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Conserved domains on  [gi|568989149|ref|XP_006519790|]
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sarcolemmal membrane-associated protein isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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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 1.84e-80

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: 254.11  E-value: 1.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679    1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568989149  83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679   79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 3.23e-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: 101.99  E-value: 3.23e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989149 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911    1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
156-795 8.49e-19

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: 92.04  E-value: 8.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   234 DSLRKELIALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKidemEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQ 385
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   386 EKTLKEC-SSLEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSP--SKEKSSDDT 462
Cdd:TIGR02168  552 VENLNAAkKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   463 TDAQMDEQDLNEPLAKVSL-----------LKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQkcfELQALlEEER 531
Cdd:TIGR02168  632 DNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK---ALAEL-RKEL 707
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   532 KAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLRQA---AAEAVSERDTDFVSL 605
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEEL 787
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   606 QEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL----------QGELEKLKKEWDVLETE 672
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEEL 867
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   673 CHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQk 752
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ- 942
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 568989149   753 eyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:TIGR02168  943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
 
Name Accession Description Interval E-value
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
3-130 1.84e-80

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: 254.11  E-value: 1.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679    1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568989149  83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679   79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 3.23e-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: 101.99  E-value: 3.23e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989149 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911    1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
156-795 8.49e-19

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: 92.04  E-value: 8.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   234 DSLRKELIALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKidemEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQ 385
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   386 EKTLKEC-SSLEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSP--SKEKSSDDT 462
Cdd:TIGR02168  552 VENLNAAkKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   463 TDAQMDEQDLNEPLAKVSL-----------LKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQkcfELQALlEEER 531
Cdd:TIGR02168  632 DNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK---ALAEL-RKEL 707
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   532 KAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLRQA---AAEAVSERDTDFVSL 605
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEEL 787
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   606 QEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL----------QGELEKLKKEWDVLETE 672
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEEL 867
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   673 CHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQk 752
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ- 942
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 568989149   753 eyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:TIGR02168  943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
28-105 6.36e-13

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 64.13  E-value: 6.36e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149   28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498   1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
PTZ00121 PTZ00121
MAEBL; Provisional
229-787 6.64e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  229 KNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAnkyn 308
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA---- 1324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  309 gavNEIKDLSDKLKvaeGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQA-KIEALQADNDFTNERLTALQVR-LEHLQE 386
Cdd:PTZ00121 1325 ---EEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAKKKAEEKKkADEAKK 1398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  387 KTLKECSSLEHLLSKSggdctfihqflECQKKlmvQGHLTKVVEESKLSKENQAKAKESDLSDTLspskEKSSDDTTDAQ 466
Cdd:PTZ00121 1399 KAEEDKKKADELKKAA-----------AAKKK---ADEAKKKAEEKKKADEAKKKAEEAKKADEA----KKKAEEAKKAE 1460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  467 MDEQDLNEPlAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQElARTSKQKCFELQAlLEEERKAYRNQVEESAKQIQ 546
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKK-AEEAKKADEAKKAEEAKKAD 1537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  547 VLQVQLQKLHMDMENLQEE--KDTEISSTRDKLLSAQDEILLLRQA--AAEAVSERDTDFVSLQEELKKVRAE----LEG 618
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEE 1617
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  619 WRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQ 698
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  699 KQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEK 775
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEK 1777
                         570
                  ....*....|..
gi 568989149  776 QSITDELKQCKD 787
Cdd:PTZ00121 1778 EAVIEEELDEED 1789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
161-765 1.05e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196  218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 241 IALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196  298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 321 LKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEHLLS 400
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 401 KsggdctfihqflecQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDlnEPLAKVS 480
Cdd:COG1196  447 A--------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLEGV 510
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 481 LLKDDLQGTQSETEAKQDIQHLRKELVEAqelartskqkcfeLQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDME 560
Cdd:COG1196  511 KAALLLAGLRGLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 561 NLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLqssfqlr 640
Cdd:COG1196  578 PLDKIRARAALAAALARGAIGAAVDLVASDLREA-DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV------- 649
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 641 cqqcedqqREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK 720
Cdd:COG1196  650 --------TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 568989149 721 QVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 765
Cdd:COG1196  722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
14-106 7.49e-11

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 59.20  E-value: 7.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716    8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
                         90
                 ....*....|....
gi 568989149  93 pPCEILSGDIIQFG 106
Cdd:COG1716   75 -PAPLRDGDVIRLG 87
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
28-85 5.00e-08

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 49.87  E-value: 5.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149    28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240   1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
256-769 8.47e-08

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: 55.95  E-value: 8.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE---ELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576   12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEHLQEKTLKECSSLEHLLSKsggdctFI 409
Cdd:pfam01576   92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISE------FT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   410 HQFLECQKKLMVQGHLtKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DD 485
Cdd:pfam01576  166 SNLAEEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEE 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   486 LQGTQS--ETEAKQDIQHLRK---------ELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQK 554
Cdd:pfam01576  245 LQAALArlEEETAQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   555 LHMDMENLQ----EEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYE 627
Cdd:pfam01576  325 REQEVTELKkaleEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   628 NEIRSLQSS---FQLRCQQCEDQQREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQS 701
Cdd:pfam01576  405 HKRKKLEGQlqeLQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQK 484
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149   702 FELTSDLsilqmtrKELEKQVGSLKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 769
Cdd:pfam01576  485 LNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
649-775 6.38e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   649 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 724
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568989149   725 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 775
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
 
Name Accession Description Interval E-value
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
3-130 1.84e-80

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: 254.11  E-value: 1.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679    1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568989149  83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679   79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
163-225 3.23e-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: 101.99  E-value: 3.23e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989149 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911    1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
156-795 8.49e-19

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: 92.04  E-value: 8.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   234 DSLRKELIALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKidemEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQ 385
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   386 EKTLKEC-SSLEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSP--SKEKSSDDT 462
Cdd:TIGR02168  552 VENLNAAkKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGVLVVDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   463 TDAQMDEQDLNEPLAKVSL-----------LKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQkcfELQALlEEER 531
Cdd:TIGR02168  632 DNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK---ALAEL-RKEL 707
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   532 KAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLRQA---AAEAVSERDTDFVSL 605
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEEL 787
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   606 QEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL----------QGELEKLKKEWDVLETE 672
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEEL 867
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   673 CHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQk 752
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ- 942
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 568989149   753 eyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:TIGR02168  943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
FHA_DMA-like cd22692
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ...
27-108 1.31e-17

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: 79.92  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692   38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115

                 ...
gi 568989149 106 GVD 108
Cdd:cd22692  116 GMD 118
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
6-126 3.96e-15

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: 72.72  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695    2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695   82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-795 2.32e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 77.40  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETT--- 253
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   334 KGQAEKKELQT---KIDEMEEKEQELQAKIEALQAdndftneRLTALQVRLEHLQEKTLKECSSL-EHLLSKSGGDCTFI 409
Cdd:TIGR02168  373 RLEELEEQLETlrsKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   410 HQFLEcqkklMVQGHLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKDDLQ 487
Cdd:TIGR02168  446 EEELE-----ELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSGLS 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   488 G-------------------------------TQSETEAKQDIQHLRK-----------------ELVEAQELARTSKQK 519
Cdd:TIGR02168  520 GilgvlselisvdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEG 599
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   520 CFELQALLEEERKAYRNQVE------------ESAKQIQVLQVQLQKL-----------------HMDMENLQEEKDTEI 570
Cdd:TIGR02168  600 FLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREI 679
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   571 SSTRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQRE 650
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   651 ---------------------------EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFE 703
Cdd:TIGR02168  756 lteleaeieeleerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   704 LTSDLSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELK 783
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          730
                   ....*....|..
gi 568989149   784 QCKDNLKLLREK 795
Cdd:TIGR02168  912 ELRRELEELREK 923
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
13-106 2.30e-13

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: 66.53  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060    6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
                         90
                 ....*....|....
gi 568989149  93 PPCEILSGDIIQFG 106
Cdd:cd00060   72 PPVPLQDGDVIRLG 85
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
28-105 6.36e-13

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 64.13  E-value: 6.36e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149   28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498   1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
167-204 1.36e-12

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: 62.50  E-value: 1.36e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568989149 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868    1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
PTZ00121 PTZ00121
MAEBL; Provisional
229-787 6.64e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  229 KNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAnkyn 308
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA---- 1324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  309 gavNEIKDLSDKLKvaeGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQA-KIEALQADNDFTNERLTALQVR-LEHLQE 386
Cdd:PTZ00121 1325 ---EEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAKKKAEEKKkADEAKK 1398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  387 KTLKECSSLEHLLSKSggdctfihqflECQKKlmvQGHLTKVVEESKLSKENQAKAKESDLSDTLspskEKSSDDTTDAQ 466
Cdd:PTZ00121 1399 KAEEDKKKADELKKAA-----------AAKKK---ADEAKKKAEEKKKADEAKKKAEEAKKADEA----KKKAEEAKKAE 1460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  467 MDEQDLNEPlAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQElARTSKQKCFELQAlLEEERKAYRNQVEESAKQIQ 546
Cdd:PTZ00121 1461 EAKKKAEEA-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKK-AEEAKKADEAKKAEEAKKAD 1537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  547 VLQVQLQKLHMDMENLQEE--KDTEISSTRDKLLSAQDEILLLRQA--AAEAVSERDTDFVSLQEELKKVRAE----LEG 618
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEeakkAEE 1617
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  619 WRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQ 698
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  699 KQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE---KTQTVLSELKLKFEMTEQEK 775
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAHLKKEEEKKAEEIRKEK 1777
                         570
                  ....*....|..
gi 568989149  776 QSITDELKQCKD 787
Cdd:PTZ00121 1778 EAVIEEELDEED 1789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
161-765 1.05e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196  218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 241 IALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196  298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 321 LKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEHLLS 400
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 401 KsggdctfihqflecQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDlnEPLAKVS 480
Cdd:COG1196  447 A--------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLEGV 510
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 481 LLKDDLQGTQSETEAKQDIQHLRKELVEAqelartskqkcfeLQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDME 560
Cdd:COG1196  511 KAALLLAGLRGLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 561 NLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLqssfqlr 640
Cdd:COG1196  578 PLDKIRARAALAAALARGAIGAAVDLVASDLREA-DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV------- 649
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 641 cqqcedqqREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK 720
Cdd:COG1196  650 --------TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 568989149 721 QVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 765
Cdd:COG1196  722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
52-106 2.42e-11

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: 61.53  E-value: 2.42e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568989149  52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686   48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
14-106 7.49e-11

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 59.20  E-value: 7.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716    8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
                         90
                 ....*....|....
gi 568989149  93 pPCEILSGDIIQFG 106
Cdd:COG1716   75 -PAPLRDGDVIRLG 87
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
250-794 3.78e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 324 AEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQ------VRLEHLQEKTLKECSSLEH 397
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKekaeeyIKLSEFYEEYLDELREIEK 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 398 LLSKSGGDCTFIHQFL-ECQKKLMVQGHLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPL 476
Cdd:PRK03918 315 RLSRLEEEINGIEERIkELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 477 AKVSLLKDDLQGTQSE-TEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKA-----YRNQVEESAKQIQVLQV 550
Cdd:PRK03918 394 EELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeYTAELKRIEKELKEIEE 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 551 QLQKLHMDMENLqeekdteisstrDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEI 630
Cdd:PRK03918 474 KERKLRKELREL------------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 631 RSLQSSFqlrcqqcedqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLS----SELQRQEKELHNSQKQSFELTS 706
Cdd:PRK03918 542 KSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKD 609
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 707 DLSILQMTRKELEKQVGSLKEQhLRDAADLKTLLSKAENQAKDVQKEY-EKTQTVLSELKLKFEM----TEQEKQSITDE 781
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRelagLRAELEELEKR 688
                        570
                 ....*....|...
gi 568989149 782 LKQCKDNLKLLRE 794
Cdd:PRK03918 689 REEIKKTLEKLKE 701
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
499-795 1.18e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.39  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   499 IQHLRKELVEAQELARTSKQKCFELQALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLL 578
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   579 SAQDEIL-LLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsfQLRCQQCE-DQQREEATRLQ 656
Cdd:TIGR02169  265 KRLEEIEqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   657 GELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR----- 731
Cdd:TIGR02169  343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseel 422
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149   732 -----DAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:TIGR02169  423 adlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
163-662 4.69e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 243 LQEDkhsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDEcthlKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196  349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEE----LLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 323 VAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEHLLSKS 402
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 403 GGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEkssDDTTDAQMDEQDLNEPLAKVSLL 482
Cdd:COG1196  501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE---DDEVAAAAIEYLKAAKAGRATFL 577
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 483 KDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEER--KAYRNQVEESAKQIQVLQVQLQKLHMDME 560
Cdd:COG1196  578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlvAARLEAALRRAVTLAGRLREVTLEGEGGS 657
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 561 NLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLR 640
Cdd:COG1196  658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 568989149 641 CQQCE--------------------DQQREEATRLQGELEKL 662
Cdd:COG1196  738 LEELLeeeelleeealeelpeppdlEELERELERLEREIEAL 779
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
298-795 5.24e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.05  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 378 QVRLEHlQEKTLKECSSLEHLLSKsggdctfihqflecqkklmvqghLTKVVEESKLSKENqAKAKESDLSDTLSPSKEK 457
Cdd:PRK02224 240 DEVLEE-HEERREELETLEAEIED-----------------------LRETIAETEREREE-LAEEVRDLRERLEELEEE 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 458 SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSE-TEAKQDIQHLRKELVEAQELARTskqkcfelqalLEEERKAYRN 536
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQAHNEEAESLREDADD-----------LEERAEELRE 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 537 QVEESakqiqvlqvqlqklhmdmenlqeekDTEISSTRDKLLSAQDEILLLR---QAAAEAVSERDTDFVSLQEELKKVR 613
Cdd:PRK02224 364 EAAEL-------------------------ESELEEAREAVEDRREEIEELEeeiEELRERFGDAPVDLGNAEDFLEELR 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 614 AELEGWRKAASEYENEIRSLQSSF----QLR----CQQCE------------DQQREEATRLQGELEKLKKEWDVLETEC 673
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERL 498
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 674 HSLKkenvllssELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKE 753
Cdd:PRK02224 499 ERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREAAAEAEEE 566
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 568989149 754 YEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKDNLKLLREK 795
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-790 6.54e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.70  E-value: 6.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   197 QEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETTAKESLRRV--LQEKIE-V 268
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEkL 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   269 VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKE---LQTK 345
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEE 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   346 IDEMEEKEQELQAKIEALQADNDFTNER--------------------------------LTALQV----RLEHL---QE 386
Cdd:TIGR02169  478 YDRVEKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgvhgtvaqlgsvgeryATAIEVaagnRLNNVvveDD 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   387 KTLKECssLEHLLSKSGGDCTFI--------HQFLECQKKLMVQGHLTKVVE-------------ESKLSKENQAKAK-- 443
Cdd:TIGR02169  558 AVAKEA--IELLKRRKAGRATFLplnkmrdeRRDLSILSEDGVIGFAVDLVEfdpkyepafkyvfGDTLVVEDIEAARrl 635
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   444 ---------ESDLSD--------------------TLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtQSETE 494
Cdd:TIGR02169  636 mgkyrmvtlEGELFEksgamtggsraprggilfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS--QELSD 713
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   495 AKQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEIS 571
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   572 STRDKLLSAQDEIlllrqaaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREE 651
Cdd:TIGR02169  794 PEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   652 AtRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR 731
Cdd:TIGR02169  864 E-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989149   732 DAADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkDNLK 790
Cdd:TIGR02169  943 DEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
233-784 9.43e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 233 EDSLRKELIALQEDKhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:COG1196  222 LKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQVRLEHLQEKTLKEC 392
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAE 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 393 SSLEHLLSksggdctfihQFLECQKKLMVQghltkvvEESKLSKENQAKAKESDLSDTLspsKEKSSDDTTDAQMDEQDL 472
Cdd:COG1196  372 AELAEAEE----------ELEELAEELLEA-------LRAAAELAAQLEELEEAEEALL---ERLERLEEELEELEEALA 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 473 NEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKcfELQALLEEERKAYRNQVEESAKQIQVLQVQL 552
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLLLLLEAEADYEGFLEG 509
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 553 QKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAE-----LEGWRKAASEYE 627
Cdd:COG1196  510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALA 589
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 628 NEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSD 707
Cdd:COG1196  590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568989149 708 LSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 784
Cdd:COG1196  670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
267-790 1.29e-08

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: 58.49  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKI 346
Cdd:TIGR04523  37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLEHLLSKSGGDCTFIHQFLECQKKLM 420
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  421 VQGHLTKVVEESKLSKENQAKAKESD-------LSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSET 493
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISElkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  494 E-AKQDIQHLRKELVEAQ-ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE---KDT 568
Cdd:TIGR04523 277 EqNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnSES 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  569 EISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCED-- 646
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIK----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlk 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  647 ----QQREEATRLQGE-------LEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTR 715
Cdd:TIGR04523 433 etiiKNNSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989149  716 KELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMteQEKQSITDELKQCKDNLK 790
Cdd:TIGR04523 513 KDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLK 581
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
164-204 1.42e-08

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: 51.19  E-value: 1.42e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568989149 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912    5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
563-795 1.51e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 563 QEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQL--- 639
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 640 ---RCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK 716
Cdd:COG1196  296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 717 ELEKQVGSLKEQHL---RDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 793
Cdd:COG1196  376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                 ..
gi 568989149 794 EK 795
Cdd:COG1196  456 EE 457
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
14-110 1.76e-08

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


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 53.00  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670    7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
                         90       100
                 ....*....|....*....|....*
gi 568989149  87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670   80 RN-----NTVLLSdGDVIEIAHSAT 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
162-387 3.13e-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: 57.39  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   162 SQELFQLSQY--LQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcsknqtEDSLRKE 239
Cdd:TIGR02169  664 GGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ------EEEKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   240 LIALQEDKHSYETTAKESLRrvlQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQ-EELRELANKYNGAVNEIKDLS 318
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVK---SELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149   319 DKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
228-720 4.70e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 228 SKNQTEDSLRKELIALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 302 ELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTK---IDEMEEKEQELQAKIEALQADNDfTNERLT 375
Cdd:PRK03918 290 EKAEEYiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHE-LYEEAK 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 376 ALQVRLEHLQEKtlKECSSLEHLLSKsggdctfiHQFLEcQKKLMVQGHLTKVveeskLSKENQAKAKESDLSDTLSPSK 455
Cdd:PRK03918 369 AKKEELERLKKR--LTGLTPEKLEKE--------LEELE-KAKEEIEEEISKI-----TARIGELKKEIKELKKAIEELK 432
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 456 E-KSSDDTTDAQMDEQD----LNEPLAKVSLLKDDLQGTQS-ETEAKQDIQHLRKELVEAQELaRTSKQKCFELQALLEE 529
Cdd:PRK03918 433 KaKGKCPVCGRELTEEHrkelLEEYTAELKRIEKELKEIEEkERKLRKELRELEKVLKKESEL-IKLKELAEQLKELEEK 511
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 530 ERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE--KDTEISSTRDKLLSAQDEillLRQAAAEAVSERDTDFVSLQE 607
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDE---LEEELAELLKELEELGFESVE 588
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 608 ELKKVRAELEGWRK---AASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQGELEKLKKEWDVL-----ETECHSLKKE 679
Cdd:PRK03918 589 ELEERLKELEPFYNeylELKDAEKELEREEKELK-KLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREE 667
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 568989149 680 NVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK 720
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
28-85 5.00e-08

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 49.87  E-value: 5.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149    28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240   1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
235-787 5.25e-08

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: 56.57  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  235 SLRKELIALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQT---KIDEMEEKEQELQAKIEAL--QADNDFTNErltalqvrlehlqek 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKE--------------- 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  388 tlkecsslehllsksggdctfIHQFLECQKKlmvqghlTKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQM 467
Cdd:TIGR04523 312 ---------------------LKSELKNQEK-------KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSE 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  468 DEQDLNEPLAKVSLLKDDLQGTQSETEA-KQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAK 543
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLEKEIERLKETIIKNNS 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  544 QIQvlqvqlqklhmDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAaaeaVSERDTDFVSLQEELKKVRAELEGWRKAA 623
Cdd:TIGR04523 441 EIK-----------DLTNQDSVKELIIKNLDNTRESLETQLKVLSRS----INKIKQNLEQKQKELKSKEKELKKLNEEK 505
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  624 SEYENEIRSL---QSSFQLRCQQCEdqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLssELQRQEKELHNSQKq 700
Cdd:TIGR04523 506 KELEEKVKDLtkkISSLKEKIEKLE----SEKKEKESKISDLEDELNKDDFELKKENLEKEID--EKNKEIEELKQTQK- 578
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  701 sfELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITD 780
Cdd:TIGR04523 579 --SLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652

                  ....*..
gi 568989149  781 ELKQCKD 787
Cdd:TIGR04523 653 TIKEIRN 659
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
29-119 6.07e-08

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: 52.03  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685   31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
                         90
                 ....*....|....*.
gi 568989149 106 G--VDVTENTRKVTHG 119
Cdd:cd22685  105 GhkNGRRVKQWPYQKS 120
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
256-769 8.47e-08

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: 55.95  E-value: 8.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE---ELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576   12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEHLQEKTLKECSSLEHLLSKsggdctFI 409
Cdd:pfam01576   92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISE------FT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   410 HQFLECQKKLMVQGHLtKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLK--DD 485
Cdd:pfam01576  166 SNLAEEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAelRAQLAKkeEE 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   486 LQGTQS--ETEAKQDIQHLRK---------ELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQK 554
Cdd:pfam01576  245 LQAALArlEEETAQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   555 LHMDMENLQ----EEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYE 627
Cdd:pfam01576  325 REQEVTELKkaleEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   628 NEIRSLQSS---FQLRCQQCEDQQREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQS 701
Cdd:pfam01576  405 HKRKKLEGQlqeLQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQK 484
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989149   702 FELTSDLsilqmtrKELEKQVGSLKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 769
Cdd:pfam01576  485 LNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
263-667 1.76e-07

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: 55.06  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   263 QEKIEVVRKLSEVERSLSNTEDEcthLKEMNERTQ--EELRELANKYNGAVNEIKDLSDKLKVAEGKQEEiqqkgqAEKK 340
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDI---LNELERQLKslERQAEKAERYKELKAELRELELALLVLRLEELR------EELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQeKTLKECSSLEHllsksggdctfihqflECQKKLM 420
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ-KELYALANEIS----------------RLEQQKQ 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   421 VQghltkvvEESKLSKENQAKAKESDLsdtlspskekssddttdaQMDEQDLNEPLAKVSLLKDDLQgtqsetEAKQDIQ 500
Cdd:TIGR02168  306 IL-------RERLANLERQLEELEAQL------------------EELESKLDELAEELAELEEKLE------ELKEELE 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   501 HLRKELVEAQELARTSKQKCFELQALLEEERKAY---RNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISS-TRDK 576
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAE 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   577 LLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSsfqlRCQQCEDQQREEATRLQ 656
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSE 506
                          410
                   ....*....|.
gi 568989149   657 GELEKLKKEWD 667
Cdd:TIGR02168  507 GVKALLKNQSG 517
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
239-776 1.81e-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: 55.12  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   239 ELIALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:pfam15921  279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   312 NEIKDLSDKLKVAEGKQEEiqqkgqaekkELQTKIDEMEEKEQELQAKIEalqaDNDFTNERLTALQVRLEHLQEKTLK- 390
Cdd:pfam15921  359 TEARTERDQFSQESGNLDD----------QLQKLLADLHKREKELSLEKE----QNKRLWDRDTGNSITIDHLRRELDDr 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   391 --ECSSLEHLLSKSGGDC--TFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSD--TLSPSKEKSSDDTTD 464
Cdd:pfam15921  425 nmEVQRLEALLKAMKSECqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKkmTLESSERTVSDLTAS 504
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   465 AQMDEQDLNEPLAKVSLLKD----DLQGTQSETEAKQDIQHLRKElVEAQELARTSKQKCFEL---------QALLEEER 531
Cdd:pfam15921  505 LQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGDHLRNVQTE-CEALKLQMAEKDKVIEIlrqqienmtQLVGQHGR 583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   532 KAYRNQVEesaKQIQVLQVQLQKLHM-DMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAE---AVSERDTDFVSLQE 607
Cdd:pfam15921  584 TAGAMQVE---KAQLEKEINDRRLELqEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlrAVKDIKQERDQLLN 660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   608 ELKKVRAEL-----------EGWRKAASEYENEIRSLQssFQLRCQQCEDQQ----------------------REEATR 654
Cdd:pfam15921  661 EVKTSRNELnslsedyevlkRNFRNKSEEMETTTNKLK--MQLKSAQSELEQtrntlksmegsdghamkvamgmQKQITA 738
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   655 LQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVgslkeqhlrdaA 734
Cdd:pfam15921  739 KRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV-----------A 807
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 568989149   735 DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 776
Cdd:pfam15921  808 NMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
FHA_FKH1-like cd22701
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ...
27-106 8.10e-07

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: 48.00  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701   18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92

                 ....*
gi 568989149 102 IIQFG 106
Cdd:cd22701   93 LIQIG 97
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
212-794 9.31e-07

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 52.74  E-value: 9.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606  323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606  398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   372 eRLTALQVRLEHLQEKTLKECSSLEHLLSKSGGDCtfihqfLECQKKLMVQGHLTKVVEESKLSKENQAKAKESD-LSDT 450
Cdd:TIGR00606  465 -QLEGSSDRILELDQELRKAERELSKAEKNSLTET------LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtRTQM 537
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   451 LSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQElartskqkcfELQAlLEEE 530
Cdd:TIGR00606  538 EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNK----------ELAS-LEQN 606
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   531 RKAYRNQveesakqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQdeilllrqaaaeAVSERDTDFVSLQEELK 610
Cdd:TIGR00606  607 KNHINNE-------------------------LESKEEQLSSYEDKLFDVC------------GSQDEESDLERLKEEIE 649
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   611 KVRAELEGWRKAASEYENEIRSLQSSFQLRCQQC------EDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLL- 683
Cdd:TIGR00606  650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMl 729
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   684 ------SSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL--KEQHLRDAADLKTLLSKAENQAKDVQKEYE 755
Cdd:TIGR00606  730 glapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIA 809
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 568989149   756 KTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 794
Cdd:TIGR00606  810 QQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
161-794 1.45e-06

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: 52.04  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921   83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   237 RKELIA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 305
Cdd:pfam15921  152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   306 kyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKEL-QTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL 384
Cdd:pfam15921  232 -------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   385 QEKTLKECSSLEHLLSKSGGDCTFIHQFLECQKKLMvqghltkvveESKLSK-ENQAKAKESDLSDTLSPSKEKSSDD-T 462
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY----------EDKIEElEKQLVLANSELTEARTERDQFSQESgN 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   463 TDAQMDE--QDLNEPLAKVSLLKDDLQGT-QSETEAKQDIQHLRKEL----VEAQELARTSKQKCFELQALLEEERKAYR 535
Cdd:pfam15921  375 LDDQLQKllADLHKREKELSLEKEQNKRLwDRDTGNSITIDHLRRELddrnMEVQRLEALLKAMKSECQGQMERQMAAIQ 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   536 NQVEESAKqiqvlqvqlqklhmdmenlqeekdteISSTRDKLLSAQDeilLLRQAAAEAVSERDTdFVSLQEELKKVRAE 615
Cdd:pfam15921  455 GKNESLEK--------------------------VSSLTAQLESTKE---MLRKVVEELTAKKMT-LESSERTVSDLTAS 504
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   616 LEGWRKAASEYENEIRSLQSSFQLRCQqcedqqreeatrlqgELEKLKKEWDVL---ETECHSLKKENVLLSSELQRQEK 692
Cdd:pfam15921  505 LQEKERAIEATNAEITKLRSRVDLKLQ---------------ELQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQ 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   693 ELHNSQKQSFELTSDLSILQMTRKELEKQVG----SLKE-QHLRDAADLKtlLSKAENQAKDVQKEYEKTQTVLSELKLK 767
Cdd:pfam15921  570 QIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLELEKVKLVNAGSERLRA 647
                          650       660
                   ....*....|....*....|....*..
gi 568989149   768 FEMTEQEKQSITDELKQCKDNLKLLRE 794
Cdd:pfam15921  648 VKDIKQERDQLLNEVKTSRNELNSLSE 674
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
25-114 1.89e-06

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: 47.35  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663   20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
                         90
                 ....*....|.
gi 568989149 104 QFGVDVTENTR 114
Cdd:cd22663   91 QLGVPPENKEP 101
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
26-106 1.89e-06

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: 46.64  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698   21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85

                 .
gi 568989149 106 G 106
Cdd:cd22698   86 G 86
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
27-117 2.13e-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: 46.97  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678   24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
                         90
                 ....*....|.
gi 568989149 107 vdvTENTRKVT 117
Cdd:cd22678   95 ---SETKILVR 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
522-795 2.79e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 522 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTd 601
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR- 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 602 fvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLKKEWDVLETEchslKKENV 681
Cdd:COG1196  300 ---LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEA----LLEAE 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 682 LLSSELQRQEKELhnsQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVL 761
Cdd:COG1196  372 AELAEAEEELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
                        250       260       270
                 ....*....|....*....|....*....|....
gi 568989149 762 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:COG1196  449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
55-108 3.57e-06

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: 46.16  E-value: 3.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568989149  55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704   39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
PTZ00121 PTZ00121
MAEBL; Provisional
228-799 4.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  228 SKNQTEDSLRKELIALQEDKHSYETT--AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHlKEMNERTQEELR--EL 303
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEEArkAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR-KAEEVRKAEELRkaED 1198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  304 ANKYNGA--VNEIKDLSDKLKVAEGKQ-EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR 380
Cdd:PTZ00121 1199 ARKAEAArkAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  381 LEHLQEKTLKECSSLEHLLSKSGGDCTFIHQFLECQKKlmVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSD 460
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  461 DTTD-----AQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQElARTSKQKCFELQALLEEERKA-- 533
Cdd:PTZ00121 1357 DEAEaaeekAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKAde 1435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  534 YRNQVEESAKQIQVLQVQLQKLHMD--MENLQEEKDTEISSTRDKLLSAQDEillLRQAAAEAvsERDTDFVSLQEELKK 611
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADE---AKKKAEEA--KKKADEAKKAAEAKK 1510
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  612 VRAELegwRKA--ASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQR 689
Cdd:PTZ00121 1511 KADEA---KKAeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  690 QEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK----EQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 765
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
                         570       580       590
                  ....*....|....*....|....*....|....
gi 568989149  766 LKfemtEQEKQSITDELKQCKDNLKLLREKGNNK 799
Cdd:PTZ00121 1668 KK----AEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
210-795 5.22e-06

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: 50.45  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169  186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   282 TEDECTH----LKEMNERT-----------QEELRELANKYNGAVNEIKDLSDKLKVAEGKQ------------------ 328
Cdd:TIGR02169  263 LEKRLEEieqlLEELNKKIkdlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLakleaeidkllaeieele 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   329 EEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLEHLLSKSGGD 405
Cdd:TIGR02169  343 REIEEE-RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREineLKRELDRLQEELQRLSEE 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   406 CTFIHQFLEC--QKKLMVQGHLTKVVEESKLSKEN----------------QAKAKESDLSDTLSPSKEKSSDDTTDAQM 467
Cdd:TIGR02169  422 LADLNAAIAGieAKINELEEEKEDKALEIKKQEWKleqlaadlskyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARA 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   468 DEQDLNEPLAKVSLLKDDLQG-------------------------------TQSETEAKQDIQHLRKE----------- 505
Cdd:TIGR02169  502 SEERVRGGRAVEEVLKASIQGvhgtvaqlgsvgeryataievaagnrlnnvvVEDDAVAKEAIELLKRRkagratflpln 581
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   506 -------------------------------------------LVEAQELAR---------TSKQKCFELQALL----EE 529
Cdd:TIGR02169  582 kmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAARrlmgkyrmvTLEGELFEKSGAMtggsRA 661
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   530 ERKAYRNQVEESAKqiqvlqvqLQKLHMDMENLQEEKDTeISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEEL 609
Cdd:TIGR02169  662 PRGGILFSRSEPAE--------LQRLRERLEGLKRELSS-LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   610 KKVRAELEGWRKAASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQGELEKLKKE-----WDVLETECHSLKKENVLLS 684
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIE 811
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   685 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL-KEQHLRDA--ADLKTLLSKAENQAKDVQKEYEKTQTVL 761
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIeKEIENLNGkkEELEEELEELEAALRDLESRLGDLKKER 891
                          730       740       750
                   ....*....|....*....|....*....|....
gi 568989149   762 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
258-396 1.01e-05

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: 47.61  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568989149 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLE 396
Cdd:COG1579   92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
310-542 1.31e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtl 389
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 390 kecssLEHLLS---KSGGDCTFIHQFLEcqkklmvQGHLTKVVeeSKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ 466
Cdd:COG3883   88 -----LGERARalyRSGGSVSYLDVLLG-------SESFSDFL--DRLSALSKIADADADLLEELKADKAELEAKKAELE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 467 MDEQDLNEPLAKVSLLKDDLQGTQSETEA-----KQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEES 541
Cdd:COG3883  154 AKLAELEALKAELEAAKAELEAQQAEQEAllaqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233

                 .
gi 568989149 542 A 542
Cdd:COG3883  234 A 234
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
234-671 1.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 234 DSLRKELIALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717   74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKE 391
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 392 CSSLEH-------------------LLSKSGGDCTFIHQFLECQKKLMVQGHLTkVVEESKLSKENQAKAKESDLSDTLs 452
Cdd:COG4717  233 ENELEAaaleerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEELQAL- 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 453 PSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgtqsetEAKQDIQHLRKELVEAQELARTSKQKCF--ELQALLE-- 528
Cdd:COG4717  311 PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLREAEELEEELQLEELeqEIAALLAea 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 529 --EERKAYRNQVEESAKqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvsERDTDFVSLQ 606
Cdd:COG4717  380 gvEDEEELRAALEQAEE-------------------YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELE 438
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989149 607 EELKKVRAELEGWRKAASEYENEIRSLQSSFQLrcqqceDQQREEATRLQGELEKLKKEWDVLET 671
Cdd:COG4717  439 EELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
605-789 2.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 605 LQEELKKVRAELegwrkaaseYENEIRSLQSSfqlrcqqcEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLS 684
Cdd:COG1196  218 LKEELKELEAEL---------LLLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 685 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTL---LSKAENQAKDVQKEYEKTQTVL 761
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAEL 360
                        170       180
                 ....*....|....*....|....*...
gi 568989149 762 SELKLKFEMTEQEKQSITDELKQCKDNL 789
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEEL 388
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
52-106 2.21e-05

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: 44.18  E-value: 2.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568989149  52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674   48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
51-106 2.53e-05

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: 44.08  E-value: 2.53e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989149  51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677   41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
289-781 2.59e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 369 F--TNERLTALQVRLEHLQEKtlkecssLEHLLSKsggdctfIHQFLECQKKLmvqghltkvveESKLSKENQAKAKESD 446
Cdd:COG4717  127 LlpLYQELEALEAELAELPER-------LEELEER-------LEELRELEEEL-----------EELEAELAELQEELEE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 447 LSDTLSPSKEKssddttDAQMDEQDLNEPLAKVSLLKDDLQGTQSETE-AKQDIQHLRKELVEAQELARTSKQKCFELQA 525
Cdd:COG4717  182 LLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEeLEEELEQLENELEAAALEERLKEARLLLLIA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 526 LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSL 605
Cdd:COG4717  256 AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 606 QEELKKVRAELEGWRKAASEYENEIRslqssfQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSS 685
Cdd:COG4717  336 PEELLELLDRIEELQELLREAEELEE------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 686 ELQRQEKELHNSQKQSF--ELTSDLSILQMTRKELEKQVgslkEQHLRDAADLKTLLSKAENQAKdvqkeyektqtvLSE 763
Cdd:COG4717  410 QLEELLGELEELLEALDeeELEEELEELEEELEELEEEL----EELREELAELEAELEQLEEDGE------------LAE 473
                        490
                 ....*....|....*...
gi 568989149 764 LKLKFEMTEQEKQSITDE 781
Cdd:COG4717  474 LLQELEELKAELRELAEE 491
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
28-106 2.90e-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: 43.48  E-value: 2.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680   23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
14-106 2.97e-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: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682   14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
                         90
                 ....*....|...
gi 568989149  94 pCEILSGDIIQFG 106
Cdd:cd22682   77 -CDLQNGDQIKIG 88
46 PHA02562
endonuclease subunit; Provisional
289-540 3.22e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA--- 365
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDell 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 366 ----DNDFTNERLTALQVRLEHLQEKtLKECSSLEHLLSKsGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKENQAK 441
Cdd:PHA02562 245 nlvmDIEDPSAALNKLNTAAAKIKSK-IEQFQKVIKMYEK-GGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 442 AKEsdlsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGTQSET-EAKQDIQHLRKELV-EAQELArtskqk 519
Cdd:PHA02562 323 DEL-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEFVdNAEELA------ 382
                        250       260
                 ....*....|....*....|.
gi 568989149 520 cfELQALLEEERKAYRNQVEE 540
Cdd:PHA02562 383 --KLQDELDKIVKTKSELVKE 401
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
12-103 3.22e-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: 43.43  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690    8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
                         90
                 ....*....|....*.
gi 568989149  88 GSEesppCEILSGDII 103
Cdd:cd22690   77 GSQ----SLLQDGDEI 88
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
251-795 3.34e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.66  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   327 KQEEIQQKGQ---AEKKELQTKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSL 395
Cdd:pfam02463  251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   396 EHLLSKsggdctfIHQFLECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEP 475
Cdd:pfam02463  331 KKEKEE-------IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   476 LAKVSLLKDDLQGTQSETEAKQDIQhlrKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKL 555
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   556 HMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQS 635
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   636 SFQLRCQQCEDQQREEATRLQGELEKLKKEWDvletecHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTR 715
Cdd:pfam02463  561 EERQKLVRALTELPLGARKLRLLIPKLKLPLK------SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL 634
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   716 KELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:pfam02463  635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
339-777 4.24e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.04  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  339 KKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtlkecsslEHLLSKSggdctfihqflecQKK 418
Cdd:pfam05557  15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR--------EAEAEEA-------------LRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  419 LMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtqsETEAK-Q 497
Cdd:pfam05557  74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD----LLKAKaS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  498 DIQHLRKELVEAQELARTSKQKCFELQalleeerkaYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISstrdKL 577
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  578 LSAQDEILLLR------QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRS--LQSSFQLRCQQCEDQQR 649
Cdd:pfam05557 217 NENIENKLLLKeevedlKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLK 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  650 EEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDL----SILQMTRKEL-EKQVGS 724
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELtMSNYSP 376
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568989149  725 LKEQHLRDAADlktLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 777
Cdd:pfam05557 377 QLLERIEEAED---MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
153-388 4.43e-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: 46.68  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942   10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 233 EDSLRKELIALQEDKHSYETTAKESLRRV----LQEKIEVV---RKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:COG4942   85 LAELEKEIAELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 306 KyngaVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQ 385
Cdd:COG4942  165 L----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240

                 ...
gi 568989149 386 EKT 388
Cdd:COG4942  241 ERT 243
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
13-110 6.98e-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: 42.22  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665    7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
                         90       100
                 ....*....|....*....|.
gi 568989149  92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665   74 KPNVryELIDGDLLLFG-DVK 93
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
52-107 7.40e-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: 42.70  E-value: 7.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989149  52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667   40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
568-800 1.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  568 TEISSTRDKLLSAQDEILLLRQAAAEAvserdTDFVSLQEELKKVRAELEGWR-----KAASEYENEIRSLQSsfQLrcq 642
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELA-----ERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRA--EL--- 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  643 qceDQQREEATRLQGELEKLKKEWDVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsfeltsdlsiLQMTRKELEKQ 721
Cdd:COG4913   305 ---ARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEAL 367
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  722 VGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQckdnlklLREKGNNKP 800
Cdd:COG4913   368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-------LERRKSNIP 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
177-798 1.24e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  177 HREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKE 256
Cdd:TIGR04523  33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  257 SLRRVLQEKIEVvrKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQ 336
Cdd:TIGR04523 113 KNDKEQKNKLEV--ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  337 AEKKELQ------TKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLEHLLSKSGgdctfih 410
Cdd:TIGR04523 191 KIKNKLLklelllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN------- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  411 qflECQKKLmvqghltkvveESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMD-EQDLNEPLAKVSLLKDDL--- 486
Cdd:TIGR04523 264 ---KIKKQL-----------SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIqnq 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  487 --QGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHmDMENLQE 564
Cdd:TIGR04523 330 isQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQ 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  565 EKDTEISSTRDKLLSAQDEILLLRQAAAEAVSE------RDTDFVSLQEELKKVRAELEgwrKAASEYENEIRSLQSSFQ 638
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikdltnQDSVKELIIKNLDNTRESLE---TQLKVLSRSINKIKQNLE 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  639 LRCQQCEDQQRE------EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELhnsQKQSFELTSDLsiLQ 712
Cdd:TIGR04523 486 QKQKELKSKEKElkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL---NKDDFELKKEN--LE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  713 MTRKELEKQVGSLKEQH---LRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE--------------K 775
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEneklssiiknikskK 640
                         650       660
                  ....*....|....*....|...
gi 568989149  776 QSITDELKQCKDNLKLLREKGNN 798
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRNKWPE 663
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
18-86 1.43e-04

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: 41.54  E-value: 1.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694    8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
229-756 1.91e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.42  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   229 KNQTEDSLRKeliaLQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA---- 304
Cdd:TIGR00606  586 INQTRDRLAK----LNKELASLEQN-KNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAmlag 660
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   305 --NKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDftnERLTALQVRLE 382
Cdd:TIGR00606  661 atAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD---EMLGLAPGRQS 737
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   383 HLQEKTlKECSSLEHLLSKSGGDCTFIHQFLECQKKLMvqghltkvveesklskenqakakesdlsDTLSPSKEKSSDDT 462
Cdd:TIGR00606  738 IIDLKE-KEIPELRNKLQKVNRDIQRLKNDIEEQETLL----------------------------GTIMPEEESAKVCL 788
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   463 TDAQMDEQdLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESA 542
Cdd:TIGR00606  789 TDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN 867
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   543 KQIQVLQVQLQKLHM--DMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWR 620
Cdd:TIGR00606  868 ELKSEKLQIGTNLQRrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   621 KAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKenvllSSELQRQEKELHNSQKQ 700
Cdd:TIGR00606  948 EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLT 1022
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568989149   701 SFELTSDLSILQMTRKELEKQVG-----SLKEQHLRDAADLKtLLSKAENQAKDVQKEYEK 756
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGqmqvlQMKQEHQKLEENID-LIKRNHVLALGRQKGYEK 1082
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
49-105 1.93e-04

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: 41.51  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568989149  49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672   39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-350 2.21e-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: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYE---T 252
Cdd:COG4913   241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913   320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
                         170       180       190
                  ....*....|....*....|....*....|...
gi 568989149  318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:COG4913   400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
484-694 2.25e-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: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  484 DDLQGTQSETE-AKQDIQHLRkELVEAQELARTSKQKCFELQALLEEeRKAYRNQVEesakqiqvlqvqLQKLHMDMENL 562
Cdd:COG4913   235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  563 QEEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSS--- 636
Cdd:COG4913   301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568989149  637 --------------FQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKEL 694
Cdd:COG4913   378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
555-813 2.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 555 LHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQ 634
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 635 SSFQLRcqqcedQQREEATRLQGELEKLKKEWDvletechslkkenvllssELQRQEKELHNSQKQSFELTSDLSILQMT 714
Cdd:COG4717  123 KLLQLL------PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 715 RKELEKQVGSLKEQHLRDAAdlktllskaenqakdvqKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 794
Cdd:COG4717  179 LEELLEQLSLATEEELQDLA-----------------EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
                        250
                 ....*....|....*....
gi 568989149 795 KGNNKPWPWMPMLAALVAV 813
Cdd:COG4717  242 EERLKEARLLLLIAAALLA 260
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
558-799 3.87e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 558 DMENLQEEKDTEISSTRDKLLSAQDEILLLRqAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsf 637
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 638 QLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK- 716
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 717 --ELEKQVGSLKEQHlRDAADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 794
Cdd:PRK03918 347 lkELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419

                 ....*
gi 568989149 795 KGNNK 799
Cdd:PRK03918 420 EIKEL 424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
572-763 4.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  572 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcedQQREE 651
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  652 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEkQVGSLKEQHLR 731
Cdd:COG4913   680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----------LDELQDRLE-AAEDLARLELR 748
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568989149  732 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSE 763
Cdd:COG4913   749 ALLEERFAAALGDAVERELRENLEERIDALRA 780
46 PHA02562
endonuclease subunit; Provisional
560-795 4.81e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.46  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 560 ENLQEEK--DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF 637
Cdd:PHA02562 178 ELNQQIQtlDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 638 QlrcqqcedQQREEATRLQGELEKLKKEWDVLE--TECHSLKkenvllsSELQRQEKELHNSQKQSFELTSDLSILQMTR 715
Cdd:PHA02562 258 N--------KLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCT-------QQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 716 KELEKQVGSLKEQHLR------DAADLKTLLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKDNL 789
Cdd:PHA02562 323 DELEEIMDEFNEQSKKllelknKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDEL 388

                 ....*.
gi 568989149 790 KLLREK 795
Cdd:PHA02562 389 DKIVKT 394
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
53-106 4.96e-04

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: 39.93  E-value: 4.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568989149  53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700   36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
25-108 5.14e-04

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: 40.49  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702   31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103

                 ....*....
gi 568989149 100 GDIIQFGVD 108
Cdd:cd22702  104 SDVIEFGSD 112
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
162-773 5.54e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  238 KELIALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  316 DLsdKLKVAEGKQEeiQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNER-------LTALQVRLEHLQEKT 388
Cdd:pfam10174 286 FM--KNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRaailqteVDALRLRLEEKESFL 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  389 LKECSSLEHLLSKSGGDCTFIHQFlecqkklmvqghltKVVEESKLSKENQAKAKESDLSDTLspsKEKssddttDAQMD 468
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDL--------------KDMLDVKERKINVLQKKIENLQEQL---RDK------DKQLA 418
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  469 EqdlneplakvslLKDDLQGTQSETEAKQdiqhlrkELVEAQELARTSKQKCFE-LQALLEEERKAYRNQVEESAKQIQV 547
Cdd:pfam10174 419 G------------LKERVKSLQTDSSNTD-------TALTTLEEALSEKERIIErLKEQREREDRERLEELESLKKENKD 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  548 LQVQLQKLHMDMenlqEEKDTEISSTRDKLLSAQDEILLLRQAAAE---AVSERDTDFVSLQEELKKVRaELEGWRKAAS 624
Cdd:pfam10174 480 LKEKVSALQPEL----TEKESSLIDLKEHASSLASSGLKKDSKLKSleiAVEQKKEECSKLENQLKKAH-NAEEAVRTNP 554
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  625 EYENEIRSLQSSFQLRcqqcedqqREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfel 704
Cdd:pfam10174 555 EINDRIRLLEQEVARY--------KEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN---- 622
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  705 tsdlsiLQMTRKELEKQVGSLKEQHLRDAADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 773
Cdd:pfam10174 623 ------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
16-111 6.43e-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: 39.59  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693    7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
                         90
                 ....*....|....*..
gi 568989149  95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693   73 VVVQPGDTIRIGATVFE 89
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
52-106 7.70e-04

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


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 39.40  E-value: 7.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568989149  52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683   28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
163-401 9.70e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  242 ALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913   696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  318 SDKLKVAEGKQEEIQQKGQAEKKELqtkIDEMEEKEQELQAKIEALQADNDFTNE---RLTALQ-VRLEHLQEK---TLK 390
Cdd:COG4913   765 RELRENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEylaLLDRLEeDGLPEYEERfkeLLN 841
                         250
                  ....*....|...
gi 568989149  391 ECS--SLEHLLSK 401
Cdd:COG4913   842 ENSieFVADLLSK 854
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
489-728 1.07e-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: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 489 TQSETEAKQDIQHLRKELVEAQELARTSKQKcfelQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEekdt 568
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 569 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQssfqlrcqqcedQQ 648
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 649 REEATRLQGELEKLKKEWDVLETEchsLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ 728
Cdd:COG4942  159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
510-712 1.14e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  510 QELARTSKQKcfelqaLLEEERKayRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQ 589
Cdd:pfam17380 396 QELEAARKVK------ILEEERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  590 AAAE-----AVSERDTDFVSLQEELKK--VRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR----EEATRLQGE 658
Cdd:pfam17380 468 QEEErkrkkLELEKEKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQE 547
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568989149  659 LEKLKK--EWDVLETECHSlKKENVLLSSELQRQEKELHNSQKQsFELTSDLSILQ 712
Cdd:pfam17380 548 MEERRRiqEQMRKATEERS-RLEAMEREREMMRQIVESEKARAE-YEATTPITTIK 601
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
511-767 1.28e-03

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: 42.19  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  511 ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQA 590
Cdd:pfam07888  30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  591 AAEAVSERDTdfVSLQEELKKVR-AELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEatrlQGELEKLKKEWDVL 669
Cdd:pfam07888 110 SEELSEEKDA--LLAQRAAHEARiRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQT 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  670 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELE---KQVGSLKEQ---HLRDAADLKTLLSKA 743
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERlnaSERKVEGLGEELSSM 263
                         250       260
                  ....*....|....*....|....
gi 568989149  744 ENQAKDVQKEYEKTQTVLSELKLK 767
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQ 287
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
27-106 1.42e-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: 38.60  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668   19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
584-803 1.48e-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: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 584 ILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLK 663
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 664 KEWDVLETECHSLKKE-----------------NVLLSSE--------LQRQEKELHNSQKQSFELTSDLSILQMTRKEL 718
Cdd:COG4942   90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 719 EKQVGSLKE---QHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 795
Cdd:COG4942  170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249

                 ....*...
gi 568989149 796 GNNKPWPW 803
Cdd:COG4942  250 ALKGKLPW 257
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
49-112 1.58e-03

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: 39.34  E-value: 1.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681   64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
651-774 1.78e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 41.23  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  651 EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNsQKQSFELTSDLSilqmtrkELEKQVGSLKeqhl 730
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568989149  731 rdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 774
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
mukB PRK04863
chromosome partition protein MukB;
449-672 2.17e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  449 DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEAQELARTSKQKCFELQALLe 528
Cdd:PRK04863  890 ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE---QFEQLKQDYQQAQQTQRDAKQQAFALTEVV- 965
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  529 eERKAYRNqVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeissTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQE- 607
Cdd:PRK04863  966 -QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEl 1039
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568989149  608 --ELKK--VRAElEGWRKAASEYENEIRSLQSSFQLRCQQCEDQ---QREEATRLQGELEKLKKEWDVLETE 672
Cdd:PRK04863 1040 kqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLTKKLRKLERDYHEMREQ 1110
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
431-798 2.24e-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: 41.63  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  431 ESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDlqgTQSETEAKQDiqHLRKELveaq 510
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDE---NLKELIEKKD--HLTKEL---- 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  511 ELARTSKQKCFELQALLEEE-----------RKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstRDKLLS 579
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDlqiatkticqlTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEK 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  580 AQDEILLLRQAAAEAVSERD--TDFVSLQE----ELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedqqreeat 653
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------- 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  654 RLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL-------- 725
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhq 519
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568989149  726 ------KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 798
Cdd:pfam05483 520 ediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
1-106 2.32e-03

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: 41.29  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456    1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568989149  76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456   69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
257-543 2.36e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771  13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTnERLTALQVRLEHLQEKtlkecsslehllsksggdcTF 408
Cdd:PRK05771  85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGF-------------------KY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 409 IHQFLecqkklmvqGHLTK-VVEESKL--SKENQAKAKESDLSDTLS--PSKEkssddttdaqmDEQDLNEPLAKVSLLK 483
Cdd:PRK05771 145 VSVFV---------GTVPEdKLEELKLesDVENVEYISTDKGYVYVVvvVLKE-----------LSDEVEEELKKLGFER 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568989149 484 DDLQ--GTQSET--EAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAK 543
Cdd:PRK05771 205 LELEeeGTPSELirEIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
522-753 2.51e-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: 40.90  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 522 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEkdteISSTRDKLLSAQDEILLLRQAAAEavserdtd 601
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAE-------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 602 fvsLQEELKKVRAELEGWRKaasEYENEIRSLQSS-------FQLRCQQCEDQQREeATRLQGELEKLKKEWDVLETECH 674
Cdd:COG4942   88 ---LEKEIAELRAELEAQKE---ELAELLRALYRLgrqpplaLLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 675 SLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ---HLRDAADLKTLLSKAENQAKDVQ 751
Cdd:COG4942  161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAA 240

                 ..
gi 568989149 752 KE 753
Cdd:COG4942  241 ER 242
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
327-778 2.54e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   327 KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA------------DNDFTNERLTALQVRLEH----------- 383
Cdd:TIGR00618  236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAqeavleetqeriNRARKAAPLAAHIKAVTQieqqaqrihte 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   384 LQEKTLKECSSLEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKE-------------NQAKAKESDLSDT 450
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREiscqqhtltqhihTLQQQKTTLTQKL 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   451 LSPSKEKSSDDTTDAQMDEQDLNEplakvsllkDDLQGTQSETEAKQDIQHLRKELVE--AQELARTSKQKcfelQALLE 528
Cdd:TIGR00618  396 QSLCKELDILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYAELCAaaITCTAQCEKLE----KIHLQ 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   529 EERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVS-LQE 607
Cdd:TIGR00618  463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAqLET 542
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   608 ELKKVRAELEGWRKAASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSEL 687
Cdd:TIGR00618  543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   688 QRQEKELHNSQ-KQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKL 766
Cdd:TIGR00618  622 QPEQDLQDVRLhLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
                          490
                   ....*....|..
gi 568989149   767 KFEMTEQEKQSI 778
Cdd:TIGR00618  702 CQTLLRELETHI 713
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
300-387 2.75e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                 ....*...
gi 568989149 380 RLEHLQEK 387
Cdd:COG3883  204 ELAAAEAA 211
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
274-776 2.80e-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: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLkvaegkQEEIQQKGQAEKK--ELQTKIDEMEE 351
Cdd:pfam01576  205 ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL------EEETAQKNNALKKirELEAQISELQE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   352 K-EQELQAKIEALQADNDFtNERLTALQVRLEhlqeKTLKECSSLEHLLSKSGGDCTFIHQFLECQKKL-------MVQG 423
Cdd:pfam01576  279 DlESERAARNKAEKQRRDL-GEELEALKTELE----DTLDTTAAQQELRSKREQEVTELKKALEEETRSheaqlqeMRQK 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   424 H------LTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDT-----------------------TDAQMDEQDLNE 474
Cdd:pfam01576  354 HtqaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqdsehkrkklegqlqelqarlSESERQRAELAE 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   475 PLAKVSLLKDDLQGTQSETEAK-----QDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQ 546
Cdd:pfam01576  434 KLSKLQSELESVSSLLNEAEGKniklsKDVSSLESQLQDTQELLQEETRQKLNLSTrlrQLEDERNSLQEQLEEEEEAKR 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   547 VLQVQLQKLHM---DMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERD---TDFVSLQEELKKVRAELEGWR 620
Cdd:pfam01576  514 NVERQLSTLQAqlsDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDkleKTKNRLQQELDDLLVDLDHQR 593
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   621 KAASEYEN----------EIRSLQSSFQLRCQQCEDQQREEATR---LQGELEKLKKEWDVLETECHSLKKENVLLSSEL 687
Cdd:pfam01576  594 QLVSNLEKkqkkfdqmlaEEKAISARYAEERDRAEAEAREKETRalsLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   688 QRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAEN--QAKDVQKEYEKTQTVLSELK 765
Cdd:pfam01576  674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERdlQARDEQGEEKRRQLVKQVRE 753
                          570
                   ....*....|.
gi 568989149   766 LKFEMTEQEKQ 776
Cdd:pfam01576  754 LEAELEDERKQ 764
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
274-381 3.10e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.99  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568989149  341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-401 3.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 236 LRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 316 DLSDKLKVAEGKQEEIQQKGQA-EKKELQTKIDEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEKTlKE 391
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKEELEEREKAK-KE 712
                        170
                 ....*....|
gi 568989149 392 CSSLEHLLSK 401
Cdd:PRK03918 713 LEKLEKALER 722
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
256-359 4.13e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
                         90       100
                 ....*....|....*....|....*
gi 568989149 335 GQAEkKELQTKIDEMEEKEQELQAK 359
Cdd:PRK00409 603 SVKA-HELIEARKRLNKANEKKEKK 626
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
576-753 4.26e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 576 KLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIrslqssfqlrcqqceDQQREEATRL 655
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---------------EEVEARIKKY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 656 QGELEKLK--KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQmtrKELEKQVGSLKEQHLRDA 733
Cdd:COG1579   79 EEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELE 155
                        170       180
                 ....*....|....*....|
gi 568989149 734 ADLKTLLSKAENQAKDVQKE 753
Cdd:COG1579  156 AELEELEAEREELAAKIPPE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
236-386 4.33e-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: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  236 LRKELIALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlkemnerTQEELRELANKYNgavnE 313
Cdd:COG4913   615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568989149  314 IKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQE 386
Cdd:COG4913   680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAE-------EELDELQDRLEAAED 741
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
208-366 4.75e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQTKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396

                 ....*....
gi 568989149 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
236-366 5.53e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 236 LRKELIALQEDKHSYETTAKESLRRV--LQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNE 313
Cdd:COG1579   50 AKTELEDLEKEIKRLELEIEEVEARIkkYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MER 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568989149 314 IKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579  119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
207-500 5.94e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.41  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  207 LIDEDRLLSRLE--------VMGNQLQAcsKNQTEDSLRKELIALQEDKHSYETTAKESLRRVlQEKIEVVRKLSEVERS 278
Cdd:PTZ00108 1001 LGKLERELARLSnkvrfikhVINGELVI--TNAKKKDLVKELKKLGYVRFKDIIKKKSEKITA-EEEEGAEEDDEADDED 1077
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  279 LSNTEDECT---HLKEMN--ERTQEELRELANKYNGAVNEIKDLSDKlkvaegkqeEIQQKGQAEKKELQTKIDEMEEKE 353
Cdd:PTZ00108 1078 DEEELGAAVsydYLLSMPiwSLTKEKVEKLNAELEKKEKELEKLKNT---------TPKDMWLEDLDKFEEALEEQEEVE 1148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  354 QELQAKIEALQADNDFTNERltaLQVRLEHLQEKTLKECSSLEHLLSKSGGDCTFIHQFlecQKKLMVQGHLTKVVEESK 433
Cdd:PTZ00108 1149 EKEIAKEQRLKSKTKGKASK---LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSD---EKRKLDDKPDNKKSNSSG 1222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568989149  434 LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQ 500
Cdd:PTZ00108 1223 SDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPS 1289
PRK01156 PRK01156
chromosome segregation protein; Provisional
256-620 6.27e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI--------------KDLSDKL 321
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIeslkkkieeyskniERMSAFI 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR--------------LEHLQEK 387
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgeekSNHIINH 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 388 TLKECSSLEHLLSKSGGDCTFIHQFLECQKKLmvQGHLTKVVEESKLSKENQAKAKESDLSD---TLSPSKEK------- 457
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR--KEYLESEEINKSINEYNKIESARADLEDikiKINELKDKhdkyeei 551
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 458 ----SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSEtEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKA 533
Cdd:PRK01156 552 knryKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANN 630
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 534 YRNQVEEsakqIQVLQVQLQKLHMDMENLQEEkdteiSSTRDKLLSAQDEIlllrqaaAEAVSERDTDFVSLQEELKKVR 613
Cdd:PRK01156 631 LNNKYNE----IQENKILIEKLRGKIDNYKKQ-----IAEIDSIIPDLKEI-------TSRINDIEDNLKKSRKALDDAK 694

                 ....*..
gi 568989149 614 AELEGWR 620
Cdd:PRK01156 695 ANRARLE 701
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
649-775 6.38e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149   649 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 724
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568989149   725 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 775
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
337-742 8.25e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 39.66  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  337 AEKKELQTKIDEMEEKEQELQAKIEALQAD-NDFTNERLTALQVRLEHLQEKTLKECSSLehlLSKSGGDCTFIHQFLEC 415
Cdd:pfam13166  89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANlQKLDKEKEKLEADFLDECWKKIKRKKNSA---LSEALNGFKYEANFKSR 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  416 QKKLMVQghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDttDAQMDEqdlnepLAKVSLLKDDLQGTQSETEA 495
Cdd:pfam13166 166 LLREIEK----DNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFN--VIDFDA------LEKAEILIQKVIGKSSAIEE 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  496 KQDIQHLRKELVEAQELARTSKQKC-F---ELQALLEEERKAYRNQ-VEEsakqiqvlqvqlqklhmDMENLQEEKDTEI 570
Cdd:pfam13166 234 LIKNPDLADWVEQGLELHKAHLDTCpFcgqPLPAERKAALEAHFDDeFTE-----------------FQNRLQKLIEKVE 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  571 SSTRDKL--LSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRK---AASEYE------NEIRSLQSS--- 636
Cdd:pfam13166 297 SAISSLLaqLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKdpfKSIELDsvdakiESINDLVASine 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  637 -----------FQLRCQQCEDQ-QREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELhnsqkqsfel 704
Cdd:pfam13166 377 liakhneitdnFEEEKNKAKKKlRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEI---------- 446
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 568989149  705 tsdlsilqmtrKELEKQVGslkeQHLRDAADLKTLLSK 742
Cdd:pfam13166 447 -----------KELEAQLR----DHKPGADEINKLLKA 469
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
172-387 8.35e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 8.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 172 LQEALHREQMLEQKLATLQRLLAITQEAsdtswqalIDEDRL-LSRLEVMGNQLQACSKNQTEDSLRKELIAlqeDKHSY 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRET--------IEEKRErAEELRERAAELEAEAEEKREAAAEAEEEA---EEARE 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnERTQEELRELANKYNGAVNEIKDLSDKLKVAEGK-QE 329
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDEI-------ERLREKREALAELNDERRERLAEKRERKRELEAEfDE 645
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568989149 330 EIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTN---ERLTALQVRLEHLQEK 387
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENR 706
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
172-361 9.21e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 38.35  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHSYE 251
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149  252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619  69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568989149  322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
592-754 9.24e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 9.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 592 AEAVSERDTDfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedQQREEATRLQGELEKLKKEWDVLET 671
Cdd:COG2433  379 EEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE--------RLEAEVEELEAELEEKDERIERLER 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989149 672 ECHSLKKE---NVLLSSELQRQEKELHNsqkqsfeLTSDLSILQMTRKELEKQVGSLKE----QHLRDAADLKTLLSKAE 744
Cdd:COG2433  449 ELSEARSEerrEIRKDREISRLDREIER-------LERELEEERERIEELKRKLERLKElwklEHSGELVPVKVVEKFTK 521
                        170
                 ....*....|
gi 568989149 745 NQAKDVQKEY 754
Cdd:COG2433  522 EAIRRLEEEY 531
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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