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Conserved domains on  [gi|1907135714|ref|XP_036014705|]
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kinesin-like protein KIF16B isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 51-399 1.89e-176

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 537.71  E-value: 1.89e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01365     16 EKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  131 CVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDLL-RRKSSKTFNLRVR 209
Cdd:cd01365     95 CLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDLLnPKPKKNKGNLKVR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE--MPCETVSKIHLVDL 287
Cdd:cd01365    174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEtnLTTEKVSKISLVDL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  288 AGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIA 367
Cdd:cd01365    254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1907135714  368 TISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:cd01365    330 AISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 480-596 8.98e-77

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.


The actual alignment was detected with superfamily member cd22732:

Pssm-ID: 469597 [Multi-domain]  Cd Length: 117  Bit Score: 249.47  E-value: 8.98e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22732      1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907135714  560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22732     81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-1126 1.08e-17

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196    290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG1196    446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  884 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196    521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  944 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 1022
Cdd:COG1196    601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1023 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1102
Cdd:COG1196    681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL-----EEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          490       500
                   ....*....|....*....|....
gi 1907135714 1103 DPariSAYIEEEVQRRLHDLHRAI 1126
Cdd:COG1196    756 LP---EPPDLEELERELERLEREI 776
Kinesin_assoc super family cl24686
Kinesin-associated;
398-510 1.77e-11

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 64.86  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  398 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 428
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  429 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 496
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 1907135714  497 LLSTGIILYHLKEG 510
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 51-399 1.89e-176

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 537.71  E-value: 1.89e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01365     16 EKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  131 CVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDLL-RRKSSKTFNLRVR 209
Cdd:cd01365     95 CLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDLLnPKPKKNKGNLKVR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE--MPCETVSKIHLVDL 287
Cdd:cd01365    174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEtnLTTEKVSKISLVDL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  288 AGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIA 367
Cdd:cd01365    254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1907135714  368 TISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:cd01365    330 AISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin pfam00225
Kinesin motor domain;
47-392 1.37e-144

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 450.10  E-value: 1.37e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   47 LFSGEKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFE 126
Cdd:pfam00225    5 LNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVESVLE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNL 206
Cdd:pfam00225   72 GYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSKIHLV 285
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLV 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  286 DLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTI 364
Cdd:pfam00225  230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGNSKTL 298

                          330       340
                   ....*....|....*....|....*...
gi 1907135714  365 MIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:pfam00225  299 MIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 47-399 1.42e-142

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 444.71  E-value: 1.42e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714    47 LFSGEKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFE 126
Cdd:smart00129   11 LNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEETAAPLVDSVLE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfnL 206
Cdd:smart00129   78 GYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLLNPSSKK---L 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVD 286
Cdd:smart00129  153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   287 LAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMI 366
Cdd:smart00129  233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDSLGGNSKTLMI 302

                           330       340       350
                    ....*....|....*....|....*....|...
gi 1907135714   367 ATISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:smart00129  303 ANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
61-541 6.03e-89

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 302.04  E-value: 6.03e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   61 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 129
Cdd:COG5059     18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  130 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 209
Cdd:COG5059     91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:COG5059    166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:COG5059    244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  370 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 439
Cdd:COG5059    314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  440 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 510
Cdd:COG5059    394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1907135714  511 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 541
Cdd:COG5059    474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 480-596 8.98e-77

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 249.47  E-value: 8.98e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22732      1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907135714  560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22732     81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 49-426 3.11e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 276.43  E-value: 3.11e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   49 SGEKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDfsfYSADTKSpdyvSQEMVFKTLGTDVVKSAFEGY 128
Cdd:PLN03188    93 NGVSDSGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQTFTFD---SIADPES----TQEDIFQLVGAPLVENCLAGF 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  129 NACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTEVSYLEIYNERVR 193
Cdd:PLN03188   166 NSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCRCSFLEIYNEQIT 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  194 DLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFT-IKFTQAKFDA 272
Cdd:PLN03188   244 DLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTcVVESRCKSVA 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  273 E-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQVFVPYRDSVLTW 351
Cdd:PLN03188   321 DgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQRHIPYRDSRLTF 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  352 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAEIARLKtllAQGN 425
Cdd:PLN03188   394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVK---ANGN 470


                   .
gi 1907135714  426 Q 426
Cdd:PLN03188   471 N 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-1126 1.08e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196    290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG1196    446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  884 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196    521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  944 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 1022
Cdd:COG1196    601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1023 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1102
Cdd:COG1196    681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL-----EEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          490       500
                   ....*....|....*....|....
gi 1907135714 1103 DPariSAYIEEEVQRRLHDLHRAI 1126
Cdd:COG1196    756 LP---EPPDLEELERELERLEREI 776
Kinesin_assoc pfam16183
Kinesin-associated;
398-510 1.77e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 64.86  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  398 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 428
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  429 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 496
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 1907135714  497 LLSTGIILYHLKEG 510
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 642-1137 7.84e-11

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: 67.30  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 708
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  709 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLH---------- 778
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqqkttlt 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  779 -QEQNAQSAKLRLEKRRLEEEEKEQVQRV-----AHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 852
Cdd:TIGR00618  393 qKLQSLCKELDILQREQATIDTRTSAFRDlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  853 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 931
Cdd:TIGR00618  472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  932 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVG---- 992
Cdd:TIGR00618  544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqp 623

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  993 -EKEEQIAQYQANASQ-LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1068
Cdd:TIGR00618  624 eQDLQDVRLHLQQCSQeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135714 1069 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARISAYIEEEVQRRLHdlHRAIGDANHTPADVM 1137
Cdd:TIGR00618  704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK--ARTEAHFNNNEEVTA 772
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 658-907 8.86e-11

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: 67.07  E-value: 8.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  658 RKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkdllaekerfeEERLREQQGLEQ 737
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ------------AAIYAEQERMAM 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  738 QRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleeeekeqvQRVAHLEEQLRK 815
Cdd:pfam17380  345 ERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN------------------ERVRQELEAARK 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  816 RQdtaplLCPGEAQRA-QEEKRELESIREALLQAK--EMRAGGDHTCRdELERAQQYFLEfKRRQLVKLASLEKDLVQQK 892
Cdd:pfam17380  404 VK-----ILEEERQRKiQQQKVEMEQIRAEQEEARqrEVRRLEEERAR-EMERVRLEEQE-RQQQVERLRQQEEERKRKK 476

                          250
                   ....*....|....*
gi 1907135714  893 DLLSKEVQEEKVALE 907
Cdd:pfam17380  477 LELEKEKRDRKRAEE 491
PTZ00121 PTZ00121
MAEBL; Provisional
 589-861 1.90e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  589 KEAAKLREKRKSGLLSSFSLSMTDLSKSCEN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 666
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  667 KQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSfhiENKLKDllaekerfeeerlreqqglEQQRRQEEESL 746
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKA---EEAKKA-------------------EEDEKKAAEAL 1694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  747 FRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQlrkrqdtap 821
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE--------- 1765

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907135714  822 llcpgEAQRAQEEKRELESIREALLQAKE--MRAGGDHTCRD 861
Cdd:PTZ00121  1766 -----EEKKAEEIRKEKEAVIEEELDEEDekRRMEVDKKIKD 1802
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
505-585 4.51e-07

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 4.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  505 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 582
Cdd:COG1716     16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                   ...
gi 1907135714  583 FRF 585
Cdd:COG1716     91 LRF 93
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 505-589 2.01e-04

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


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 41.86  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  505 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQCS--VNGVQIVDAT-QLNQGAVILLGRTn 581
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDL-GSGNGtlVNGQRVTELGiALRPGDRIELGQT- 86


                   ....*...
gi 1907135714  582 MFRFNHPK 589
Cdd:pfam16697   87 EFCLVPAD 94
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 51-399 1.89e-176

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 537.71  E-value: 1.89e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01365     16 EKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  131 CVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDLL-RRKSSKTFNLRVR 209
Cdd:cd01365     95 CLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDLLnPKPKKNKGNLKVR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE--MPCETVSKIHLVDL 287
Cdd:cd01365    174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEtnLTTEKVSKISLVDL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  288 AGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIA 367
Cdd:cd01365    254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1907135714  368 TISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:cd01365    330 AISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin pfam00225
Kinesin motor domain;
47-392 1.37e-144

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 450.10  E-value: 1.37e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   47 LFSGEKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFE 126
Cdd:pfam00225    5 LNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVESVLE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNL 206
Cdd:pfam00225   72 GYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSKIHLV 285
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLV 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  286 DLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTI 364
Cdd:pfam00225  230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGNSKTL 298

                          330       340
                   ....*....|....*....|....*...
gi 1907135714  365 MIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:pfam00225  299 MIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 47-399 1.42e-142

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 444.71  E-value: 1.42e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714    47 LFSGEKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFE 126
Cdd:smart00129   11 LNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEETAAPLVDSVLE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfnL 206
Cdd:smart00129   78 GYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLLNPSSKK---L 152

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVD 286
Cdd:smart00129  153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   287 LAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMI 366
Cdd:smart00129  233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDSLGGNSKTLMI 302

                           330       340       350
                    ....*....|....*....|....*....|...
gi 1907135714   367 ATISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:smart00129  303 ANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 51-390 7.32e-132

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 414.73  E-value: 7.32e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd00106     15 EARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGTAKPLVDSALEGYNG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  131 CVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEALFSRINETtRWDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLRVR 209
Cdd:cd00106     80 TIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDLLSPVPKK--PLSLR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:cd00106    157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLVDLAG 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:cd00106    237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305

                          330       340
                   ....*....|....*....|.
gi 1907135714  370 SPADVNYGETLSTLRYANRAK 390
Cdd:cd00106    306 SPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 51-392 4.93e-110

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 353.69  E-value: 4.93e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   51 EKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01371     16 EKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDETARPLVDSVLEGYNG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  131 CVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLR 207
Cdd:cd01371     84 TIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIRDLLGKDQTK--RLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  208 VREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--DAEMPCeTVSKIHLV 285
Cdd:cd01371    160 LKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeDGENHI-RVGKLNLV 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  286 DLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIM 365
Cdd:cd01371    239 DLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTRLLQDSLGGNSKTVM 307

                          330       340
                   ....*....|....*....|....*..
gi 1907135714  366 IATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01371    308 CANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 85-392 5.41e-110

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 353.94  E-value: 5.41e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   85 ERTKTFTYDFSFysaDTKSPdyvsQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPR 158
Cdd:cd01372     37 GTDKSFTFDYVF---DPSTE----QEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01372    110 AIQHIFKKIEKKK--DTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQ 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNIN 310
Cdd:cd01372    188 GSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISIN 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  311 KSLVTLGNVISALADLSQDAAnplvkkkqvFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01372    268 SGLLALGNVISALGDESKKGA---------HVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRAR 338


                   ..
gi 1907135714  391 NI 392
Cdd:cd01372    339 NI 340
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 40-401 2.43e-99

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 323.69  E-value: 2.43e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   40 VEILAAVLFSGEKDLEAKFIIQMEK-SKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLGT 118
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKlSSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVGK 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  119 DVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEALFSRIN--ETTRWDEASFRTEVSYLEIY 188
Cdd:cd01373     65 PIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEIY 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  189 NERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQA 268
Cdd:cd01373    145 NEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESW 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  269 KFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaanplvkkKQVFVPYRDSV 348
Cdd:cd01373    222 EKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDSK 293

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907135714  349 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 401
Cdd:cd01373    294 LTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 82-392 4.56e-99

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 323.14  E-value: 4.56e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   82 SGRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICE 161
Cdd:cd01370     55 KRRNKELKYVFDRVF-------DETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMK 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  162 ALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNI 241
Cdd:cd01370    128 ELFKRIESLK--DEKEFEVSMSYLEIYNETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNR 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  242 NRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCET-VSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVI 320
Cdd:cd01370    203 NRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCI 282

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714  321 SALADLsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01370    283 NALADP---------GKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 72-394 2.16e-98

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 320.31  E-value: 2.16e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   72 LKIPEGGTG----DSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGKSYTMM 147
Cdd:cd01366     25 ITFPDEDGQtielTSIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LVQSALDGYNVCIFAYGQTGSGKTYTME 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  148 GNSGDSGLIPRICEALFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGP-YVEDLSKH 224
Cdd:cd01366     97 GPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPGNAPQKKLEIRHDSEKGDtTVTNLTEV 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  225 LVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfdaempceTVSKIHLVDLAGSERADATGA 298
Cdd:cd01366    174 KVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--------SVGKLNLVDLAGSERLNKSGA 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  299 TGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGE 378
Cdd:cd01366    246 TGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNE 313

                          330
                   ....*....|....*.
gi 1907135714  379 TLSTLRYANRAKNIIN 394
Cdd:cd01366    314 TLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 90-392 1.15e-97

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 318.12  E-value: 1.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   90 FTYDFSFysaDTKSPDYVsqemVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINE 169
Cdd:cd01374     41 FTFDHVF---GGDSTNRE----VYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  170 TTRWDeasFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATG 249
Cdd:cd01374    114 TPDRE---FLLRVSYLEIYNEKINDLL---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETD 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  250 MNDVSSRSHAIFTIK-FTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsq 328
Cdd:cd01374    188 MNERSSRSHTIFRITiESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE--- 264

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135714  329 daanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01374    265 -------GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 82-392 7.69e-96

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 312.73  E-value: 7.69e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   82 SGRERTKTFTYDFSFYsADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPR 158
Cdd:cd01369     37 ATSETGKTFSFDRVFD-PNT------TQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01369    110 IVQDIFETIYSMD--ENLEFHVKVSYFEIYMEKIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDE 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAkfDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGN 318
Cdd:cd01369    185 GKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGN 262

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135714  319 VISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01369    263 VINALTD-----------GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
61-541 6.03e-89

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 302.04  E-value: 6.03e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   61 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 129
Cdd:COG5059     18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  130 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 209
Cdd:COG5059     91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:COG5059    166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:COG5059    244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  370 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 439
Cdd:COG5059    314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  440 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 510
Cdd:COG5059    394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1907135714  511 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 541
Cdd:COG5059    474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 79-401 1.20e-84

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 281.91  E-value: 1.20e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   79 TGDSGRERTKTFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN--------- 149
Cdd:cd01364     40 GGLADKSSTKTYTFDMVFGPE-------AKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytw 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  150 --SGDSGLIPRICEALFSRINETtrwdEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHL 225
Cdd:cd01364    113 elDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVSYLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEIT 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  226 VQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETV---SKIHLVDLAGSERADATGATGVR 302
Cdd:cd01364    189 VHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI--TIHIKETTIDGEELvkiGKLNLVDLAGSENIGRSGAVDKR 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  303 LKEGGNINKSLVTLGNVISALADlsqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLST 382
Cdd:cd01364    267 AREAGNINQSLLTLGRVITALVE------------RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLST 334

                          330
                   ....*....|....*....
gi 1907135714  383 LRYANRAKNIINKPTINED 401
Cdd:cd01364    335 LEYAHRAKNIKNKPEVNQK 353
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 480-596 8.98e-77

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 249.47  E-value: 8.98e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22732      1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907135714  560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22732     81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 49-426 3.11e-75

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 276.43  E-value: 3.11e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   49 SGEKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDfsfYSADTKSpdyvSQEMVFKTLGTDVVKSAFEGY 128
Cdd:PLN03188    93 NGVSDSGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQTFTFD---SIADPES----TQEDIFQLVGAPLVENCLAGF 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  129 NACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTEVSYLEIYNERVR 193
Cdd:PLN03188   166 NSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCRCSFLEIYNEQIT 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  194 DLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFT-IKFTQAKFDA 272
Cdd:PLN03188   244 DLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTcVVESRCKSVA 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  273 E-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQVFVPYRDSVLTW 351
Cdd:PLN03188   321 DgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQRHIPYRDSRLTF 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  352 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAEIARLKtllAQGN 425
Cdd:PLN03188   394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVK---ANGN 470


                   .
gi 1907135714  426 Q 426
Cdd:PLN03188   471 N 471
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 105-390 8.03e-72

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 244.41  E-value: 8.03e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  105 DYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEALFSRINEttRWDEAsFRTE 181
Cdd:cd01375     57 HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVH 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  182 VSYLEIYNERVRDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSH 258
Cdd:cd01375    134 VSYLEIYNEQLYDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  259 AIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKK 338
Cdd:cd01375    214 CIFTIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KD 282

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907135714  339 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01375    283 RTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 64-390 6.65e-70

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 239.22  E-value: 6.65e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   64 KSKTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKS 143
Cdd:cd01368     28 INSTTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  144 YTMMGNSGDSGLIPRICEALFSRINETTRWdeasfrteVSYLEIYNERVRDLLRRKSSKTF----NLRVREHPKEGPYVE 219
Cdd:cd01368    104 YTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLEPSPSSPTkkrqSLRLREDHNGNMYVA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  220 DLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE------TVSKIHLVDLAGSERA 293
Cdd:cd01368    176 GLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVDqdkdqiTVSQLSLVDLAGSERT 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  294 DATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaANPLVKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPAD 373
Cdd:cd01368    256 SRTQNTGERLKEAGNINTSLMTLGTCIEVL-------RENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCA 328

                          330
                   ....*....|....*..
gi 1907135714  374 VNYGETLSTLRYANRAK 390
Cdd:cd01368    329 SDYDETLHVMKFSAIAQ 345
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 84-390 1.02e-67

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 232.01  E-value: 1.02e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   84 RERTKTFTYDF-SFYSADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEA 162
Cdd:cd01376     38 RNHGETLKYQFdAFYGEES------TQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  163 LFsRINETTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNIN 242
Cdd:cd01376    112 LL-QMTRKEAW---ALSFTMSYLEIYQEKILDLLEPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  243 RTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISA 322
Cdd:cd01376    185 RTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNA 263

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135714  323 LadlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01376    264 L------------NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 89-390 4.11e-66

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 227.56  E-value: 4.11e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   89 TFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG----NSGDSGLIPRICEALF 164
Cdd:cd01367     51 TFRFDYVFDES-------SSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVF 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  165 SRINETTRWDEasFRTEVSYLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRT 244
Cdd:cd01367    124 RLLNKLPYKDN--LGVTVSFFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRT 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  245 TAATGMNDVSSRSHAIFTIKFTQAKFDAempceTVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISAL 323
Cdd:cd01367    198 TGQTSANSQSSRSHAILQIILRDRGTNK-----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRAL 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135714  324 AdlsqdaanplvkKKQVFVPYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01367    273 G------------QNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 480-588 2.01e-65

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 216.75  E-value: 2.01e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22708      1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80

                           90       100
                   ....*....|....*....|....*....
gi 1907135714  560 GVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22708     81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 480-598 1.37e-49

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 171.88  E-value: 1.37e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22731      1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907135714  560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKR 598
Cdd:cd22731     81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 472-595 1.48e-33

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 125.90  E-value: 1.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  472 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTeqdIVLHGLDLESEHCVFENAGGTVTLIPL 551
Cdd:cd22713      1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907135714  552 rGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLR 595
Cdd:cd22713     78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 487-587 3.00e-31

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 118.88  E-value: 3.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  487 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDA 566
Cdd:cd22705      1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80

                           90       100
                   ....*....|....*....|.
gi 1907135714  567 TQLNQGAVILLGRTNMFRFNH 587
Cdd:cd22705     81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 484-588 9.28e-27

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 106.20  E-value: 9.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  484 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQI 563
Cdd:cd22707      4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83

                           90       100
                   ....*....|....*....|....*
gi 1907135714  564 VDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22707     84 SEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 488-596 1.20e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 106.17  E-value: 1.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGT-----VTLIPLRGSQCSVNGVQ 562
Cdd:cd22726      2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907135714  563 IVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22726     82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 488-590 3.88e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 104.35  E-value: 3.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22727      3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82

                           90       100
                   ....*....|....*....|....*...
gi 1907135714  563 IVDATQLNQGAVILLGRTNMFRFNHPKE 590
Cdd:cd22727     83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 488-588 1.22e-24

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 99.98  E-value: 1.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDA 566
Cdd:cd22709      1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80

                           90       100
                   ....*....|....*....|..
gi 1907135714  567 TQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22709     81 TELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 106-322 6.51e-24

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 100.11  E-value: 6.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  106 YVSQEMVFKTLGtDVVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEALFSRIN--ETTRWDEASFRTev 182
Cdd:cd01363     29 SESQPHVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT-- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  183 syleiynervrdllrrkssktfnlrvrehpkegpyvedlskhlVQNYSDVEELMDAGNINRtTAATGMNDVSSRSHAIFT 262
Cdd:cd01363    100 -------------------------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIE 135

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  263 IkftqakfdaempcetvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 322
Cdd:cd01363    136 I--------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 505-588 1.96e-19

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 85.04  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  505 YHLKEgQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFR 584
Cdd:cd22706     19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97


                   ....
gi 1907135714  585 FNHP 588
Cdd:cd22706     98 LNCP 101
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 488-587 4.17e-19

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 84.15  E-value: 4.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAsteqDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22728      2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETYVNGKQ 77

                           90       100
                   ....*....|....*....|....*
gi 1907135714  563 IVDATQLNQGAVILLGRTNMFRFNH 587
Cdd:cd22728     78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-1126 1.08e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196    290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG1196    446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  884 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196    521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  944 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 1022
Cdd:COG1196    601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1023 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1102
Cdd:COG1196    681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL-----EEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          490       500
                   ....*....|....*....|....
gi 1907135714 1103 DPariSAYIEEEVQRRLHDLHRAI 1126
Cdd:COG1196    756 LP---EPPDLEELERELERLEREI 776
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 487-588 2.82e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 73.51  E-value: 2.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  487 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRG-SQCSV 558
Cdd:cd22711      1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907135714  559 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22711     77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 64-196 5.27e-15

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 73.79  E-value: 5.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714   64 KSKTTITNLKIPEGGTGDSG-RERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGk 142
Cdd:pfam16796   30 PELLSEAQIDYPDETSSDGKiGSKNKSFSFDRVFPPESE-------QEDVFQEISQ-LVQSCLDGYNVCIFAYGQTGSG- 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714  143 sytmmgnsGDSGLIPRICEALFSRINETTR-WDeasFRTEVSYLEIYNERVRDLL 196
Cdd:pfam16796  101 --------SNDGMIPRAREQIFRFISSLKKgWK---YTIELQFVEIYNESSQDLL 144
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 490-598 9.11e-13

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 66.45  E-value: 9.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  490 LIGIDDDLLSTGIILYHLKeGQTYVGredASTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22729      4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907135714  569 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 598
Cdd:cd22729     80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 490-588 2.48e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 64.93  E-value: 2.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  490 LIGIDDDLLSTGIILYHLKEgQTYVGREDAsteQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22730      4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79

                           90       100
                   ....*....|....*....|
gi 1907135714  569 LNQGAVILLGRTNMFRFNHP 588
Cdd:cd22730     80 LHHGDRILWGNNHFFRINLP 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 655-1126 4.74e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 4.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  655 ESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKR-----RSFH-IENKLKDLLAEKE 722
Cdd:COG1196    155 EERRAIIEEaagiSKYKERKEEAErkLEATEENLE----RLEDILGELERQLEPLERqaekaERYReLKEELKELEAELL 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  723 RFEEERLREQQGLEQQRRQEEESlfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeeekeQ 802
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---------------L 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  803 VQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLA 882
Cdd:COG1196    294 LAELARLEQDIARLEE--------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  883 SLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQnhlpaL 962
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEA-------------------------LRAAAELAAQLEELEEAEEALLE-----R 415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  963 LEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQ 1042
Cdd:COG1196    416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1043 QREALEQAVAKLEQRRSALQRcstldleiqeQRQKLGSLHTSEWSGWQASLETDGEalemdpARISAYIEEEVQRRLHDL 1122
Cdd:COG1196    496 LLEAEADYEGFLEGVKAALLL----------AGLRGLAGAVAVLIGVEAAYEAALE------AALAAALQNIVVEDDEVA 559


                   ....
gi 1907135714 1123 HRAI 1126
Cdd:COG1196    560 AAAI 563
Kinesin_assoc pfam16183
Kinesin-associated;
398-510 1.77e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 64.86  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  398 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 428
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  429 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 496
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 1907135714  497 LLSTGIILYHLKEG 510
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 642-1137 7.84e-11

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: 67.30  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 708
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  709 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLH---------- 778
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqqkttlt 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  779 -QEQNAQSAKLRLEKRRLEEEEKEQVQRV-----AHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 852
Cdd:TIGR00618  393 qKLQSLCKELDILQREQATIDTRTSAFRDlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  853 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 931
Cdd:TIGR00618  472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  932 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVG---- 992
Cdd:TIGR00618  544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqp 623

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  993 -EKEEQIAQYQANASQ-LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1068
Cdd:TIGR00618  624 eQDLQDVRLHLQQCSQeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135714 1069 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARISAYIEEEVQRRLHdlHRAIGDANHTPADVM 1137
Cdd:TIGR00618  704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK--ARTEAHFNNNEEVTA 772
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 658-907 8.86e-11

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: 67.07  E-value: 8.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  658 RKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkdllaekerfeEERLREQQGLEQ 737
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ------------AAIYAEQERMAM 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  738 QRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleeeekeqvQRVAHLEEQLRK 815
Cdd:pfam17380  345 ERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN------------------ERVRQELEAARK 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  816 RQdtaplLCPGEAQRA-QEEKRELESIREALLQAK--EMRAGGDHTCRdELERAQQYFLEfKRRQLVKLASLEKDLVQQK 892
Cdd:pfam17380  404 VK-----ILEEERQRKiQQQKVEMEQIRAEQEEARqrEVRRLEEERAR-EMERVRLEEQE-RQQQVERLRQQEEERKRKK 476

                          250
                   ....*....|....*
gi 1907135714  893 DLLSKEVQEEKVALE 907
Cdd:pfam17380  477 LELEKEKRDRKRAEE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 646-1056 1.08e-10

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: 67.00  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  646 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENkLKDLLAEK 721
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  722 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeEEKE 801
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-----------EAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  802 QVQRVAHLEEQLRkrqdtaplLCPGEAQRAQEEKRELESIREALlqAKEMRAGGdhTCRDELERAQQYFLEFKRRQLVKL 881
Cdd:TIGR02168  822 LRERLESLERRIA--------ATERRLEDLEEQIEELSEDIESL--AAEIEELE--ELIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  882 ASLEKDLvQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPA 961
Cdd:TIGR02168  890 ALLRSEL-EELSEELRELESKRSELRR------------------------ELEELREKLAQLELRLEGLEVRIDNLQER 944

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  962 LLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeQIAQYQANASQLQQ---------LRATFEFtanvarQEEKVRRKE 1032
Cdd:TIGR02168  945 LSEEYSLTLEEAEALENKIED--------------DEEEARRRLKRLENkikelgpvnLAAIEEY------EELKERYDF 1004

                          410       420
                   ....*....|....*....|....
gi 1907135714 1033 KEilesqekQQREALEQAVAKLEQ 1056
Cdd:TIGR02168 1005 LT-------AQKEDLTEAKETLEE 1021
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 657-1063 2.62e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 65.86  E-value: 2.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  657 KRKLIEEM-------EEKQKSdKAELErmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEEERL 729
Cdd:TIGR02169  155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYEL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  730 REQ-QGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKEQVQ-RVA 807
Cdd:TIGR02169  229 LKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQLRVKeKIG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  808 HLEEQLRKRQDTAPLlCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVKLASLEKD 887
Cdd:TIGR02169  298 ELEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDKLTEEYAE 361

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  888 LVQQKDLLSKEVQEEkvalehvkcdaggDPSFLATddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhLPALLEEKQ 967
Cdd:TIGR02169  362 LKEELEDLRAELEEV-------------DKEFAET-----------RDELKDYREKLEKLKREINELKRE-LDRLQEELQ 416

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  968 RvldaldsgvlgldttlcqvekevgeKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE--SQEKQQR 1044
Cdd:TIGR02169  417 R-------------------------LSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAAdlSKYEQEL 471

                          410
                   ....*....|....*....
gi 1907135714 1045 EALEQAVAKLEQRRSALQR 1063
Cdd:TIGR02169  472 YDLKEEYDRVEKELSKLQR 490
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 640-910 4.39e-10

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: 64.76  E-value: 4.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFER--QQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEvetRRKETEIVQRQIRKQE-ESLKRRSFH 709
Cdd:pfam17380  295 KMEQERlrQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAME---RERELERIRQEERKRElERIRQEEIA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  710 IE-NKLKDLlaekerfeeerlreqQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 788
Cdd:pfam17380  372 MEiSRMREL---------------ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  789 RLEKRRLEEEEKEQVQRVaHLEEQlrKRQDTAPLLCPGEAQRaQEEKRELESIREALLQAKEMRAggdHTCRDELERAQQ 868
Cdd:pfam17380  434 QREVRRLEEERAREMERV-RLEEQ--ERQQQVERLRQQEEER-KRKKLELEKEKRDRKRAEEQRR---KILEKELEERKQ 506

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907135714  869 YFLEFKRRQLVklasLEKDLVQQKDLLSKEVQEEKVALEHVK 910
Cdd:pfam17380  507 AMIEEERKRKL----LEKEMEERQKAIYEEERRREAEEERRK 544
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 489-585 6.72e-10

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: 57.67  E-value: 6.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  489 HLIGIDDDllsTGIILYHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQC--SVNGVQIVDA 566
Cdd:cd00060      1 RLIVLDGD---GGGREFPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDL-GSTNgtFVNGKRITPP 73

                           90
                   ....*....|....*....
gi 1907135714  567 TQLNQGAVILLGRTNmFRF 585
Cdd:cd00060     74 VPLQDGDVIRLGDTT-FRF 91
PTZ00121 PTZ00121
MAEBL; Provisional
 589-861 1.90e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  589 KEAAKLREKRKSGLLSSFSLSMTDLSKSCEN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 666
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  667 KQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSfhiENKLKDllaekerfeeerlreqqglEQQRRQEEESL 746
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKA---EEAKKA-------------------EEDEKKAAEAL 1694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  747 FRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQlrkrqdtap 821
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE--------- 1765

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907135714  822 llcpgEAQRAQEEKRELESIREALLQAKE--MRAGGDHTCRD 861
Cdd:PTZ00121  1766 -----EEKKAEEIRKEKEAVIEEELDEEDekRRMEVDKKIKD 1802
PTZ00121 PTZ00121
MAEBL; Provisional
 642-1185 5.45e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 5.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQI---RKQEESLKRRSFhiENKLKDLL 718
Cdd:PTZ00121  1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAE--EKKKADEA 1396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  719 AEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEKRRLEE 797
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKAD 1473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  798 EEKEQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyflEFKR 875
Cdd:PTZ00121  1474 EAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAKKAeeAKKADEAKKAEEAKKADEAKKAE----EKKK 1547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  876 RQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLL 955
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  956 QNhlpallEEKQRvldaldSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEI 1035
Cdd:PTZ00121  1626 KK------AEEEK------KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1036 LESQEKQQREA------LEQAVAKLEQRRSALQ----RCSTLDLEIQEQRQKLGSLHTSEWSG---WQASLETDGEALEM 1102
Cdd:PTZ00121  1694 LKKEAEEAKKAeelkkkEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEEEKkkiAHLKKEEEKKAEEI 1773

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1103 DPARiSAYIEEEV----QRRLHDLHRAIGDANHTPADVMKSNEELHNGTTQRKLKYETGqpwsapcvipllSKDAADSPS 1178
Cdd:PTZ00121  1774 RKEK-EAVIEEELdeedEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA------------IKEVADSKN 1840


                   ....*..
gi 1907135714 1179 VLREESE 1185
Cdd:PTZ00121  1841 MQLEEAD 1847
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 737-1101 6.30e-09

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: 61.23  E-value: 6.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  737 QQRRQEEES-LFRIREELRKLQ----ELNS-----HEQAEKVQIFQELDRlhQEQNAQsaklrlekrrleeeEKEQVQRV 806
Cdd:TIGR02168  171 KERRKETERkLERTRENLDRLEdilnELERqlkslERQAEKAERYKELKA--ELRELE--------------LALLVLRL 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  807 AHLEEQLRKRQDtapllcpgEAQRAQEEKRELES-IREALLQAKEMRAgGDHTCRDELERAQQYFLEFKRRQlvklasle 885
Cdd:TIGR02168  235 EELREELEELQE--------ELKEAEEELEELTAeLQELEEKLEELRL-EVSELEEEIEELQKELYALANEI-------- 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  886 KDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflatddgnilggppdldKIKTAETRLQSREHQLQDLLQNH--LPALL 963
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEKLEELKEELesLEAEL 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  964 EEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQyqaNASQLQQLRATFE-FTANVARQEEKVRRKEKEILESQEKQ 1042
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIAS---LNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKE 437

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714 1043 QREAL---EQAVAKLEQRRSAL-QRCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALE 1101
Cdd:TIGR02168  438 LQAELeelEEELEELQEELERLeEALEELREELEEAEQALDAAERelAQLQARLDSLERLQENLE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
645-1081 8.61e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 8.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSfhIENKLKDLLAEKERF 724
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  725 EEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIF-QELDRLHQEQNAQSAKLRLEKrrleeeekeqv 803
Cdd:COG4717    152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQ----------- 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL------LQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 877
Cdd:COG4717    220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALlglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  878 LVKLASLEKDLVQQKDLLSKEVQEEkvalehvkCDAGGDPSFLATDDgnILGGPPDLDKIKTAETRLQSREHQLQdllqn 957
Cdd:COG4717    300 LGKEAEELQALPALEELEEEELEEL--------LAALGLPPDLSPEE--LLELLDRIEELQELLREAEELEEELQ----- 364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  958 hLPALLEEKQRVLDALDsgvlgldttlCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQ----------EEK 1027
Cdd:COG4717    365 -LEELEQEIAALLAEAG----------VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealdeeelEEE 433

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135714 1028 VRRKEKEILESQEkqQREALEQAVAKLEQRRSALQRCSTLD---LEIQEQRQKLGSL 1081
Cdd:COG4717    434 LEELEEELEELEE--ELEELREELAELEAELEQLEEDGELAellQELEELKAELREL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 640-1143 8.61e-09

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: 60.84  E-value: 8.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREEL--------EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSF 708
Cdd:TIGR02168  324 QLEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  709 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQE-EESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAK 787
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  788 LRLEKrrleeeekeqvQRVAHLEEQLRKRQDtapllcPGEAQRAQEEKR-----------ELESIREALLQAKEMRAGG- 855
Cdd:TIGR02168  484 LAQLQ-----------ARLDSLERLQENLEG------FSEGVKALLKNQsglsgilgvlsELISVDEGYEAAIEAALGGr 546

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  856 -DHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK-------VALEHVKCDAGGDPSF-------- 919
Cdd:TIGR02168  547 lQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgVAKDLVKFDPKLRKALsyllggvl 626

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  920 --------------------LATDDGNIL-------GGPPDLD--------KIKTAETRLQSREHQLQDLLQNhlpalLE 964
Cdd:TIGR02168  627 vvddldnalelakklrpgyrIVTLDGDLVrpggvitGGSAKTNssilerrrEIEELEEKIEELEEKIAELEKA-----LA 701

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  965 EKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQR 1044
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1045 EALEQAVAKLEQrrsALQRCSTLDLEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPArisayieeEVQRRLHDLHR 1124
Cdd:TIGR02168  782 AEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEE-----AANLRERLESLERRIA--------ATERRLEDLEE 845

                          570
                   ....*....|....*....
gi 1907135714 1125 AIGDANHTPADVMKSNEEL 1143
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEEL 864
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 640-853 1.03e-08

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: 60.52  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQeveTRRKETEIVQRQIRKQEESLKRRSFHIENKlkdl 717
Cdd:pfam17380  382 RLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQREVRRLEEERAREMERVRLE---- 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  718 laekerfeeeRLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQ---IFQELdrlhqEQNAQSAKLRLEKRR 794
Cdd:pfam17380  455 ----------EQERQQQVERLRQQEEE---RKRKKLELEKEKRDRKRAEEQRrkiLEKEL-----EERKQAMIEEERKRK 516

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135714  795 LEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRA 853
Cdd:pfam17380  517 LLEKEMEERQKAIYEEERRREAE---------EERRKQQEMEERRRIQEQMRKATEERS 566
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 640-868 1.16e-08

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 59.97  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetRRKEtEIVQRQIRKQEESLKRRsfhiENKLKDLLa 719
Cdd:pfam15709  347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ----RRFE-EIRLRKQRLEEERQRQE----EEERKQRL- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  720 ekerfeeerlREQQGLEQQRRQEEEslFRireelRKLQELNSHEQAEkvqifqELDRLHQEQnaqsaklrlekrrleeee 799
Cdd:pfam15709  413 ----------QLQAAQERARQQQEE--FR-----RKLQELQRKKQQE------EAERAEAEK------------------ 451

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135714  800 keqvQRVAHLEEQLRKRQDTapLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQ 868
Cdd:pfam15709  452 ----QRQKELEMQLAEEQKR--LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
PTZ00121 PTZ00121
MAEBL; Provisional
 640-1077 1.30e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIEEM----EEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEEslKRRSFHIE 711
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAkkkaEEKKKADeakkKAEEAKKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAK 1476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  712 NKLKDLLAEKERFEEERLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLE 791
Cdd:PTZ00121  1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  792 KRRLEeeekeQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKReLESIREALLQAKEMRAggdhtcrDELERAQQyfl 871
Cdd:PTZ00121  1554 AEELK-----KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKA-------EEAKKAEE--- 1617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  872 EFKRRQLVKLASLEKDLVQQkdlLSKEVQEEKVALEHVKCDAggdpsflatddgnilggppDLDKIKTAETRLQSREHQL 951
Cdd:PTZ00121  1618 AKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAE-------------------EENKIKAAEEAKKAEEDKK 1675

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  952 QdllQNHLPALLEEKQRVLDALdsgvlgldttlcQVEKEVGEKEEQIAQYQAN-ASQLQQLRATFEFTANVARQEEKVRR 1030
Cdd:PTZ00121  1676 K---AEEAKKAEEDEKKAAEAL------------KKEAEEAKKAEELKKKEAEeKKKAEELKKAEEENKIKAEEAKKEAE 1740

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907135714 1031 KEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQK 1077
Cdd:PTZ00121  1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-1057 1.42e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196    325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ------ELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeeALLELLAELLEEAALLEAALAELLE 484

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  798 EEKEQVQRVAHLEEQLRKRQ------------DTAPLLCPGEAQRAQEEKRELESIREALLqakemrAGGDHTCRDELER 865
Cdd:COG1196    485 ELAEAAARLLLLLEAEADYEgflegvkaalllAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEV 558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  866 AQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKV--ALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196    559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  944 LQSREHQLQDL--------------------LQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQA 1003
Cdd:COG1196    639 AVTLAGRLREVtlegeggsaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1004 NASQLQQLRATFEFT--------------------------ANVARQEEKVRRKEKEI-------------LESQE---- 1040
Cdd:COG1196    719 EELEEEALEEQLEAEreelleelleeeelleeealeelpepPDLEELERELERLEREIealgpvnllaieeYEELEeryd 798

                          490
                   ....*....|....*....
gi 1907135714 1041 --KQQREALEQAVAKLEQR 1057
Cdd:COG1196    799 flSEQREDLEEARETLEEA 817
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 647-1058 1.43e-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: 60.08  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  647 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEE 726
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGL-------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  727 ERLREQQGLEQQRRQEEESLFRIREELRKLQE--------LNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleee 798
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleeaLNDLEARLSHSRIPEIQAELSKLEEEVS------------ 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  799 ekEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELErAQQYFLEFKRRQL 878
Cdd:TIGR02169  809 --RIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIE-NLNGKKEELEEEL 870

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  879 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDlLQNH 958
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELE------------------------RKIEELEAQIEKKRKRLSE-LKAK 925

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  959 LPALLEEKQRVLDALDSGVlgldttlcqvekEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE 1037
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDE------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEyEEVLKRLDELKE 993

                          410       420
                   ....*....|....*....|...
gi 1907135714 1038 SQEK--QQREALEQAVAKLEQRR 1058
Cdd:TIGR02169  994 KRAKleEERKAILERIEEYEKKK 1016
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 640-917 1.62e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  720 EKERFEEERLREQQGLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQ---ELDRLHQEQNAQSAKLRLEKRRLE 796
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLE 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  797 EEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhTCRDELERAQQYFLEFkRR 876
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-------ELREELEEAEQALDAA-ER 482

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907135714  877 QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDP 917
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 649-1085 5.45e-08

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: 58.06  E-value: 5.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  649 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL------LAEKE 722
Cdd:TIGR00618  170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKR 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  723 RFEEERLREQQGLEQQRRQEEE--SLFRIREELRKLQELNSH------EQAEKVQIFQELDRLHQEQNAQSAK------- 787
Cdd:TIGR00618  250 EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmk 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  788 -LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEK---RELESIREALLQAKEMRAGGDHTCRDel 863
Cdd:TIGR00618  330 rAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKELDILQR-- 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  864 ERAQQYFLEFKRRQL-VKLASLEKDLV-QQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGppDLDKIKTAE 941
Cdd:TIGR00618  408 EQATIDTRTSAFRDLqGQLAHAKKQQElQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--TKEQIHLQE 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  942 TRLQSREHQLQDLLQNhLPALLEEKQRVLDA--LDSGVLGLDTTLCQVEKEVGEKEE---------------QIAQYQAN 1004
Cdd:TIGR00618  486 TRKKAVVLARLLELQE-EPCPLCGSCIHPNParQDIDNPGPLTRRMQRGEQTYAQLEtseedvyhqltserkQRASLKEQ 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1005 ASQLQQ-------LRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQK 1077
Cdd:TIGR00618  565 MQEIQQsfsiltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644


                   ....*...
gi 1907135714 1078 LGSLHTSE 1085
Cdd:TIGR00618  645 LTALHALQ 652
PTZ00121 PTZ00121
MAEBL; Provisional
 642-1153 5.84e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 5.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQRE---ELEKLESKRKLIEEmEEKQKSDKAELERMQQEV-----ETRRKETEIVQRQIRKQEESLKR---RSFHI 710
Cdd:PTZ00121  1078 DFDFDAKEdnrADEATEEAFGKAEE-AKKTETGKAEEARKAEEAkkkaeDARKAEEARKAEDARKAEEARKAedaKRVEI 1156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  711 ENKLKDllaEKERFEEERLREQQGLEQQRRQEEeslFRIREELRKLQELNSHEQA---EKVQIFQELDRLHQEQNAQsAK 787
Cdd:PTZ00121  1157 ARKAED---ARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAArkaEEERKAEEARKAEDAKKAE-AV 1229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  788 LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELER 865
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeeKKKADEAKKAEEKKKADEAKK 1309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  866 AQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGdpsflATDDGNILGGPPDLDKIKTAETRLQ 945
Cdd:PTZ00121  1310 KAE-----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA-----AADEAEAAEEKAEAAEKKKEEAKKK 1379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  946 SREHQL---QDLLQNHLPALLEEKQRVLDALDSGvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQlratfefTANVA 1022
Cdd:PTZ00121  1380 ADAAKKkaeEKKKADEAKKKAEEDKKKADELKKA---------AAAKKKADEAKKKAEEKKKADEAKK-------KAEEA 1443

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1023 RQEEKVRRK--EKEILESQEKQQREA--LEQAVAKLEQRRSAlqrcSTLDLEIQEQRQKLGSLHTSEWSGWQA-SLETDG 1097
Cdd:PTZ00121  1444 KKADEAKKKaeEAKKAEEAKKKAEEAkkADEAKKKAEEAKKA----DEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAE 1519

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907135714 1098 EALEMDPARisayiEEEVQRRLHDLHRAigdANHTPADVMKSNEELHNGTTQRKLK 1153
Cdd:PTZ00121  1520 EAKKADEAK-----KAEEAKKADEAKKA---EEKKKADELKKAEELKKAEEKKKAE 1567
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 485-588 6.59e-08

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 52.69  E-value: 6.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  485 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDASTEQ-DIVLHGLDLESEHCV-----------FENAGGT-- 545
Cdd:cd22712      1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907135714  546 --VTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22712     76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 640-901 1.48e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETRRKETEIVQRQI---RKQEESLKRRSFHIENKL 714
Cdd:TIGR02169  202 RLRREREKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEIselEKRLEEIEQLLEELNKKI 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  715 KDL------------------LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDR 776
Cdd:TIGR02169  282 KDLgeeeqlrvkekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  777 LHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESireallqakemrAGGD 856
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK-----RELDRLQEELQRLSE------------ELAD 424

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907135714  857 HtcRDELERAQQYFLEFKRRQLVKLASLEKD---LVQQKDLLSKEVQE 901
Cdd:TIGR02169  425 L--NAAIAGIEAKINELEEEKEDKALEIKKQewkLEQLAADLSKYEQE 470
PTZ00121 PTZ00121
MAEBL; Provisional
 644-1155 2.10e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 2.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIE--EMEEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL 717
Cdd:PTZ00121  1276 EARKADELKKAEEKKKADEakKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  718 LAEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNSHEQAEKVQIfQELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:PTZ00121  1356 ADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKA 1433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  798 EEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGGDhtCRDELERAQQYFLEFK 874
Cdd:PTZ00121  1434 DEAKKKAEEAKKADEAKKKAE--------EAKKAEEAKKKAEEAKkadEAKKKAEEAKKADE--AKKKAEEAKKKADEAK 1503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  875 RRQLVKLASLEKDLVQQKdllsKEVQEEKVALEHVKCDAGGDPSFLATDDgnilggppDLDK---IKTAETRLQSREHQL 951
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEA----KKADEAKKAEEAKKADEAKKAEEKKKAD--------ELKKaeeLKKAEEKKKAEEAKK 1571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  952 QDLLQNHLPALLEEKQRVLDALDSGVLGLDTtlcQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRK 1031
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYE---EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1032 EKEILESQEKQQREALEQAVAKLEQRRSAlqrcSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARISAYI 1111
Cdd:PTZ00121  1649 AEELKKAEEENKIKAAEEAKKAEEDKKKA----EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1907135714 1112 EEEVQRRLHDLHRAiGDANHTPADVMKSNEELHNGTTQRKLKYE 1155
Cdd:PTZ00121  1725 EEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
505-585 4.51e-07

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 4.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  505 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 582
Cdd:COG1716     16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                   ...
gi 1907135714  583 FRF 585
Cdd:COG1716     91 LRF 93
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
644-957 5.36e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKER 723
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEeekeqv 803
Cdd:COG4372    109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE------ 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEkRELESIREALLQAKEMRAGGDHTcRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG4372    183 QALDELLKEANRNAEKEEELAEAEKLIESLP-RELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEI 260

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135714  884 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQN 957
Cdd:COG4372    261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 639-1074 5.48e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 54.98  E-value: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFERQQREElEKLESKRKLIEEMEEKQK--------------SDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 704
Cdd:pfam02463  253 IESSKQEIEKEE-EKLAQVLKENKEEEKEKKlqeeelkllakeeeELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  705 RRSFHIENKLKDLLAEKERFEEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQifQELDRLHQEQNAQ 784
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE--ELELKSEEEKEAQ 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  785 SAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEA---QRAQEEKRELESIREALLQAKEMRAGGDHTCRD 861
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  862 ELERAQQYFLEFKRRQLVK-LASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTA 940
Cdd:pfam02463  489 LLSRQKLEERSQKESKARSgLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  941 ETR-----LQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQ-------ANASQL 1008
Cdd:pfam02463  569 ALTelplgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakAKESGL 648

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907135714 1009 QQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAV----------AKLEQRRSALQRCSTLDLEIQEQ 1074
Cdd:pfam02463  649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEAEELLA 724
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
645-1062 5.90e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQ---QEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEK 721
Cdd:COG4717    115 REELEKLEKLLQLLPLYQELEALE----AELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  722 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKL-QELNSHE-QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEE 799
Cdd:COG4717    191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELeEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  800 KEQ--------VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFL 871
Cdd:COG4717    271 LILtiagvlflVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  872 EFKRRQLVKLASLEKDLVQQkdllskEVQEEKVALEHvKCDAGGDPSFLAtddgnilggppdLDKIKTAETRLQSREHQL 951
Cdd:COG4717    347 EELQELLREAEELEEELQLE------ELEQEIAALLA-EAGVEDEEELRA------------ALEQAEEYQELKEELEEL 407

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  952 QDLLQNHLPALLEEkqrvLDALDSGVLgldttlcqvekevgekEEQIAQYQANASQLQQLRAtfEFTANVARQEEKVRRK 1031
Cdd:COG4717    408 EEQLEELLGELEEL----LEALDEEEL----------------EEELEELEEELEELEEELE--ELREELAELEAELEQL 465

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1907135714 1032 EKEILESQEKQQREALEQAVAKLEQRRSALQ 1062
Cdd:COG4717    466 EEDGELAELLQELEELKAELRELAEEWAALK 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
644-1101 6.24e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETeiVQRQIRKQEESLKRRsfhiENKLKDLLAEKER 723
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEER----ERRRARLEALLAA 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRleeeekeQV 803
Cdd:COG4913    371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR-------LL 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLC------PGEAQ--------------------------------------------RAQE 833
Cdd:COG4913    444 ALRDALAEALGLDEAELPFVGelievrPEEERwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervRTGL 523

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  834 EKRELESIREALLQAK--------------EMRAGGDHTC---RDELER--------------------------AQQYF 870
Cdd:COG4913    524 PDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdsPEELRRhpraitragqvkgngtrhekddrrriRSRYV 603

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  871 LEFKRRQlvKLASLEKDLVQQKDLLSkEVQEEKVALEhvkcDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQ 950
Cdd:COG4913    604 LGFDNRA--KLAALEAELAELEEELA-EAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  951 LQDLLQNhlPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRR 1030
Cdd:COG4913    677 LERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135714 1031 KEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKlgslHTSEWSGWQASLETDGEALE 1101
Cdd:COG4913    755 FAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRA----FNREWPAETADLDADLESLP 815
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 645-1041 6.55e-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: 54.68  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELE-KLESKRK-------LIEEMEEKQKSdkaeLERmQQEVETRRKEteivqrqIRKQEESLKRRSFHIE-NKLK 715
Cdd:TIGR02168  171 KERRKETErKLERTREnldrledILNELERQLKS----LER-QAEKAERYKE-------LKAELRELELALLVLRlEELR 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  716 DLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLhqEQNAQsaklrlekrrl 795
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQ----------- 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  796 eeeekEQVQRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEMRAGgdhtCRDELERAQQYFLEFKR 875
Cdd:TIGR02168  306 -----ILRERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELES----LEAELEELEAELEELES 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  876 R------QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdldkiktAETRLQSREH 949
Cdd:TIGR02168  373 RleeleeQLETLRSKVAQLELQIASLNNEIERLEARLER-------------------------------LEDRRERLQQ 421

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  950 QLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQ----YQANASQLQQLRATFEFTANVARQE 1025
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENL 501

                          410
                   ....*....|....*.
gi 1907135714 1026 EKVRRKEKEILESQEK 1041
Cdd:TIGR02168  502 EGFSEGVKALLKNQSG 517
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 644-1081 1.47e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.43  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETR---------------RKETEIVQRQIRKQEES--LKRR 706
Cdd:TIGR00618  430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtkeqihlqetRKKAVVLARLLELQEEPcpLCGS 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  707 SFHIENKLKDLLaekerFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:TIGR00618  510 CIHPNPARQDID-----NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  787 KLRLEKRRleeeekeqVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA 866
Cdd:TIGR00618  585 DIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  867 QQYflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQS 946
Cdd:TIGR00618  657 QER----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  947 REHQLQDLLQNHLPALLEEKQRVLDAL-------DSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAtfefta 1019
Cdd:TIGR00618  733 DLAAREDALNQSLKELMHQARTVLKARteahfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA------ 806

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714 1020 nvaRQEEKVRRKEKEILESQEKQQREaLEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1081
Cdd:TIGR00618  807 ---EIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 640-837 2.27e-06

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 52.26  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:pfam15709  354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  720 EKERFEEERLREQQGLEQQRRQEEEslFRIREELRKLQELNSHEQaekvqifqeLDRLHQEQNAQSaklrlekrrleeee 799
Cdd:pfam15709  434 ELQRKKQQEEAERAEAEKQRQKELE--MQLAEEQKRLMEMAEEER---------LEYQRQKQEAEE-------------- 488

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907135714  800 keqvQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRE 837
Cdd:pfam15709  489 ----KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 642-847 2.29e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM-------QQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKl 714
Cdd:pfam13868  170 EREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELK- 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  715 kdllaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELnshEQAEKVQIFQELDRLHQEQNAQsaklrlekrr 794
Cdd:pfam13868  249 -----------------ERRLAEEAEREEEEFERMLRKQAEDEEI---EQEEAEKRRMKRLEHRRELEKQ---------- 298

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907135714  795 leeEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQ 847
Cdd:pfam13868  299 ---IEEREEQRAAEREEELEEGER--------LREEEAERRERIEEERQKKLK 340
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 646-968 3.60e-06

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: 52.28  E-value: 3.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  646 QQREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFE 725
Cdd:pfam02463  192 LEELKLQELKLKEQAKKALEYYQLKEKLELEE---EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  726 EERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQA-----EKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEK 800
Cdd:pfam02463  269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  801 EQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK 880
Cdd:pfam02463  349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  881 lasLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsFLATDDGNILggppDLDKIKTAETRLQSREHQLQDLLQNHLP 960
Cdd:pfam02463  429 ---LEILEEEEESIELKQGKLTEEKEELEK--------QELKLLKDEL----ELKKSEDLLKETQLVKLQEQLELLLSRQ 493


                   ....*...
gi 1907135714  961 ALLEEKQR 968
Cdd:pfam02463  494 KLEERSQK 501
RNase_Y_N pfam12072
RNase Y N-terminal region;
657-770 4.42e-06

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 49.50  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  657 KRKLIEEMEEKQKSdKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEEERLREQQGLE 736
Cdd:pfam12072   52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEK----KEKELEAQQQQLE 123

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907135714  737 QQRRQEEEslfRIREELRKLQELN--SHEQAEKVQI 770
Cdd:pfam12072  124 EKEEELEE---LIEEQRQELERISglTSEEAKEILL 156
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 666-903 5.30e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  666 EKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhIENKLKDLlaekerfeeerLREQQGLEQQRRQEEES 745
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAAL-----------ARRIRALEQELAALEAE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  746 LFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRqdtapllcp 825
Cdd:COG4942     85 LAELEKEIAELRA----ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ--------- 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135714  826 geAQRAQEEKRELESIREALLQAKEMRAGGdhtcRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK 903
Cdd:COG4942    152 --AEELRADLAELAALRAELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 645-891 5.51e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 5.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENK 713
Cdd:pfam13868    2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  714 LKDLLAEKERFEEERLR-EQQGLEQQRRQEEESLFRIREELRK-----------LQELNSHEQAEKVQIFQELDRLHQ-- 779
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKqrqlreeidefNEEQAEWKELEKEEEREEDERILEyl 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  780 -EQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLcpgEAQRAQEEKRELESIREALLQAKEMRAggdht 858
Cdd:pfam13868  162 kEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL---RAKLYQEEQERKERQKEREEAEKKARQ----- 233

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907135714  859 cRDELERAQQYFLEFKRRQLVKLASLEKDLVQQ 891
Cdd:pfam13868  234 -RQELQQAREEQIELKERRLAEEAEREEEEFER 265
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 644-910 5.81e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:pfam13868   87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 feeerlrEQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIfqELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:pfam13868  167 -------REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL--RAKLYQEEQERKERQKEREEAEKKARQRQEL 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKE---MRAGGDHTCRDELERAQQYFLEFKRRQlvK 880
Cdd:pfam13868  238 QQAREEQIELKERR---------LAEEAEREEEEFERMLRKQAEDEEieqEEAEKRRMKRLEHRRELEKQIEEREEQ--R 306

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907135714  881 LASLEKDLvQQKDLLSKEVQEEKVALEHVK 910
Cdd:pfam13868  307 AAEREEEL-EEGERLREEEAERRERIEEER 335
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 639-766 5.85e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 48.11  E-value: 5.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETRRKETEivqRQIRKQEESLKRRSFHIENKLKDll 718
Cdd:pfam05672   23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE---RRREEEERQRKAEEEAEEREQRE-- 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907135714  719 aekerfeeerlreQQGLEQQRRQEEESLFRIREEL-RKLQELNSHEQAE 766
Cdd:pfam05672   93 -------------QEEQERLQKQKEEAEAKAREEAeRQRQEREKIMQQE 128
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
827-1081 6.16e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  827 EAQRAQEEKRELESIREALLQAKEmraggdhtCRDELERAQQYFLEFkRRQLVKLASLEkdlvQQKDLLSKEVQEEKVAL 906
Cdd:COG4913    226 AADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERY-AAARERLAELE----YLRAALRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  907 EHVKCDAGGDpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLcq 986
Cdd:COG4913    293 LEAELEELRA----------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-- 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  987 vekevgekeeqiAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILEsQEKQQREALEQAVAKLEQRRSALQRcs 1065
Cdd:COG4913    355 ------------EERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLE-ALEEELEALEEALAEAEAALRDLRR-- 419

                          250
                   ....*....|....*.
gi 1907135714 1066 tldlEIQEQRQKLGSL 1081
Cdd:COG4913    420 ----ELRELEAEIASL 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
648-1130 7.93e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 7.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  648 REELEKLESKRKLIEEMEE------KQKSDKAELERMQQ--EVETRRKETEIVQRQIRKQEESLKRrsfhienkLKDLLA 719
Cdd:COG4913    241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR--------LEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  720 EKERFEEERLREQQGLEQQRRQEE-ESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 798
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  799 EKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAqqyfLEFKRRQ- 877
Cdd:COG4913    389 AAALLEALEEELEALEEALAEA----EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA----LGLDEAEl 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  878 -----LVKLASLEKD----------------LVQQKDL-----------LSKEVQEEKVALEH-----VKCDAGGDPSFL 920
Cdd:COG4913    461 pfvgeLIEVRPEEERwrgaiervlggfaltlLVPPEHYaaalrwvnrlhLRGRLVYERVRTGLpdperPRLDPDSLAGKL 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  921 ATDDG-------NILGGPPDLDKIKTAE--------------TRLQSREHQLQDllQNHLP----------ALLEEKQRV 969
Cdd:COG4913    541 DFKPHpfrawleAELGRRFDYVCVDSPEelrrhpraitragqVKGNGTRHEKDD--RRRIRsryvlgfdnrAKLAALEAE 618

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  970 LDALDSGVLGLDTTLcqvekevGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEI--LES------QEK 1041
Cdd:COG4913    619 LAELEEELAEAEERL-------EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerLDAssddlaALE 691

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1042 QQREALEQAVAKLEQRRSALQ-RCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEmdpARISAYIEEEVQRRLH 1120
Cdd:COG4913    692 EQLEELEAELEELEEELDELKgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELR 768

                          570
                   ....*....|.
gi 1907135714 1121 D-LHRAIGDAN 1130
Cdd:COG4913    769 EnLEERIDALR 779
PTZ00121 PTZ00121
MAEBL; Provisional
 642-1142 8.21e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 8.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSD---KAELERMQQEV---ETRRKETEIVQR--------QIRKQEESLKRRS 707
Cdd:PTZ00121  1252 EEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAkkaEEKKKADEAKKKaeeakkadEAKKKAEEAKKKA 1331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  708 FHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE--QNAQS 785
Cdd:PTZ00121  1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--KKAEEKKKADEAKKKAEEdkKKADE 1409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  786 AKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGgdhtcrDE 862
Cdd:PTZ00121  1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---------EAKKADEAKKKAEEAKkaeEAKKKAEEAKKA------DE 1474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  863 LERAQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDpsflaTDDGNILGGPPDLDKIKTAET 942
Cdd:PTZ00121  1475 AKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEE 1544

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  943 RLQSREHQLQDLLQNhlpalLEEKQRVLDALDSgvlgldttlcQVEKEVGEKEEQIAQyQANASQLQQLRATFE----FT 1018
Cdd:PTZ00121  1545 KKKADELKKAEELKK-----AEEKKKAEEAKKA----------EEDKNMALRKAEEAK-KAEEARIEEVMKLYEeekkMK 1608

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1019 ANVARQEEKVRRKEKEILESQE-----KQQREALEQAVAKLEQRRSALQ----RCSTLDLEIQEQRQKLGSLHTSEWSGW 1089
Cdd:PTZ00121  1609 AEEAKKAEEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907135714 1090 QASLETDGEALEMDPARISAYIEEEVQRRLHDLHRAiGDANHTPADVMKSNEE 1142
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAE 1740
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 640-971 8.91e-06

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: 50.28  E-value: 8.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE---SLKRRSFH 709
Cdd:pfam07888   68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  710 IENKLKDLlaekerfeeerLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqiFQELDRLHQEQNAQSAKLR 789
Cdd:pfam07888  148 RETELERM-----------KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQ 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  790 LEKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELES-----------IREALLQAKEMR--- 852
Cdd:pfam07888  213 DTITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSSmaaqrdrtqaeLHQARLQAAQLTlql 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  853 AGGDHTCRDELERAQQyflefKRRQLVKLASLEKDLVQQ--KDLLSKE--VQEEKVALEHVKCDaggdpsflatddgniL 928
Cdd:pfam07888  289 ADASLALREGRARWAQ-----ERETLQQSAEADKDRIEKlsAELQRLEerLQEERMEREKLEVE---------------L 348

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907135714  929 GGPPDLDKIKTAETRLQSREHQL-QDLLQNHLPALLEEKQRVLD 971
Cdd:pfam07888  349 GREKDCNRVQLSESRRELQELKAsLRVAQKEKEQLQAEKQELLE 392
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 645-903 9.91e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 9.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhienklkdllaeker 723
Cdd:COG4942     26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------------------ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 feeerlreqqgLEQQRRQEEESLFRIREELRK-LQELNSHEQAEKVQIFqeldrLHQEQNAQSAKLRLEKRRLEEEEKEQ 802
Cdd:COG4942     88 -----------LEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  803 VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELERAQQYFLEfKRRQLVKLA 882
Cdd:COG4942    152 AEELRADLAELAALRAEL----EAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAE-LAAELAELQ 219

                          250       260
                   ....*....|....*....|.
gi 1907135714  883 SLEKDLVQQKDLLSKEVQEEK 903
Cdd:COG4942    220 QEAEELEALIARLEAEAAAAA 240
PRK12704 PRK12704
phosphodiesterase; Provisional
 647-774 1.12e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.16  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  647 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEE 726
Cdd:PRK12704    45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK----KEK 117

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907135714  727 ERLREQQGLEQQRRQEEEslfRIREELRKLQELN--SHEQAeKVQIFQEL 774
Cdd:PRK12704   118 ELEQKQQELEKKEEELEE---LIEEQLQELERISglTAEEA-KEILLEKV 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 804-1126 1.16e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA---QQYFLEFKRRQLVK 880
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  881 LASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsfLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLP 960
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  961 ALLEEKQRVLDALDSgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQE 1040
Cdd:TIGR02168  825 RLESLERRIAATERR---------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1041 KQQREALEQAVAKL---EQRRSALQR--------CSTLDLEIQEQRQKLGSLHTSEWSGWQASLEtdgEALEMDPARISA 1109
Cdd:TIGR02168  890 ALLRSELEELSEELrelESKRSELRReleelrekLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDD 966

                          330
                   ....*....|....*..
gi 1907135714 1110 yiEEEVQRRLHDLHRAI 1126
Cdd:TIGR02168  967 --EEEARRRLKRLENKI 981
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
710-1131 1.20e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  710 IENKLKDLLAEKERFEEERLREQQGLEQQRRQ---EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  787 KLRLEKRRLEEEEKEqvQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELE-SIREALLQAKEMRAGGDHTCRDELER 865
Cdd:COG4717    131 YQELEALEAELAELP--ERLEELEERLEELRELE-----EELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  866 AQQYFLEFKRRQLV---KLASLEKDLVQ-QKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGN------------ILG 929
Cdd:COG4717    204 LQQRLAELEEELEEaqeELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlsliltiagvlfLVL 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  930 GPPDLDKIKTAETRLQSREHQLQDLLQNHLPALleEKQRVLDALDSgvLGLDTTLcqVEKEVGEKEEQIAQYQANASQLQ 1009
Cdd:COG4717    284 GLLALLFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAE 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1010 QLRAtfeftanvARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQrqkLGSLHTSEWSGW 1089
Cdd:COG4717    358 ELEE--------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL---LGELEELLEALD 426

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1907135714 1090 QASLETDGEALEMDparisayiEEEVQRRLHDLHRAIGDANH 1131
Cdd:COG4717    427 EEELEEELEELEEE--------LEELEEELEELREELAELEA 460
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 642-910 1.21e-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: 50.36  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEK---------------LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRR 706
Cdd:pfam02463  212 YYQLKEKLELEEeyllyldylklneerIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  707 SFHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHE---QAEKVQIFQELDRLHQEQNA 783
Cdd:pfam02463  292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEikrEAEEEEEEELEKLQEKLEQL 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  784 QSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRAggdhTCRDEL 863
Cdd:pfam02463  372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEK---------EAQLLLELARQLEDLLKEEKKEELEIL----EEEEES 438

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907135714  864 ERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVK 910
Cdd:pfam02463  439 IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 820-1081 1.34e-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: 49.76  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  820 APLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQyflefKRRQLVK-LASLEKDLVQQKDLLsKE 898
Cdd:COG4942     11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-----------ELAALKK-----EEKALLKqLAALERRIAALARRI-RA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  899 VQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSG- 976
Cdd:COG4942     74 LEQELAALEA------------------------ELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPe 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  977 -VLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLE 1055
Cdd:COG4942    130 dFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                          250       260
                   ....*....|....*....|....*.
gi 1907135714 1056 QRRSALQrcstldlEIQEQRQKLGSL 1081
Cdd:COG4942    210 ELAAELA-------ELQQEAEELEAL 228
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 640-1081 1.61e-05

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: 50.17  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLesKRKLIEEMEEKQKsdkaELERMQQEVETRR-----KETEIVQRQIRKQEESLKRRSFHIENK- 713
Cdd:pfam01576  195 RLKKEEKGRQELEKA--KRKLEGESTDLQE----QIAELQAQIAELRaqlakKEEELQAALARLEEETAQKNNALKKIRe 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  714 LKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQ--EQNAQSaklrle 791
Cdd:pfam01576  269 LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKalEEETRS------ 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  792 krrleeeEKEQVQrvahleeQLRKRQDTApllcpgeaqraqeekreLESIREALLQAKEMRAGgdhtcrdeLERAQQYfL 871
Cdd:pfam01576  343 -------HEAQLQ-------EMRQKHTQA-----------------LEELTEQLEQAKRNKAN--------LEKAKQA-L 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  872 EFKRRQLVK----LASLEKDLVQQKDLLSKEVQEEKVAL---EHVKCDAGGDPSFLATDDGNILGGPPDLDK--IKTAEt 942
Cdd:pfam01576  383 ESENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLsesERQRAELAEKLSKLQSELESVSSLLNEAEGknIKLSK- 461

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  943 RLQSREHQLQD---LLQNHLPALLEEKQRvLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATFEFTA 1019
Cdd:pfam01576  462 DVSSLESQLQDtqeLLQEETRQKLNLSTR-LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA---QLSDMKKKLEEDA 537

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135714 1020 NVARQEEKVRRKEKEILESQeKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSL 1081
Cdd:pfam01576  538 GTLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQeLDDLLVDLDHQRQLVSNL 599
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 642-765 1.80e-05

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: 49.74  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetrRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAE 720
Cdd:pfam17380  447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKE 521

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907135714  721 KERFEEERLREQQG--LEQQRR--QEEESLFRIREELRKLQELNSHEQA 765
Cdd:pfam17380  522 MEERQKAIYEEERRreAEEERRkqQEMEERRRIQEQMRKATEERSRLEA 570
PTZ00121 PTZ00121
MAEBL; Provisional
 640-1155 2.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQrEELEKLESKRKLIE-----EMEEKQKSDKAELERMQQEV----ETRRKETEIVQRQIRKQEESLKRRSfhi 710
Cdd:PTZ00121  1165 KAEEARKA-EDAKKAEAARKAEEvrkaeELRKAEDARKAEAARKAEEErkaeEARKAEDAKKAEAVKKAEEAKKDAE--- 1240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  711 enklkdllaEKERFEEERLREQQGLEQQRR-----------QEEESlfRIREELRKLQELNSHEQAEKVQIFQELDRLHQ 779
Cdd:PTZ00121  1241 ---------EAKKAEEERNNEEIRKFEEARmahfarrqaaiKAEEA--RKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  780 -----------EQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQ--------LRKRQDTAPLLCPGEAQRAQEEKRELES 840
Cdd:PTZ00121  1310 kaeeakkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaadeaeaAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  841 IR---EALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQK--DLLSKEVQEEKVAlEHVKCDAGg 915
Cdd:PTZ00121  1390 KKkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKA-EEAKKKAE- 1467

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  916 dpsflatddgnilggppdlDKIKTAETRLQSREHQLQDLLQNHlpalLEEKQRVLDALDSgvlgldttlcQVEKEVGEKE 995
Cdd:PTZ00121  1468 -------------------EAKKADEAKKKAEEAKKADEAKKK----AEEAKKKADEAKK----------AAEAKKKADE 1514

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  996 EQIAQYQANASQLQqlRATFEFTANVARQEEKVR-----RKEKEILESQEKQQreaLEQAVAKLEQRRSALQRCSTLDlE 1070
Cdd:PTZ00121  1515 AKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKkadelKKAEELKKAEEKKK---AEEAKKAEEDKNMALRKAEEAK-K 1588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1071 IQEQRQKLGSLHTSEWSGWQASletdgEALEMDPARISA---YIEEEVQRRLHDLHRAIGDANHTPADVMKSNEELHNGT 1147
Cdd:PTZ00121  1589 AEEARIEEVMKLYEEEKKMKAE-----EAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663


                   ....*...
gi 1907135714 1148 TQRKLKYE 1155
Cdd:PTZ00121  1664 AEEAKKAE 1671
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 648-908 3.67e-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: 48.81  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  648 REELEKLESKRKLIEEMEEK-QKSDKAELERMQQEVETRRKETEIVQRQIRKQEES------LKRRSFHIENKLKDLlae 720
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELeeeyllYLDYLKLNEERIDLL--- 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  721 kerfeeerlreqQGLEQQRRQEEESLFRIRE-ELRKL-QELNSHEQAEKVQIFQELDRLHQEqnAQSAKLRLEKRRLEEE 798
Cdd:pfam02463  243 ------------QELLRDEQEEIESSKQEIEkEEEKLaQVLKENKEEEKEKKLQEEELKLLA--KEEEELKSELLKLERR 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  799 EKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGgdhtcRDELERAQQYFLEFKRRQL 878
Cdd:pfam02463  309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-----QEKLEQLEEELLAKKKLES 383

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907135714  879 VKLASLEKDLVQQKDLLSKEVQEEKVALEH 908
Cdd:pfam02463  384 ERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 738-1117 5.64e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.41  E-value: 5.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  738 QRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRL-----HQEQNAQSAklrlekrrleeeekeqvqrvahlEEQ 812
Cdd:COG3096    279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsaresDLEQDYQAA-----------------------SDH 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  813 LRKRQdtapllcpgEAQRAQEE----KRELESIREALLQAKEMRAGGDH---TCRDELERAQQYFLEFKrrqlVKLASLE 885
Cdd:COG3096    336 LNLVQ---------TALRQQEKieryQEDLEELTERLEEQEEVVEEAAEqlaEAEARLEAAEEEVDSLK----SQLADYQ 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  886 KDL-VQQKDLLskEVQEEKVALEHVKcdaggdpsflatddgnILGGPPDLDkIKTAETRLQSREHQLQDLLQnhlpALLE 964
Cdd:COG3096    403 QALdVQQTRAI--QYQQAVQALEKAR----------------ALCGLPDLT-PENAEDYLAAFRAKEQQATE----EVLE 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  965 EKQRVLDA------------LDSGVLGlDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATF-EFTANVARQEEKVR-- 1029
Cdd:COG3096    460 LEQKLSVAdaarrqfekayeLVCKIAG-EVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERll 538

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1030 -------------RKEKEILESQEKQQREALEQAVAKLEQRRSALQRcsTLDlEIQEQRQKLGSLhTSEWSGWQASLET- 1095
Cdd:COG3096    539 eefcqrigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ--QLE-QLRARIKELAAR-APAWLAAQDALERl 614

                          410       420
                   ....*....|....*....|....*
gi 1907135714 1096 ---DGEALEmDPARISAYIEEEVQR 1117
Cdd:COG3096    615 reqSGEALA-DSQEVTAAMQQLLER 638
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
648-907 5.86e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 5.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  648 REELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEN--KLKDLLAEKE 722
Cdd:PRK03918   227 EKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  723 RFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEEE 799
Cdd:PRK03918   307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----KKKLKELEKRLEELeerHELYEEAKAKKEELERLKKRLT 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  800 KEQVQRVAHLEEQLRKRQDTAPLlcpgEAQRAQEEKRELESIREALLQAKEMRAGGDH---TCRDELEraQQYFLEFKRR 876
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAKGkcpVCGRELT--EEHRKELLEE 456

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907135714  877 QLVKLASLEKDLVQQKDLLSKeVQEEKVALE 907
Cdd:PRK03918   457 YTAELKRIEKELKEIEEKERK-LRKELRELE 486
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 639-705 7.64e-05

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: 47.81  E-value: 7.64e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135714  639 LRLEFERQQREELEKlESKRKLIE-EMEEKQKSDKAELERMQQEvETRRKETEI-----VQRQIRKQEESLKR 705
Cdd:pfam17380  497 LEKELEERKQAMIEE-ERKRKLLEkEMEERQKAIYEEERRREAE-EERRKQQEMeerrrIQEQMRKATEERSR 567
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
646-903 8.57e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  646 QQREELEKLESKRK-LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLlaekerf 724
Cdd:COG4372     10 KARLSLFGLRPKTGiLIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  725 eeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlEKRRLEEEEKEQVQ 804
Cdd:COG4372     83 --------EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREE 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  805 RVAHLEEQLRKRQDTAPLLcpGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASL 884
Cdd:COG4372    151 ELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228

                          250
                   ....*....|....*....
gi 1907135714  885 EKDLVQQKDLLSKEVQEEK 903
Cdd:COG4372    229 AKLGLALSALLDALELEED 247
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 735-1078 8.90e-05

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: 47.43  E-value: 8.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  735 LEQQR-RQEEESLFRIREELRKLQELNSHEQAE---KVQIFQELDRLHQEQNaqsaklrlekrrleeeekEQVQRVaHLE 810
Cdd:pfam17380  296 MEQERlRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERE------------------RELERI-RQE 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  811 EqlRKRQDtapllcpgEAQRAQEEKRELESIREalLQAKEM-RAGGDHTCRDELERAQQYFLEFKRRQlvklaslekdlv 889
Cdd:pfam17380  357 E--RKREL--------ERIRQEEIAMEISRMRE--LERLQMeRQQKNERVRQELEAARKVKILEEERQ------------ 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  890 qqkdllsKEVQEEKVALEHVKCDaggdpsflatddgnilggppdldkiktaetRLQSREHQLQdllqnhlpALLEEKQRV 969
Cdd:pfam17380  413 -------RKIQQQKVEMEQIRAE------------------------------QEEARQREVR--------RLEEERARE 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  970 LDALDSgvlgldttlcqvekevgekeeqiaQYQANASQLQQLRatfeftanvarQEEKVRRKEKEILESQEKQQREAleq 1049
Cdd:pfam17380  448 MERVRL------------------------EEQERQQQVERLR-----------QQEEERKRKKLELEKEKRDRKRA--- 489

                          330       340
                   ....*....|....*....|....*....
gi 1907135714 1050 avakLEQRRSALQRcstldlEIQEQRQKL 1078
Cdd:pfam17380  490 ----EEQRRKILEK------ELEERKQAM 508
Caldesmon pfam02029
Caldesmon;
644-878 9.94e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 47.17  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREEleklESKRKLIEEMEEKQK---------SDKAELERMQQEVETR---RKETEIVQRQIRKQEESLKRRSFHI- 710
Cdd:pfam02029   66 DRTAKRE----ERRQKRLQEALERQKefdptiadeKESVAERKENNEEEENsswEKEEKRDSRLGRYKEEETEIREKEYq 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  711 ENKLKDllaekerfeEERLREQQGLEQQRRQEEESLFR----IREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:pfam02029  142 ENKWST---------EVRQAEEEGEEEEDKSEEAEEVPtenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  787 KLRLEKRRLEEEEKEQVQRVAH---------------LEEQLRKRQDTAPLLCPGEAQRAQEEKRELESI------REAL 845
Cdd:pfam02029  213 EEEVTKLKVTTKRRQGGLSQSQereeeaevfleaeqkLEELRRRRQEKESEEFEKLRQKQQEAELELEELkkkreeRRKL 292

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907135714  846 LQAKEMRaggdhtcRDELERAQQYFLEFKRRQL 878
Cdd:pfam02029  293 LEEEEQR-------RKQEEAERKLREEEEKRRM 318
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 648-1131 1.03e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  648 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF---HIENKLKDLLAEKERF 724
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  725 EEERLREQQGLEQQRRQ----------EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRR 794
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKleqlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  795 L-----EEEEKEQV--QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDH---------- 857
Cdd:TIGR02169  520 IqgvhgTVAQLGSVgeRYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlsilsedgvi 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  858 -------TCRDELERAQQYF---------LEFKRRQL--VKLASLEKDLVQQ-------------KDLLSKEVQEEKVAL 906
Cdd:TIGR02169  600 gfavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRL 679

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  907 EHVKCDAGGDPSFLATDDGNILGGPPDL-DKIKTAETRLQSREHQLQDLLQNH--LPALLEEKQRVLDALDSGVLGLDTT 983
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSE 759

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  984 LCQVEKEVGEKEEQIAQYQA---------NASQLQQLRATFEFT-ANVARQEEKVRRKEKEIleSQEKQQREALEQAVAK 1053
Cdd:TIGR02169  760 LKELEARIEELEEDLHKLEEalndlearlSHSRIPEIQAELSKLeEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQE 837

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1054 LEQRRSALQ-RCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALEMDPARISAYIeEEVQRRLHDLHRAIGDAN 1130
Cdd:TIGR02169  838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQL-RELERKIEELEAQIEKKR 916


                   .
gi 1907135714 1131 H 1131
Cdd:TIGR02169  917 K 917
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 507-585 1.03e-04

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


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 42.97  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  507 LKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLrgSQCS---VNGVQIVDATQLNQGAVILLGrTNM 582
Cdd:cd22673     18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENL--STTNptlVNGKAIEKSAELKDGDVITIG-GRS 91


                   ...
gi 1907135714  583 FRF 585
Cdd:cd22673     92 FRF 94
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
645-910 1.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVetrrKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERF 724
Cdd:PRK03918   175 KRRIERLEKFIKRT---ENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEELEKE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  725 EEERLREQQGLEQQRRQEEESLFRIREELRKLQEL--NSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQ 802
Cdd:PRK03918   247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  803 VQRVAHLEEQLRKRQDTAPLLcpGEAQRAQEE----KRELESIREALLQAKEMRAggDHTCRdELERAQQYFLEFKRRQL 878
Cdd:PRK03918   327 EERIKELEEKEERLEELKKKL--KELEKRLEEleerHELYEEAKAKKEELERLKK--RLTGL-TPEKLEKELEELEKAKE 401

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907135714  879 vKLASLEKDLVQQKDLLSKEVQEEKVALEHVK 910
Cdd:PRK03918   402 -EIEEEISKITARIGELKKEIKELKKAIEELK 432
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 505-589 2.01e-04

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


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 41.86  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  505 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQCS--VNGVQIVDAT-QLNQGAVILLGRTn 581
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDL-GSGNGtlVNGQRVTELGiALRPGDRIELGQT- 86


                   ....*...
gi 1907135714  582 MFRFNHPK 589
Cdd:pfam16697   87 EFCLVPAD 94
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 642-1057 2.27e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 46.28  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRR-----------KETEIVQRQIRKQEESLKRRSFHI 710
Cdd:pfam07111  141 ELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRageakqlaeaqKEAELLRKQLSKTQEELEAQVTLV 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  711 ENklkdlLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQ--------------ELNSHEQAEKVQIFQELDR 776
Cdd:pfam07111  221 ES-----LRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqsltHMLALQEEELTRKIQPSDS 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  777 LHQE--QNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLlcpgeaQRAQEEKRELESIREALLQAK----E 850
Cdd:pfam07111  296 LEPEfpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL------QEQVTSQSQEQAILQRALQDKaaevE 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  851 MRAGGDHTCRDELERAQqyflEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSF-----LATDDG 925
Cdd:pfam07111  370 VERMSAKGLQMELSRAQ----EARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLsnrlsYAVRKV 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  926 NILGGPPdLDKIKTAETRLQS-----REHQLQDLLQNHLPALLEEKQRvLDAldsgVLGLDTTLCQVEKEVGEKEEQIAQ 1000
Cdd:pfam07111  446 HTIKGLM-ARKVALAQLRQEScppppPAPPVDADLSLELEQLREERNR-LDA----ELQLSAHLIQQEVGRAREQGEAER 519

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1001 YQAN--ASQL-QQLRATFEFTANVARQEEKVRRKEKEILES-----QE-KQQRE----ALEQAVAKLEQR 1057
Cdd:pfam07111  520 QQLSevAQQLeQELQRAQESLASVGQQLEVARQGQQESTEEaaslrQElTQQQEiygqALQEKVAEVETR 589
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
641-908 2.37e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  641 LEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrrsfhiENKLKDLLA 719
Cdd:COG4372     68 LEQARSELEQLeEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ--------RKQLEAQIA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  720 EKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKV--QIFQELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:COG4372    140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkEANRNAEKEEELAEAEKLIESLPRELAEE 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  798 EEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 877
Cdd:COG4372    220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907135714  878 LVKLASLEKDLVQQKDLLSKEVQEEKVALEH 908
Cdd:COG4372    300 LLLNLAALSLIGALEDALLAALLELAKKLEL 330
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 639-713 2.68e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 43.12  E-value: 2.68e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714  639 LRLEFERQQREELEKLESKRKliEEMEEKQKsdKAELERmQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 713
Cdd:pfam15346   71 RKEEEERKKREELERILEENN--RKIEEAQR--KEAEER-LAMLEEQRRMKEERQRREKEEEEREKREQQKILNK 140
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
682-1081 2.78e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  682 VETRRKETEIVQRQIRKQEESLKRRSFH-----IENKLKDLLAEKERFEEERLREQQGLEQ---------QRRQEEESL- 746
Cdd:PRK02224   178 VERVLSDQRGSLDQLKAQIEEKEEKDLHerlngLESELAELDEEIERYEEQREQARETRDEadevleeheERREELETLe 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  747 -------------FRIREELRK-----------LQELNSHEQAEkvqifQELDRLHQE--QNAQSAKLRLEKRRLEEEEK 800
Cdd:PRK02224   258 aeiedlretiaetEREREELAEevrdlrerleeLEEERDDLLAE-----AGLDDADAEavEARREELEDRDEELRDRLEE 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  801 EQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFlEFKRRQLVK 880
Cdd:PRK02224   333 CRVAAQAHNEEAESLREDADDL--EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF-GDAPVDLGN 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  881 LASLEKDLVQQKDLLSKEVQEEKVALEHV--------------KCDAGGDPsflatddgniLGGPPDLDKIKTAETRLQS 946
Cdd:PRK02224   410 AEDFLEELREERDELREREAELEATLRTArerveeaealleagKCPECGQP----------VEGSPHVETIEEDRERVEE 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  947 REHQLQDLLQNHlpALLEEKqrvLDALDSGVlgldttlcqvekevgEKEEQIAQYQANASQLQQLRATFEFTANVARQEE 1026
Cdd:PRK02224   480 LEAELEDLEEEV--EEVEER---LERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERA 539

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714 1027 KVRRKEKEILESQEKQQREA-----------------LEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1081
Cdd:PRK02224   540 EELRERAAELEAEAEEKREAaaeaeeeaeeareevaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 639-850 3.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFeRQQREELEKLESKR-----------KLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS 707
Cdd:TIGR02168  815 LNEEA-ANLRERLESLERRIaaterrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  708 FHIENKLKDLlaekerfeeerlreqQGLEQQRRQEEESLFRIREELRKLQElnsHEQAEKVQIFQELDRLHQEQNAQSAK 787
Cdd:TIGR02168  894 SELEELSEEL---------------RELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEE 955

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135714  788 LRLEKRRLEEEEKEQVQRVAHLEEQLrKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 850
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKI-KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 641-1051 3.65e-04

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: 45.55  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  641 LEFERQQREELEKLesKRKLIEEMEekqkSDKAELE------RMQQEVETRRkETEIVQRQIRKQEES---------LKR 705
Cdd:pfam01576  280 LESERAARNKAEKQ--RRDLGEELE----ALKTELEdtldttAAQQELRSKR-EQEVTELKKALEEETrsheaqlqeMRQ 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  706 RSFHIENKLKDLLAEKERFEEERLREQQGLE-------------QQRRQEEESlfRIREELRKLQELNS-HEQAEKVQif 771
Cdd:pfam01576  353 KHTQALEELTEQLEQAKRNKANLEKAKQALEsenaelqaelrtlQQAKQDSEH--KRKKLEGQLQELQArLSESERQR-- 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  772 QEL-DRLHQEQNAQSAKLRLEKRRLEEEEKEQvQRVAHLEEQLrkrQDTAPLLcpgeaqraQEEKRE----------LES 840
Cdd:pfam01576  429 AELaEKLSKLQSELESVSSLLNEAEGKNIKLS-KDVSSLESQL---QDTQELL--------QEETRQklnlstrlrqLED 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  841 IREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHvKCDAggdpsfl 920
Cdd:pfam01576  497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEE-KAAA------- 567

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  921 atddgnilggppdLDKIKTAETRLQsreHQLQDLL-----QNHLPALLEEKQRVLDALdsgvlgldttlcqvekevgeke 995
Cdd:pfam01576  568 -------------YDKLEKTKNRLQ---QELDDLLvdldhQRQLVSNLEKKQKKFDQM---------------------- 609

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135714  996 eqIAQYQANASQLQQLRATFEFTA--------NVARQEEKVRRKEKEiLESQEKQQREALEQAV 1051
Cdd:pfam01576  610 --LAEEKAISARYAEERDRAEAEAreketralSLARALEEALEAKEE-LERTNKQLRAEMEDLV 670
mukB PRK04863
chromosome partition protein MukB;
640-895 5.34e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEK----LESKRKLIEEMEE---KQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-FHIE 711
Cdd:PRK04863   895 RVEEIREQLDEAEEakrfVQQHGNALAQLEPivsVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhFSYE 974

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  712 NKLKDLlaekerfeEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNaqsaklrle 791
Cdd:PRK04863   975 DAAEML--------AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA----QLAQYNQVLASLKSSYDAKR--------- 1033

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  792 krrleeeekeqvQRVAHLEEQLrkrQDTAPLLCPGEAQRAQEEKRELesirEALLQAKEMRaggdhtcRDELERaQQYFL 871
Cdd:PRK04863  1034 ------------QMLQELKQEL---QDLGVPADSGAEERARARRDEL----HARLSANRSR-------RNQLEK-QLTFC 1086

                          250       260
                   ....*....|....*....|....*
gi 1907135714  872 EFKRRQLVK-LASLEKDLVQQKDLL 895
Cdd:PRK04863  1087 EAEMDNLTKkLRKLERDYHEMREQV 1111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1128 5.52e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 5.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIrKQEESLKRRSFHIENKLKDL-- 717
Cdd:PRK03918   274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKLKELek 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  718 -LAEKERFEEERLREQQGLEQQRRQEEESLFRIREEL-RKLQELnsheQAEKVQIFQELDRLHQEQNAQSaklrlekrrl 795
Cdd:PRK03918   353 rLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLeKELEEL----EKAKEEIEEEISKITARIGELK---------- 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  796 eeeekeqvQRVAHLE---EQLRKRQDTAPlLCpgeaQRAQEEKRELESIREALLQAKEMRAggdhtcrdELERAQQYFLE 872
Cdd:PRK03918   419 --------KEIKELKkaiEELKKAKGKCP-VC----GRELTEEHRKELLEEYTAELKRIEK--------ELKEIEEKERK 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  873 FKRR--QLVKLASLEKDLVQQKDLLS--KEVQEE--KVALEHVKCDAG---GDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:PRK03918   478 LRKElrELEKVLKKESELIKLKELAEqlKELEEKlkKYNLEELEKKAEeyeKLKEKLIKLKGEIKSLKKELEKLEELKKK 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  944 LQSREHQLQDllqnhlpaLLEEKQRVLDALDSgvLGLDTtlcqvekevgekeeqiaqYQANASQLQQLRATFE--FTANV 1021
Cdd:PRK03918   558 LAELEKKLDE--------LEEELAELLKELEE--LGFES------------------VEELEERLKELEPFYNeyLELKD 609

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1022 ARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTL--DLEIQEQRQKLGSLhTSEWSGWQASLETDGEA 1099
Cdd:PRK03918   610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLEL-SRELAGLRAELEELEKR 688

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1907135714 1100 LEmdpaRISAYIE---------EEVQRRLHDLHRAIGD 1128
Cdd:PRK03918   689 RE----EIKKTLEklkeeleerEKAKKELEKLEKALER 722
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 645-744 7.73e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 44.36  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQevetrRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerf 724
Cdd:pfam09731  319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFE-----REREEIRESYEEKLRTELERQAEAHEEHLKDVLV----- 386

                           90       100
                   ....*....|....*....|
gi 1907135714  725 eeerlreQQGLEQQRRQEEE 744
Cdd:pfam09731  387 -------EQEIELQREFLQD 399
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 740-1061 8.01e-04

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: 44.40  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  740 RQEEESLFRiREELRKLQElnSHEQAEKVqiFQELDRLHQEQNAQSAKlrlekrrleeeekeqvqrvahLEEQLrkrQDT 819
Cdd:pfam01576    2 RQEEEMQAK-EEELQKVKE--RQQKAESE--LKELEKKHQQLCEEKNA---------------------LQEQL---QAE 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  820 APLLCPGEAQRAQ--EEKRELESIrealLQAKEMRAGgdhtcrDELERAQQYFLEFKRRQlVKLASLEKDLVQQKDLLSK 897
Cdd:pfam01576   53 TELCAEAEEMRARlaARKQELEEI----LHELESRLE------EEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQK 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  898 eVQEEKVALEhVKCDAGGDPSFLATDDGNILGGPPDL--DKIKTAETRLQSREHQLQDL--LQNHLPALLEEKQRVLDAL 973
Cdd:pfam01576  122 -LQLEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLleERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKKE 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  974 DSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATF-----EFTANVARQEE----------KVRRKEKEILES 1038
Cdd:pfam01576  200 EKGRQELEKAKRKLEGESTDLQEQIAELQA---QIAELRAQLakkeeELQAALARLEEetaqknnalkKIRELEAQISEL 276

                          330       340
                   ....*....|....*....|...
gi 1907135714 1039 QEKQQREalEQAVAKLEQRRSAL 1061
Cdd:pfam01576  277 QEDLESE--RAARNKAEKQRRDL 297
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 512-577 9.16e-04

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 39.48  E-value: 9.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135714  512 TYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQ-CSVNGVQI-VDATQLNQGAVILL 577
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNgTFVNGQRLgPEPVRLKDGDVIRL 66
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 736-1063 9.63e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.49  E-value: 9.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  736 EQQRRQEEEslFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRV--------- 806
Cdd:pfam15558   35 EELRRRDQK--RQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQenqrqekle 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  807 -AHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREA---LLQAKEMRAggdhtCRDELERAQQyflEFKRRQLVKLA 882
Cdd:pfam15558  113 rARQEAEQRKQC---------QEQRLKEKEEELQALREQnslQLQERLEEA-----CHKRQLKERE---EQKKVQENNLS 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  883 SLEKDLVQQKDLLSKEVQEE---KVALEHvkcdaggdpSFLATDDgnilgGPPDLDKIKTAETRLQSREHQLQdLLQNHL 959
Cdd:pfam15558  176 ELLNHQARKVLVDCQAKAEEllrRLSLEQ---------SLQRSQE-----NYEQLVEERHRELREKAQKEEEQ-FQRAKW 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  960 PALLEEKQRV--LDALdsgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARqeEKVRRKEKEILE 1037
Cdd:pfam15558  241 RAEEKEEERQehKEAL-----------------AELADRKIQQARQVAHKTVQDKAQRARELNLER--EKNHHILKLKVE 301

                          330       340
                   ....*....|....*....|....*.
gi 1907135714 1038 SQEKQQREALEQAVAKLEQRRSALQR 1063
Cdd:pfam15558  302 KEEKCHREGIKEAIKKKEQRSEQISR 327
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
644-984 1.08e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETRRKETEIVQRQIRKQEeslkrrsfhienKLKDLLAEKER 723
Cdd:COG3064     11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifQELDRLHQEQNAQSAklrLEKRRLEEEEKEQV 803
Cdd:COG3064     78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKA---EEAKRKAEEEAKRKA---EEERKAAEAEAAAK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG3064    152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  884 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALL 963
Cdd:COG3064    232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311

                          330       340
                   ....*....|....*....|.
gi 1907135714  964 EEKQRVLDALDSGVLGLDTTL 984
Cdd:COG3064    312 AAEEAVLAAAAAAGALVVRGG 332
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 649-1158 1.15e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.06  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  649 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrqirKQEESLKRRSFHIENKLKDLLAEKERFEEER 728
Cdd:pfam12128  461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQA 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  729 LREQQGLEQQRRQEEESLFR-IREELrkLQELNSHEQAEKVQIFQELD----RLHQEQnaqsaklrlekrrleeeekEQV 803
Cdd:pfam12128  534 GTLLHFLRKEAPDWEQSIGKvISPEL--LHRTDLDPEVWDGSVGGELNlygvKLDLKR-------------------IDV 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL--LQAKEMRAGgdHTCRDELERAQQYFLEFKRRQLvkl 881
Cdd:pfam12128  593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELekASREETFAR--TALKNARLDLRRLFDEKQSEKD--- 667

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  882 aSLEKDLVQQKDLLSKEVQE---EKVALEHvkcdagGDPSFLatddgnilggppdldkiktAETRLQSREHQLQdlLQNH 958
Cdd:pfam12128  668 -KKNKALAERKDSANERLNSleaQLKQLDK------KHQAWL-------------------EEQKEQKREARTE--KQAY 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  959 LPALLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeqiaQYQANASQLQQLRATfeFTANVARQEEKVRRKEKEILES 1038
Cdd:pfam12128  720 WQVVEGALDAQLALLKAAIAARRS-----------------GAKAELKALETWYKR--DLASLGVDPDVIAKLKREIRTL 780

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1039 QEKQQR-EALEQAVAKLEQ--------RRSALQ-RCSTLDLEIQEQRQKLGSLhTSEWSGWQASLETDGEALEMDPARIS 1108
Cdd:pfam12128  781 ERKIERiAVRRQEVLRYFDwyqetwlqRRPRLAtQLSNIERAISELQQQLARL-IADTKLRRAKLEMERKASEKQQVRLS 859

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907135714 1109 AYIE--EEVQRRLHDLHRAIGD--ANHTPADVMKSNEELhngttQRKLKYETGQ 1158
Cdd:pfam12128  860 ENLRglRCEMSKLATLKEDANSeqAQGSIGERLAQLEDL-----KLKRDYLSES 908
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 486-588 1.32e-03

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 40.17  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  486 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFE-------NAGGTVTLIPLRGSQCSV 558
Cdd:cd22733      4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907135714  559 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22733     84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
PRK12704 PRK12704
phosphodiesterase; Provisional
 646-719 1.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 1.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714  646 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:PRK12704    68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 639-1043 1.36e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQ--EVETRR-----KETEIVQRQIR---KQEESLKRRSF 708
Cdd:pfam10174  350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERKinvlqKKIENLQEQLRdkdKQLAGLKERVK 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  709 HIEN----------KLKDLLAEKERFEEERLREQQGLEQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRL- 777
Cdd:pfam10174  426 SLQTdssntdtaltTLEEALSEKERIIERLKEQREREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDLk 502

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  778 -HQEQNAQSAKLRLEKRRLEEEEKEQ-VQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQAKEMRAGg 855
Cdd:pfam10174  503 eHASSLASSGLKKDSKLKSLEIAVEQkKEECSKLENQLKKAHNAE------EAVRTNPEINDRIRLLEQEVARYKEESG- 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  856 dhTCRDELERaqqyflefkrrqlvkLASLEKDLVQQKDLLSKEVQE-EKVALEHVKCdaggdpsfLATDDGNILGGPPDL 934
Cdd:pfam10174  576 --KAQAEVER---------------LLGILREVENEKNDKDKKIAElESLTLRQMKE--------QNKKVANIKHGQQEM 630

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  935 DKIKTAETRLQSREHqlQDLLQNHLPALLEEkqrVLDALDSGVLGLDTTlcqvekevgekeeqiaqyQANASQLQQLRAT 1014
Cdd:pfam10174  631 KKKGAQLLEEARRRE--DNLADNSQQLQLEE---LMGALEKTRQELDAT------------------KARLSSTQQSLAE 687

                          410       420       430
                   ....*....|....*....|....*....|
gi 1907135714 1015 FEFTANVARQEekvRRKE-KEILESqeKQQ 1043
Cdd:pfam10174  688 KDGHLTNLRAE---RRKQlEEILEM--KQE 712
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 633-907 1.41e-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: 43.56  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  633 IKGPICLRLEFERQQREELEKLESKRKLIeEMEEKQKSdkAELERMQQEVETRRKETEIVQRQIRKQEESLKrrsfhiEN 712
Cdd:pfam05483  354 FEATTCSLEELLRTEQQRLEKNEDQLKII-TMELQKKS--SELEEMTKFKNNKEVELEELKKILAEDEKLLD------EK 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  713 KLKDLLAEKERFEEERLReqqGLEQQRRQEEESL------FRIREE--LRKLQELNSHEQAEK---VQIFQELDRLHQEq 781
Cdd:pfam05483  425 KQFEKIAEELKGKEQELI---FLLQAREKEIHDLeiqltaIKTSEEhyLKEVEDLKTELEKEKlknIELTAHCDKLLLE- 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  782 NAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgeAQRAQEEKRELESIREALLQAK-EMRAGGDHTcr 860
Cdd:pfam05483  501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL-------EEKEMNLRDELESVREEFIQKGdEVKCKLDKS-- 571

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907135714  861 DELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSK---EVQEEKVALE 907
Cdd:pfam05483  572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALK 621
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 644-832 1.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK---------- 713
Cdd:COG3883     29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvl 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  714 -----LKDLLAEKERFEEERLREQQGLEQQRRQeeeslfriREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 788
Cdd:COG3883    109 lgsesFSDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907135714  789 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 832
Cdd:COG3883    181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
PRK11637 PRK11637
AmiB activator; Provisional
 1002-1085 1.80e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1002 QANASQLQQLRAtfEFTANVARQEEKvRRKEKEILESQEKQQrealeqavAKLEQRRSALQRC-STLDLEIQEQRQKLGS 1080
Cdd:PRK11637   169 QETIAELKQTRE--ELAAQKAELEEK-QSQQKTLLYEQQAQQ--------QKLEQARNERKKTlTGLESSLQKDQQQLSE 237


                   ....*
gi 1907135714 1081 LHTSE 1085
Cdd:PRK11637   238 LRANE 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
640-1063 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQ-REELEKLESKRKLIEEMEEKQKsdkaELERMQQEVETRRKETEIVqRQIRKQEESLKRR--SFHIEnKLKD 716
Cdd:PRK03918   318 RLEEEINGiEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA-KAKKEELERLKKRltGLTPE-KLEK 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  717 LLAEKERFEEERLREQQGLEQQR---RQEEESLFRIREELRKLQ--------ELNSHEQAEKVQIF-QELDRLHQEqnaq 784
Cdd:PRK03918   392 ELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKELLEEYtAELKRIEKE---- 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  785 saklrlekrrleeeekeqVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELE 864
Cdd:PRK03918   468 ------------------LKEIEEKERKLRKELR--------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  865 RAQQYFLEFKRRqLVKL----ASLEKDLVQQKDLLSK---------EVQEEKVALEHVKCDAGgdpsFLATDDGN----- 926
Cdd:PRK03918   522 KKAEEYEKLKEK-LIKLkgeiKSLKKELEKLEELKKKlaelekkldELEEELAELLKELEELG----FESVEELEerlke 596

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  927 ----------ILGGPPDL------------------DKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVL 978
Cdd:PRK03918   597 lepfyneyleLKDAEKELereekelkkleeeldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  979 GLDttlcqvekevgekeeqiAQYQANASQLQQLRATFEftaNVARQEEKVRRKEKEIlesqekqqrEALEQAVAKLEQRR 1058
Cdd:PRK03918   677 GLR-----------------AELEELEKRREEIKKTLE---KLKEELEEREKAKKEL---------EKLEKALERVEELR 727


                   ....*
gi 1907135714 1059 SALQR 1063
Cdd:PRK03918   728 EKVKK 732
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 639-773 1.86e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.21  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFERQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVETRRKEteivqRQIRKQEESLKRRSFHIENKLKDLL 718
Cdd:pfam11600   16 QRLEKDKERLRRQLKLEAEK---EEKERLKEEAKAEKERAKEEARRKKEE-----EKELKEKERREKKEKDEKEKAEKLR 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714  719 AEKERFEEERLREQQGLEQQRRQEEESlfRIREELRKLQElnshEQAEKVQIFQE 773
Cdd:pfam11600   88 LKEEKRKEKQEALEAKLEEKRKKEEEK--RLKEEEKRIKA----EKAEITRFLQK 136
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 639-784 1.91e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.02  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  639 LRLEFERQQREELEKLESKRKLIEEMEEKQksdkaELERMQQEvETRRKeteIVQRQIRKQEESLKRRSFHiENKLKDL- 717
Cdd:pfam15709  389 IRLRKQRLEEERQRQEEEERKQRLQLQAAQ-----ERARQQQE-EFRRK---LQELQRKKQQEEAERAEAE-KQRQKELe 458

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135714  718 --LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVqIFQELDRLHQEQNAQ 784
Cdd:pfam15709  459 mqLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARL-ALEEAMKQAQEQARQ 522
PRK12704 PRK12704
phosphodiesterase; Provisional
 832-1066 2.17e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  832 QEEKRELESI-REALLQAKEMRaggdHTCRDELERaqqyflEFKRRQlVKLASLEKDLVQQKDLLSKEvqeekvalehvk 910
Cdd:PRK12704    45 EEAKKEAEAIkKEALLEAKEEI----HKLRNEFEK------ELRERR-NELQKLEKRLLQKEENLDRK------------ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  911 cdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhlpalLEEKQRVLDALdsgvlgldttlcqvEKE 990
Cdd:PRK12704   102 -----------------------LELLEKREEELEKKEKELEQKQQE-----LEKKEEELEEL--------------IEE 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  991 VGEKEEQIAQY---QANASQLQQLRATfeftanvARQE--EKVRRKEKEILESQEKQQREALEQAVakleqrrsalQRCS 1065
Cdd:PRK12704   140 QLQELERISGLtaeEAKEILLEKVEEE-------ARHEaaVLIKEIEEEAKEEADKKAKEILAQAI----------QRCA 202


                   .
gi 1907135714 1066 T 1066
Cdd:PRK12704   203 A 203
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 644-704 2.27e-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: 41.83  E-value: 2.27e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135714  644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 704
Cdd:COG1579    109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 645-719 2.31e-03

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 39.97  E-value: 2.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135714  645 RQQREELEKLESKRKLIEEM-EEKQKSDKAELERMQ-QEVETRRKETEIVQRQIRKQEESLKR-RSFHIENKLKDLLA 719
Cdd:pfam04696   22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKrEEREELFEERRAEQIELRALEEKLELkELMETWHENLKALA 99
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 736-1093 2.75e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  736 EQQRRQEEESLFRIREELRKLQElNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRK 815
Cdd:pfam12128  216 SRLNRQQVEHWIRDIQAIAGIMK-IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  816 RQDTApllcpgeAQRAQEEKRELESIREALLQakemraggdhtCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLL 895
Cdd:pfam12128  295 LDDQW-------KEKRDELNGELSAADAAVAK-----------DRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  896 SkEVQEEKVALE--HVKCDAGGDPSFLATDDGN---ILGGPPDLDKIKTAETR--------LQSREHQLQDLLQNHLPAL 962
Cdd:pfam12128  357 E-NLEERLKALTgkHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEF 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  963 LEEKQRVLDALdsgvlgldttlcqvekevGEKEEQIAQYQANASQLQQLRAtFEFTANVARQEEKVRRKEKEILESQEKQ 1042
Cdd:pfam12128  436 NEEEYRLKSRL------------------GELKLRLNQATATPELLLQLEN-FDERIERAREEQEAANAEVERLQSELRQ 496

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907135714 1043 QREALEQAVAKLEQRRSALQRCSTLDLEIQEQ-RQKLGSLH---TSEWSGWQASL 1093
Cdd:pfam12128  497 ARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLhflRKEAPDWEQSI 551
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 645-745 2.92e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 724
Cdd:COG3883    136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215

                           90       100
                   ....*....|....*....|.
gi 1907135714  725 EEERLREQQGLEQQRRQEEES 745
Cdd:COG3883    216 AAAAAAAAAAAAAAAAAAAAA 236
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 640-773 3.14e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.03  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELER-MQQEV-ETRRKETEIvqRQIRKQ-EESLKRRSFHIEnklkd 716
Cdd:pfam15346   23 RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEReREAELeEERRKEEEE--RKKREElERILEENNRKIE----- 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135714  717 llaekerfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQE 773
Cdd:pfam15346   96 -------------------EAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 640-907 3.20e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.25  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrRSFHIENKLKDL 717
Cdd:COG5185    254 KLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  718 LAEKERFEEERlreQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvQIFQELD-------RLHQEQNAQSAKLRL 790
Cdd:COG5185    331 KRETETGIQNL---TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-ELDSFKDtiestkeSLDEIPQNQRGYAQE 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  791 EKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREallqaKEMRAGGDhtcrDELERAQQYF 870
Cdd:COG5185    407 ILATLEDTLKAADRQIEELQRQIEQATS--------SNEEVSKLLNELISELN-----KVMREADE----ESQSRLEEAY 469

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1907135714  871 LEFKRRQLVKLASLEKDLVQ---QKDLLSKEVQEEKVALE 907
Cdd:COG5185    470 DEINRSVRSKKEDLNEELTQiesRVSTLKATLEKLRAKLE 509
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 641-706 3.22e-03

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 41.51  E-value: 3.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714  641 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETRRKETEivqRQIRKQEESLKRR 706
Cdd:pfam12037   76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 638-886 3.46e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  638 CLRLEFERQQREELEKLESKRKLIEEMEE--KQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENKL 714
Cdd:pfam13868  106 IVERIQEEDQAEAEEKLEKQRQLREEIDEfnEEQAEWKELEKEEEREEDERILEYLKEKAEREEErEAEREEIEEEKERE 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  715 KDLLAEkerfeeerlreQQGLEQQRRQEEESLF--RIREELRKLQELNSHEQAEK-VQIFQELDRLHQEQNAQSAKLRLE 791
Cdd:pfam13868  186 IARLRA-----------QQEKAQDEKAERDELRakLYQEEQERKERQKEREEAEKkARQRQELQQAREEQIELKERRLAE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  792 KRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELES-IREALLQAKEMRAggdhtcRDELERAQQYF 870
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKqIEEREEQRAAERE------EELEEGERLRE 322

                          250
                   ....*....|....*.
gi 1907135714  871 LEFKRRQLVKLASLEK 886
Cdd:pfam13868  323 EEAERRERIEEERQKK 338
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 645-745 3.50e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 724
Cdd:COG3883    129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208

                           90       100
                   ....*....|....*....|.
gi 1907135714  725 EEERLREQQGLEQQRRQEEES 745
Cdd:COG3883    209 EAAAAAAAAAAAAAAAAAAAA 229
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
645-780 3.59e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLLAEk 721
Cdd:COG1340     95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135714  722 erfeeerlreqqgLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQELDRLHQE 780
Cdd:COG1340    169 -------------LKELRKEAEE----IHKKIKELAEEAQELHEEMIELYKEADELRKE 210
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
645-847 4.13e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQREELEKLESKRKLIEE--MEEKQKSDK-AELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLL 718
Cdd:COG1340     88 NELREELDELRKELAELNKagGSIDKLRKEiERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELR 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  719 AEKERFEEERLREQQGLE------QQRRQEEESLFRIREELRKlqELNS-HEQAekVQIFQELDRLHQEQNAQSaklrle 791
Cdd:COG1340    167 AELKELRKEAEEIHKKIKelaeeaQELHEEMIELYKEADELRK--EADElHKEI--VEAQEKADELHEEIIELQ------ 236

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907135714  792 krrleeeekeqvQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQ 847
Cdd:COG1340    237 ------------KELRELRKELKKLRKKQ------RALKREKEKEELEEKAEEIFE 274
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 645-781 6.21e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 39.08  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  645 RQQRE--ELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDllaeke 722
Cdd:pfam12474    6 EQQKDrfEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRAEQKKRLKMFRESLKQEKKELK------ 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714  723 rfeeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHE---QAEKVQIFQELDRLHQEQ 781
Cdd:pfam12474   80 ----------QEVEKLPKFQRKEAKRQRKEELELEQKHEELeflQAQSEALERELQQLQNEK 131
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 610-1078 7.34e-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: 41.25  E-value: 7.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  610 MTDLSKSCENL-SAVMLYNPGLFPIKGPICLRLEFERQQ---------REELEKLESkrKLIEEMEEKQK---SDKAELE 676
Cdd:pfam05483   25 KSNLSKNGENIdSDPAFQKLNFLPMLEQVANSGDCHYQEglkdsdfenSEGLSRLYS--KLYKEAEKIKKwkvSIEAELK 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  677 RMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKL---KDLL----AEKERFEEERLREQQGLEQQRRQEEEslfri 749
Cdd:pfam05483  103 QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIqenKDLIkennATRHLCNLLKETCARSAEKTKKYEYE----- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  750 REELRKL-QELNSHEQaEKVQIFQELdRLhQEQNAQsaklrlekRRLEEEEKEQVQRVAHLEEQLRK----RQDTAPLLC 824
Cdd:pfam05483  178 REETRQVyMDLNNNIE-KMILAFEEL-RV-QAENAR--------LEMHFKLKEDHEKIQHLEEEYKKeindKEKQVSLLL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  825 PGEAQRAQEEKR---ELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFK------RRQLVKLASLEKDLVQQKDLL 895
Cdd:pfam05483  247 IQITEKENKMKDltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKTI 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  896 SKEVQEEKVALEHVKcDAGGDPSFLATDDGNILGGPPDLdkIKTAETRLQSREHQLQDL---LQNHLPALLE------EK 966
Cdd:pfam05483  327 CQLTEEKEAQMEELN-KAKAAHSFVVTEFEATTCSLEEL--LRTEQQRLEKNEDQLKIItmeLQKKSSELEEmtkfknNK 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  967 QRVLDALDSgVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAT----FEFTANVARQEEKVRRKEKEILESQ--- 1039
Cdd:pfam05483  404 EVELEELKK-ILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdLEIQLTAIKTSEEHYLKEVEDLKTElek 482

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1907135714 1040 EKQQREALEQAVAKLE-QRRSALQRCSTLDLEIQEQRQKL 1078
Cdd:pfam05483  483 EKLKNIELTAHCDKLLlENKELTQEASDMTLELKKHQEDI 522
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 640-1057 7.55e-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: 41.03  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  640 RLEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLL 718
Cdd:pfam07888   35 RLEECLQERAELlQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  719 AEKERFEEERLREQQ----------GLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQI-----------------F 771
Cdd:pfam07888  115 EEKDALLAQRAAHEArireleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqaklqqteeelrslskeF 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  772 QELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELESireallqa 848
Cdd:pfam07888  195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSS-------- 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  849 keMRAGGDHTcRDELERAQqyfLEFKRRQLvKLASLEKDLVQQKDLLSKEVQEEKVALEhvkcdaggdpsflatddgnil 928
Cdd:pfam07888  263 --MAAQRDRT-QAELHQAR---LQAAQLTL-QLADASLALREGRARWAQERETLQQSAE--------------------- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  929 ggpPDLDKIKTAETRLQSREHQLQDllqnhlpallEEKQRVldaldsgvlGLDTTLCQVEKEVGekeeqiAQYQANASQL 1008
Cdd:pfam07888  315 ---ADKDRIEKLSAELQRLEERLQE----------ERMERE---------KLEVELGREKDCNR------VQLSESRREL 366

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1907135714 1009 QQLRATFeftanvarqeeKVRRKEKEILESqEKQQreaLEQAVAKLEQR 1057
Cdd:pfam07888  367 QELKASL-----------RVAQKEKEQLQA-EKQE---LLEYIRQLEQR 400
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
933-1126 7.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  933 DLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSGVlgldtTLCQVEKEVGEKEEQIAQYQANASQLQQL 1011
Cdd:COG4913    236 DLERAHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAAL-----RLWFAQRRLELLEAELEELRAELARLEAE 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714 1012 RATFEftANVARQEEKVRRKEKEILES------QEKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSLHtS 1084
Cdd:COG4913    311 LERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEAlLAALGLPLPASAEEFAALR-A 387

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907135714 1085 EWSGWQASLETDGEALEMDPARISAyIEEEVQRRLHDLHRAI 1126
Cdd:COG4913    388 EAAALLEALEEELEALEEALAEAEA-ALRDLRRELRELEAEI 428
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 642-852 9.36e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 9.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  642 EFERQQREELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFH-----IENK 713
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELEEDLSSleqEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAE 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135714  714 LKDLLAEKERFEEERLREQQGLeQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRLH---QEQNAQSAKLRL 790
Cdd:TIGR02169  800 LSKLEEEVSRIEARLREIEQKL-NRLTLEKEYL---EKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEA 875

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135714  791 EKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESIREALLQAKEMR 852
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKI-----EELEAQIEKKRKRLSELKAKLEALEEE 932
 
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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