEALTKKCQELEEAKRE 414
Cdd:COG2433   463 KDREiSRLDREIERLERELEEERERIEE 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-416 1.64e-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: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016   84 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 163
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  164 KDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 243
Cdd:TIGR02168  745 LEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  244 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 315
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  316 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 387
Cdd:TIGR02168  886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1720415016  388 QEQEQALREEVEALTKKCQEL--------EEAKREEK 416
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELgpvnlaaiEEYEELKE 1000
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 73-673 2.05e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016   73 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 150
Cdd:pfam15921  331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  151 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 224
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  225 MSsaLLNLTRSVQELT----------------------------EENQSLKEDLDRmLSNSPT----------------- 259
Cdd:pfam15921  489 MT--LESSERTVSDLTaslqekeraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvie 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  260 --------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDL 326
Cdd:pfam15921  566 ilrqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERL 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  327 PKVAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK----- 385
Cdd:pfam15921  646 RAVKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdgha 725

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  386 -----GRQEQEQALREEVEALTKKCQELEEAkreeknsfvavTHEAHPElhapspcsRHSEPDSDNSAGEEGSSqppAPC 460
Cdd:pfam15921  726 mkvamGMQKQITAKRGQIDALQSKIQFLEEA-----------MTNANKE--------KHFLKEEKNKLSQELST---VAT 783

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  461 SEERREAAIRTLQAQWKAHRRK--KREAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSS 532
Cdd:pfam15921  784 EKNKMAGELEVLRSQERRLKEKvaNMEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSS 858

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  533 PAPRVLSPISPAEENPTqeeaviviqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELC 612
Cdd:pfam15921  859 MKPRLLQPASFTRTHSN------------------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL 908

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415016  613 asEELRETSASEPAPSVPYSAQGGHG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 673
Cdd:pfam15921  909 --QELRSVINEEPTVQLSKAEDKGRApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-512 3.93e-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: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKNSFVAVTHEAHPELHApspcsRHSEPDSDNSAGEEGSSQppapcsEERREAAIRTLQAQwkAHRRKKREAALDEAA 492
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAEL------AAQLEELEEAEEAL--LERLERLEEELEELE 427

                         170       180
                  ....*....|....*....|
gi 1720415016 493 TVLQAAFRGHLARSKLVRSK 512
Cdd:COG1196   428 EALAELEEEEEEEEEALEEA 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-508 4.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 492
Cdd:COG1196   431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                         170
                  ....*....|....*.
gi 1720415016 493 TVLQAAFRGHLARSKL 508
Cdd:COG1196   501 ADYEGFLEGVKAALLL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-500 6.69e-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: 6.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  150 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 223
Cdd:TIGR02168  198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  224 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 303
Cdd:TIGR02168  274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  304 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 383
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  384 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 463
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1720415016  464 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 500
Cdd:TIGR02168  458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 76-416 9.69e-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: 45.78  E-value: 9.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 155
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGK---KPMVEKKLGVKRqkkmssalLNL 232
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKdltNQDSVKELIIKN--------LDN 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 233 TRSVQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNIS 312
Cdd:TIGR04523 462 TRESLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 313 VQKQpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQ 388
Cdd:TIGR04523 523 KEKI-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1720415016 389 EQEQALREEVEALTKKC----QELEEAKREEK 416
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKIssleKELEKAKKENE 627
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-498 1.07e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 413 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 492
Cdd:COG1196   333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397


                  ....*.
gi 1720415016 493 TVLQAA 498
Cdd:COG1196   398 LAAQLE 403
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 147-418 1.20e-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: 45.40  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 147 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 226
Cdd:TIGR04523  77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 227 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 305
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 306 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 384
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720415016 385 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 418
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
333-419 1.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG4372    59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138


                  ....*..
gi 1720415016 413 REEKNSF 419
Cdd:COG4372   139 AELQSEI 145
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 76-401 1.92e-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: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 155
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 226
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 227 SALLNLTRSVQELTEENQSLKEDLDRML-----SNSPTISKIKGYGDWSKpRLLRRIAELEKKVSS-----SESPKQSTS 296
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLgilreVENEKNDKDKKIAELES-LTLRQMKEQNKKVANikhgqQEMKKKGAQ 636

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 297 ELVNPNPLVRSPSNISVQKQPkgdqspEDLPKVAPCEEQE------HLQGTVKSLREELGAL------QEQLLEKDLEMK 364
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQL------EELMGALEKTRQEldatkaRLSSTQQSLAEKDGHLtnlraeRRKQLEEILEMK 710

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1720415016 365 Q-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 401
Cdd:pfam10174 711 QeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 82-417 1.99e-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: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016   82 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 161
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  162 KEKDNTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEatgkkpmVEKKLGVKRQKKMSSALLNLTRSVQEL 239
Cdd:TIGR02168  305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  240 TEENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKG 319
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  320 DQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVE 399
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLD 492

                          330
                   ....*....|....*...
gi 1720415016  400 ALTKKCQELEEAKREEKN 417
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKA 510
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 481-512 2.70e-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: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720415016 481 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 512
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 69-414 2.96e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016   69 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 140
Cdd:TIGR02169  162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  141 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 214
Cdd:TIGR02169  241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  215 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 290
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  291 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQllqs 369
Cdd:TIGR02169  390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKK---- 452

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1720415016  370 kidLEKELETAREGEKGRQEQEQALREEVEALTKkcqELEEAKRE 414
Cdd:TIGR02169  453 ---QEWKLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRE 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-422 3.07e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 273 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 348
Cdd:COG4717    99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720415016 349 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 422
Cdd:COG4717   179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 76-419 4.04e-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: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 155
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRlqtllasSEATGKKPMVEKKLGVKRQKKMssaLLNLTRS 235
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKE---LKKLNEE 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 236 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 315
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 316 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 395
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637

                         330       340
                  ....*....|....*....|....
gi 1720415016 396 EEVEALTKKCQELEEAKREEKNSF 419
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
333-414 6.45e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124


                  ..
gi 1720415016 413 RE 414
Cdd:COG4372   125 QD 126
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-414 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  78 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 146
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 147 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLASSEATGKKpmVEKKLgvKRQKKMS 226
Cdd:PRK03918  268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERI--KELEEKE 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 227 SALLNLTRSVQELTEENQSLKED---LDRMLSNSPTISKIKG-YGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNP 301
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKrLTGLTPEKLEKELEELEKaKEEIEEEISKITARIGEL 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 302 NPLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKEL 377
Cdd:PRK03918  418 KKEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1720415016 378 ETAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 414
Cdd:PRK03918  490 KKESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
76-414 1.76e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 152
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 153 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 232
Cdd:PRK02224  350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 233 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 312
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 313 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 379
Cdd:PRK02224  453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1720415016 380 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 414
Cdd:PRK02224  528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 488-508 2.62e-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: 2.62e-03
                           10        20
                   ....*....|....*....|.
gi 1720415016  488 LDEAATVLQAAFRGHLARSKL 508
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
342-411 2.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720415016  342 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 411
Cdd:COG4913    663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 413-686 2.85e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  413 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 490
Cdd:PHA03307    80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  491 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 567
Cdd:PHA03307   160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  568 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSV-PYSAQGGHGDCPSSSSL 646
Cdd:PHA03307   240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASS 316

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1720415016  647 EAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPP 686
Cdd:PHA03307   317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 155-363 3.14e-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: 40.61  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 155 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 233
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 234 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 308
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720415016 309 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 363
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
PHA03247 PHA03247
large tegument protein UL36; Provisional
 428-712 3.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  428 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 507
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  508 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 587
Cdd:PHA03247  2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  588 SLTPSG--SASPPSLRASPGVIRKELCASEELRETSASEPAPSVPysaqgghgdcpsSSSLEAVPSMKDAMCEERSSSPR 665
Cdd:PHA03247  2760 PPTTAGppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP------------ADPPAAVLAPAAALPPAASPAGP 2827

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720415016  666 SAGPSLAEPSPPelqPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 712
Cdd:PHA03247  2828 LPPPTSAQPTAP---PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-416 4.23e-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: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 412
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318


                  ....
gi 1720415016 413 REEK 416
Cdd:COG1196   319 EELE 322
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
214-414 5.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 214 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 293
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 294 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 373
Cdd:COG3206   277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720415016 374 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 414
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 490-508 5.15e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 34.99  E-value: 5.15e-03
                          10
                  ....*....|....*....
gi 1720415016 490 EAATVLQAAFRGHLARSKL 508
Cdd:pfam00612   2 KAAIKIQAAWRGYLARKRY 20
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 343-416 5.51e-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: 5.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720415016 343 KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 416
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 333-423 5.75e-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: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 389
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720415016 390 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 423
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
76-431 6.21e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  76 REKEDMYDEIIELKKsLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrgpdfvrTLAEKKPdtgwviTGLKQRIF 155
Cdd:PRK02224  149 SDRQDMIDDLLQLGK-LEEYRERASDARLGVERVLSDQRGSLDQLKA------------QIEEKEE------KDLHERLN 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQCKEKDNTINKL--QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATgkkpmVEKKLGVKRQKKmssallNLT 233
Cdd:PRK02224  210 GLESELAELDEEIERYeeQREQARETRDEADEVLEEHEERREELETLEAEIEDL-----RETIAETERERE------ELA 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 234 RSVQELTEENQSLKEDLDRMLSNSptiskikGYGDWSKPRLLRRIAELEKKVSSSEspkqstselvnpnplvrspsnisv 313
Cdd:PRK02224  279 EEVRDLRERLEELEEERDDLLAEA-------GLDDADAEAVEARREELEDRDEELR------------------------ 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 314 qkqpkgdqspEDLPKVAPceEQEHLQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAREGEKGRQEQEQA 393
Cdd:PRK02224  328 ----------DRLEECRV--AAQAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEE 388

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1720415016 394 LREEVEALTKKCQELEEAkREEKNSFVAVTHEAHPELH 431
Cdd:PRK02224  389 LEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELR 425
PHA03378 PHA03378
EBNA-3B; Provisional
 440-713 6.27e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 440 SEPDSDNSAGEEGSSQP---PAPCSEERREAAIRTLQAqwkAHRRKKREAALDEAATVlqAAFRGHLARSKLVRSK---- 512
Cdd:PHA03378  369 CDPDEDKSGAEALASIPqtlPDPPTVYGRPKVFARKAD---LKSTKKCRAIVTDPSVI--KAIEEEHRKKKAARTEqpra 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 513 VPDSRSPSLPgLLSPLNQSSPAP----RVLSPISPAEENP-TQEEAVIVIQSILRGYLAQARFIASCCREIAASSQRETV 587
Cdd:PHA03378  444 TPHSQAPTVV-LHRPPTQPLEGPtgplSVQAPLEPWQPLPhPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDMEQRVMA 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 588 SLTPSGSASPPSLRASPGVIRKELCASEElretsasEPAPSVPYSAQggHGDCPSSSSLEAVPSMKDAMCEERSSSPRSA 667
Cdd:PHA03378  523 TLLPPSPPQPRAGRRAPCVYTEDLDIESD-------EPASTEPVHDQ--LLPAPGLGPLQIQPLTSPTTSQLASSAPSYA 593

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720415016 668 GPSL------AEPSPPELQplSPPPVEDICSDDSDDIIFSPFLPRKKSPSPF 713
Cdd:PHA03378  594 QTPWpvphpsQTPEPPTTQ--SHIPETSAPRQWPMPLRPIPMRPLRMQPITF 643
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 375-517 6.40e-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: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 375 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 449
Cdd:cd22307    57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415016 450 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 517
Cdd:cd22307   129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 333-414 6.71e-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: 38.75  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 333 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 403
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103

                          90
                  ....*....|.
gi 1720415016 404 KCQELEEAKRE 414
Cdd:COG1579   104 RISDLEDEILE 114
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-418 8.05e-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: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  83 DEIIELKKSLHMQKSDVDLMRTKLRRLEEE-------NSRKDRQIEQLldpsrgPDFVRTLAEKKPDTGWVITGLKQRIF 155
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkYNDLKKQKEEL------ENELNLLEKEKLNIQKNIDKIKNKLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 156 RLEQQ---CKEKDNTINKLQTdmKTTNLEEMRIAMETYYE----EIHRLQTLLASSE-----ATGKKPMVEKKLGVKRQK 223
Cdd:TIGR04523 198 KLELLlsnLKKKIQKNKSLES--QISELKKQNNQLKDNIEkkqqEINEKTTEISNTQtqlnqLKDEQNKIKKQLSEKQKE 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 224 --KMSSALLNLTRSVQELTEE------------NQSLKEDL---DRMLSNSPT-ISKIKGygdwSKPRLLRRIAELEKKV 285
Cdd:TIGR04523 276 leQNNKKIKELEKQLNQLKSEisdlnnqkeqdwNKELKSELknqEKKLEEIQNqISQNNK----IISQLNEQISQLKKEL 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 286 SSSESPKQS-TSELVNPNPLVRS---------------PSNIS-----VQKQPKGDQSPEDLPKVAPCE------EQEHL 338
Cdd:TIGR04523 352 TNSESENSEkQRELEEKQNEIEKlkkenqsykqeiknlESQINdleskIQNQEKLNQQKDEQIKKLQQEkellekEIERL 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016 339 QGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQALREeveaLTKKCQELEEAKREEKN 417
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlSRSINKIKQNLEQKQKE----LKSKEKELKKLNEEKKE 507


                  .
gi 1720415016 418 S 418
Cdd:TIGR04523 508 L 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
336-505 8.48e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  336 EHLQGTVKSLREELGALQEQLLEKDLEMKQL----------------------LQSKI-DLEKELETAREGE---KGRQE 389
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIaELEAELERLDASSddlAALEE 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415016  390 QEQALREEVEALTKKCQELEEAKR---EEKNSFVAVTHEAHPELhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERRE 466
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGrleKELEQAEEELDELQDRL----------------EAAEDLARLELRALLEERFA 756

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1720415016  467 AAIRTLQ----AQWKAHRRKKREAALDEAATVLQAAFRGHLAR 505
Cdd:COG4913    757 AALGDAVerelRENLEERIDALRARLNRAEEELERAMRAFNRE 799
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 334-411 9.61e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 9.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415016 334 EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEA 411
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-------QAEIDKLQAEIAEAEAEIEERREE 87
 
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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