NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1952581446|ref|XP_038668781|]
View 

sarcolemma associated protein a isoform X15 [Scyliorhinus canicula]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
3-130 2.84e-81

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: 257.58  E-value: 2.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446   3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679     1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952581446  83 QRLSRGSEESPPCELLSGDIIQFGVDVTENTRKVTHGCIVSTVKLFMP 130
Cdd:cd22679    79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 1.08e-26

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


:

Pssm-ID: 409287 [Multi-domain]  Cd Length: 63  Bit Score: 103.53  E-value: 1.08e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581446 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911     1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
163-858 4.58e-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: 76.63  E-value: 4.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVT 242
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKY-NGAVNELKEFTEKL 321
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  322 KQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQ-----EKNIKDHNSIG 396
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEgfsegVKALLKNQSGL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  397 IQVDDLLpkingstdkehfllksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDmfeshlENNQTTEED---LKNd 473
Cdd:TIGR02168  519 SGILGVL------------------------SELISVDEGYEAAIEAALGGRLQAVVV------ENLNAAKKAiafLKQ- 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  474 SERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS--SEDTTDYQMDEQELNESLNK 540
Cdd:TIGR02168  568 NELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRI 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  541 VSLLKDELQCAHVQTGDSEREKQ---ELQQELKEAQelaisskQKCFEMQALLEEerktAKKQVEESTRQIQALQAHLHK 617
Cdd:TIGR02168  648 VTLDGDLVRPGGVITGGSAKTNSsilERRREIEELE-------EKIEELEEKIAE----LEKALAELRKELEELEEELEQ 716
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  618 LQKDIEilreDKEIEIIETRDQLASTHKEIvalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlq 697
Cdd:TIGR02168  717 LRKELE----ELSRQISALRKDLARLEAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---- 784
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  698 tklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVS 777
Cdd:TIGR02168  785 ----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  778 RKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKL 854
Cdd:TIGR02168  861 IEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                   ....
gi 1952581446  855 LQQK 858
Cdd:TIGR02168  941 LQER 944
 
Name Accession Description Interval E-value
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
3-130 2.84e-81

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: 257.58  E-value: 2.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446   3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679     1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952581446  83 QRLSRGSEESPPCELLSGDIIQFGVDVTENTRKVTHGCIVSTVKLFMP 130
Cdd:cd22679    79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 1.08e-26

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409287 [Multi-domain]  Cd Length: 63  Bit Score: 103.53  E-value: 1.08e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581446 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911     1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
28-105 7.92e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 69.91  E-value: 7.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446  28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCELLSGDIIQF 105
Cdd:pfam00498   1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
163-858 4.58e-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: 76.63  E-value: 4.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVT 242
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKY-NGAVNELKEFTEKL 321
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  322 KQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQ-----EKNIKDHNSIG 396
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEgfsegVKALLKNQSGL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  397 IQVDDLLpkingstdkehfllksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDmfeshlENNQTTEED---LKNd 473
Cdd:TIGR02168  519 SGILGVL------------------------SELISVDEGYEAAIEAALGGRLQAVVV------ENLNAAKKAiafLKQ- 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  474 SERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS--SEDTTDYQMDEQELNESLNK 540
Cdd:TIGR02168  568 NELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRI 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  541 VSLLKDELQCAHVQTGDSEREKQ---ELQQELKEAQelaisskQKCFEMQALLEEerktAKKQVEESTRQIQALQAHLHK 617
Cdd:TIGR02168  648 VTLDGDLVRPGGVITGGSAKTNSsilERRREIEELE-------EKIEELEEKIAE----LEKALAELRKELEELEEELEQ 716
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  618 LQKDIEilreDKEIEIIETRDQLASTHKEIvalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlq 697
Cdd:TIGR02168  717 LRKELE----ELSRQISALRKDLARLEAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---- 784
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  698 tklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVS 777
Cdd:TIGR02168  785 ----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  778 RKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKL 854
Cdd:TIGR02168  861 IEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                   ....
gi 1952581446  855 LQQK 858
Cdd:TIGR02168  941 LQER 944
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
14-106 6.14e-13

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 65.36  E-value: 6.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716     8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
                          90
                  ....*....|....
gi 1952581446  93 pPCELLSGDIIQFG 106
Cdd:COG1716    75 -PAPLRDGDVIRLG 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
532-823 5.23e-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: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 532 QELNESLN--KVSLLKDELQCAHVQTGDSEREKQELQQELKEAQElaisskqkcfeMQALLEEERKTAKKQVEESTRQIQ 609
Cdd:COG1196   216 RELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEA-----------ELAELEAELEELRLELEELELELE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 610 ALQAHLHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWR 683
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 684 QTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 763
Cdd:COG1196   365 EALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 764 SVKLTKDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 823
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
329-860 2.89e-10

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: 63.97  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 329 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTalqVRLEQLQEKN---IKDHNSIGIQVDDLLPK 405
Cdd:pfam05483  88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVS---LKLEEEIQENkdlIKENNATRHLCNLLKET 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 406 INGSTDKEHfllKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHL------ENNQTTEEDLK---NDSER 476
Cdd:pfam05483 164 CARSAEKTK---KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFklkedhEKIQHLEEEYKkeiNDKEK 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 477 FKATLIAE--DDHTKVTEETKLLKE-----NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQ 549
Cdd:pfam05483 241 QVSLLLIQitEKENKMKDLTFLLEEsrdkaNQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 550 CAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILR 626
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFK 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 627 EDKEIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtkl 700
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV------- 473
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 701 qlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 780
Cdd:pfam05483 474 --------EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 781 LEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 860
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
28-85 3.90e-09

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.95  E-value: 3.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446   28 VKIGRSvarcrPAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240   1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
275-831 1.78e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 275 VERSLSNTEDECTHLKEMNDRTQEelRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQK------ALSEKKELQHRIDE 348
Cdd:PRK02224  178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETrdeadeVLEEHEERREELET 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 349 MEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNikdhnsigiqvDDLLPKIN-GSTDKEHFLLKS---GGDCS 424
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER-----------DDLLAEAGlDDADAEAVEARReelEDRDE 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 425 ELFQQFIECKNKLKAPVEPTQNNR--ISNVEDMFESHLENNQTTEEDLKNDSE---RFKATLIAEDDHTKVTEETKLLKE 499
Cdd:PRK02224  325 ELRDRLEECRVAAQAHNEEAESLRedADDLEERAEELREEAAELESELEEAREaveDRREEIEELEEEIEELRERFGDAP 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 500 NQLEAKEsDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQC----------AHVQTGDSEREK-QELQQE 568
Cdd:PRK02224  405 VDLGNAE-DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRERvEELEAE 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 569 LKEAQElaisskqkcfEMQALleEERKTAKKQVEESTRQIQALQAHLhklqKDIEILREDKEIEIIETRDQLASTHKEIV 648
Cdd:PRK02224  484 LEDLEE----------EVEEV--EERLERAEDLVEAEDRIERLEERR----EDLEELIAERRETIEEKRERAEELRERAA 547
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 649 ALRQTAVE----AATGRE------SDIAILQGELHKVQTELEQWRqTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQL 718
Cdd:PRK02224  548 ELEAEAEEkreaAAEAEEeaeearEEVAELNSKLAELKERIESLE-RIRTLLAAIADAED---------------EIERL 611
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 719 QGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRL 793
Cdd:PRK02224  612 REKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENEL 690
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 794 QETNGLRVKLAHAENETQKFQKQY---EADQTMYLELKEKL 831
Cdd:PRK02224  691 EELEELRERREALENRVEALEALYdeaEELESMYGDLRAEL 731
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
49-106 3.58e-03

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: 40.82  E-value: 3.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581446  49 KVLSRNHA-LIWFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEESppceLLSGDIIQFG 106
Cdd:TIGR03354  43 RHVSGRHArIRYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNPVR----LEQGDRLRLG 95
 
Name Accession Description Interval E-value
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
3-130 2.84e-81

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: 257.58  E-value: 2.84e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446   3 SALAIFTCRPNSHPFQERHVYLDEPVKIGRSVARCRPAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINS 82
Cdd:cd22679     1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952581446  83 QRLSRGSEESPPCELLSGDIIQFGVDVTENTRKVTHGCIVSTVKLFMP 130
Cdd:cd22679    79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 1.08e-26

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409287 [Multi-domain]  Cd Length: 63  Bit Score: 103.53  E-value: 1.08e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581446 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911     1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
FHA_DMA-like cd22692
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ...
27-108 1.45e-18

forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438744 [Multi-domain]  Cd Length: 139  Bit Score: 83.00  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  27 PVKIGRSVARCRPAQNNAT-FDCKVLSRNHALIWfdHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQF 105
Cdd:cd22692    38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115

                  ...
gi 1952581446 106 GVD 108
Cdd:cd22692   116 GMD 118
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
6-126 3.77e-16

forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438747 [Multi-domain]  Cd Length: 133  Bit Score: 75.80  E-value: 3.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446   6 AIFTCRPNSHPFQERHV---YLDEPVKIGRSVARCRPAQN---------------NATFDCKVLSRNHALIWFDHKTGKF 67
Cdd:cd22695     2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  68 YLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFGVDVTEntrKVTHGCIVSTVK 126
Cdd:cd22695    82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
13-106 5.30e-15

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: 71.15  E-value: 5.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  13 NSHPFQERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060     6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRI------T 71
                          90
                  ....*....|....
gi 1952581446  93 PPCELLSGDIIQFG 106
Cdd:cd00060    72 PPVPLQDGDVIRLG 85
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
28-105 7.92e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 69.91  E-value: 7.92e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446  28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLSRgseesPPCELLSGDIIQF 105
Cdd:pfam00498   1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
163-858 4.58e-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: 76.63  E-value: 4.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGirKELVT 242
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKY-NGAVNELKEFTEKL 321
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  322 KQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQ-----EKNIKDHNSIG 396
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------RLDSLERLQENLEgfsegVKALLKNQSGL 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  397 IQVDDLLpkingstdkehfllksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDmfeshlENNQTTEED---LKNd 473
Cdd:TIGR02168  519 SGILGVL------------------------SELISVDEGYEAAIEAALGGRLQAVVV------ENLNAAKKAiafLKQ- 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  474 SERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS--SEDTTDYQMDEQELNESLNK 540
Cdd:TIGR02168  568 NELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGVlvVDDLDNALELAKKLRPGYRI 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  541 VSLLKDELQCAHVQTGDSEREKQ---ELQQELKEAQelaisskQKCFEMQALLEEerktAKKQVEESTRQIQALQAHLHK 617
Cdd:TIGR02168  648 VTLDGDLVRPGGVITGGSAKTNSsilERRREIEELE-------EKIEELEEKIAE----LEKALAELRKELEELEEELEQ 716
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  618 LQKDIEilreDKEIEIIETRDQLASTHKEIvalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlq 697
Cdd:TIGR02168  717 LRKELE----ELSRQISALRKDLARLEAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---- 784
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  698 tklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVS 777
Cdd:TIGR02168  785 ----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  778 RKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKL 854
Cdd:TIGR02168  861 IEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940

                   ....
gi 1952581446  855 LQQK 858
Cdd:TIGR02168  941 LQER 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
203-845 1.12e-13

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: 75.48  E-value: 1.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  203 SWQALIDE-DRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELVTLQEDKHSYETT---AKESLRRVLQEKIEVVRKLS 273
Cdd:TIGR02168  233 RLEELREElEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEME 350
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  351 EKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSE 425
Cdd:TIGR02168  393 LQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleeaLEE 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  426 LFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFESHLENNQTTEEDLKN------------------------------- 472
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaalgg 545
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  473 ---------------------DSERFKATLIAEDD--HTKVTEETKLLKENQ---------LEAKESDMSDTLSPSKDRS 520
Cdd:TIGR02168  546 rlqavvvenlnaakkaiaflkQNELGRVTFLPLDSikGTEIQGNDREILKNIegflgvakdLVKFDPKLRKALSYLLGGV 625
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  521 --SEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSE----------REKQELQQELKEAQELAISSKQKCFEM-- 586
Cdd:TIGR02168  626 lvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAktnssilerrREIEELEEKIEELEEKIAELEKALAELrk 705
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  587 -QALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAATGRE 662
Cdd:TIGR02168  706 eLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  663 SdiaiLQGELHKVQTELEQWRQTASEYESEIFNlqtklqlqtqqqkdkQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 742
Cdd:TIGR02168  786 E----LEAQIEQLKEELKALREALDELRAELTL---------------LNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  743 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVklahAENETQKFQKQYEADQT 822
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELRE 922
                          730       740
                   ....*....|....*....|...
gi 1952581446  823 MYLELKEKLDKTQKENESITDEL 845
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERL 945
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
167-204 1.97e-13

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409286 [Multi-domain]  Cd Length: 38  Bit Score: 64.81  E-value: 1.97e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1952581446 167 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21868     1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
14-106 6.14e-13

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 65.36  E-value: 6.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  14 SHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHktGKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716     8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
                          90
                  ....*....|....
gi 1952581446  93 pPCELLSGDIIQFG 106
Cdd:COG1716    75 -PAPLRDGDVIRLG 87
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
52-106 1.32e-12

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: 65.38  E-value: 1.32e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEESPPCELLSGDIIQFG 106
Cdd:cd22686    48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
182-853 1.02e-11

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: 68.94  E-value: 1.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAysknqTEDGIRKELVTLQEDKHSYETTAKESLrrv 261
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-----EIEELEREIEEERKRRDKLTEEYAELK--- 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  262 lQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAL---SE 338
Cdd:TIGR02169  364 -EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleEE 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  339 KKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKdhnsIGIQVDDLLPKINGSTDKEHFLLK 418
Cdd:TIGR02169  443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKA 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  419 SGGDCSELFQQFIECKNKLKAPVEPTQNNRISN--VED--------------------------MFESHLENNQTTEE-- 468
Cdd:TIGR02169  519 SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvVEDdavakeaiellkrrkagratflplnkMRDERRDLSILSEDgv 598
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  469 -----DLKNDSERFKA--------TLIAEDDHTK---------VTEETKLLKENQL-------EAKESDMSDTLSPSKDR 519
Cdd:TIGR02169  599 igfavDLVEFDPKYEPafkyvfgdTLVVEDIEAArrlmgkyrmVTLEGELFEKSGAmtggsraPRGGILFSRSEPAELQR 678
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  520 SSEDTTDYQMDE----QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERK 595
Cdd:TIGR02169  679 LRERLEGLKRELsslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEIE 754
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  596 TAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA---LRQTAVEAATGRES-DIAILQGE 671
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrieARLREIEQKLNRLTlEKEYLEKE 834
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  672 LHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQ 751
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  752 WFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHAENETQKFQ-------KQYEADQT 822
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEYEEVLK 986
                          730       740       750
                   ....*....|....*....|....*....|.
gi 1952581446  823 MYLELKEKLDKTQKENESITDELENCkENLK 853
Cdd:TIGR02169  987 RLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
532-823 5.23e-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: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 532 QELNESLN--KVSLLKDELQCAHVQTGDSEREKQELQQELKEAQElaisskqkcfeMQALLEEERKTAKKQVEESTRQIQ 609
Cdd:COG1196   216 RELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEA-----------ELAELEAELEELRLELEELELELE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 610 ALQAHLHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWR 683
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 684 QTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 763
Cdd:COG1196   365 EALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 764 SVKLTKDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 823
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
157-387 1.72e-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: 65.09  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  157 SPSMYSQELFQLSQY--LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEd 234
Cdd:TIGR02169  659 SRAPRGGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE- 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  235 girkelvtLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ-EELRELANKYNGAVNE 313
Cdd:TIGR02169  738 --------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSR 809
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581446  314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
329-860 2.89e-10

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: 63.97  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 329 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTalqVRLEQLQEKN---IKDHNSIGIQVDDLLPK 405
Cdd:pfam05483  88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVS---LKLEEEIQENkdlIKENNATRHLCNLLKET 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 406 INGSTDKEHfllKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHL------ENNQTTEEDLK---NDSER 476
Cdd:pfam05483 164 CARSAEKTK---KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFklkedhEKIQHLEEEYKkeiNDKEK 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 477 FKATLIAE--DDHTKVTEETKLLKE-----NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQ 549
Cdd:pfam05483 241 QVSLLLIQitEKENKMKDLTFLLEEsrdkaNQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 550 CAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---ILR 626
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtKFK 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 627 EDKEIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqtkl 700
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV------- 473
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 701 qlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 780
Cdd:pfam05483 474 --------EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 781 LEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 860
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
164-204 1.15e-09

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 54.28  E-value: 1.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 204
Cdd:cd21912     5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
590-857 1.31e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 590 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 662
Cdd:COG1196   205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 663 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 742
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 743 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 822
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1952581446 823 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 857
Cdd:COG1196   426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
28-119 1.31e-09

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 57.04  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  28 VKIGRSVARCRPAQNNATFDcKVLSRNHALIW---FDHKTGKFYLQDTkSSNGTFINSQRLSRGSEEsppcELLSGDIIQ 104
Cdd:cd22685    30 YRIGRNPEVCDVFLCSSQHP-NLISREHAEIHaerDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTIT 103
                          90
                  ....*....|....*..
gi 1952581446 105 FG--VDVTENTRKVTHG 119
Cdd:cd22685   104 FGhkNGRRVKQWPYQKS 120
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
28-85 3.90e-09

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.95  E-value: 3.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446   28 VKIGRSvarcrPAQNNATFDCKVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240   1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
FHA_FKH1-like cd22701
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ...
27-106 5.41e-09

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: 54.55  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  27 PVKIGRSVARcRPAQNNATFDC-----KVLSRNHALIWFDHKTGKFYLQdTKSSNGTFINSQRLSRGseeSPPCELLSGD 101
Cdd:cd22701    18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92

                  ....*
gi 1952581446 102 IIQFG 106
Cdd:cd22701    93 LIQIG 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
294-847 7.82e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 294 DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALsekkELQHRIDEMEEKEQLLQARIEALQADNDFTNER 373
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEER 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 374 LTALQVRLEQLQEknikdhnsigiQVDDLLPKINGSTDKEHfllksggdcsELFQQFIECKNKLKAPVEpTQNNRISNVE 453
Cdd:COG1196   311 RRELEERLEELEE-----------ELAELEEELEELEEELE----------ELEEELEEAEEELEEAEA-ELAEAEEALL 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 454 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTdyQMDEQE 533
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEE 446
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 534 LNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEES-----TRQI 608
Cdd:COG1196   447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglAGAV 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 609 QALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT---------GRESDIAILQGELHKVQTEL 679
Cdd:COG1196   527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkiraRAALAAALARGAIGAAVDLV 604
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 680 EQWRQTASEYESEIFNL---QTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEE 756
Cdd:COG1196   605 ASDLREADARYYVLGDTllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 757 LRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM---YLELKEKLDK 833
Cdd:COG1196   685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleELPEPPDLEE 764
                         570
                  ....*....|....
gi 1952581446 834 TQKENESITDELEN 847
Cdd:COG1196   765 LERELERLEREIEA 778
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
533-846 1.14e-08

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: 59.31  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  533 ELNESLNKVSLLKDELQcAHVQTGDSEREKQELQQELK-EAQELAisskqkcfemQALLEEERKTAKKQVEESTRQIQAL 611
Cdd:TIGR02169  181 EVEENIERLDLIIDEKR-QQLERLRREREKAERYQALLkEKREYE----------GYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  612 QAHLHKLQKDIEilreDKEIEIIETRDQLASTHKEIVALRqtaveaatgrESDIAILQGELHKVQTELEQWRQTASEYES 691
Cdd:TIGR02169  250 EEELEKLTEEIS----ELEKRLEEIEQLLEELNKKIKDLG----------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  692 EIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDA 771
Cdd:TIGR02169  316 EL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  772 SGLEVSRKALEVEVGTLKEQRLQ------------------------ETNGLRVKLAHAENETQKFQKQYEADQTMYLEL 827
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRlseeladlnaaiagieakineleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
                          330
                   ....*....|....*....
gi 1952581446  828 KEKLDKTQKENESITDELE 846
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELA 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
563-858 2.33e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  563 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 642
Cdd:TIGR02168  216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  643 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 722
Cdd:TIGR02168  279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  723 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 799
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  800 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 858
Cdd:TIGR02168  427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
14-110 2.42e-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: 52.62  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  14 SHPFQERHV---YLDEPVKIGRSvARCRPAQNNATfdckvLSRNHALIW---FDHKTG-KFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670     7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSApLVYVEDL-SSNGTYLNGKLIG 79
                          90       100
                  ....*....|....*....|....*
gi 1952581446  87 RGseespPCELLS-GDIIQFGVDVT 110
Cdd:cd22670    80 RN-----NTVLLSdGDVIEIAHSAT 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
161-387 4.18e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKEL 240
Cdd:COG1196   218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 241 VTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEK 320
Cdd:COG1196   298 ARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 321 LKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1196   374 LAEAEEELEELAEElleALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
271-857 1.14e-07

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: 55.80  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 271 KLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAlsekKELQHRIDEME 350
Cdd:TIGR04523  97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----NDLKKQKEELE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 351 EKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTDKehfLLKSGGDCSELFQQF 430
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 431 IECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATlIAEDDHTKVTEETKLLKEnQLEAKESDMS 510
Cdd:TIGR04523 249 SNTQTQLNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-ISDLNNQKEQDWNKELKS-ELKNQEKKLE 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 511 DTlspskdrssedttdyqmdEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSK----QKCFEM 586
Cdd:TIGR04523 325 EI------------------QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqSYKQEI 386
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 587 QAL------LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVALRQTAVEAATG 660
Cdd:TIGR04523 387 KNLesqindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 661 RES---DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCD 737
Cdd:TIGR04523 463 RESletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---------------EKKELEEKVKDLTKKISSLKEKIE 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 738 SLRQEKVLLTEKLQWFEEELrcaqqQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQ 814
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLI 602
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 1952581446 815 KQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQ 857
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
55-108 1.25e-07

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: 50.40  E-value: 1.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952581446  55 HALIWFDHKTGKFYLQDTKSSNGTFINSQRLSrgseESPPCELLSGDIIQFGVD 108
Cdd:cd22704    39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
25-114 1.47e-07

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: 50.43  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  25 DEPVKIGRSVArcrpAQNNATFDC-KVLSRNHALIWFDhKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDII 103
Cdd:cd22663    20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
                          90
                  ....*....|.
gi 1952581446 104 QFGVDVTENTR 114
Cdd:cd22663    91 QLGVPPENKEP 101
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
275-831 1.78e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 275 VERSLSNTEDECTHLKEMNDRTQEelRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQK------ALSEKKELQHRIDE 348
Cdd:PRK02224  178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETrdeadeVLEEHEERREELET 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 349 MEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNikdhnsigiqvDDLLPKIN-GSTDKEHFLLKS---GGDCS 424
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER-----------DDLLAEAGlDDADAEAVEARReelEDRDE 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 425 ELFQQFIECKNKLKAPVEPTQNNR--ISNVEDMFESHLENNQTTEEDLKNDSE---RFKATLIAEDDHTKVTEETKLLKE 499
Cdd:PRK02224  325 ELRDRLEECRVAAQAHNEEAESLRedADDLEERAEELREEAAELESELEEAREaveDRREEIEELEEEIEELRERFGDAP 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 500 NQLEAKEsDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQC----------AHVQTGDSEREK-QELQQE 568
Cdd:PRK02224  405 VDLGNAE-DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRERvEELEAE 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 569 LKEAQElaisskqkcfEMQALleEERKTAKKQVEESTRQIQALQAHLhklqKDIEILREDKEIEIIETRDQLASTHKEIV 648
Cdd:PRK02224  484 LEDLEE----------EVEEV--EERLERAEDLVEAEDRIERLEERR----EDLEELIAERRETIEEKRERAEELRERAA 547
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 649 ALRQTAVE----AATGRE------SDIAILQGELHKVQTELEQWRqTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQL 718
Cdd:PRK02224  548 ELEAEAEEkreaAAEAEEeaeearEEVAELNSKLAELKERIESLE-RIRTLLAAIADAED---------------EIERL 611
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 719 QGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRL 793
Cdd:PRK02224  612 REKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENEL 690
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 794 QETNGLRVKLAHAENETQKFQKQY---EADQTMYLELKEKL 831
Cdd:PRK02224  691 EELEELRERREALENRVEALEALYdeaEELESMYGDLRAEL 731
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
182-832 2.62e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.74  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTakeslrrv 261
Cdd:pfam15921  243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-------- 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  262 lqekieVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKE 341
Cdd:pfam15921  315 ------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  342 LQHRIDEMEEKEQLLQAR-------IEALQADNDFTNERLTALQVRLEQLQEKnikdhnsIGIQVDDLLPKINGSTDkeh 414
Cdd:pfam15921  389 REKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSE-------CQGQMERQMAAIQGKNE--- 458
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  415 fllkSGGDCSELFQQFIECKNKLKAPVEPTQNNRISnvedmfeshLENNQTTEEDLKND-SERFKATLIAEDDHTKVTEE 493
Cdd:pfam15921  459 ----SLEKVSSLTAQLESTKEMLRKVVEELTAKKMT---------LESSERTVSDLTASlQEKERAIEATNAEITKLRSR 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  494 TKL-LKENQLEAKESDMSDTLSPSKD----RSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQE 568
Cdd:pfam15921  526 VDLkLQELQHLKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  569 LKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIEIIETRDQLASTHKEIV 648
Cdd:pfam15921  606 LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNEVKTSRNELNSLSEDYE 677
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  649 ALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQKGEAVQLQGKldeLQKQ 728
Cdd:pfam15921  678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SDGHAMKVAMG---MQKQ 735
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  729 SNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQE-TNGLRVKLAH 805
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQERRLKEkVANMEVALDK 815
                          650       660
                   ....*....|....*....|....*....
gi 1952581446  806 AENETQKFQK--QYEADQTMYLELKEKLD 832
Cdd:pfam15921  816 ASLQFAECQDiiQRQEQESVRLKLQHTLD 844
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
30-106 3.78e-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: 3.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446  30 IGRSVArcrpaqNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRGseesppcELLSGDIIQFG 106
Cdd:cd22698    25 IGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQLG 86
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
254-841 5.14e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQ 333
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 334 kalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLlpkingstdke 413
Cdd:COG1196   317 ----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL----------- 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 414 hfllksggdcSELFQQFIECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKvTEE 493
Cdd:COG1196   382 ----------EELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALE 445
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 494 TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQ 573
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 574 ELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKeieiIETRDQLASTHKEIVALRQT 653
Cdd:COG1196   526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK----IRARAALAAALARGAIGAAV 601
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 654 AVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEifnlqtklqlQTQQQKDKQKGEAVQLQGKLDELQKQSNGLK 733
Cdd:COG1196   602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV----------TLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 734 NDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKF 813
Cdd:COG1196   672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
                         570       580
                  ....*....|....*....|....*...
gi 1952581446 814 QKQYEADQTMYLELKEKLDKTQKENESI 841
Cdd:COG1196   752 ALEELPEPPDLEELERELERLEREIEAL 779
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
27-117 1.59e-06

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: 47.36  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  27 PVKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgSEESPPCELLSGDIIQFG 106
Cdd:cd22678    24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
                          90
                  ....*....|.
gi 1952581446 107 vdvTENTRKVT 117
Cdd:cd22678    95 ---SETKILVR 102
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
234-758 2.34e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 234 DGIRKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNgavnE 313
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYI----K 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 314 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL----------LQARIEALQADNDfTNERLTALQVRLEQ 383
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHE-LYEEAKAKKEELER 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 384 LQ--------EKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGdcsELFQQFIECKN-KLKAPV---EPTQNNRisn 451
Cdd:PRK03918  377 LKkrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK---ELKKAIEELKKaKGKCPVcgrELTEEHR--- 450
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 452 VEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKE----NQLEAKESDMSdtlSPSKDRSSEDTTDY 527
Cdd:PRK03918  451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLK---KYNLEELEKKAEEY 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 528 QMDEQELNESLNKVSLLKDELQcahvQTGDSEREKQELQQELKEAQElaisskqkcfEMQALLEEERKTAKKQVEESTRQ 607
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE----------ELAELLKELEELGFESVEELEER 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 608 IQALQAHLHKLqkdIEILREDKEIEIIEtrdqlasthKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQtas 687
Cdd:PRK03918  594 LKELEPFYNEY---LELKDAEKELEREE---------KELKKLEEELDKA----FEELAETEKRLEELRKELEELEK--- 654
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581446 688 EYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ--EKVLLTEKLQWFEEELR 758
Cdd:PRK03918  655 KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakKELEKLEKALERVEELR 727
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
557-780 2.52e-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: 50.53  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 557 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 636
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 637 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 714
Cdd:COG4942    96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581446 715 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 780
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
51-106 3.04e-06

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: 46.78  E-value: 3.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581446  51 LSRNHALIWF----DHKTGKFYLQDTKSSNGTFINSQRLsrgseesPP---CELLSGDIIQFG 106
Cdd:cd22677    41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
469-810 5.20e-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: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 469 DLKNDSERFKATLI------AEDDHTKVTEETKLLKE--NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNK 540
Cdd:COG1196   217 ELKEELKELEAELLllklreLEAELEELEAELEELEAelEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 541 VSLLKDELQCAHVQTGDSEREKQELQQELKEAQelaisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQK 620
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 621 DIEILREdKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKL 700
Cdd:COG1196   366 ALLEAEA-ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEA 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 701 QLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSR 778
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLA 523
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1952581446 779 KALEVEVGTLKEQRLQETNGLRVKLAHAENET 810
Cdd:COG1196   524 GAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
PTZ00121 PTZ00121
MAEBL; Provisional
225-865 5.58e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  225 QAYSKNQTEDGIRKELVTLQEDKHSYETTAK-ESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR 301
Cdd:PTZ00121  1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  302 ELANKyngaVNELKEFTEKLKQAEGKQ-------EEIQQKALSEKK--ELQHRIDEMEEKEQLLQARIEALQADNDFTNE 372
Cdd:PTZ00121  1275 EEARK----ADELKKAEEKKKADEAKKaeekkkaDEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  373 RLTALQVRLEQLQEKNIKDH--NSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRIS 450
Cdd:PTZ00121  1351 EAEAAADEAEAAEEKAEAAEkkKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  451 NVEDMFESHLENNQTTEEDLKNDSERFKAtliaeDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMD 530
Cdd:PTZ00121  1431 KKADEAKKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  531 EQELNESlnkvsllkDELQCAHVQTGDSEREKQELQQ---ELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQ 607
Cdd:PTZ00121  1506 AEAKKKA--------DEAKKAEEAKKADEAKKAEEAKkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  608 IQALQAhlhklqkdiEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGREsdiailqgELHKVQTELEQWRQTAS 687
Cdd:PTZ00121  1578 MALRKA---------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKK 1640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  688 EYESEIFNLQTKLQLQTQQQ--KDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLR---QEKVLLTEKLQWFEEELRCAQQ 762
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEE 1720
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  763 QSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESIT 842
Cdd:PTZ00121  1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
                          650       660
                   ....*....|....*....|...
gi 1952581446  843 DELencKENLKLLQQKGNNGGLF 865
Cdd:PTZ00121  1801 KDI---FDNFANIIEGGKEGNLV 1820
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
601-861 6.94e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  601 VEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELE 680
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA----EEELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  681 QWRQTASEYESEIfnlqtklqlqtqqqkdkqkgeaVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCA 760
Cdd:TIGR02168  271 ELRLEVSELEEEI----------------------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  761 QQQSVKLTKDAsglevsrKALEVEVGTLKEQRlqetNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENES 840
Cdd:TIGR02168  329 ESKLDELAEEL-------AELEEKLEELKEEL----ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
                          250       260
                   ....*....|....*....|.
gi 1952581446  841 ITDELENCKENLKLLQQKGNN 861
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRER 418
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
49-105 7.30e-06

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438724 [Multi-domain]  Cd Length: 108  Bit Score: 45.75  E-value: 7.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446  49 KVLSRNHALIWFDHKtGKFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQF 105
Cdd:cd22672    39 KLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
52-106 7.58e-06

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: 45.72  E-value: 7.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  52 SRNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22674    48 SRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
25-108 8.36e-06

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: 45.88  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  25 DEPVKIGRsvarcRPAQNNAT----FDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSR-GSEESPPCELLS 99
Cdd:cd22702    31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103

                  ....*....
gi 1952581446 100 GDIIQFGVD 108
Cdd:cd22702   104 SDVIEFGSD 112
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
239-630 1.50e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 239 ELVTLQEDKHSYE------------TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRElanK 306
Cdd:pfam07888   5 ELVTLEEESHGEEggtdmllvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES---R 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 307 YNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQllqaRIEALQADNDFTNERLTALQVRLEQLQE 386
Cdd:pfam07888  82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA----RIRELEEDIKTLTQRVLERETELERMKE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 387 KNIKDHNSIGIQVDDllpkingSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnvedmfesHLENNQTT 466
Cdd:pfam07888 158 RAKKAGAQRKEEEAE-------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------------QLQDTITT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 467 EEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLLKD 546
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASLALR 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 547 ELQC-------AHVQTGDSEREK-QELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKL 618
Cdd:pfam07888 297 EGRArwaqereTLQQSAEADKDRiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376
                         410
                  ....*....|..
gi 1952581446 619 QKDIEILREDKE 630
Cdd:pfam07888 377 QKEKEQLQAEKQ 388
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
256-857 1.68e-05

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: 48.89  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  256 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI 331
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  332 QQKALSEKKELQHRIDEMEEkeqllqariealQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTD 411
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIENIVTK-IDKKKNIYDEIKKLLNEIAEIEK 1204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  412 KEHFL-------LKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFES--HLENNQTTEEDLKNDSERFKATLI 482
Cdd:TIGR01612 1205 DKTSLeevkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISHD 1284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  483 AEDDHTKVTEE---------TKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHV 553
Cdd:TIGR01612 1285 DDKDHHIISKKhdenisdirEKSLKIIEDFSEESDINDI----KKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI 1360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  554 Q---------TGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHlhklqkdieI 624
Cdd:TIGR01612 1361 KkiidevkeyTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNH---------I 1431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  625 LREDKEieiIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ-----GELHKVQTELEQWRQTASEYESEI------ 693
Cdd:TIGR01612 1432 LSEESN---IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHIDKSKGCKDEAdknaka 1508
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  694 --FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKlqwFEEELRCAQQQSVKLTKDA 771
Cdd:TIGR01612 1509 ieKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK---SEQKIKEIKKEKFRIEDDA 1585
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  772 SGLEVSRKA---LEVEVGTLKEQRLQETNgLRVKLAHAENETQKFQKQ-----YEADQTMYLELKEKLDKTQKENESITD 843
Cdd:TIGR01612 1586 AKNDKSNKAaidIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKissfsIDSQDTELKENGDNLNSLQEFLESLKD 1664
                          650
                   ....*....|....
gi 1952581446  844 ELENCKENLKLLQQ 857
Cdd:TIGR01612 1665 QKKNIEDKKKELDE 1678
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
13-110 1.75e-05

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: 44.14  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  13 NSHPFQERHVYLDE-PVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDHKTgkFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665     7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
                          90       100
                  ....*....|....*....|.
gi 1952581446  92 SPPC--ELLSGDIIQFGvDVT 110
Cdd:cd22665    74 KPNVryELIDGDLLLFG-DVK 93
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
28-106 1.78e-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: 44.25  E-value: 1.78e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  28 VKIGRSVarcrpaQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRlsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22680    23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
52-107 1.94e-05

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: 44.24  E-value: 1.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  52 SRNHALIWFDHKTG---------KFYLQDTkSSNGTFINSQRLSRGSEesppCELLSGDIIQFGV 107
Cdd:cd22667    40 SRKHATLTVLHPEAnlsdpdtrpELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
18-86 2.23e-05

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: 43.86  E-value: 2.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  18 QERHVYLDEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFDhkTGKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694     8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
1-106 2.58e-05

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: 47.45  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446   1 MPSALAIFTCRPNSHPFQERHVYLDEPVKIGRSvARC-----RPAQnnatfdckVLSRNHALIWFDHktGKFYLQDTkSS 75
Cdd:COG3456     1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1952581446  76 NGTFIN--SQRLSRGSEEsppcELLSGDIIQFG 106
Cdd:COG3456    69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
337-681 2.89e-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: 48.13  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  337 SEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQekniKDHNSIGIQVDDLLPKINGSTDKehfl 416
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEER---- 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  417 lksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATliaEDDHTKVTEETKL 496
Cdd:TIGR02168  749 -----------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  497 LKENQLEAKEsdmsdtlspskdRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELa 576
Cdd:TIGR02168  815 LNEEAANLRE------------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE- 881
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  577 issKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKeivALRQT 653
Cdd:TIGR02168  882 ---RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeglEVRIDNLQERLSEEYS---LTLEE 955
                          330       340
                   ....*....|....*....|....*...
gi 1952581446  654 AVEAATGRESDIAILQGELHKVQTELEQ 681
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKIKE 983
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
12-103 2.90e-05

second 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 second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 43.82  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  12 PNSHPfqerHVYL-DEPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFD-HKTGK--FYLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690     8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKrSGKGLddVYVTDT-STNGTFINNNRLGK 76
                          90
                  ....*....|....*.
gi 1952581446  88 GSEesppCELLSGDII 103
Cdd:cd22690    77 GSQ----SLLQDGDEI 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
264-692 3.06e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  264 EKIEVVR-KLSEVERSLSNTEDECTHLKEMNDRTQEElRELANKYNGAVNELKEFTEKLKQAEgkqeeiQQKALSEKKEL 342
Cdd:TIGR02169  170 RKKEKALeELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  343 QHRIDEMEEKEQLLQARIEALqadndftNERLTALQVRLEQLQEKnikdhnsigiqvddllpkINGSTDKEHFLLKSggD 422
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKK------------------IKDLGEEEQLRVKE--K 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  423 CSELFQQFIECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQL 502
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKER--ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  503 EAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEaqelaisskqk 582
Cdd:TIGR02169  374 EEVDKEFAET----RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE----------- 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  583 cfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiietrdqlasthkeivalrqtaveaatgre 662
Cdd:TIGR02169  439 -------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE---------------------------------- 477
                          410       420       430
                   ....*....|....*....|....*....|
gi 1952581446  663 sdIAILQGELHKVQTELEQWRQTASEYESE 692
Cdd:TIGR02169  478 --YDRVEKELSKLQRELAEAEAQARASEER 505
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
233-661 3.78e-05

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: 47.74  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  233 EDGIRKELVTLQ----EDKHSYETTAK--ESLRRVLQEKIEVVRKLSE------VERSL-SNTEDECTHLKEMNdrtqEE 299
Cdd:TIGR01612 1269 EMDIKAEMETFNishdDDKDHHIISKKhdENISDIREKSLKIIEDFSEesdindIKKELqKNLLDAQKHNSDIN----LY 1344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  300 LRELANKYN-GAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL--LQARIEALQADNDFTN--ERL 374
Cdd:TIGR01612 1345 LNEIANIYNiLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeCKSKIESTLDDKDIDEciKKI 1424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  375 TALQVRLeqLQE--------KNIKDHNSigiQVDDLLPKINGSTDKEHFLLKSGGD------------CSELFQQFIECK 434
Cdd:TIGR01612 1425 KELKNHI--LSEesnidtyfKNADENNE---NVLLLFKNIEMADNKSQHILKIKKDnatndhdfnineLKEHIDKSKGCK 1499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  435 NKLKAPVEPTQNNRIsnvedMFESHLEN-----NQTTEEDLKNDSERFKA---TLIAE--DDHTKVT--EETKLLKENQL 502
Cdd:TIGR01612 1500 DEADKNAKAIEKNKE-----LFEQYKKDvtellNKYSALAIKNKFAKTKKdseIIIKEikDAHKKFIleAEKSEQKIKEI 1574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  503 EAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQqelKEAQELAISSKQK 582
Cdd:TIGR01612 1575 KKEKFRIEDDAA-KNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFS---IDSQDTELKENGD 1650
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  583 CFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 661
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN 1729
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
49-112 3.83e-05

forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438733 [Multi-domain]  Cd Length: 129  Bit Score: 43.97  E-value: 3.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  49 KVLSRNHALIWFDHKTG--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---ELLSGDIIQFGVDVTEN 112
Cdd:cd22681    64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
267-392 4.01e-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: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 267 EVVRKLSEveRSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLK-QAEGKQEEIQ--QKALSEKKELQ 343
Cdd:COG2433   380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaELEEKDERIErlERELSEARSEE 457
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1952581446 344 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDH 392
Cdd:COG2433   458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
30-106 4.02e-05

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: 43.29  E-value: 4.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446  30 IGRSVarcrpaQNNATFDCKVLSRNHALiwFDHKTGKFYLQDTKSSNGTFINSQRLSRGSEesppCELLSGDIIQFG 106
Cdd:cd22682    24 IGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS----CDLQNGDQIKIG 88
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
246-860 4.17e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  246 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDectHLKEMNDRTqEELRELANKYNGAVNELKEFTEKLKQAE 325
Cdd:pfam15921  131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED---MLEDSNTQI-EQLRKMMLSHEGVLQEIRSILVDFEEAS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  326 GKQ-------------------EEIQQKALSEKKELQHRI----DEMEEKEQLLQARIE-ALQADNDFTNERLTALQVRL 381
Cdd:pfam15921  201 GKKiyehdsmstmhfrslgsaiSKILRELDTEISYLKGRIfpveDQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEI 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  382 EQLQEKNI---KDHNSIGIQVDDLLPKI-NGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 457
Cdd:pfam15921  281 TGLTEKASsarSQANSIQSQLEIIQEQArNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE 360
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  458 SHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDttDYQMDEQEL--- 534
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLeal 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  535 ----------------------NESLNKVSLLKDELQcahvqtgDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 592
Cdd:pfam15921  435 lkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLE-------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  593 ERKTAKKQVEESTR-------QIQALQ------AHLHKLQKDIEILR-----EDKEIEI----IETRDQLASTHKEIVAL 650
Cdd:pfam15921  508 KERAIEATNAEITKlrsrvdlKLQELQhlknegDHLRNVQTECEALKlqmaeKDKVIEIlrqqIENMTQLVGQHGRTAGA 587
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  651 RQtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSN 730
Cdd:pfam15921  588 MQ--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERD 656
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  731 GLKNDCDSLRQEKVLLTEKLQWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENE 809
Cdd:pfam15921  657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952581446  810 TQKfQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 860
Cdd:pfam15921  737 TAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
258-858 4.26e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 258 LRRVLQ-EKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQqKA 335
Cdd:PRK03918  151 VRQILGlDDYEnAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 336 LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDhnsigiqvddlLPKINGSTDKEHF 415
Cdd:PRK03918  230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKE-----------LKELKEKAEEYIK 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 416 LlksggdcSELFQQFIECKNKLKAPVEpTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHtKVTEETK 495
Cdd:PRK03918  298 L-------SEFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAK 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 496 LLKEN--QLEAKESDMSdtlspskdrssedttdyqmdEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQ 573
Cdd:PRK03918  369 AKKEEleRLKKRLTGLT--------------------PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 574 ELAISSKQKCFEMQALLEEERKtaKKQVEESTRQIQALQAHLHKLQKDIEILR-EDKEIEIIETRDqlasthKEIVALRQ 652
Cdd:PRK03918  429 EELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRkELRELEKVLKKE------SELIKLKE 500
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 653 TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGL 732
Cdd:PRK03918  501 LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-----KSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 733 KNDCDSLRQEKVlltEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR--LQETNGLRVKLAHAENET 810
Cdd:PRK03918  576 LKELEELGFESV---EELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFeeLAETEKRLEELRKELEEL 652
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446 811 QKF--QKQYEADQTMYLEL-------KEKLDKTQKENESITDELENCKENLKLLQQK 858
Cdd:PRK03918  653 EKKysEEEYEELREEYLELsrelaglRAELEELEKRREEIKKTLEKLKEELEEREKA 709
PTZ00121 PTZ00121
MAEBL; Provisional
239-861 4.87e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  239 ELVTLQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKE 316
Cdd:PTZ00121  1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  317 FTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNS 394
Cdd:PTZ00121  1362 AEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  395 IGIQVDDLLPKINGSTDKEHFLLKSggdcselfqqfiecKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDS 474
Cdd:PTZ00121  1442 EAKKADEAKKKAEEAKKAEEAKKKA--------------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  475 ERFKATLIAEDDHTKVTEETKllkenqlEAKESDMSDTLSPSKDRSSEDTTDyQMDEQELNESLNKVSLLKDELQCAHVQ 554
Cdd:PTZ00121  1508 AKKKADEAKKAEEAKKADEAK-------KAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMA 1579
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  555 TGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAK--KQVEESTRQIQALQAHLHKLQKDIEILREDKEIE 632
Cdd:PTZ00121  1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  633 IIEtRDQLASTHKEIVALRQTA---------VEAATGRESDIAILQGELHKVQTElEQWRQTASEYESEIFNLQTKLQLQ 703
Cdd:PTZ00121  1660 KIK-AAEEAKKAEEDKKKAEEAkkaeedekkAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKKAEEENKIKAEEAKK 1737
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  704 TQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEK-VLLTEKLQWFEEELRCAQQQSVKLTKDASG-LEVSRKAL 781
Cdd:PTZ00121  1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIKDIFDNFAnIIEGGKEG 1817
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  782 EVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENlKLLQQKGNN 861
Cdd:PTZ00121  1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKIDKD 1896
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-359 5.78e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  178 REQML--EQKLATLQRLLANTQEAsDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYE---T 252
Cdd:COG4913    241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEF 317
Cdd:COG4913    320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1952581446  318 TEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEK-----EQLLQAR 359
Cdd:COG4913    400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRksnipARLLALR 446
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
164-841 6.97e-05

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: 46.89  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  164 ELFQLSQYLQEA---------LHREQMLEQKLATLQRLLANTQeaSDSSWQALIDEDRLLSRLEVMGNQLQaysknQTED 234
Cdd:TIGR00618  171 NLFPLDQYTQLAlmefakkksLHGKAELLTLRSQLLTLCTPCM--PDTYHERKQVLEKELKHLREALQQTQ-----QSHA 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  235 GIRKELvTLQEDKHSYETTAKESLRRV------------LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRE 302
Cdd:TIGR00618  244 YLTQKR-EAQEEQLKKQQLLKQLRARIeelraqeavleeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  303 LANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKK-ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 381
Cdd:TIGR00618  323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  382 EQLQEknikdhnsigiQVDDLLPKINGSTDKEHFLLKSGGDCsELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLE 461
Cdd:TIGR00618  403 DILQR-----------EQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  462 NNQTtEEDLKNDSERFKATliaeddHTKVTEETKLLKENQLEAKESDMS-DTLSPSKDRSSEDTTDYQMDEQELNESLNK 540
Cdd:TIGR00618  471 REQQ-LQTKEQIHLQETRK------KAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  541 VSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQK 620
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  621 DIEILREDKEIEIIETRDQLASTHKEivalrQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKL 700
Cdd:TIGR00618  624 EQDLQDVRLHLQQCSQELALKLTALH-----ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  701 QLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDcdsLRQEKVLLTEKLQWFEEELRCAQQQSVkltkdasgLEVSRKA 780
Cdd:TIGR00618  699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKART--------EAHFNNN 767
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581446  781 LEVevgTLKEQRLQEtnglrvkLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESI 841
Cdd:TIGR00618  768 EEV---TAALQTGAE-------LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-630 7.10e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 7.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  294 DRTQEELRELankyNGAVNELKEFTEKLK-QAEGKQEEIQQKAlsEKKELQH-----RIDEMEEKEQLLQARIEALQADN 367
Cdd:TIGR02168  182 ERTRENLDRL----EDILNELERQLKSLErQAEKAERYKELKA--ELRELELallvlRLEELREELEELQEELKEAEEEL 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  368 DFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLpkingstdkehfllksggdcselfqqfiecknklkapvepTQNN 447
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELY----------------------------------------ALAN 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  448 RISNVEDMFESH---LENNQTTEEDLKNDSERFKATLI-AEDDHTKVTEETKLLKEN--QLEAKESDMSDTLSPSKDRSS 521
Cdd:TIGR02168  296 EISRLEQQKQILrerLANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEEleSLEAELEELEAELEELESRLE 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  522 EDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ-------------- 587
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleeleeeleelqee 455
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1952581446  588 -ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE 630
Cdd:TIGR02168  456 lERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
53-106 7.39e-05

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: 42.24  E-value: 7.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952581446  53 RNHALIWFDHKTGKFYLQDTKSSNGTFINSQRLSRGSeesppCELLSGDIIQFG 106
Cdd:cd22700    36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAA-----VRLAPGDVLRFG 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
182-387 8.40e-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: 45.91  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 182 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVTLQEDKHSYETtAKESLRRV 261
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKEIAELRA-ELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 262 LQEKIEVVRKLSEVER--------SLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEE 330
Cdd:COG4942   106 LAELLRALYRLGRQPPlalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLaelAALRAELEAERAELEALLAELEE 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446 331 IQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
592-792 1.20e-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: 45.53  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 592 EERKTAKKQVEESTRQIQALQAHLHKLQKDI-EILREDKEIE--IIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 668
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALErrIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 669 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 743
Cdd:COG4942    96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1952581446 744 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 792
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
258-387 1.82e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI----QQ 333
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEY 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446 334 KALS-EKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG1579    92 EALQkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
523-692 1.93e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  523 DTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQE--LAISSKQKcfemqALLEEERKTAKKQ 600
Cdd:COG4913    279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqiRGNGGDRL-----EQLEREIERLERE 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  601 VEESTRQIQALQAHLHKLQKDIeilrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELE 680
Cdd:COG4913    354 LEERERRRARLEALLAALGLPL----PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
                          170
                   ....*....|..
gi 1952581446  681 QWRQTASEYESE 692
Cdd:COG4913    430 SLERRKSNIPAR 441
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
152-365 2.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 152 KVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 231
Cdd:COG4717    60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 232 TEDGIRKELVTLQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMND-RTQEELRELANKYNGA 310
Cdd:COG4717   133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446 311 VNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQA 365
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIA 255
mukB PRK04863
chromosome partition protein MukB;
253-619 2.22e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  253 TAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELR--ELANKYNGAVNEL-----------KEFTE 319
Cdd:PRK04863   297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRqqEKIERYQADLEELeerleeqnevvEEADE 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  320 KLKQAEGKQEEIQQKALSEKKEL---QHRIDEMEEK----EQLLQA--RIEALQADNDFT----NERLTALQVRLEQLQE 386
Cdd:PRK04863   377 QQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRaiqyQQAVQAleRAKQLCGLPDLTadnaEDWLEEFQAKEQEATE 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  387 KNI---------KDHNSIGIQVDDLLPKINGSTDKEhfllksggDCSELFQQFIECKNKLKAPVEPTQNNRISNVEdmFE 457
Cdd:PRK04863   457 ELLsleqklsvaQAAHSQFEQAYQLVRKIAGEVSRS--------EAWDVARELLRRLREQRHLAEQLQQLRMRLSE--LE 526
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  458 SHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEEtkllKENQLEakesdmsdTLSPSKDRSSEDTTDYQMDEQELNES 537
Cdd:PRK04863   527 QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE----LEARLE--------SLSESVSEARERRMALRQQLEQLQAR 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  538 LNKVSLLKDELQCAhvqtgdserekQELQQELKEAQELAISSKQKCFE-MQALLEEERKtAKKQVEESTRQIQALQAHLH 616
Cdd:PRK04863   595 IQRLAARAPAWLAA-----------QDALARLREQSGEEFEDSQDVTEyMQQLLERERE-LTVERDELAARKQALDEEIE 662

                   ...
gi 1952581446  617 KLQ 619
Cdd:PRK04863   663 RLS 665
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
198-387 2.43e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 198 EASDSSWQALIdEDRLLSRLEvmgNQLQAYSKNQTEDGIR--KELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEV 275
Cdd:COG4717    33 EAGKSTLLAFI-RAMLLERLE---KEADELFKPQGRKPELnlKELKELEEELKEAEEKEEE-YAELQEELEELEEELEEL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 276 ERSLSNTEDECTHLKEMND---------RTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRI 346
Cdd:COG4717   108 EAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 347 DEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4717   188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
559-742 2.87e-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: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  559 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRD 638
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  639 QLASTHKEIVALRQ---TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgea 715
Cdd:COG4913    693 QLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--- 769
                          170       180
                   ....*....|....*....|....*..
gi 1952581446  716 vQLQGKLDELQKQSNGLKNDCDSLRQE 742
Cdd:COG4913    770 -NLEERIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
565-763 2.96e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 565 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 644
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 645 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 721
Cdd:COG4717   123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952581446 722 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 763
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
16-111 4.14e-04

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: 39.98  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  16 PFQERHVYLD-EPVKIGRSvarcrpAQNNATFDCKVLSRNHALIWFdhKTGKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693     7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
                          90
                  ....*....|....*..
gi 1952581446  95 CELLSGDIIQFGVDVTE 111
Cdd:cd22693    73 VVVQPGDTIRIGATVFE 89
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
554-689 4.26e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 554 QTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKE 630
Cdd:COG3206   213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNH 290
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446 631 IEIIETRDQLASTHKEIVALRQTAVEAAtgrESDIAILQGELHKVQTELEQWRQTASEY 689
Cdd:COG3206   291 PDVIALRAQIAALRAQLQQEAQRILASL---EAELEALQAREASLQAQLAQLEARLAEL 346
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
163-362 5.67e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.53  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 163 QELFQLSQYLQEALHREQML----------------EQKLATLQRLLANTQ---EASDSSWQALIDEDR-LLSRLEVMGN 222
Cdd:COG0497   172 KELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAEklrEALQEALEALSGGEGgALDLLGQALR 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 223 QLQAYSKNQTEdgirkelvtLQEdkhsyettAKESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLKEMNDRtQEELRE 302
Cdd:COG0497   252 ALERLAEYDPS---------LAE--------LAERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRR 310
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446 303 LANKYNGAVNELKEFTEKLKQaegKQEEIQQKAlSEKKELQHRIDEMEEK-----EQLLQARIEA 362
Cdd:COG0497   311 LARKYGVTVEELLAYAEELRA---ELAELENSD-ERLEELEAELAEAEAElleaaEKLSAARKKA 371
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
52-106 6.62e-04

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: 39.97  E-value: 6.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  52 SRNHALIWF----------DHKTGKFYLQDTKSSNGTFINSQRLsrgsEESPPCELLSGDIIQFG 106
Cdd:cd22676    42 SKQHAVIQFrevekrnegdVIENIRPYIIDLGSTNGTFLNGEKI----EPRRYYELREKDVLKFG 102
46 PHA02562
endonuclease subunit; Provisional
289-546 6.99e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 289 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALqadnd 368
Cdd:PHA02562  165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 369 ftNERLTALQVRLEQlQEKNIKDHNSIGIQVDDLLPKINgstdKEHFLLKSGGDCSELFQQFIECKNKLKA----PVEPT 444
Cdd:PHA02562  240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKikdkLKELQ 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 445 Q-----NNRISNVEDMFESHLEnNQTTEEDLKNDSERFKATLIAEDDHTKVTEetKLLKenQLEAKESDMSDTLSPSKDR 519
Cdd:PHA02562  313 HsleklDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIE--ELQAEFVDNAEELAKLQDE 387
                         250       260
                  ....*....|....*....|....*..
gi 1952581446 520 SSEDTTDYQMDEQELNESLNKVSLLKD 546
Cdd:PHA02562  388 LDKIVKTKSELVKEKYHRGIVTDLLKD 414
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
310-387 8.91e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 8.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446 310 AVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
211-651 9.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 211 DRLLSRLEVMGNQLQAYSKNQTE-DGIRKELVTLQEDKHsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHL 289
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEElEELEEELEELEAELE--ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 290 KEmndrTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKElqhRIDEMEEKEQLLQARIEALQADNDF 369
Cdd:COG4717   152 EE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE---ELEELQQRLAELEEELEEAQEELEE 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 370 TNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSELFQQFIECKNKLKAPVEPT 444
Cdd:COG4717   225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvLGLLALLFLLLAREKASLGKEA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 445 QNNRISNVEDMFESHLENNQTTEEDLKND---SERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSS 521
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 522 EDTTDYQMDEQELNESLNKVSLLKDELQcahvqtGDSEREKQELQQELKEAQELAISSkqkcfemqalLEEERKTAKKQV 601
Cdd:COG4717   385 EELRAALEQAEEYQELKEELEELEEQLE------ELLGELEELLEALDEEELEEELEE----------LEEELEELEEEL 448
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952581446 602 EESTRQIQALQAHLHKLQKDIEIlrEDKEIEIIETRDQLASTHKEIVALR 651
Cdd:COG4717   449 EELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALK 496
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
50-106 1.12e-03

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: 38.99  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446  50 VLSRNHALIWFDHKTGkfYLQDTKSSNGTFINSQRLsrgseeSPPCELLSGDIIQFG 106
Cdd:cd22668    36 GVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
500-693 1.19e-03

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: 42.06  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 500 NQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAISS 579
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 580 KQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLASTHKEIVALRQT 653
Cdd:COG4942   110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEALLAELEEERAA 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952581446 654 AVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 693
Cdd:COG4942   190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
163-366 1.21e-03

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: 42.06  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID--------EDRLLSRLEVMGNQLQAYSKNQTED 234
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelRAELEAQKEELAELLRALYRLGRQP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 235 GIrkELVTLQEDKHSYETTAK--ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNDRTQEELRELAnkyngav 311
Cdd:COG4942   121 PL--ALLLSPEDFLDAVRRLQylKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLAELEEERAALE------- 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446 312 nelkefteklkQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAD 366
Cdd:COG4942   192 -----------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
586-835 1.24e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 586 MQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIeiIETRDQLASTHKEIVALRQTAVEAatgrESDI 665
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEA----RAEL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 666 AILQGELHKVQTELEQWRQTASEyeseifnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 745
Cdd:COG3206   236 AEAEARLAALRAQLGSGPDALPE-------------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 746 LTEKLQwfeeelRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKeQRLQETNGLRVKLAhaenetqKFQKQYEADQTMYL 825
Cdd:COG3206   303 LRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLE-ARLAELPELEAELR-------RLEREVEVARELYE 368
                         250
                  ....*....|
gi 1952581446 826 ELKEKLDKTQ 835
Cdd:COG3206   369 SLLQRLEEAR 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
297-387 1.79e-03

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: 41.67  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 297 QEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA 376
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                          90
                  ....*....|.
gi 1952581446 377 LQVRLEQLQEK 387
Cdd:COG4942    95 LRAELEAQKEE 105
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
590-858 1.83e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 590 LEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIE-------IIETRDQLASTHKEIVALRQ 652
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKEleqnnkkIKELEKQLNQLKSEISDLNN 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 653 TAVEAATGR-ESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgeavQLQGKLDELQKqsng 731
Cdd:TIGR04523 303 QKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR----ELEEKQNEIEK---- 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 732 LKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRV 801
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKEL 454
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446 802 KLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 858
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
159-325 2.31e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 159 SMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIRk 238
Cdd:COG3206   215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD- 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 239 eLVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFT 318
Cdd:COG3206   293 -VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371

                  ....*..
gi 1952581446 319 EKLKQAE 325
Cdd:COG3206   372 QRLEEAR 378
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
532-681 2.63e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 532 QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQELAisskqkcfemqalleeERKTAKKQVEESTRQIQAL 611
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----------------KKYEEQLGNVRNNKEYEAL 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581446 612 QAHLHKLQKDIEILrEDKEIEIIETRD----QLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQ 681
Cdd:COG1579    95 QKEIESLKRRISDL-EDEILELMERIEeleeELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
172-387 2.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 172 LQEALHREQMLEQKLATLQRLLAnTQEASdsswqalIDEDRL-LSRLEVMGNQLQAYSKNQTEDGIRKELvtlQEDKHSY 250
Cdd:PRK02224  504 LVEAEDRIERLEERREDLEELIA-ERRET-------IEEKRErAEELRERAAELEAEAEEKREAAAEAEE---EAEEARE 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEC-------THLKEMNDRTQEEL-------RELANKYNGAvnELKE 316
Cdd:PRK02224  573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDEIerlrekrEALAELNDERRERLaekrerkRELEAEFDEA--RIEE 650
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581446 317 FTEKLKQAEGKQEEIQQKalsekkelqhrIDEMEEKEQLLQARIEALQADndftNERLTALQVRLEQLQEK 387
Cdd:PRK02224  651 AREDKERAEEYLEQVEEK-----------LDELREERDDLQAEIGAVENE----LEELEELRERREALENR 706
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
263-861 3.22e-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: 41.31  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  263 QEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGA----------VNELKEFTEKLKQAEGKQEEIQ 332
Cdd:pfam01576   12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRLEEEEERS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  333 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHnsigiqvddllpkingstdK 412
Cdd:pfam01576   92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS-------------------K 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  413 EHFLLKSggDCSELFQQFIECKNKLKAPveptqnNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAE--DDHTKV 490
Cdd:pfam01576  153 ERKLLEE--RISEFTSNLAEEEEKAKSL------SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEstDLQEQI 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  491 TEETKLLKE--NQLEAKESDMSDTLspskDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQE 568
Cdd:pfam01576  225 AELQAQIAElrAQLAKKEEELQAAL----ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  569 LKE--------------AQELAISSKQKCFEMQALLEEERKTAKKQVEE-STRQIQALQahlhKLQKDIEILREDKeIEI 633
Cdd:pfam01576  301 LEAlkteledtldttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEmRQKHTQALE----ELTEQLEQAKRNK-ANL 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  634 IETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYEsEIFNLQTKLQLQTQQQKDKQKG 713
Cdd:pfam01576  376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA-EKLSKLQSELESVSSLLNEAEG 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  714 EAVQLQGKLDELQKQSnglkNDCDSLRQE----KVLLTEKLQWFEEELRCAQQQsvkltkdASGLEVSRKALEVEVGTLK 789
Cdd:pfam01576  455 KNIKLSKDVSSLESQL----QDTQELLQEetrqKLNLSTRLRQLEDERNSLQEQ-------LEEEEEAKRNVERQLSTLQ 523
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446  790 EQ------RLQETNGlrvKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGNN 861
Cdd:pfam01576  524 AQlsdmkkKLEEDAG---TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
559-858 3.37e-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: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  559 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRD 638
Cdd:COG4913    351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIA 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  639 QLASTHK----EIVALRQTAVEAATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQ 697
Cdd:COG4913    430 SLERRKSnipaRLLALRDALAEALGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRL 508
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  698 TKLQ-------LQTQQQKDKQKGEAVQLQGKL---------------------------DELQ------------KQSNG 731
Cdd:COG4913    509 HLRGrlvyervRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGT 588
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  732 L--KNDCDSLRQEKVL---LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHA 806
Cdd:COG4913    589 RheKDDRRRIRSRYVLgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASA 666
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  807 ENETQKFQKQY---EADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 858
Cdd:COG4913    667 EREIAELEAELerlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
213-669 3.48e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 213 LLSRLEVMGNQlQAYSKNQTEdgIRKELVTLQEDKHSYETTAKESLRRVLQEKIEVVRK----LSEVERSLSNTEDECTH 288
Cdd:pfam10174 308 LQTKLETLTNQ-NSDCKQHIE--VLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTLAGEIRD 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 289 LKEMNDRTQEELRELANKYNGAVNELKEfteKLKQAEGKQEEIQ----------------QKALSEKKELQHRIDEMEEK 352
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQLRD---KDKQLAGLKERVKslqtdssntdtalttlEEALSEKERIIERLKEQRER 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 353 E-QLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFI 431
Cdd:pfam10174 462 EdRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 432 ECKN-KLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLkndsERFKATLiaeddhtKVTEETKLLKENQLEAKESdms 510
Cdd:pfam10174 542 KAHNaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV----ERLLGIL-------REVENEKNDKDKKIAELES--- 607
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 511 dtlspskdrssedTTDYQMDEQElneslnkvsllKDELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfEMQALL 590
Cdd:pfam10174 608 -------------LTLRQMKEQN-----------KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL--QLEELM 661
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 591 EEERKTaKKQVEESTRQIQALQAHLHKLQKDIEILRedkeieiIETRDQLasthKEIVALRQTAVEAA-TGRESDIAILQ 669
Cdd:pfam10174 662 GALEKT-RQELDATKARLSSTQQSLAEKDGHLTNLR-------AERRKQL----EEILEMKQEALLAAiSEKDANIALLE 729
prfA PRK00591
peptide chain release factor 1; Validated
560-611 3.57e-03

peptide chain release factor 1; Validated


Pssm-ID: 234801 [Multi-domain]  Cd Length: 359  Bit Score: 40.45  E-value: 3.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952581446 560 REKQELQQELKEAQELAISSKQKcfEMQALLEEERKTAKKQVEESTRQIQAL 611
Cdd:PRK00591   52 REYKQAQEDLEEAKEMLEEESDP--EMREMAKEELKELEERLEELEEELKIL 101
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
49-106 3.58e-03

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: 40.82  E-value: 3.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952581446  49 KVLSRNHA-LIWFDhktGKFYLQDTkSSNGTFINS--QRLSRGSEESppceLLSGDIIQFG 106
Cdd:TIGR03354  43 RHVSGRHArIRYRD---GAYLLTDL-STNGVFLNGsgSPLGRGNPVR----LEQGDRLRLG 95
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
168-352 3.72e-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: 41.21  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  168 LSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSwQALIDEDRLlsRLEVMGNQLQAYSKNQTEdgIRKELVTLQED- 246
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNG--KKEELEEELEELEAALRD--LESRLGDLKKEr 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  247 -KHSYETTAKESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTH--------------------LKEMNDRTQEELRELA 304
Cdd:TIGR02169  892 dELEAQLRELERKIEELEAQIEKKRKrLSELKAKLEALEEELSEiedpkgedeeipeeelsledVQAELQRVEEEIRALE 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1952581446  305 NKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEK 352
Cdd:TIGR02169  972 PVNMLAIQEYEEVLKRLDELKEKRAKLEE----ERKAILERIEEYEKK 1015
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
28-106 4.19e-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: 37.47  E-value: 4.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581446  28 VKIGRSvarcrpAQNNATFDCKVLSRNHALIwfDHKTGKFYLQDTKSSNGTFINSQRLSRgseesppCELLSGDIIQFG 106
Cdd:cd22737    23 VRIGRA------SDNDIVIPEGSVSRHHATL--VPTPGGTQIRDLRSTNGTFVNGLRVDA-------ALLHDGDVVTIG 86
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
270-387 4.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  270 RKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNgAVNELKEFTEKLKQAEGKQEEIQQ---------KALSEKK 340
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAEREIAEleaelerldASSDDLA 688
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1952581446  341 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 387
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
597-791 4.74e-03

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: 40.13  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 597 AKKQVEESTRQIQALQAHLHKLQKDIEILREDKEI---EIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELH 673
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 674 KVQTELEQWRQTASEY-----------------ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDC 736
Cdd:COG4942    94 ELRAELEAQKEELAELlralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446 737 DSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQ 791
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
52-106 4.83e-03

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: 37.19  E-value: 4.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1952581446  52 SRNHALIWFDhKTGKFYLQDTKSSNGTFINsqrlsrGSEESPPCELLSGDIIQFG 106
Cdd:cd22673    41 SREHCRIEVD-ENGKAYLENLSTTNPTLVN------GKAIEKSAELKDGDVITIG 88
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
289-693 5.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 289 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsekkeLQHRIDEMEEKEQLLQARIEALQADND 368
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE--------LQEELEELEEELEELEAELEELREELE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 369 FTnERLTALQVRLEQLQEKNIKDhNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNR 448
Cdd:COG4717   120 KL-EKLLQLLPLYQELEALEAEL-AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 449 ISNVEDMF------ESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE----------------------------- 493
Cdd:COG4717   198 AEELEELQqrlaelEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiag 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 494 -------------TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYqMDEQELNESLNKVSLLKDELQCAHVQTGDSER 560
Cdd:COG4717   278 vlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREA 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 561 EK-------QELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilREDKEIEI 633
Cdd:COG4717   357 EEleeelqlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEEL 434
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952581446 634 IETRDQLASTHKEIVALRQtaveaatgresDIAILQGELHKVQT--ELEQWRQTASEYESEI 693
Cdd:COG4717   435 EELEEELEELEEELEELRE-----------ELAELEAELEQLEEdgELAELLQELEELKAEL 485
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
236-858 5.38e-03

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: 40.73  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  236 IRKELVTLQEDKHSYETTAKesLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNDRTQEELRELANKYNGAV 311
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKK--LIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  312 NELKEFTEKLKQAEGKQEEIQ---QKALSEKKELQHRIDEMEEKEQ--------LLQARIEALQADNDFTNERLTALQVR 380
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESSkqeIEKEEEKLAQVLKENKEEEKEKklqeeelkLLAKEEEELKSELLKLERRKVDDEEK 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  381 LEQLQEKNIKDHNSI------------------------GIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNK 436
Cdd:pfam02463  316 LKESEKEKKKAEKELkkekeeieelekelkeleikreaeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  437 LKAPVEPTQNNRISN--VEDMFESHLENNQTTEEDLKNDSERFKATL---IAEDDHTKVTEETKLLKENQLEAKESDMSD 511
Cdd:pfam02463  396 ELELKSEEEKEAQLLleLARQLEDLLKEEKKEELEILEEEEESIELKqgkLTEEKEELEKQELKLLKDELELKKSEDLLK 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  512 TLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDELQCAHVQT----GDSEREKQELQQELKEAQELAISSKQKCFEMQ 587
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggrIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  588 ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAI 667
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  668 LQGELHKVQTELEQWRQTASEYESEI--FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVL 745
Cdd:pfam02463  636 KLKESAKAKESGLRKGVSLEEGLAEKseVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  746 LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAE-----NETQKFQKQYEAD 820
Cdd:pfam02463  716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeerekTEKLKVEEEKEEK 795
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1952581446  821 QTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 858
Cdd:pfam02463  796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
256-365 6.19e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNDRTQEELRELANKYNGAVNELKE----------FTEKLKQA 324
Cdd:PRK00409  526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelrQLQKGGYA 602
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 325 EGKQEEIQQKalseKKELQHRIDEMEEKEQLLQARIEALQA 365
Cdd:PRK00409  603 SVKAHELIEA----RKRLNKANEKKEKKKKKQKEKQEELKV 639
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
255-389 6.40e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 39.71  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEgkqeEIQQK 334
Cdd:COG4026   113 KNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILE----EEFDN 188
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446 335 ALSEKKELQHRIDEMEEKEQLLQARIEALQAD---NDFTNERLTALQVrlEQLQEKNI 389
Cdd:COG4026   189 IKSEYSDLKSRFEELLKKRLLEVFSLEELWKElfpEELPEEDFIYFAT--ENLKPGKI 244
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
181-669 7.40e-03

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: 40.09  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 181 MLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIRKELVTLQEDKHSYETTAKESL 258
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKTICQLTEEKEAQMEELN 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 259 RRVLQEKIEVvrklSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ------ 332
Cdd:pfam05483 342 KAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaed 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 333 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRlEQLQEKNIKDHNSIgiQVDDLLPKINGSTDK 412
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTE--LEKEKLKNIELTAHC 494
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 413 EHFLLKSggdcSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKV-- 490
Cdd:pfam05483 495 DKLLLEN----KELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCkl 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 491 --TEETKLLKENQLEAKESDMSDTLSPSKD--RSSEDTTDYQMDEQELNESLNK-------------VSLLKDELQCAHV 553
Cdd:pfam05483 569 dkSEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQENKALKKkgsaenkqlnayeIKVNKLELELASA 648
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 554 QT------------------------GDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQ 609
Cdd:pfam05483 649 KQkfeeiidnyqkeiedkkiseekllEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 610 ALQAHlhklQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ 669
Cdd:pfam05483 729 LYKNK----EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
PRK11281 PRK11281
mechanosensitive channel MscK;
551-695 8.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  551 AHVQTGDSEREKQELQQELKEAQElaisskqkcfemQALLEEERKTAKKQVEESTRQIQALQahlhKLQKDIEILRedKE 630
Cdd:PRK11281    27 ARAASNGDLPTEADVQAQLDALNK------------QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLK--QQ 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581446  631 IEiiETRDQLASTHKEIVALRQTAVEAATGRESDIAI--LQGELHKVQTELEQWRQTASEYESEIFN 695
Cdd:PRK11281    89 LA--QAPAKLRQAQAELEALKDDNDEETRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVS 153
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
274-381 8.34e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 274 EVERSLSNTEDECTHLKEMNDRTQEELRELANKY---NGAVNELKEFTEKLKQAEGKQEEIQQKALSEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1952581446 341 ELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
PTZ00121 PTZ00121
MAEBL; Provisional
238-533 8.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  238 KELVTLQEDKHSYETTAKESLRRVLQE----KIEVVRKLSEVER---SLSNTEDECTHLKEMNDRTQEELRELANKYNGA 310
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  311 VNELKEfTEKLKQAE----GKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQvrlEQLQE 386
Cdd:PTZ00121  1712 AEEKKK-AEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDE 1787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  387 KNIKDHNSIGIQVDDLLpkingstDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRIsNVEDMFESHLEN-NQT 465
Cdd:PTZ00121  1788 EDEKRRMEVDKKIKDIF-------DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL-EEADAFEKHKFNkNNE 1859
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581446  466 TEEDLKNDSERFKATLIAEDDHTKVtEETKLLKENQLEAKESDMSDTLSPSKDrssEDTTDYQMDEQE 533
Cdd:PTZ00121  1860 NGEDGNKEADFNKEKDLKEDDEEEI-EEADEIEKIDKDDIEREIPNNNMAGKN---NDIIDDKLDKDE 1923
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
546-758 9.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 9.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  546 DELQCAHvQTGDSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEIL 625
Cdd:COG4913    235 DDLERAH-EALEDAREQIELLEPIRELAERYAAARER----LAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  626 REDKEieiiETRDQLASTHKEIVALRQtAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES-------------E 692
Cdd:COG4913    308 EAELE----RLEARLDALREELDELEA-QIRGNGGDR--LEQLEREIERLERELEERERRRARLEAllaalglplpasaE 380
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  693 IFNLQTKLQLQTQQQKDKQKGEAVQ----LQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 758
Cdd:COG4913    381 EFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
163-391 9.33e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  163 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWqALIDEDRLLSRLEVMGNQLQAYSKNQTE-DGIRKELV 241
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  242 TLQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNDRTQEELRELANKYNGAVNE---- 313
Cdd:COG4913    696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGdave 764
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446  314 ---LKEFTEKLKQAEGKQEEIQQKAL-----------SEKKELQHRIDEMEEKEQLLQaRIEA----------LQADNDF 369
Cdd:COG4913    765 relRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLPEYLALLD-RLEEdglpeyeerfKELLNEN 843
                          250       260
                   ....*....|....*....|..
gi 1952581446  370 TNERLTALQVRLEQlQEKNIKD 391
Cdd:COG4913    844 SIEFVADLLSKLRR-AIREIKE 864
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
532-858 9.66e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 532 QELNESLNKVSLLKDELQCAHVQTGDSEREKQELQQELKEAQElaiSSKQKCFEMQALLEEERKTAKKQVEESTRQIQAL 611
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 612 QAHLHKLQKDIEILREdkEIEIIETRDQLASTHKEIVALRQTAVEAATgresdIAILQGELHKVQTELEQWRQTASEYES 691
Cdd:COG4717   212 EEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLG 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 692 EIFNLQTKLQLQTQQQKDKQkgEAVQLQGKLDELQKQSngLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDA 771
Cdd:COG4717   285 LLALLFLLLAREKASLGKEA--EELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581446 772 SGLEVSRKALEVE-------VGTLKE-----QRLQETNGLRVKLAHAENETQKFQKQYEA--DQTMYLELKEKLDKTQKE 837
Cdd:COG4717   361 EELQLEELEQEIAallaeagVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEE 440
                         330       340
                  ....*....|....*....|.
gi 1952581446 838 NESITDELENCKENLKLLQQK 858
Cdd:COG4717   441 LEELEEELEELREELAELEAE 461
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH