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Conserved domains on  [gi|1034555185|ref|XP_016855699|]
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forkhead-associated domain-containing protein 1 isoform X22 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
19-114 4.86e-51

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 174.75  E-value: 4.86e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700      1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
                           90
                   ....*....|....*..
gi 1034555185   98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700     80 VLRFGFGGLPYELVVDN 96
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
663-1205 7.03e-18

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: 90.00  E-value: 7.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  663 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  738 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 816
Cdd:COG1196    293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  817 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:COG1196    369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  897 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 971
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  972 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1034
Cdd:COG1196    526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1035 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1107
Cdd:COG1196    606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1108 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1187
Cdd:COG1196    686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
                          570
                   ....*....|....*...
gi 1034555185 1188 RQKKALSELRARIKELEK 1205
Cdd:COG1196    764 ELERELERLEREIEALGP 781
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
308-1002 7.04e-14

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: 77.02  E-value: 7.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  308 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 467
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 546
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  547 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 616
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  617 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 665
Cdd:TIGR02168  535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  666 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 711
Cdd:TIGR02168  615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  712 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 791
Cdd:TIGR02168  690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  792 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 871
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  872 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 951
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  952 SqrhgFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 1002
Cdd:TIGR02168  898 E----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
VI_FHA super family cl37254
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
36-202 3.16e-07

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


The actual alignment was detected with superfamily member TIGR03354:

Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 54.30  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354   27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354  100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
                          170
                   ....*....|....*.
gi 1034555185  187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354  179 EPTMVPPFVPLPAPEP 194
 
Name Accession Description Interval E-value
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
19-114 4.86e-51

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 174.75  E-value: 4.86e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700      1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
                           90
                   ....*....|....*..
gi 1034555185   98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700     80 VLRFGFGGLPYELVVDN 96
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
35-101 1.48e-18

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 81.08  E-value: 1.48e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185   35 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 101
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
663-1205 7.03e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 7.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  663 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  738 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 816
Cdd:COG1196    293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  817 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:COG1196    369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  897 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 971
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  972 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1034
Cdd:COG1196    526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1035 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1107
Cdd:COG1196    606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1108 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1187
Cdd:COG1196    686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
                          570
                   ....*....|....*...
gi 1034555185 1188 RQKKALSELRARIKELEK 1205
Cdd:COG1196    764 ELERELERLEREIEALGP 781
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
29-110 4.49e-17

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 77.69  E-value: 4.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   29 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:COG1716     16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92

                   ...
gi 1034555185  108 YEL 110
Cdd:COG1716     93 FRL 95
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
292-1080 6.06e-15

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: 80.50  E-value: 6.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  292 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 370
Cdd:TIGR02169  233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  371 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 450
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  451 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 530
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  531 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 605
Cdd:TIGR02169  455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  606 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLI 659
Cdd:TIGR02169  527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLV 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  660 YLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEK---LREHLAEKEKL-------NEERLEQEEKLKAKIRQLTEEKAAL 729
Cdd:TIGR02169  607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAmtggsraPRGGILFSRSEPAELQRLRERLEGL 686
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  730 E---EYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 806
Cdd:TIGR02169  687 KrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  807 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 886
Cdd:TIGR02169  766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  887 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 966
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  967 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1046
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1034555185 1047 QEVIMKLRKDLTEAHSRMSDLRGelnEKQKMELE 1080
Cdd:TIGR02169  971 EPVNMLAIQEYEEVLKRLDELKE---KRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
308-1002 7.04e-14

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: 77.02  E-value: 7.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  308 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 467
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 546
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  547 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 616
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  617 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 665
Cdd:TIGR02168  535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  666 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 711
Cdd:TIGR02168  615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  712 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 791
Cdd:TIGR02168  690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  792 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 871
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  872 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 951
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  952 SqrhgFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 1002
Cdd:TIGR02168  898 E----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
303-869 3.92e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 3.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  303 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 382
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  383 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 462
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  463 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 542
Cdd:COG1196    377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 618
Cdd:COG1196    446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  619 QKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSL-----YLIYLLEHYKKLMSQAQELQIK-FNSSQETQQSLLQE 692
Cdd:COG1196    519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRaRAALAAALARGAIG 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  693 KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 772
Cdd:COG1196    599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  773 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 852
Cdd:COG1196    679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
                          570
                   ....*....|....*..
gi 1034555185  853 EKEKKKVQDLENRLTKQ 869
Cdd:COG1196    759 PPDLEELERELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
692-1150 6.71e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 770
Cdd:PTZ00121  1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  771 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 850
Cdd:PTZ00121  1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  851 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 930
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  931 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 1010
Cdd:PTZ00121  1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1011 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1090
Cdd:PTZ00121  1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1091 kelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1150
Cdd:PTZ00121  1785 -----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
230-985 2.00e-10

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 65.76  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK-KKLESERLSSAAKLKEEELELKSE 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  390 LKSQNKDKDHQLEALGSRCSVL-KEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR 468
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEkKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  469 EKSKVEEK---LQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKIT 542
Cdd:pfam02463  483 QEQLELLLsrqKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV 622
Cdd:pfam02463  563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  623 -----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 697
Cdd:pfam02463  643 akesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  698 LAEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKN 774
Cdd:pfam02463  723 LADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  775 RvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEK 854
Cdd:pfam02463  803 L-RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELE 880
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  855 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 934
Cdd:pfam02463  881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  935 RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 985
Cdd:pfam02463  961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
35-82 3.68e-09

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 53.72  E-value: 3.68e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1034555185    35 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 82
Cdd:smart00240    1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
658-973 1.06e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 56.67  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  658 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 735
Cdd:pfam17380  274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  736 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 796
Cdd:pfam17380  345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  797 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 876
Cdd:pfam17380  425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  877 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 955
Cdd:pfam17380  496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
                          330
                   ....*....|....*....
gi 1034555185  956 GFEEEIM-EYKEQIKQHAQ 973
Cdd:pfam17380  572 EREREMMrQIVESEKARAE 590
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
36-202 3.16e-07

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 54.30  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354   27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354  100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
                          170
                   ....*....|....*.
gi 1034555185  187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354  179 EPTMVPPFVPLPAPEP 194
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
252-828 4.20e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 4.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  252 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 331
Cdd:PRK03918   152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  332 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 411
Cdd:PRK03918   225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  412 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQ--EDSRRKLLQL 488
Cdd:PRK03918   299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  489 QEMGNRESVIKI----------------------NLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLiekitqvTE 546
Cdd:PRK03918   375 ERLKKRLTGLTPeklekeleelekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TE 447
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  547 DNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvSGLQKVVLDVL 626
Cdd:PRK03918   448 EHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEEL 520
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  627 RHALSWLEEVEQLLRDLgilpsspnKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLRE 696
Cdd:PRK03918   521 EKKAEEYEKLKEKLIKL--------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEE 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  697 HLAEKEKLNEERLE---QEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEK 773
Cdd:PRK03918   593 RLKELEPFYNEYLElkdAEKELEREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185  774 NRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLEN 828
Cdd:PRK03918   672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE 725
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
690-814 7.17e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 7.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   690 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtleeerkrMQEL-ESLLAQQKKALAKS 768
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE--------LEDCdPTELDRAKEKLKKL 216
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1034555185   769 ITQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 814
Cdd:smart00787  217 LQEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
 
Name Accession Description Interval E-value
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
19-114 4.86e-51

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 174.75  E-value: 4.86e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700      1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
                           90
                   ....*....|....*..
gi 1034555185   98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700     80 VLRFGFGGLPYELVVDN 96
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
35-101 1.48e-18

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 81.08  E-value: 1.48e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185   35 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 101
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
663-1205 7.03e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 7.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  663 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  738 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 816
Cdd:COG1196    293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  817 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:COG1196    369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  897 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 971
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  972 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1034
Cdd:COG1196    526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1035 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1107
Cdd:COG1196    606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1108 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1187
Cdd:COG1196    686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
                          570
                   ....*....|....*...
gi 1034555185 1188 RQKKALSELRARIKELEK 1205
Cdd:COG1196    764 ELERELERLEREIEALGP 781
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
28-109 1.18e-17

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 79.24  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd00060     14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90

                   ..
gi 1034555185  108 YE 109
Cdd:cd00060     91 FE 92
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
29-110 4.49e-17

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 77.69  E-value: 4.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   29 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:COG1716     16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92

                   ...
gi 1034555185  108 YEL 110
Cdd:COG1716     93 FRL 95
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
292-1080 6.06e-15

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: 80.50  E-value: 6.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  292 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 370
Cdd:TIGR02169  233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  371 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 450
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  451 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 530
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  531 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 605
Cdd:TIGR02169  455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  606 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLI 659
Cdd:TIGR02169  527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLV 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  660 YLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEK---LREHLAEKEKL-------NEERLEQEEKLKAKIRQLTEEKAAL 729
Cdd:TIGR02169  607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAmtggsraPRGGILFSRSEPAELQRLRERLEGL 686
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  730 E---EYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 806
Cdd:TIGR02169  687 KrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  807 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 886
Cdd:TIGR02169  766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  887 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 966
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  967 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1046
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1034555185 1047 QEVIMKLRKDLTEAHSRMSDLRGelnEKQKMELE 1080
Cdd:TIGR02169  971 EPVNMLAIQEYEEVLKRLDELKE---KRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
308-1002 7.04e-14

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: 77.02  E-value: 7.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  308 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 467
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 546
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  547 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 616
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  617 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 665
Cdd:TIGR02168  535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  666 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 711
Cdd:TIGR02168  615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  712 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 791
Cdd:TIGR02168  690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  792 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 871
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  872 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 951
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  952 SqrhgFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 1002
Cdd:TIGR02168  898 E----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
261-970 7.22e-14

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: 77.02  E-value: 7.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYsKVLCQTLSE 340
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  341 RNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKD-----EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELesKLDELAEElaeleEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  414 ELKQE----DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAEL-----RKSCTEQSVISRTLREKSKVEEKLQEDSRRK 484
Cdd:TIGR02168  380 QLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERL 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  485 LLQLQEMGNRESVIKINLERAVGQLEHFRSQV--IKATYGRAKPFRD--KPVTDQQL-IEKITQVTEDNINFQqKKWTLQ 559
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLdsLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD-EGYEAA 538
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  560 KETQLSNSKQEETTEN-------IEKLRTSLDSCQACMKISCCSHDlKKEVDLLQHLQVSPPVSG-----------LQKV 621
Cdd:TIGR02168  539 IEAALGGRLQAVVVENlnaakkaIAFLKQNELGRVTFLPLDSIKGT-EIQGNDREILKNIEGFLGvakdlvkfdpkLRKA 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  622 VLDVLRHaLSWLEEVEQLLRDLGILPSSPN----------KGFSLY----------------LIYLLEHYKKLMSQAQEL 675
Cdd:TIGR02168  618 LSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrreIEELEEKIEELEEKIAEL 696
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  676 QIKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTE-------EKAALEEYITQERNR------A 740
Cdd:TIGR02168  697 EKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTELEAEIEELEERleeaeeE 776
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  741 KETLEEERkrmQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK 820
Cdd:TIGR02168  777 LAEAEAEI---EELEAQIEQLKEELKAL--------REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  821 RKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT 900
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  901 KATESLKAESLALKLNETLAELettktkmimvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ 970
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERL----------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
37-110 3.96e-13

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438756 [Multi-domain]  Cd Length: 102  Bit Score: 66.57  E-value: 3.96e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185   37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22704     21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
29-109 3.41e-12

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 63.79  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   29 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 105
Cdd:cd22665     16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93

                   ....
gi 1034555185  106 LTYE 109
Cdd:cd22665     94 CQYV 97
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
29-103 6.81e-12

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 62.71  E-value: 6.81e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185   29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 103
Cdd:cd22693     13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
690-1409 2.26e-11

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: 68.93  E-value: 2.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  690 LQEKLREH-----LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQernraketLEEERKRMQELESLLAQQKKA 764
Cdd:TIGR02168  218 LKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--------LEELRLEVSELEEEIEELQKE 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  765 LaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYE 844
Cdd:TIGR02168  290 L-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  845 krkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNET-LAELE 923
Cdd:TIGR02168  369 ---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  924 TTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQK----------VTQHHKKIE 993
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkaLLKNQSGLS 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  994 GEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmAYEHL-----------------IDDLLAAQKEILSQ 1046
Cdd:TIGR02168  520 GILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-AIAFLkqnelgrvtflpldsikGTEIQGNDREILKN 596
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1047 QEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKMELEQNVV----------------------LVQQQS 1090
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktnsSILERR 676
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1091 KELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTEKEQKPRKKTQTcDTSVQIEPVHTEAFSSSQEQQSF 1170
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSK 754
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1171 SDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKpdlptLSRIEI 1250
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLES 828
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1251 LAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSKTLGSLMNIKnMSGHVSMKYLSRQEREKVNQLRQRD 1325
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEELSEELRELE 907
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1326 ldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQVAKLEDDIYKEAEEKALLKEA-LERMEHQLcqeKR 1404
Cdd:TIGR02168  908 -----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRL---KR 976

                   ....*
gi 1034555185 1405 INRAI 1409
Cdd:TIGR02168  977 LENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
303-869 3.92e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 3.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  303 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 382
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  383 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 462
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  463 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 542
Cdd:COG1196    377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 618
Cdd:COG1196    446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  619 QKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSL-----YLIYLLEHYKKLMSQAQELQIK-FNSSQETQQSLLQE 692
Cdd:COG1196    519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRaRAALAAALARGAIG 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  693 KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 772
Cdd:COG1196    599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  773 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 852
Cdd:COG1196    679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
                          570
                   ....*....|....*..
gi 1034555185  853 EKEKKKVQDLENRLTKQ 869
Cdd:COG1196    759 PPDLEELERELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
692-1150 6.71e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 770
Cdd:PTZ00121  1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  771 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 850
Cdd:PTZ00121  1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  851 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 930
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  931 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 1010
Cdd:PTZ00121  1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1011 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1090
Cdd:PTZ00121  1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1091 kelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1150
Cdd:PTZ00121  1785 -----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
684-987 9.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 9.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLlqEKLREHLAEKEKlNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQK 762
Cdd:COG1196    183 ATEENL--ERLEDILGELER-QLEPLERQAEKAERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  763 KALAKsITQEKNRVKEALEEEQTRVQEL---EERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISEs 839
Cdd:COG1196    260 AELAE-LEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  840 niayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 919
Cdd:COG1196    338 ----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185  920 AELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 987
Cdd:COG1196    414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
34-102 1.24e-10

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 59.43  E-value: 1.24e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185   34 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22683     22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
254-796 1.26e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  254 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 333
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  334 LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  414 ELKQEDAHRELREAQEKELKL----CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 489
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  490 EMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQLIEKITQVTEDNINFQQKKWTLQkETQLS 565
Cdd:COG1196    467 ELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL-EAALA 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  566 NSKQEETTEN-------IEKLRTSLDSCQACMKIScCSHDLKKEVDLLQHLQVSPPVSGLQkvVLDVLRHALSWLEEVEQ 638
Cdd:COG1196    546 AALQNIVVEDdevaaaaIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDTL 622
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  639 LLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAK 718
Cdd:COG1196    623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185  719 IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksITQEKNRVKEALEEEQTRVQELEERLAR 796
Cdd:COG1196    703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--EALEELPEPPDLEELERELERLEREIEA 778
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
230-985 2.00e-10

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 65.76  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK-KKLESERLSSAAKLKEEELELKSE 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  390 LKSQNKDKDHQLEALGSRCSVL-KEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR 468
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEkKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  469 EKSKVEEK---LQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKIT 542
Cdd:pfam02463  483 QEQLELLLsrqKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV 622
Cdd:pfam02463  563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  623 -----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 697
Cdd:pfam02463  643 akesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  698 LAEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKN 774
Cdd:pfam02463  723 LADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  775 RvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEK 854
Cdd:pfam02463  803 L-RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELE 880
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  855 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 934
Cdd:pfam02463  881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  935 RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 985
Cdd:pfam02463  961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
250-999 3.74e-10

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: 64.70  E-value: 3.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  250 LGKEVSRLSDYEIESKYKDviIANLQNEVAELSQKVSEtttSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKG 329
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEK--IGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  330 YSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDI--------------LAKDEQVQQLKEEVSHLKSQNK 395
Cdd:TIGR02169  352 RDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreinelkrelDRLQEELQRLSEELADLNAAIA 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  396 DKDHQLEALGSRCSVLKEELKQEDAHRE----LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS 471
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  472 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-----------------RSQVIKATYGRAKPFRDKPVTD 534
Cdd:TIGR02169  511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDL 590
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  535 QQLIEK-ITQVTEDNINFQQK-----KWTLQkETQLsnskqeetTENIEKLRTSLDSCQAcmkisccshdLKKEVDLLQH 608
Cdd:TIGR02169  591 SILSEDgVIGFAVDLVEFDPKyepafKYVFG-DTLV--------VEDIEAARRLMGKYRM----------VTLEGELFEK 651
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  609 lqvSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQikfnsSQETQQS 688
Cdd:TIGR02169  652 ---SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-----LQSELRRIENRLDELSQEL-----SDASRKI 718
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  689 LLQEKLREHLAEKEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYItQERNRAKETLEEERKRMQELESLLAQQKkalAK 767
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEARLSHSR---IP 794
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  768 SITQEKNRVKEALEEEQTRVQELEERLAR---QKEVLESSIAHEKRKAKEALESEKrkvqdlenhlTQQKEISESNIayE 844
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIK----------SIEKEIENLNG--K 862
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  845 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESlalkLNETLAELET 924
Cdd:TIGR02169  863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA----LEEELSEIED 938
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185  925 TKTKMIMVEERLILQQKMVKALQDEQESQRhGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATL 999
Cdd:TIGR02169  939 PKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
277-866 1.03e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  277 EVAELSQKVSETTTSRQNE------KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKN 350
Cdd:COG1196    210 EKAERYRELKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQA 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK 430
Cdd:COG1196    289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  431 ELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG1196    369 EA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  511 HFRSQVIKATygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacm 590
Cdd:COG1196    446 EAAEEEAELE------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----- 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  591 kisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILpsspnkgfSLYLIYLLEHYKKL 668
Cdd:COG1196    509 -------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVA--------AAAIEYLKAAKAGR 573
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  669 MSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEER 748
Cdd:COG1196    574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  749 KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEN 828
Cdd:COG1196    654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1034555185  829 HLTQQKEISESNIAYEkrKAKEAMEKEKKKVQDLENRL 866
Cdd:COG1196    734 REELLEELLEEEELLE--EEALEELPEPPDLEELEREL 769
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
36-110 1.32e-09

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 57.04  E-value: 1.32e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185   36 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22691     32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
36-102 2.23e-09

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 56.03  E-value: 2.23e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555185   36 TIGRHENSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22677     25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
720-1129 2.68e-09

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: 62.01  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  720 RQLTEEKAALEEYiTQERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKE 799
Cdd:TIGR02169  156 RKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKRE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  800 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQ-QKEISESNIAYEKRKAKeamekekkkVQDLENRLTKQKEELELKeq 878
Cdd:TIGR02169  223 YEGYELLKEKEALERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQL---------LEELNKKIKDLGEEEQLR-- 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  879 kedvLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFE 958
Cdd:TIGR02169  292 ----VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  959 EEIMEYKEQIKQHAQT---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDD 1035
Cdd:TIGR02169  368 DLRAELEEVDKEFAETrdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEE 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1036 LLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELK 1115
Cdd:TIGR02169  415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
                          410
                   ....*....|....
gi 1034555185 1116 ALEEALRASQEKHR 1129
Cdd:TIGR02169  494 EAEAQARASEERVR 507
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
35-82 3.68e-09

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 53.72  E-value: 3.68e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1034555185    35 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 82
Cdd:smart00240    1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
703-1138 4.33e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 4.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  703 KLNEERLEQEEKLKAkirqlTEEKAALEEYITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEA 779
Cdd:COG1196    169 KYKERKEEAERKLEA-----TEENLERLEDILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  780 LEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkv 859
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------- 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  860 QDLENRLTKQKEELelkeqkedvlnnklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQ 939
Cdd:COG1196    312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  940 QKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapm 1019
Cdd:COG1196    371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------- 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1020 tessakdMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEK 1099
Cdd:COG1196    442 -------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1034555185 1100 MAQMSSLVEKKDREL----KALEEALRASQEKHRLQLNTEKEQ 1138
Cdd:COG1196    515 LLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDE 557
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
28-109 8.94e-09

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 54.14  E-value: 8.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd22673     16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93

                   ..
gi 1034555185  108 YE 109
Cdd:cd22673     94 FE 95
PTZ00121 PTZ00121
MAEBL; Provisional
692-1133 9.68e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 9.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKAL---- 765
Cdd:PTZ00121  1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKAdelk 1411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  766 -----------AKSITQEKNRVKEALE--EEQTRVQELEERLARQKEVLESS-IAHEKRKAKEALE--SEKRKVQDLENH 829
Cdd:PTZ00121  1412 kaaaakkkadeAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKkaEEAKKADEAKKK 1491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  830 LTQ-QKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVlnnKLSDALAMVEETQKT----KATE 904
Cdd:PTZ00121  1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADELKKAEELKKAeekkKAEE 1568
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  905 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQK 984
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  985 VTQHHKkiEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKeilsqqevIMKLRKDLTEAHSRM 1064
Cdd:PTZ00121  1649 AEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKA 1718
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185 1065 SDLRG--ELNEKQKMELEQNVVLVQQQSKELSV---LKEKMAQMSSLVEKKDRELKA-----LEEALRASQEKHRLQLN 1133
Cdd:PTZ00121  1719 EELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRMEVD 1797
PTZ00121 PTZ00121
MAEBL; Provisional
667-1027 1.06e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  667 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA----KIRQLTEEKAALEEYITQERNRAKE 742
Cdd:PTZ00121  1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKADE 1514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  743 TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQElEERLARQKEVLESSIAHEKRKAKEALESEKRK 822
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  823 VQDLENHLTQQKEI--SESNIAYEKRKAKEAMEKEKKKVQDLEN--RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 898
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  899 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 978
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  979 EEKlQKVTQHHKKIEGEIATLKDNDPAPKEE--RPQDPLVAPMTESSAKDM 1027
Cdd:PTZ00121  1754 EEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
36-174 1.09e-08

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 59.00  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   36 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 110
Cdd:COG3456     29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185  111 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 174
Cdd:COG3456    102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
692-1129 1.68e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKsI 769
Cdd:PRK03918   234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELRE-I 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  770 TQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAK 849
Cdd:PRK03918   313 EKRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTG 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  850 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNE 917
Cdd:PRK03918   384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKR 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  918 TLAELETTKT-------------KMIMVEERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE----------------- 966
Cdd:PRK03918   464 IEKELKEIEEkerklrkelreleKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeiks 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  967 ------QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQ 1040
Cdd:PRK03918   544 lkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREE 618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1041 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKA 1116
Cdd:PRK03918   619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
                          490
                   ....*....|...
gi 1034555185 1117 LEEALRASQEKHR 1129
Cdd:PRK03918   699 LKEELEEREKAKK 711
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
37-102 2.37e-08

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 53.44  E-value: 2.37e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185   37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 102
Cdd:cd22724     25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
32-109 2.52e-08

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 53.00  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   32 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 105
Cdd:cd22670     21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99

                   ....
gi 1034555185  106 LTYE 109
Cdd:cd22670    100 FVYV 103
PTZ00121 PTZ00121
MAEBL; Provisional
699-1246 3.45e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 3.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  699 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQElesllAQQKKALAKSITQEKNRVKE 778
Cdd:PTZ00121  1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAE 1346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  779 ALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALE--SEKRKVQDLENHLTQQK----EISESNIAYEKRKAKEAM 852
Cdd:PTZ00121  1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKkkadELKKAAAAKKKADEAKKK 1426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  853 EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSDALAMVEETQKT-----KATESLKAESLALKLNETLAELETTKT 927
Cdd:PTZ00121  1427 AEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAKK 1504
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  928 KMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ-----HAQTIVSLEEKlQKVTQHHKKIEGEIATLKDN 1002
Cdd:PTZ00121  1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkKAEELKKAEEK-KKAEEAKKAEEDKNMALRKA 1583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1003 DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDLRGELNEKQKMELEQN 1082
Cdd:PTZ00121  1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1083 VVLVQQQSKElsvlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFS 1162
Cdd:PTZ00121  1661 IKAAEEAKKA----EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1163 SSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKA--RSPDHKDHQNESFLDLKNLRMENNVQKILLDAKP 1240
Cdd:PTZ00121  1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816

                   ....*.
gi 1034555185 1241 DLPTLS 1246
Cdd:PTZ00121  1817 GNLVIN 1822
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
37-110 4.22e-08

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 52.62  E-value: 4.22e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185   37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 110
Cdd:cd22725     25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
PTZ00121 PTZ00121
MAEBL; Provisional
678-1414 4.49e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 4.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  678 KFNSSQETQQSLLQEKLREHLAEKeKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESL 757
Cdd:PTZ00121  1099 KAEEAKKTETGKAEEARKAEEAKK-KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  758 LAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL--ESEKRKVQDLENHLTQQKe 835
Cdd:PTZ00121  1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdAEEAKKAEEERNNEEIRK- 1256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  836 ISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELElkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLALKL 915
Cdd:PTZ00121  1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA-----------KKAEEKKKADEAKK-KAEEAKKADEAKKKA 1324
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  916 NETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGE 995
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  996 IATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliddllaaqKEILSQQEVIMKLRKDLTEAhSRMSDLRGELNEKQ 1075
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAK 1470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1076 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1155
Cdd:PTZ00121  1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1156 VHT-----EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENN 1230
Cdd:PTZ00121  1551 LKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1231 VQKILLDAKPDLPTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYL 1310
Cdd:PTZ00121  1631 EKKKVEQLKKKEAE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1311 SRQEREKVNQLRQRDLDLVfDKITQLKNQ----LGRKEELLRGYEKDVEQLRRSKVSiEMYQSQVAKLEDDIYKEAEEKA 1386
Cdd:PTZ00121  1697 EAEEAKKAEELKKKEAEEK-KKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
                          730       740
                   ....*....|....*....|....*...
gi 1034555185 1387 LLKEALERMEHQLCQEKRINRAIRQQKE 1414
Cdd:PTZ00121  1775 KEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
34-102 4.95e-08

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 51.94  E-value: 4.95e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185   34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 102
Cdd:cd22694     17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
30-103 5.93e-08

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 51.98  E-value: 5.93e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185   30 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 103
Cdd:cd22678     20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
PTZ00121 PTZ00121
MAEBL; Provisional
692-1203 7.01e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEEKLKA--KIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKALAK 767
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKadAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAK 1384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  768 SITQEKNRVKEA---LEEEQTRVQELEERLARQKEVLESSI-AHEKRKAKEALE--SEKRKVQDLENHLTQQKEISESNI 841
Cdd:PTZ00121  1385 KKAEEKKKADEAkkkAEEDKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKK 1464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  842 AYEkrkakeamekekkkvqdlENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT-----KATESLKAESlALKLN 916
Cdd:PTZ00121  1465 KAE------------------EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAaeakkKADEAKKAEE-AKKAD 1525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  917 ETLAELETTKTKMIMVEERLILQQKMVKAlqdeqESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQhhKKIEGEI 996
Cdd:PTZ00121  1526 EAKKAEEAKKADEAKKAEEKKKADELKKA-----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVM 1598
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  997 ATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDL-RGELNEKQ 1075
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKK 1675
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1076 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1155
Cdd:PTZ00121  1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1034555185 1156 VHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKEL 1203
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
658-973 1.06e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 56.67  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  658 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 735
Cdd:pfam17380  274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  736 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 796
Cdd:pfam17380  345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  797 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 876
Cdd:pfam17380  425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  877 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 955
Cdd:pfam17380  496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
                          330
                   ....*....|....*....
gi 1034555185  956 GFEEEIM-EYKEQIKQHAQ 973
Cdd:pfam17380  572 EREREMMrQIVESEKARAE 590
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
6-103 1.47e-07

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438738 [Multi-domain]  Cd Length: 123  Bit Score: 51.51  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185    6 PCRLFIYGKTERMKAylksaeG--FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFV 81
Cdd:cd22686      3 PCIRVIVVESPSLQV------GslFIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYL 76
                           90       100
                   ....*....|....*....|....*..
gi 1034555185   82 NECHIQNVAVKLIP-----GDILRFGS 103
Cdd:cd22686     77 NGVRISQPKEKSDPyplthGDELKIGE 103
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
238-1115 1.70e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 56.13  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  238 LAQQDKDEIILLL-GKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKeisqkcQVLDEDIDAKQKEI 316
Cdd:pfam02463  138 LVQGGKIEIIAMMkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL------QELKLKEQAKKALE 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  317 QSLKSQISALQKGYSKV-----LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEvsHLK 391
Cdd:pfam02463  212 YYQLKEKLELEEEYLLYldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELK 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  392 SQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelRKSCTEQSVISRTLREKS 471
Cdd:pfam02463  290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQE 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  472 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLE-RAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtEDNIN 550
Cdd:pfam02463  367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI--ELKQG 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  551 FQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHlqvSPPVSGLQKVVLDVLRHAL 630
Cdd:pfam02463  445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE---SKARSGLKVLLALIKDGVG 521
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  631 SWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK---EKLNEE 707
Cdd:pfam02463  522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiaVLEIDP 601
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  708 RLEQEEKLKAKIRQLTEEKAAL-----EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEE 782
Cdd:pfam02463  602 ILNLAQLDKATLEADEDDKRAKvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  783 EQTRVQELE-----ERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKK 857
Cdd:pfam02463  682 QEKAESELAkeeilRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  858 KVQDLENRLTKQKEELELKEQKEDVLNN--KLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 935
Cdd:pfam02463  762 KEEEKSELSLKEKELAEEREKTEKLKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  936 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV--TQHHKKIEGEIATLKDNDPAPKEERpqd 1013
Cdd:pfam02463  842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKeeKEKEEKKELEEESQKLNLLEEKENE--- 918
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1014 pLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKEL 1093
Cdd:pfam02463  919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
                          890       900
                   ....*....|....*....|..
gi 1034555185 1094 SVLKEKMAQMSSLVEKKDRELK 1115
Cdd:pfam02463  998 ERLEEEKKKLIRAIIEETCQRL 1019
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
690-1000 1.77e-07

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: 56.23  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  690 LQEKLREHLAEKEKLNEERLE-------QEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELESLLAQQK 762
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRL 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  763 KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--N 840
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  841 IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLA 920
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  921 ELETTKTKMIMVEERLilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 1000
Cdd:TIGR02169  428 AIAGIEAKINELEEEK-------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
699-1067 2.41e-07

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: 55.46  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  699 AEKEKLNEErLEQEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELE-SLLAQQKKALAKSITQEKNRVk 777
Cdd:TIGR02169  170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQL- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  778 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRkakeamekekk 857
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER----------- 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  858 KVQDLENRLTKQKEELELKEQKEDVLNNKLsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMimveerli 937
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------- 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  938 lqqkmvKALQDEQESQRhgfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLva 1017
Cdd:TIGR02169  381 ------AETRDELKDYR----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-- 448
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1018 pmtESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDL 1067
Cdd:TIGR02169  449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
36-202 3.16e-07

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 54.30  E-value: 3.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354   27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354  100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
                          170
                   ....*....|....*.
gi 1034555185  187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354  179 EPTMVPPFVPLPAPEP 194
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
635-1407 3.39e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 54.98  E-value: 3.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  635 EVEQLLRDLGILPSSPN-------------------------KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL 689
Cdd:pfam02463  120 EVAELLESQGISPEAYNflvqggkieiiammkperrleieeeAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  690 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSI 769
Cdd:pfam02463  200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  770 TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAK 849
Cdd:pfam02463  280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  850 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTktkm 929
Cdd:pfam02463  360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE---- 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  930 imvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQT-IVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKE 1008
Cdd:pfam02463  436 ---EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETqLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1009 ERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1088
Cdd:pfam02463  513 LALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1089 QSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQ 1168
Cdd:pfam02463  593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1169 SFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDLPTLSRI 1248
Cdd:pfam02463  673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1249 EILAPQNGLCNARFGSAMEKSGKMDV----AEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ- 1323
Cdd:pfam02463  753 EKSRLKKEEKEEEKSELSLKEKELAEerekTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKe 832
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1324 --RDLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQ 1401
Cdd:pfam02463  833 eeLEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912

                   ....*.
gi 1034555185 1402 EKRINR 1407
Cdd:pfam02463  913 EEKENE 918
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
37-102 4.91e-07

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 49.60  E-value: 4.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185   37 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22676     25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
554-1146 6.51e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.20  E-value: 6.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  554 KKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISccsHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL 633
Cdd:TIGR00618  220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ---QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  634 EEVE-------QLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQIKFNSSQETQQsllQEKLREHLAEKEKLNE 706
Cdd:TIGR00618  297 AHIKavtqieqQAQRIHTELQSKMRS-----RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS---QEIHIRDAHEVATSIR 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  707 ERLEQEEKLKAKIRQLTEEKAALEEyitQERNRAKETLEEERKRMQELESLLA----QQKKALAKS---ITQEKNRVKEA 779
Cdd:TIGR00618  369 EISCQQHTLTQHIHTLQQQKTTLTQ---KLQSLCKELDILQREQATIDTRTSAfrdlQGQLAHAKKqqeLQQRYAELCAA 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  780 LEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIAYE-KRKAKEAMEK 854
Cdd:TIGR00618  446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavvLARLLELQEEPCPLCGSCIHPNpARQDIDNPGP 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  855 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 934
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  935 ----RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI-EGEIATLKDNDPAPKEE 1009
Cdd:TIGR00618  606 aedmLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKM 685
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1010 RPQDPLVAPMTESSA-KDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1088
Cdd:TIGR00618  686 QSEKEQLTYWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185 1089 QSKELSVLKEKMAQMSSLV----------EKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQT 1146
Cdd:TIGR00618  766 NNEEVTAALQTGAELSHLAaeiqffnrlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
8-109 6.56e-07

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 48.95  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185    8 RLFIYGKTERMKAYLKSAEgffvlnksTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQ 87
Cdd:cd22698      4 LIEQKGSEEGKDYELDQDE--------FTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVG 73
                           90       100
                   ....*....|....*....|..
gi 1034555185   88 NVAVKliPGDILRFGSAGLTYE 109
Cdd:cd22698     74 THELK--HGDRIQLGETIFRFI 93
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
35-108 7.74e-07

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 48.53  E-value: 7.74e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555185   35 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 108
Cdd:cd22684     23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
411-803 1.20e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRkllqLQE 490
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPER----LEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  491 MGNRESvikiNLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninFQQKKWTLQKETQLSNSKQE 570
Cdd:COG4717    151 LEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELE 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  571 ETTENIEKLRTSLDSCQACMKISCCSHDLK-------KEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL---------- 633
Cdd:COG4717    224 ELEEELEQLENELEAAALEERLKEARLLLLiaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLarekaslgke 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  634 ---------------EEVEQLLRDLGiLPSSPNKGFSLYLIYLLEHYKKLMSQAQELQikfnssQETQQSLLQEKLREHL 698
Cdd:COG4717    304 aeelqalpaleeleeEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELE------EELQLEELEQEIAALL 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  699 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA--------KETLEEERKRMQELESLLAQQKKALAKSIT 770
Cdd:COG4717    377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealdEEELEEELEELEEELEELEEELEELREELA 456
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1034555185  771 QEKNRVKEAleEEQTRVQELEERLARQKEVLES 803
Cdd:COG4717    457 ELEAELEQL--EEDGELAELLQELEELKAELRE 487
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
683-841 1.40e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  683 QETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQ----ELESLL 758
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEreleERERRR 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  759 AQQKKALAkSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiAHEKRKAKEALESEKRKVQDLENHLTQQKeise 838
Cdd:COG4913    362 ARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-LAEAEAALRDLRRELRELEAEIASLERRK---- 435

                   ...
gi 1034555185  839 SNI 841
Cdd:COG4913    436 SNI 438
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
256-839 1.44e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 53.30  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  256 RLSDYEIESKYKDVIIANLQNEVAELSQKVSETTtsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSK 332
Cdd:pfam12128  259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  333 VLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQV-QQLKEEVSHLKS----QNKDKDHQLEA---- 403
Cdd:pfam12128  337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  404 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 467
Cdd:pfam12128  417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-RSQVIKATYGRAKpfrdkpVTDQQLI-------E 539
Cdd:pfam12128  495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGK------VISPELLhrtdldpE 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  540 KITQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMK-ISCCSHDLKKEVDLLQhLQVSPPVSG 617
Cdd:pfam12128  569 VWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAaAEEQLVQANGELEKAS-REETFARTA 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  618 LQKVVLDVLRhalsWLEEVEQLLRDLgilpsspNKGfslyliyLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 697
Cdd:pfam12128  648 LKNARLDLRR----LFDEKQSEKDKK-------NKA-------LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK 709
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  698 LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRmqELESL---------LAQQKKALAKS 768
Cdd:pfam12128  710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRS----GAKAELKALETWYKR--DLASLgvdpdviakLKREIRTLERK 783
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185  769 ITQEKNRVKEALEEE---QTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHL----TQQKEISES 839
Cdd:pfam12128  784 IERIAVRRQEVLRYFdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSEN 861
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
670-846 1.72e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  670 SQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA---KIRQLTEEKAALEEYI---TQERNRAKET 743
Cdd:COG4942     20 DAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELaelEKEIAELRAE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  744 LEEERKRMQE-------------LESLLAQQ-------KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES 803
Cdd:COG4942     99 LEAQKEELAEllralyrlgrqppLALLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1034555185  804 SIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 846
Cdd:COG4942    179 LLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
235-806 2.01e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKcqvLDEDIDAKQK 314
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  315 EIQSLKSQISALQkgyskvlcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQN 394
Cdd:COG1196    324 ELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  395 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 474
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  475 EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGR-----AKPFRDKPVTDQQLIEKITQVTEDNI 549
Cdd:COG1196    473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  550 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHA 629
Cdd:COG1196    553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  630 LSWLEEVEQLLRDL--------GILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK 701
Cdd:COG1196    633 EAALRRAVTLAGRLrevtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  702 EKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE--------------RNRAKETLEEERKRMQELES--LLAQqkkal 765
Cdd:COG1196    713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELleeealeelpeppdLEELERELERLEREIEALGPvnLLAI----- 787
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1034555185  766 aksitqeknrvkEALEEEQTRVQELEErlarQKEVLESSIA 806
Cdd:COG1196    788 ------------EEYEELEERYDFLSE----QREDLEEARE 812
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
278-990 2.12e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.53  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  278 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 345
Cdd:pfam12128  203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  346 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 425
Cdd:pfam12128  283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERA 505
Cdd:pfam12128  357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  506 VGQLEhfrsqvIKATYGRAKPFRDKPVTDQQLIEKITqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 585
Cdd:pfam12128  437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  586 cQACMKISCCSHDLKKEVDLLQ--HLQVSPPVSGLqkvvLDVLR-HALSWLEEV------EQLLR---DLGILPSSPNKG 653
Cdd:pfam12128  503 -QASEALRQASRRLEERQSALDelELQLFPQAGTL----LHFLRkEAPDWEQSIgkvispELLHRtdlDPEVWDGSVGGE 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  654 FSLYLIyllehykklmsqaqelqikfnssqetqqsllqeklrehlaekeKLNEERLEqeeklkakirqlTEEKAALEEYI 733
Cdd:pfam12128  578 LNLYGV-------------------------------------------KLDLKRID------------VPEWAASEEEL 602
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  734 TQERNRAKETLEEERKRMQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAK 813
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKN 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  814 EALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAM 893
Cdd:pfam12128  671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLAL 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  894 VEETqKTKATESLKAESLALK--LNETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEY 964
Cdd:pfam12128  734 LKAA-IAARRSGAKAELKALEtwYKRDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRL 812
                          730       740
                   ....*....|....*....|....*.
gi 1034555185  965 KEQIKQHAQTIVSLEEKLQKVTQHHK 990
Cdd:pfam12128  813 ATQLSNIERAISELQQQLARLIADTK 838
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
28-108 3.58e-06

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 46.94  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 97
Cdd:cd22667     15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
                           90
                   ....*....|.
gi 1034555185   98 ILRFGSAGLTY 108
Cdd:cd22667     94 VITFGVLGSKF 104
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
252-828 4.20e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 4.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  252 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 331
Cdd:PRK03918   152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  332 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 411
Cdd:PRK03918   225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  412 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQ--EDSRRKLLQL 488
Cdd:PRK03918   299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  489 QEMGNRESVIKI----------------------NLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLiekitqvTE 546
Cdd:PRK03918   375 ERLKKRLTGLTPeklekeleelekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TE 447
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  547 DNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvSGLQKVVLDVL 626
Cdd:PRK03918   448 EHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEEL 520
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  627 RHALSWLEEVEQLLRDLgilpsspnKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLRE 696
Cdd:PRK03918   521 EKKAEEYEKLKEKLIKL--------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEE 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  697 HLAEKEKLNEERLE---QEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEK 773
Cdd:PRK03918   593 RLKELEPFYNEYLElkdAEKELEREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185  774 NRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLEN 828
Cdd:PRK03918   672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE 725
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
274-835 4.45e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.51  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  274 LQNEVAELSQKVSETTTSRQNEK--EISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLS---ERNSEITSL 348
Cdd:TIGR00618  272 LRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLH 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  349 KNEGENLKRDNAITSgmvsslqkdilaKDEQVQQLKEEVSHLKSQNKDKDH---QLEALGSRCSVLKEELKQEDAHRELR 425
Cdd:TIGR00618  352 SQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAF 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS------------------KVEEKLQEDSRRKL-L 486
Cdd:TIGR00618  420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkereqqlqtkeqihlQETRKKAVVLARLLeL 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  487 QLQEMGNRESVIKINLER-AVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLS 565
Cdd:TIGR00618  500 QEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  566 NskqeETTENIEKLRtsldscqacmkisccshdlkKEVDLLQHLqvsppvsglqkvVLDVLRHALSWLEEVEQLLRDLGI 645
Cdd:TIGR00618  580 N----RSKEDIPNLQ--------------------NITVRLQDL------------TEKLSEAEDMLACEQHALLRKLQP 623
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  646 LpsspnkgfslylIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLA----EKEKLNEERLEQEEKLKAKIRQ 721
Cdd:TIGR00618  624 E------------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvLPKELLASRQLALQKMQSEKEQ 691
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  722 LTEEKAALEEYITQERNRaKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR--QKE 799
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnnEEV 770
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1034555185  800 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 835
Cdd:TIGR00618  771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
314-1000 5.42e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.17  E-value: 5.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  314 KEIQSLKSQISALQKGYsKVLCQTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQ 393
Cdd:TIGR04523   40 KKLKTIKNELKNKEKEL-KNLDKNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  394 NKDKDHQLEALGSRCSVLKEELKQEDAH-------------------------RELREAQEKELKLCKTQIQDMEKEMKK 448
Cdd:TIGR04523  112 IKNDKEQKNKLEVELNKLEKQKKENKKNidkflteikkkekeleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDK 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  449 LRAELRKSCTEQSVIsrtlrekskveEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygrakpfr 528
Cdd:TIGR04523  192 IKNKLLKLELLLSNL-----------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---------- 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  529 dkpvTDQQLIEKITQVTEDNINFQQKkwtlQKETQLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDllqh 608
Cdd:TIGR04523  251 ----TQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEIS-------------DLNNQKE---- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  609 lqvsppvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSlyliyllehykKLMSQAQELQIKFNSSQETQQS 688
Cdd:TIGR04523  306 --------------QDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSE 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  689 llqekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtLEEERKRMQELESLLAQQKKALAKS 768
Cdd:TIGR04523  361 -----KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIERLKET 434
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  769 ITQEKNRVKEaLEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNiayekrka 848
Cdd:TIGR04523  435 IIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------- 505
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  849 keamekekkkvQDLENRLTKQKEELELKEQKEDVLNNklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTK 928
Cdd:TIGR04523  506 -----------KELEEKVKDLTKKISSLKEKIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDE 565
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555185  929 MIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 1000
Cdd:TIGR04523  566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
30-102 5.75e-06

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438731 [Multi-domain]  Cd Length: 126  Bit Score: 46.88  E-value: 5.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   30 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 98
Cdd:cd22679     21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98

                   ....
gi 1034555185   99 LRFG 102
Cdd:cd22679     99 VQFG 102
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
660-792 7.86e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.60  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  660 YLLEHYKKLMSQAQElqiKFN---SSQETQQSLLQEKLREH---LAEKEKLNEERLEQEEKLKAKIRQLteeKAALEEYI 733
Cdd:PRK00409   502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185  734 TQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQEKNRVKEALEEEQTRVQELEE 792
Cdd:PRK00409   576 QQAIKEAKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKE 632
PRK11637 PRK11637
AmiB activator; Provisional
671-843 8.27e-06

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 50.08  E-value: 8.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  671 QAQELQIKFnSSQETQQSllqEKLrehLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKR 750
Cdd:PRK11637   138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELE----EKQSQQKTLLYEQQAQ 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  751 MQELESLLAQQKKALAKsitqeknrVKEALEEEQTRVQELeerlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENh 829
Cdd:PRK11637   207 QQKLEQARNERKKTLTG--------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD- 272
                          170
                   ....*....|....
gi 1034555185  830 ltQQKEISESNIAY 843
Cdd:PRK11637   273 --KQKQAKRKGSTY 284
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
378-1000 8.93e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  378 EQVQQLKEEVSHLKSQ---NKDKDHQLEalgsrcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELR 454
Cdd:COG1196    213 ERYRELKEELKELEAElllLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  455 KscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResvikinLERAVGQLEHFRSQVIKATygrakpfrdkpvtd 534
Cdd:COG1196    285 E-------AQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEELEELE-------------- 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  535 QQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTsldscqacmkisccshDLKKEVDLLQHLQVspp 614
Cdd:COG1196    337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----------------LAEELLEALRAAAE--- 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  615 vsgLQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnkgfslyliyllehykklmsQAQELQIKFNSSQETQQSLLQEKL 694
Cdd:COG1196    398 ---LAAQLEELEEAEEALLERLERLEEEL---------------------------EELEEALAELEEEEEEEEEALEEA 447
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  695 REHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE-- 772
Cdd:COG1196    448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAva 527
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  773 -----KNRVKEALEEE-----QTRVQELEERLARQKEVLESS-------IAHEKRKAKEALESEKRK-VQDLENHLTQQK 834
Cdd:COG1196    528 vligvEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARgAIGAAVDLVASD 607
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  835 EISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALK 914
Cdd:COG1196    608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  915 LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEG 994
Cdd:COG1196    688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767

                   ....*.
gi 1034555185  995 EIATLK 1000
Cdd:COG1196    768 ELERLE 773
PTZ00121 PTZ00121
MAEBL; Provisional
696-1417 1.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  696 EHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 775
Cdd:PTZ00121  1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  776 VKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKE 855
Cdd:PTZ00121  1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  856 KKKVQDLENRLTKQKEELELKEQKEdvlnnklsdalaMVEETQKTKATESLKAEslalklnetlaELETTKTKMIMVEER 935
Cdd:PTZ00121  1240 EEAKKAEEERNNEEIRKFEEARMAH------------FARRQAAIKAEEARKAD-----------ELKKAEEKKKADEAK 1296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  936 LILQQKMVKALQDEQESQRHGfeEEIMEYKEQIKQHAqtivsleEKLQKVTQHHKKiegeiatlKDNDPAPKEERPQDPL 1015
Cdd:PTZ00121  1297 KAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKA-------DAAKKKAEEAKK--------AAEAAKAEAEAAADEA 1359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1016 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1095
Cdd:PTZ00121  1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1096 lKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGV 1175
Cdd:PTZ00121  1439 -KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1176 RCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKIlldakpdlptlsrieilapqn 1255
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------------------- 1566
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1256 glcnarfgsAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQRDLDLVFDKITQ 1335
Cdd:PTZ00121  1567 ---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1336 LKNQlgRKEEllrgyEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKEP 1415
Cdd:PTZ00121  1638 LKKK--EAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710

                   ..
gi 1034555185 1416 SA 1417
Cdd:PTZ00121  1711 EA 1712
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
36-103 1.41e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 44.94  E-value: 1.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185   36 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 103
Cdd:pfam16697   20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
701-1396 1.41e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  701 KEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYITQErnraketlEEERKRMQELESLLAQQKKALaKSITQEKNRVKEA 779
Cdd:PRK03918   152 RQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRT--------ENIEELIKEKEKELEEVLREI-NEISSELPELREE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  780 LEEEQTRVQELEER------LARQKEVLESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKE 850
Cdd:PRK03918   223 LEKLEKEVKELEELkeeieeLEKELESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSE 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  851 AMEKEKKKVQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMI 930
Cdd:PRK03918   301 FYEEYLDELREIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLE 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  931 MVEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEE 1009
Cdd:PRK03918   356 ELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1010 RPQDPLV-APMTESSAKDMAYEHLIDdllaaqkeilsqqevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQnvvlvqq 1088
Cdd:PRK03918   435 KGKCPVCgRELTEEHRKELLEEYTAE---------------LKRIEKELKEIEEKERKLRKELRELEKVLKKE------- 492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1089 qsKELSVLKEKMAQMSSLVEK-KDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQtcdtsvqiepvhteafsssqeq 1167
Cdd:PRK03918   493 --SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL---------------------- 548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1168 qsfsdlgvrckgsrheEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRmennvqkilldakpdlptlSR 1247
Cdd:PRK03918   549 ----------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ER 593
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1248 IEILAPQNGLCNARFGSAMEKSGKMDVAEALELS-EKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ--R 1324
Cdd:PRK03918   594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsR 673
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555185 1325 DLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKE-ALERME 1396
Cdd:PRK03918   674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVG 746
COG5022 COG5022
Myosin heavy chain [General function prediction only];
242-844 1.56e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 49.69  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  242 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQNEVAELSQKVSEtttsrqnekeisqkcqvLDEDIdakqKEIQSLKS 321
Cdd:COG5022    843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  322 QISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRdnAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQL 401
Cdd:COG5022    900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  402 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG5022    978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  482 RRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK--PFRDKPVTDQQLIEKITQVteDNINFQQKKWTLQ 559
Cdd:COG5022   1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  560 KETQLSNSKQEETTENIEKLRTSLDSCQACMkisccshdlkKEVDLLQHLQVSPPVSGLQKV------VLDVLRHALSwl 633
Cdd:COG5022   1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGL----------FWEANLEALPSPPPFAALSEKrlyqsaLYDEKSKLSS-- 1196
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  634 EEVEQLLRDLGILPS-----SPNKGFSLYLI---YLLEHYKKLMSQAQELQIKFnssqETQQSLLQEKLREHLAEKEKLN 705
Cdd:COG5022   1197 SEVNDLKNELIALFSkifsgWPRGDKLKKLIsegWVPTEYSTSLKGFNNLNKKF----DTPASMSNEKLLSLLNSIDNLL 1272
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  706 EERLEQEEKLKAKIRQLTEEKAAL--EEYITQERNRAKETLEEERKRMQELESllaqqkkalaKSITQEKNRVKEALEee 783
Cdd:COG5022   1273 SSYKLEEEVLPATINSLLQYINVGlfNALRTKASSLRWKSATEVNYNSEELDD----------WCREFEISDVDEELE-- 1340
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555185  784 qtrvqELEERlARQKEVLESSIAH--EKRKAKEALES-------EKRKVQDLENHLTQQ--KEISESNIAYE 844
Cdd:COG5022   1341 -----ELIQA-VKVLQLLKDDLNKldELLDACYSLNPaeiqnlkSRYDPADKENNLPKEilKKIEALLIKQE 1406
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
684-1144 1.63e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLLQEKLREHLAEKE------KLNEerLEQEEK-LKAKIRQLTEEKaaleEYITQERNRAKETLEEERKRMQELES 756
Cdd:PRK02224   182 LSDQRGSLDQLKAQIEEKEekdlheRLNG--LESELAeLDEEIERYEEQR----EQARETRDEADEVLEEHEERREELET 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  757 LLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLT 831
Cdd:PRK02224   256 LEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRV 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  832 QQKEISESNIAYEKRKAKEAM--EKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVE--ETQKTKATESLk 907
Cdd:PRK02224   336 AAQAHNEEAESLREDADDLEEraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFL- 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  908 aESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 980
Cdd:PRK02224   415 -EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  981 KLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEIL-SQQEVIMKL 1053
Cdd:PRK02224   490 EVEEVEERLeraedlVEAEDRIERLEER---------------------------REDLEELIAERRETIeEKRERAEEL 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1054 RKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KMAQMSSLVEKKDRELKALEEALRASQEK 1127
Cdd:PRK02224   543 RERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
                          490
                   ....*....|....*..
gi 1034555185 1128 HRLQLNTEKEQKPRKKT 1144
Cdd:PRK02224   622 NDERRERLAEKRERKRE 638
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
230-949 1.74e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.58  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKyKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463  353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEitsLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463  432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELE---LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  390 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEmkKLRAELRKSCTEQSVISRTLRE 469
Cdd:pfam02463  509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPK 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  470 KSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNI 549
Cdd:pfam02463  587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  550 NFQQKKWTLqKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQhLQVSPPVSGLQKVVLDVLRHA 629
Cdd:pfam02463  667 SLSELTKEL-LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQK 744
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  630 LSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKfnssqetQQSLLQEKLREHLAEKEKLNEERL 709
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELL 817
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  710 EQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 789
Cdd:pfam02463  818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  790 LEErlarQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQ 869
Cdd:pfam02463  898 EKK----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  870 KEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 949
Cdd:pfam02463  974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
29-102 1.92e-05

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 44.64  E-value: 1.92e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185   29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22680     16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
442-782 1.94e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.16  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  442 MEKEMKKLRAELRKSctEQSVISRTLREKSKVE-----EKLQEDSRRKLLQLQemgnresvikINLERAVGQLEHFRSqv 516
Cdd:PRK05771     2 APVRMKKVLIVTLKS--YKDEVLEALHELGVVHiedlkEELSNERLRKLRSLL----------TKLSEALDKLRSYLP-- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  517 ikatYGRAKPFRDKPVTDQQLiEKITQVTEDNINfqqkkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkisccs 596
Cdd:PRK05771    68 ----KLNPLREEKKKVSVKSL-EELIKDVEEELE------KIEKEI-------KELEEEISELENEIKELEQ-------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  597 hdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDVLRHALswLEEVEQLLRDLGILPSSPNKGFSLY-LIYLLEHYKKLMS 670
Cdd:PRK05771   122 --EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPEDK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEE 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  671 QAQELQIKFNSSQEtqQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK---ETLEEE 747
Cdd:PRK05771   196 ELKKLGFERLELEE--EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTD 273
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034555185  748 R----------KRMQELESLLaqqKKALAKSITQEKNRVKEALEE 782
Cdd:PRK05771   274 KtfaiegwvpeDRVKKLKELI---DKATGGSAYVEFVEPDEEEEE 315
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
32-104 1.94e-05

forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438754 [Multi-domain]  Cd Length: 123  Bit Score: 45.49  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   32 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 100
Cdd:cd22702     31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108

                   ....
gi 1034555185  101 FGSA 104
Cdd:cd22702    109 FGSD 112
PLN02939 PLN02939
transferase, transferring glycosyl groups
702-989 2.80e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 48.74  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  702 EKLNEERLEQEEKLKAKiRQLTEEKaaLEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEA 779
Cdd:PLN02939   106 EAIAAIDNEQQTNSKDG-EQLSDFQ--LEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSET 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  780 LE------EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAY 843
Cdd:PLN02939   183 DAriklaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKL 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  844 EKrkakeAMEKEKKKVQDLENRLTKQKE-ELELKEQKEDVLNNKLSDALAMVEETQKtkateslKAESLAL--------- 913
Cdd:PLN02939   263 EK-----ERSLLDASLRELESKFIVAQEdVSKLSPLQYDCWWEKVENLQDLLDRATN-------QVEKAALvldqnqdlr 330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  914 ----KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 989
Cdd:PLN02939   331 dkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
662-1206 3.12e-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: 48.90  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITqERNRAK 741
Cdd:TIGR02168  202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  742 ETLEEERKRMQELESLLA---QQKKALAKSITQ---EKNRVKEALEEEQTRVQELEERLARQKEVLESsIAHEKRKAKEA 815
Cdd:TIGR02168  281 EEIEELQKELYALANEISrleQQKQILRERLANlerQLEELEAQLEELESKLDELAEELAELEEKLEE-LKEELESLEAE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  816 LESEKRKVQDLENHLTQQKEISE---SNIAYEKRKAKEAM---EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSD 889
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLE--EAELKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  890 ALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEE--EIMEYKEQ 967
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSG 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  968 IKQH---AQTIVSLEEKLQK-------------VTQHHKKIEGEIATLKDN--------------DPAPKEERPQDPLVA 1017
Cdd:TIGR02168  518 LSGIlgvLSELISVDEGYEAaieaalggrlqavVVENLNAAKKAIAFLKQNelgrvtflpldsikGTEIQGNDREILKNI 597
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1018 PMTESSAKDM-----AYEHLIDDLLA------------------------------------------------------ 1038
Cdd:TIGR02168  598 EGFLGVAKDLvkfdpKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrr 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1039 -----------AQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM-------------ELEQNVVLVQQQSKELS 1094
Cdd:TIGR02168  678 eieeleekieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdlarleaEVEQLEERIAQLSKELT 757
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1095 VLKEKMAQMSSLVEKKDRELKALE---EALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFS 1171
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1034555185 1172 DLGVRCKGS--RHEEVIQRQKKALSELRARIKELEKA 1206
Cdd:TIGR02168  838 RRLEDLEEQieELSEDIESLAAEIEELEELIEELESE 874
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
271-833 3.60e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  271 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 346
Cdd:TIGR04523  147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  347 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELRE 426
Cdd:TIGR04523  222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  427 AQEKE--LKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLER 504
Cdd:TIGR04523  302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  505 AVGQLEHFRSQVikatygrakpfrdkpvtdQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 584
Cdd:TIGR04523  382 YKQEIKNLESQI------------------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  585 scqacmkisccshDLKKEVDLLqhlqvsppvsglqkvvldvlrhalswleevEQLLRDLGILPSSPNKGFSLYLIylleH 664
Cdd:TIGR04523  444 -------------DLTNQDSVK------------------------------ELIIKNLDNTRESLETQLKVLSR----S 476
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  665 YKKLMSQAQELQIKFNSSQETQQSLLQEK--LREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAK 741
Cdd:TIGR04523  477 INKIKQNLEQKQKELKSKEKELKKLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKK 556
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  742 ETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAK---EALES 818
Cdd:TIGR04523  557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-----KEKKISSLEKELEKAKkenEKLSS 631
                          570
                   ....*....|....*
gi 1034555185  819 EKRKVQDLENHLTQQ 833
Cdd:TIGR04523  632 IIKNIKSKKNKLKQE 646
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
271-509 3.77e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  271 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 350
Cdd:COG4942     29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  351 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 423
Cdd:COG4942     98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  424 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESVIKINLE 503
Cdd:COG4942    175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249

                   ....*.
gi 1034555185  504 RAVGQL 509
Cdd:COG4942    250 ALKGKL 255
PTZ00121 PTZ00121
MAEBL; Provisional
667-1002 3.82e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  667 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEE 746
Cdd:PTZ00121  1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  747 ERKRMQELESLLAQQKKALAKSItqEKNRVKEALEEEQTRVQELEERLARQKEvlESSIAHEKRKAKEalesEKRKVQDL 826
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEE----EKKKVEQL 1638
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  827 ENHLTQQKEISES-NIAYEKRKAKEAMEKEKkkvQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATES 905
Cdd:PTZ00121  1639 KKKEAEEKKKAEElKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  906 LKAESLALKLNETLAELETTKTKmimVEERlilQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 985
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKE---AEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
                          330
                   ....*....|....*..
gi 1034555185  986 TQHHKKIEGEIATLKDN 1002
Cdd:PTZ00121  1790 EKRRMEVDKKIKDIFDN 1806
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
691-866 4.40e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  691 QEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernrakETLEEERKRMQELESLLAQQKKALAksIT 770
Cdd:COG4717     62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLP--LY 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  771 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 850
Cdd:COG4717    132 QELEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
                          170
                   ....*....|....*.
gi 1034555185  851 AMEKEKKKVQDLENRL 866
Cdd:COG4717    207 RLAELEEELEEAQEEL 222
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
681-842 5.55e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  681 SSQETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQE---- 753
Cdd:COG3883     26 SELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAeaeAEIEERREELGERARALYRsggs 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  754 ----------------------LESLLAQQKKALA--KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 809
Cdd:COG3883    102 vsyldvllgsesfsdfldrlsaLSKIADADADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQ 180
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034555185  810 RKAKEALESEKRKVQDLENHLTQQKEISESNIA 842
Cdd:COG3883    181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
692-814 7.68e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.16  E-value: 7.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHLAEKEKLNEERLEQEE-----KLKAKIRQLTEEKAALEEYITqernRAKETLEEERKRMQELESLLAQQKKALA 766
Cdd:COG2433    383 EELIEKELPEEEPEAEREKEHEereltEEEEEIRRLEEQVERLEAEVE----ELEAELEEKDERIERLERELSEARSEER 458
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185  767 KSITQEK---------NRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKE 814
Cdd:COG2433    459 REIRKDReisrldreiERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
34-106 8.16e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 42.84  E-value: 8.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555185   34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 106
Cdd:cd22668     19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
666-838 8.70e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  666 KKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqltEEKAAleeyitQERNRAKETLE 745
Cdd:PRK09510    83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAA------KAAAAAKAKAE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  746 EERKRMQELESLLAQQKKALAKSITQEKN------------RVKEALEEEQTRVQELEER---LARQKEVLESSIAHEKR 810
Cdd:PRK09510   151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeakkkaeaeaAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKA 230
                          170       180
                   ....*....|....*....|....*...
gi 1034555185  811 KAKEALESEKRKVQDLENHLTQQKEISE 838
Cdd:PRK09510   231 AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
683-819 1.04e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  683 QETQQSLLQEKLREHLAEKEKLNEERLE----QEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEE-ERKRMQELESL 757
Cdd:COG4913    307 LEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAAlGLPLPASAEEF 382
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  758 LAQQK--KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLE------SSIAHEKRKAKEALESE 819
Cdd:COG4913    383 AALRAeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEA 452
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
36-109 1.18e-04

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 42.45  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   36 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 106
Cdd:cd22697     21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98

                   ...
gi 1034555185  107 TYE 109
Cdd:cd22697     99 RYQ 101
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
367-1074 1.40e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.50  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  367 SSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKLCKTQIQDMEKE 445
Cdd:TIGR00618  162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQS 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  446 MKKLRAE---------LRKSCTEQSVISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRS 514
Cdd:TIGR00618  242 HAYLTQKreaqeeqlkKQQLLKQLRARIEELRAQEAVLEETQEriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  515 QVIKATYGRAKPFRDK-PVTDQQLIEKITQVTEDNINFQQKKWTLQKETQlsnSKQEETTENIEKLRTSLDSCQACMKIS 593
Cdd:TIGR00618  322 SRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS---CQQHTLTQHIHTLQQQKTTLTQKLQSL 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  594 CCSHD------------LKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSwLEEVEQLLRDLGILPSSPNKGFSLYLIYL 661
Cdd:TIGR00618  399 CKELDilqreqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQT 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQE--EKLKAKIRQLTEEKAALEEYITQERNR 739
Cdd:TIGR00618  478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQ 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  740 AKEtLEEERKRMQELESLLAQQKKALAKSI---TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSI------AHEKR 810
Cdd:TIGR00618  558 RAS-LKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvrLHLQQ 636
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  811 KAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDA 890
Cdd:TIGR00618  637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  891 LAMVEETQKTKATESLKAESLALKLNETLAELEtTKTKMIMVEERLILQQKMVKALQDEQESQRhgFEEEIMEYKEQIKQ 970
Cdd:TIGR00618  717 DREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAE--LSHLAAEIQFFNRL 793
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  971 HAQTIVSLEEKLQKVTQHHKKIEGeIATLKDNDPAPKEERPQDPLvapmtessAKDMAYEHLIDDLLAAQKEILSQQEVI 1050
Cdd:TIGR00618  794 REEDTHLLKTLEAEIGQEIPSDED-ILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQL 864
                          730       740
                   ....*....|....*....|....
gi 1034555185 1051 MKLRKDLTEAHSRMSDLRGELNEK 1074
Cdd:TIGR00618  865 TQEQAKIIQLSDKLNGINQIKIQF 888
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
658-1145 1.41e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.64  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  658 LIYLLEHYKKLMSQAQElQIKFNSSQETQQSLLQEKLREHLA------EKEKLNEERLEQEEKLKAK-IRQLTEEKAALE 730
Cdd:pfam05483  259 LTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKtICQLTEEKEAQM 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  731 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS------ITQEKNRVKEALEEEQTRVQELEERLARQKEVL--E 802
Cdd:pfam05483  338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILaeD 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  803 SSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 882
Cdd:pfam05483  418 EKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  883 L---NNKLS-DALAMVEETQKTKA--TESLKAESLALKLNETLAELETT-KTKMIMVEERLILQQKMVKALQDEQESQRH 955
Cdd:pfam05483  497 LlleNKELTqEASDMTLELKKHQEdiINCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENAR 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  956 GFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPM--TESSAKDMAYEHLI 1033
Cdd:pfam05483  577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKleLELASAKQKFEEII 656
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1034 DDLlaaQKEILSQQEVIMKLRKDLTEAHSRMSD---LRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKK 1110
Cdd:pfam05483  657 DNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1034555185 1111 DRELKALEEAL-------RASQEKHRLQLNTEKEQKPRKKTQ 1145
Cdd:pfam05483  734 EQEQSSAKAALeielsniKAELLSLKKQLEIEKEEKEKLKME 775
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
658-1126 1.57e-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: 46.17  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  658 LIYLLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYiTQER 737
Cdd:TIGR04523  199 LELLLSNLKKKIQKNKSLESQISELKK-QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKEL 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  738 NRAKETLEEERKRMQELESLLAQQKKALAKSITQEknrVKEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALE 817
Cdd:TIGR04523  277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------QLNEQIS 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  818 SEKRKVQDLEN-HLTQQKEISESNIAYEKrkakeAMEKEKKKVQDLENrLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:TIGR04523  346 QLKKELTNSESeNSEKQRELEEKQNEIEK-----LKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  897 TQKTKATESLKAESLALKLNETLAELETTKTKmimveerLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIV 976
Cdd:TIGR04523  420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  977 SLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDL----LAAQKEILSQQEVIMK 1052
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKEIDEKNKEIEE 572
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1053 LRKDLTEAHSRMSDLRGELNEKQK------MELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1126
Cdd:TIGR04523  573 LKQTQKSLKKKQEEKQELIDQKEKekkdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
275-830 1.59e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.58  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  275 QNEVAELSQKVSETTTSRQNEKEISQKCQvldEDIDAKQKEIQSLKS---QISALQKGYSKVLCQ-TLSERNSEITSLKN 350
Cdd:TIGR00606  425 QEQADEIRDEKKGLGRTIELKKEILEKKQ---EELKFVIKELQQLEGssdRILELDQELRKAERElSKAEKNSLTETLKK 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVShLKSQNKDKDHQLEALGSRCSvlkEELKQEDAHRELREAQEK 430
Cdd:TIGR00606  502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIRKIKSRHS---DELTSLLGYFPNKKQLED 577
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrKLLQLQEMGNRESvikinleravgQLE 510
Cdd:TIGR00606  578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED----KLFDVCGSQDEES-----------DLE 642
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  511 HFRSQVIKATYGRAkPFRDKPVTDQQLIEKIT-----------QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKL 579
Cdd:TIGR00606  643 RLKEEIEKSSKQRA-MLAGATAVYSQFITQLTdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  580 RTSLDSCQACMKISCCSHDLK-KEVDLLQH--LQVSPPVSGLQKVVLD---VLRHALSWLEEVEQLLRDLGILpsspnKG 653
Cdd:TIGR00606  722 EKRRDEMLGLAPGRQSIIDLKeKEIPELRNklQKVNRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDVTIM-----ER 796
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  654 FSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL-LQEKLREHLAEKE---KLNEERLEQEEKLKAKIRQLTEEKAAL 729
Cdd:TIGR00606  797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIElnrKLIQDQQEQIQHLKSKTNELKSEKLQI 876
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  730 EEYItQERNRAKETLEEERKRMQELESLLAQQKK---ALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 806
Cdd:TIGR00606  877 GTNL-QRRQQFEEQLVELSTEVQSLIREIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
                          570       580
                   ....*....|....*....|....
gi 1034555185  807 HEKRKAKEALESEKRKVQDLENHL 830
Cdd:TIGR00606  956 YMKDIENKIQDGKDDYLKQKETEL 979
PRK12704 PRK12704
phosphodiesterase; Provisional
726-838 1.91e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  726 KAALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEs 803
Cdd:PRK12704    26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD- 99
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034555185  804 siahekrKAKEALESEKRKVQDLENHLTQQKEISE 838
Cdd:PRK12704   100 -------RKLELLEKREEELEKKEKELEQKQQELE 127
PRK09039 PRK09039
peptidoglycan -binding protein;
304-442 2.58e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.96  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  304 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 377
Cdd:PRK09039    43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555185  378 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 442
Cdd:PRK09039   117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
690-796 2.66e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.46  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  690 LQEKLREHLAEKEKLNEErleQEEKLKAKIRQLTEEKAALEEYITQERNR-------------AKETLEEERKRMQELES 756
Cdd:COG0542    416 LERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARweaekelieeiqeLKEELEQRYGKIPELEK 492
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185  757 LLAQQKKALAKSITQEKNRVKEA-----------------LEEEQTRVQELEERLAR 796
Cdd:COG0542    493 ELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
702-815 2.95e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 2.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  702 EKLNEERLEQEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELEsllaQQKKALAKSITQEKNRVKEALE 781
Cdd:COG4942    142 KYLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALK----AERQKLLARLEKELAELAAELA 216
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1034555185  782 EEQTRVQELEERLARqkevLESSIAHEKRKAKEA 815
Cdd:COG4942    217 ELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
285-533 3.39e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  285 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSG 364
Cdd:COG4942     16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLK--------QLAALERRIAALARRIRALEQELAALEA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  365 MVSSLQKDILAKDEQVQQLKEEVSHL--KSQNKDKDHQLEALGSRCSVLKEELKQE------DAHRELREAQEKELKLCK 436
Cdd:COG4942     84 ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  437 TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQV 516
Cdd:COG4942    164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
                          250
                   ....*....|....*..
gi 1034555185  517 IKATYGRAKPFRDKPVT 533
Cdd:COG4942    244 PAAGFAALKGKLPWPVS 260
FHA_FKH1-like cd22701
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ...
28-110 3.43e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438753 [Multi-domain]  Cd Length: 106  Bit Score: 41.46  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   28 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 95
Cdd:cd22701     12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
                           90
                   ....*....|....*
gi 1034555185   96 GDILRFGSAGLTYEL 110
Cdd:cd22701     91 GSLIQIGGVLFYFLL 105
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
697-1047 3.73e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.33  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  697 HLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqernraketLEEERKRMQELESLLAQQKKA----LAKsiTQE 772
Cdd:COG3096    276 HANERRELSERALELRRELFGARRQLAEEQYRLVE------------MARELEELSARESDLEQDYQAasdhLNL--VQT 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  773 KNRVKEALEEEQTRVQELEERLARQKEVLESsiAHEKR-KAKEALESEKRKVQDLENHLT--QQ--KEISESNIAYE--- 844
Cdd:COG3096    342 ALRQQEKIERYQEDLEELTERLEEQEEVVEE--AAEQLaEAEARLEAAEEEVDSLKSQLAdyQQalDVQQTRAIQYQqav 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  845 --KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQK--------TKATESLKAESLALK 914
Cdd:COG3096    420 qaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiAGEVERSQAWQTARE 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  915 LNETLAEL-------ETTKTKMIMVEERLILQQKMVKALqdEQESQRHG--------FEEEIMEYKEQIKQHAQTIVSLE 979
Cdd:COG3096    500 LLRRYRSQqalaqrlQQLRAQLAELEQRLRQQQNAERLL--EEFCQRIGqqldaaeeLEELLAELEAQLEELEEQAAEAV 577
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  980 EKLQKVTQHHKKIEGEIATLKDNDPA-----PKEERPQDPLVAPMTESSAKDMAYEHLID---------DLLAAQKEILS 1045
Cdd:COG3096    578 EQRSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALE 657

                   ..
gi 1034555185 1046 QQ 1047
Cdd:COG3096    658 SQ 659
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
684-835 4.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLLQEKLREHLAEKEKLNEERLEQEEK-------------------LKAKIRQLTEEKAALEeyitqERNRAKETL 744
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEAELERLD-----ASSDDLAAL 690
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  745 EEERKRMQELESLLAQQKKALAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 824
Cdd:COG4913    691 EEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
                          170
                   ....*....|.
gi 1034555185  825 DLENHLTQQKE 835
Cdd:COG4913    770 NLEERIDALRA 780
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
37-117 4.97e-04

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438727 [Multi-domain]  Cd Length: 113  Bit Score: 41.00  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   37 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 113
Cdd:cd22675     33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109

                   ....
gi 1034555185  114 NPPP 117
Cdd:cd22675    110 GPPS 113
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
671-815 5.81e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  671 QAQELQIKFNSSQETQQSLLQEKLREHLAE--------------KEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE 736
Cdd:COG4942     79 AALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  737 RNR---AKETLEEERKRMQELESLLAQQKKALAKSItQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 813
Cdd:COG4942    159 LAElaaLRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                   ..
gi 1034555185  814 EA 815
Cdd:COG4942    238 AA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
905-1143 5.86e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  905 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 984
Cdd:COG4942     12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  985 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1059
Cdd:COG4942     88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1060 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1138
Cdd:COG4942    162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236

                   ....*
gi 1034555185 1139 KPRKK 1143
Cdd:COG4942    237 AAAAE 241
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
28-103 6.59e-04

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 40.20  E-value: 6.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 99
Cdd:cd22682     15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85

                   ....
gi 1034555185  100 RFGS 103
Cdd:cd22682     86 KIGN 89
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
707-835 7.88e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  707 ERLEQE-EKLKAKIRQLTEEKAALEEYItqernRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQT 785
Cdd:COG4913    238 ERAHEAlEDAREQIELLEPIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034555185  786 RVQELEERLARQKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKE 835
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEA 366
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
3-82 9.30e-04

first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 40.72  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185    3 SLEPCRLFiYGKTERMKAYLKSAEGFFvlnkstTIGRHENSDLVLQSPDIDNHHALI---EYNEAECSFVLQDFNSrNGT 79
Cdd:cd22689     22 TQEPIRDL-SGDISQVLKEKRSIKKVW------TFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGT 93

                   ...
gi 1034555185   80 FVN 82
Cdd:cd22689     94 WLN 96
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
365-508 1.03e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  365 MVSSLQKDILAKDEQVQQLKEEVSHL-KSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDME 443
Cdd:COG0542    405 EIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555185  444 KEMKKLRAELRKSCTEQSVISRTLREKSKVEE--------------KLQEDSRRKLLQLqemgnrESVIKinlERAVGQ 508
Cdd:COG0542    485 GKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNL------EEELH---ERVIGQ 554
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
271-761 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  271 IANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSKvlcqtLSERNSEITS 347
Cdd:PRK03918   268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKE-----LEEKEERLEE 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  348 LKNEGENLKRDNAITSGMVSSLQkDILAKDEQVQQLKEEvshLKSQNKDKdhqlealgsrcsvLKEELKQEDAHRELREA 427
Cdd:PRK03918   343 LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR---LTGLTPEK-------------LEKELEELEKAKEEIEE 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE--EKLQEDSRRKLLQLQEMGNRESVIKINLERA 505
Cdd:PRK03918   406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELREL 485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  506 VGQLEHFRS-QVIKATYGRAKPFRDKpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 584
Cdd:PRK03918   486 EKVLKKESElIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  585 SCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRhALSWLEEVEQLLRDLGILPSSPNKGFSlYLIYLLEH 664
Cdd:PRK03918   564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFE-ELAETEKR 641
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  665 YKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER--NRAKE 742
Cdd:PRK03918   642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALE 721
                          490
                   ....*....|....*....
gi 1034555185  743 TLEEERKRMQELESLLAQQ 761
Cdd:PRK03918   722 RVEELREKVKKYKALLKER 740
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-510 1.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  300 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 379
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  380 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 459
Cdd:COG4913    670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  460 QSVISRTLREKsKVEEKLQEDSRRKLlqLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG4913    743 ARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELE 790
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
684-912 1.22e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLLQEKLREHLAEKEKLNEE--RLEQE-EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQ 760
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAEldALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  761 QKKA-----------LAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALESEKRKVQDLENH 829
Cdd:COG3883     95 LYRSggsvsyldvllGSESFSDFLDRL-SALSKIADADADLLEELKADKAELE--------AKKAELEAKLAELEALKAE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  830 LTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAE 909
Cdd:COG3883    166 LEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244

                   ...
gi 1034555185  910 SLA 912
Cdd:COG3883    245 SAA 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
436-806 1.25e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  436 KTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResviKINLERAVGQLEHFRSQ 515
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  516 VIKatygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkiscc 595
Cdd:TIGR02168  752 LSK--------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------- 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  596 shdLKKEVDLLQ--HLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQ 673
Cdd:TIGR02168  808 ---LRAELTLLNeeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  674 ELQIKFNSSQE------TQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEE 747
Cdd:TIGR02168  877 ALLNERASLEEalallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185  748 RKRMQELESLLAQQKKALaKSITQEKNRVK----EALEEeqtrVQELEER---LARQKEVLESSIA 806
Cdd:TIGR02168  957 EALENKIEDDEEEARRRL-KRLENKIKELGpvnlAAIEE----YEELKERydfLTAQKEDLTEAKE 1017
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
694-833 1.33e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  694 LREHLAEKEklneERLEQEEKLKAKIRQLTEEKAALEEyitqernrAKETLEEERKRMQELESLLAQQKKALAKSITQEK 773
Cdd:COG4913    666 AEREIAELE----AELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  774 NRVKEALE-EEQTRVQELEERLARqkEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 833
Cdd:COG4913    734 DRLEAAEDlARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERA 792
PRK01156 PRK01156
chromosome segregation protein; Provisional
662-1078 1.34e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.35  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  662 LEHYKKLMSQAQELQiKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNR 739
Cdd:PRK01156   321 INKYHAIIKKLSVLQ-KDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  740 AKETLEEERKRMQELESLLAQQKKALAkSITQEKNRVKEALEEEQTRVQELEER---------LARQK-EVLESSIAHEK 809
Cdd:PRK01156   400 QEIDPDAIKKELNEINVKLQDISSKVS-SLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsNHIINHYNEKK 478
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  810 RKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSD 889
Cdd:PRK01156   479 SRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNR 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  890 ALAMVEETQKTKATESLKAESL--ALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQ 967
Cdd:PRK01156   555 YKSLKLEDLDSKRTSWLNALAVisLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  968 IKQhAQTIVSLEEKLQKVTQHHKKiegEIATLKDNDPAPKEerpqdpLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQ 1047
Cdd:PRK01156   635 YNE-IQENKILIEKLRGKIDNYKK---QIAEIDSIIPDLKE------ITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1034555185 1048 EVimkLRKDLTEAHSRMSDLRGELNEKQKME 1078
Cdd:PRK01156   705 EI---LRTRINELSDRINDINETLESMKKIK 732
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
33-110 1.59e-03

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438726 [Multi-domain]  Cd Length: 108  Bit Score: 39.56  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   33 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22674     27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
261-846 1.61e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSE 340
Cdd:PRK02224   198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR--------ETIAE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  341 RNSEITSLKNEgenlkrdnaitsgmvsslqkdILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvlKEELKQEDA 420
Cdd:PRK02224   270 TEREREELAEE---------------------VRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR----REELEDRDE 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  421 hrELREaqekELKLCKTQIQDMEKEMKKLRAELRKSCTEqsviSRTLREKSKVEEKLQEDSRRKllqlqemgnresviki 500
Cdd:PRK02224   325 --ELRD----RLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAELESELEEAREA---------------- 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  501 nLERAVGQLEHFRSQVIKAtygrAKPFRDKPVTDQQLIEKITQVTEDninfqqKKWTLQKETQLSNSKQEEtTENIEKLR 580
Cdd:PRK02224   379 -VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTA-RERVEEAE 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  581 TSLDS--CQACMkisccshdlkkevdllQHLQVSPPVsglqkvvlDVLRHALSWLEEVEQLLRDLGILPSSPNKGfslyl 658
Cdd:PRK02224   447 ALLEAgkCPECG----------------QPVEGSPHV--------ETIEEDRERVEELEAELEDLEEEVEEVEER----- 497
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  659 IYLLEHYKKLMSQAQELQIKfnssQETQQSLLQEKlREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:PRK02224   498 LERAEDLVEAEDRIERLEER----REDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARe 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  738 -----NRAKETLEEERKRMQELESLLA-------------QQKKALAKSITQEKNRVKE------ALEEE--QTRVQELE 791
Cdd:PRK02224   573 evaelNSKLAELKERIESLERIRTLLAaiadaedeierlrEKREALAELNDERRERLAEkrerkrELEAEfdEARIEEAR 652
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555185  792 ERLARQKEVLE--SSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISESNIAYEKR 846
Cdd:PRK02224   653 EDKERAEEYLEqvEEKLDELREERDDLQAE---IGAVENELEELEELRERREALENR 706
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
261-764 1.72e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLSE 340
Cdd:TIGR00618  434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  341 RNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELkqeda 420
Cdd:TIGR00618  513 PNPARQDIDNPGPLTRRMQRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----- 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  421 hrelrEAQEKELKLCKTQIQDMEKEMKKLRAELRkscteqsvisrtlREKSKVEEKLqeDSRRKLLQLQEMGNRESVIKI 500
Cdd:TIGR00618  587 -----PNLQNITVRLQDLTEKLSEAEDMLACEQH-------------ALLRKLQPEQ--DLQDVRLHLQQCSQELALKLT 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  501 NLERavgQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLR 580
Cdd:TIGR00618  647 ALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  581 TSLDscQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDlgilpsspnkgfslyliy 660
Cdd:TIGR00618  718 REFN--EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG------------------ 777
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  661 llehyKKLMSQAQELQIKFNSSQETQQSL--LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERN 738
Cdd:TIGR00618  778 -----AELSHLAAEIQFFNRLREEDTHLLktLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
                          490       500
                   ....*....|....*....|....*.
gi 1034555185  739 RAKETLEEERKRMQELESLLAQQKKA 764
Cdd:TIGR00618  853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
314-490 1.75e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 41.65  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  314 KEIQSLKSQISALQKG------YSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:pfam17078    3 KVIESLHDQIDALTKTnlqltvQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELrkscte 459
Cdd:pfam17078   83 EELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENY------ 156
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034555185  460 qsvISRTLREKSKVEEKLQE-DSRRKLLQLQE 490
Cdd:pfam17078  157 ---QQRISSNDKDIDTKLDSyNNKFKNLDNIY 185
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
25-103 1.76e-03

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 39.01  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   25 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 103
Cdd:cd22696     13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
PRK12704 PRK12704
phosphodiesterase; Provisional
663-816 2.01e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  663 EHYKKLMSQA-QELQIKFNSSQETQQSLLQeklrehlaeKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK 741
Cdd:PRK12704    64 EEIHKLRNEFeKELRERRNELQKLEKRLLQ---------KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE 134
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185  742 ETLEEERKRMQELESLLAQQkkalAKSITQEKnrVKEALEEEQTR-VQELEERlarqkevlessiAHE--KRKAKEAL 816
Cdd:PRK12704   135 ELIEEQLQELERISGLTAEE----AKEILLEK--VEEEARHEAAVlIKEIEEE------------AKEeaDKKAKEIL 194
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
22-109 2.06e-03

forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 38.94  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   22 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 101
Cdd:cd22669      5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81

                   ....*...
gi 1034555185  102 GSAGLTYE 109
Cdd:cd22669     82 CDHEFTFQ 89
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
37-109 2.07e-03

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 39.01  E-value: 2.07e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555185   37 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 109
Cdd:cd22737     25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
PTZ00121 PTZ00121
MAEBL; Provisional
663-905 2.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  663 EHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE 742
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  743 TLEEERKRMQEL---ESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELE-----ERLARQKEVLESSIAHEKRKAKE 814
Cdd:PTZ00121  1641 KEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalkkeAEEAKKAEELKKKEAEEKKKAEE 1720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  815 ALESEKRKVQDLENHLTQQKEisesniayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKL--SDALA 892
Cdd:PTZ00121  1721 LKKAEEENKIKAEEAKKEAEE--------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELdeEDEKR 1792
                          250
                   ....*....|...
gi 1034555185  893 MVEETQKTKATES 905
Cdd:PTZ00121  1793 RMEVDKKIKDIFD 1805
FHA_GarA-like cd22720
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ...
29-108 2.51e-03

forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438772 [Multi-domain]  Cd Length: 100  Bit Score: 38.83  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   29 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 107
Cdd:cd22720     19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94

                   .
gi 1034555185  108 Y 108
Cdd:cd22720     95 F 95
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
287-509 2.68e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.67  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  287 ETTTSRQNEKEISQKCQVLdedIDAKQKEIQSLKSQISA----LQKGYSKVLCQTLSERN---SEITSLKNEGENLKRDN 359
Cdd:pfam09787    1 NLESAKQELADYKQKAARI---LQSKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  360 AitsGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQI 439
Cdd:pfam09787   78 Q---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRI 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555185  440 QDMEKEMKKLRAELR---KSCTEQSVISRTLREkskveekLQEDSRRKLLQLQEMGNRESVIKINLERAVGQL 509
Cdd:pfam09787  142 KDREAEIEKLRNQLTsksQSSSSQSELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
666-836 2.70e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  666 KKLMSQAQELQIKFNSSQETQQSLLQE------------------------------KLREHLAEKEKLNEERLEQEEKL 715
Cdd:pfam01576  408 KKLEGQLQELQARLSESERQRAELAEKlsklqselesvssllneaegkniklskdvsSLESQLQDTQELLQEETRQKLNL 487
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  716 KAKIRQLTEEKAALEEYItQERNRAKETLEeerKRMQELESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLA 795
Cdd:pfam01576  488 STRLRQLEDERNSLQEQL-EEEEEAKRNVE---RQLSTLQAQLSDMKKKL-----EEDAGTLEALEEGKKRLQRELEALT 558
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034555185  796 RQKEvlessiahEKRKAKEALESEKRKVQ----DLENHLTQQKEI 836
Cdd:pfam01576  559 QQLE--------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQL 595
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
737-819 2.70e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.77  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  737 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLESSIAHEKRKA 812
Cdd:COG0711     33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAEAEIEQERAKA 112

                   ....*..
gi 1034555185  813 KEALESE 819
Cdd:COG0711    113 LAELRAE 119
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
683-827 2.78e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  683 QETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEE-------YITQERNRAKETLEEERKRMQELE 755
Cdd:pfam15709  357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQEEFRRKLQELQ 436
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555185  756 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAKEALESEKRKVQDLE 827
Cdd:pfam15709  437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEAEEKARLEAEERRQKEEE 503
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
661-819 2.97e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  661 LLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQL------------------ 722
Cdd:COG3883     35 AQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgses 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  723 ---------------TEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQKKALAKSITqEKNRVKEALEEEQT 785
Cdd:COG3883    114 fsdfldrlsalskiaDADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEA 192
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034555185  786 RVQELEERLARQKEVLESSIAHEKRKAKEALESE 819
Cdd:COG3883    193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
261-841 3.02e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.35  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  261 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 337
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  338 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  413 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklL 486
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------L 1343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  487 QLQEMGNRESVIKIN-LERAVGQLEHFRSQVIKATygraKPFRDKPVTDQQLIEKItqvtEDNINFQQKKWTLqkETQLS 565
Cdd:TIGR01612 1344 YLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLD 1413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  566 NSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL-----EEVEQLL 640
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHdfninELKEHID 1493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  641 RDLGI-LPSSPNKGFSLYLIYLLEHYKK----LMSQAQELQIKFNSSQETQQSllqeklREHLAEKEKLNEERLEQEEKL 715
Cdd:TIGR01612 1494 KSKGCkDEADKNAKAIEKNKELFEQYKKdvteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKS 1567
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  716 KAKIRQLTEEKAALEEYITQ--ERNRA----KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 789
Cdd:TIGR01612 1568 EQKIKEIKKEKFRIEDDAAKndKSNKAaidiQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKE 1647
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034555185  790 LEERLARQKEVLESSIAHEK--RKAKEALESEKRKVQDLENHLTQQKEISESNI 841
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKniEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
692-839 3.83e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  692 EKLREHL-AEKEKLNE--ERLEQEEK-LKAKIRQLTEEKaaleeyitQERNRAKETLEEERKRMQE-LESLLAQQKKALA 766
Cdd:PRK00409   505 EEAKKLIgEDKEKLNEliASLEELEReLEQKAEEAEALL--------KEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQ 576
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555185  767 KsitqeknRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA-KEALESekrkvqdLENHLTQQKEISES 839
Cdd:PRK00409   577 Q-------AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRlNKANEK-------KEKKKKKQKEKQEE 636
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
274-481 4.01e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  274 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 353
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  354 NLKRDNAITSGMVSSLQKDILAKD--EQVQQLkEEVSHLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQEK 430
Cdd:COG3883     90 ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEA 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG3883    169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
662-816 4.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQE--------KLREHLAEKEKLNEE------RLEQEEKLKAKIRQLTEEKA 727
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREEleklekllQLLPLYQELEALEAElaelpeRLEELEERLEELRELEEELE 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  728 ALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAH 807
Cdd:COG4717    167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

                   ....*....
gi 1034555185  808 EKRKAKEAL 816
Cdd:COG4717    243 ERLKEARLL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
683-1206 4.56e-03

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: 41.59  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  683 QETQQSLLQEKLREHLAEKEKLNEERLEQE---EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQE-LESLL 758
Cdd:TIGR02169  221 REYEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  759 AQQkkALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQ-KEIS 837
Cdd:TIGR02169  301 AEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAElEEVD 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  838 ESNIAY--EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKL 915
Cdd:TIGR02169  378 KEFAETrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  916 NETLAELETTKTKMIMVEERLILQQKMVKALQ---DEQESQRHGFEEEIMEYK---EQIKQHAQTIVSLEEKLQKV-TQH 988
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVAQLGSVgERY 537
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  989 HKKIEGE-------------------IATLKDNDPAP------KEERPQDPLVAPMTESSAKDMAY-------------- 1029
Cdd:TIGR02169  538 ATAIEVAagnrlnnvvveddavakeaIELLKRRKAGRatflplNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafk 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1030 ------------------------------------------------------------------EHLIDDLLAAQKEI 1043
Cdd:TIGR02169  618 yvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqrlrerlEGLKRELSSLQSEL 697
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1044 LSQQEVIMKLRKDLTEAHSRMSDLRGELN------EKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKAL 1117
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185 1118 EEAL---RASQEKHRLQ-----LNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHE--EVIQ 1187
Cdd:TIGR02169  778 EEALndlEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIE 857
                          650
                   ....*....|....*....
gi 1034555185 1188 RQKKALSELRARIKELEKA 1206
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAA 876
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
36-102 4.79e-03

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 38.11  E-value: 4.79e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555185   36 TIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22663     24 TVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
684-787 4.79e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLLQEKLREHLAEKEKLNEERLEQEEkLKAKIRQLTEEKAALEEYitqernrAKETLEEERKRMQELESLLAQQKK 763
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQ-SQALAEAQQQELVALEGL-------AAELEEKQQELEAQLEQLQEKAAE 209
                           90       100
                   ....*....|....*....|....*....
gi 1034555185  764 ALAKSITQEKNRVKEA-----LEEEQTRV 787
Cdd:PRK11448   210 TSQERKQKRKEITDQAakrleLSEEETRI 238
PLN02316 PLN02316
synthase/transferase
689-754 5.33e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.39  E-value: 5.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555185  689 LLQEKLREhlaeKEKLNEERLEQEeKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQEL 754
Cdd:PLN02316   250 LLEEKRRE----LEKLAKEEAERE-RQAEEQRRREEEKAAME----ADRAQAKAEVEKRREKLQNL 306
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
274-497 5.37e-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: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  274 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 349
Cdd:COG3206    180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  350 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 427
Cdd:COG3206    240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555185  428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQE-DSRRKLLQLQEMGNRESV 497
Cdd:COG3206    318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEEARLAEALTVGNV 388
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
687-846 5.40e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.51  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  687 QSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRMQELESllaqQKKALA 766
Cdd:pfam09787   17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLRE----EIQKLRGQIQQLRTELQELEA----QQQEEA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  767 KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLeSSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIA 842
Cdd:pfam09787   89 ESSREQLQELEEQLATERSARREAEAELERLQEEL-RYLEEELRRSKATLQSRIKDreaeIEKLRNQLTSKSQSSSSQSE 167

                   ....
gi 1034555185  843 YEKR 846
Cdd:pfam09787  168 LENR 171
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
243-501 5.72e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.35  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  243 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQNEVAELSQKVSETTTSrqnekeisqkCQVLDEDIDAKQKEIQSLKSQ 322
Cdd:pfam10174  392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  323 ISALQKgyskvlcqtlsERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLE 402
Cdd:pfam10174  459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  403 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLR----EKSKVEE 475
Cdd:pfam10174  521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDK 600
                          250       260
                   ....*....|....*....|....*.
gi 1034555185  476 KLQEDSRRKLLQLQEMGNRESVIKIN 501
Cdd:pfam10174  601 KIAELESLTLRQMKEQNKKVANIKHG 626
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
691-846 5.84e-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: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  691 QEKLREHLAEKEKLNEERLEQEE---KLKAKIRQLTEEKAA---LEEYITQERN-----RAKETLEEERKRM-------Q 752
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEErleALEAELDALQERREAlqrLAEYSWDEIDvasaeREIAELEAELERLdassddlA 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  753 ELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQ 832
Cdd:COG4913    689 ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
                          170
                   ....*....|....
gi 1034555185  833 QKEISESNIAYEKR 846
Cdd:COG4913    768 RENLEERIDALRAR 781
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
684-799 5.85e-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: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  684 ETQQSLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK--ETLEEERKRMQELESLLAQQ 761
Cdd:COG3206    225 ESQLAEARAELAEAEARLAAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAAL 303
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034555185  762 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKE 799
Cdd:COG3206    304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
673-803 6.10e-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: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  673 QELQIKFNSSQETQQSLLQEKLREHLAEkekLNEERLEQEEKLKAK---IRQLTEEKAALEEYITQERNRAKETLEEE-- 747
Cdd:COG3206    247 AQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555185  748 --RKRMQELESLLAQQKKALAKsitqeknrvkeaLEEEQTRVQELEERLARQKEVLES 803
Cdd:COG3206    324 alQAREASLQAQLAQLEARLAE------------LPELEAELRRLEREVEVARELYES 369
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
741-836 6.30e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 38.50  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  741 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 813
Cdd:pfam05130    4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
                           90       100
                   ....*....|....*....|...
gi 1034555185  814 EALESEKRKVQDLENHLTQQKEI 836
Cdd:pfam05130   84 PELRELWQELLELLERLKELNEL 106
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
27-82 6.63e-03

forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438718 [Multi-domain]  Cd Length: 112  Bit Score: 37.99  E-value: 6.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555185   27 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 82
Cdd:cd22666     10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
376-455 7.06e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  376 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 455
Cdd:COG2433    411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
690-814 7.17e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.39  E-value: 7.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185   690 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtleeerkrMQEL-ESLLAQQKKALAKS 768
Cdd:smart00787  145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE--------LEDCdPTELDRAKEKLKKL 216
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1034555185   769 ITQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 814
Cdd:smart00787  217 LQEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
671-783 7.27e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.96  E-value: 7.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  671 QAQELQIKFNSSQE-TQQSLLQekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERK 749
Cdd:pfam02841  173 KAEEVLQEFLQSKEaVEEAILQ--TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034555185  750 RM-QELESLLAQQKKALAKSITQEKNRVKEALEEE 783
Cdd:pfam02841  251 KMeAEREQLLAEQERMLEHKLQEQEELLKEGFKTE 285
PLN02939 PLN02939
transferase, transferring glycosyl groups
236-489 7.29e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.04  E-value: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  236 EDLAQ--QDKDEIILLLGK-EVSRLSDYEIESKYKDviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAK 312
Cdd:PLN02939   131 EDLVGmiQNAEKNILLLNQaRLQALEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  313 QKEIqslkSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKrdnaitsGMVSSLQKdilaKDEQVQQLKEEVSHLKS 392
Cdd:PLN02939   207 RNEL----LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-------AELIEVAE----TEERVFKLEKERSLLDA 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  393 QNKDKDHQLeaLGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI----------QDMEKEMKKLRAELRKSCT--EQ 460
Cdd:PLN02939   272 SLRELESKF--IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVekaalvldqnQDLRDKVDKLEASLKEANVskFS 349
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034555185  461 SVISRTLREKSK-VEEKLQEDSRRKLLQLQ 489
Cdd:PLN02939   350 SYKVELLQQKLKlLEERLQASDHEIHSYIQ 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
307-743 7.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  307 EDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNEGENLKRDnaitsgmvsslqKDILAKDEQVQQLKEE 386
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREE------------LEKLEKLLQLLPLYQE 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  387 VSHLKSQNKDKDHQLEALGSRCSVLKEELKQ----EDAHRELREAQEKELKLC----KTQIQDMEKEMKKLRAELRKSCT 458
Cdd:COG4717    134 LEALEAELAELPERLEELEERLEELRELEEEleelEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEE 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  459 EQSVISRTLREKSKVEEKLQEDSR-----RKLLQLQEMGNRESVIkINLERAVGQLEHFRSQVIKA--------TYGRAK 525
Cdd:COG4717    214 ELEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllALLFLL 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  526 PFRDKPVTDQQLIEKITQVTEDNInfQQKKWT-----LQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLK 600
Cdd:COG4717    293 LAREKASLGKEAEELQALPALEEL--EEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  601 KEVDLLQHLQVSPpvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKK-LMSQAQELQIKF 679
Cdd:COG4717    371 EIAALLAEAGVED---------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEEL 441
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555185  680 NSSQETQQSLLQEKLR-----EHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAAL---EEYITQERNRAKET 743
Cdd:COG4717    442 EELEEELEELREELAEleaelEQLEEDGEL-AELLQELEELKAELRELAEEWAALklaLELLEEAREEYREE 512
46 PHA02562
endonuclease subunit; Provisional
302-414 8.87e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  302 CQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLC--QTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQ 379
Cdd:PHA02562   287 CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTaiDELEEIMDEFNEQSKKLLELKNK-------ISTNKQSLITLVDK 359
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1034555185  380 VQQLKEEVSHLKSQNKDKD-------HQLEALGSRCSVLKEE 414
Cdd:PHA02562   360 AKKVKAAIEELQAEFVDNAeelaklqDELDKIVKTKSELVKE 401
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
671-867 9.34e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  671 QAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKlneeRLeQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLE 745
Cdd:COG3206    162 LEQNLELRREEARKALEFLEEQlpELRKELEEAEA----AL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELA 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555185  746 EERKRMQELESLLAQQKKALAK-SITQEKNRVKEALEEEQTRVQELEER----------LARQKEVLESSIAHEKRKAKE 814
Cdd:COG3206    237 EAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQEAQRILA 316
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034555185  815 ALESEKRKVQDLENHLTQQKEISESNIAyekrkakeamekekkKVQDLENRLT 867
Cdd:COG3206    317 SLEAELEALQAREASLQAQLAQLEARLA---------------ELPELEAELR 354
 
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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