START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4038 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 4117
Cdd:cd08874      1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4118 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 4197
Cdd:cd08874     81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907142925 4198 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 4242
Cdd:cd08874    161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVN 35
Cdd:cd01365    327 MIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4038 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 4117
Cdd:cd08874      1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4118 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 4197
Cdd:cd08874     81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907142925 4198 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 4242
Cdd:cd08874    161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVN 35
Cdd:cd01365    327 MIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361

kinesin-12 family protein; Provisional

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNE----DANV--KLIRELREEIERLKA 55
Cdd:PLN03188   407 MVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVKA 467

Kinesin-like protein [Cytoskeleton];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNEDANVKL--------IRELREEIERLKA----VLLNFELRNFSSL 68
Cdd:COG5059    309 VICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFreqsQLSQSSLSGIFAY 388

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907142925   69 NDDLDESLQELVFQSDLKIDTLTQHWTEKRNDRQALMEHYGVDINRKR 116
Cdd:COG5059    389 MQSLKKETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLR 436

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  143 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCT-VNGREVTASCRLTQgrdyglnsgwcv 221
Cdd:COG1716     16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTfVNGQRVTEPAPLRD------------ 80

                           90
                   ....*....|....*
gi 1907142925  222 tGAVITLGKaQKFRF 236
Cdd:COG1716     81 -GDVIRLGK-TELRF 93

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4038 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 4117
Cdd:cd08874      1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925 4118 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 4197
Cdd:cd08874     81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907142925 4198 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 4242
Cdd:cd08874    161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  119 VVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCTVNG 198
Cdd:cd22708      2 VVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVNG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907142925  199 REVTASCRLTQgrdyglnsgwcvtGAVITLGKAQKFRFNHP 239
Cdd:cd22708     82 QVITQPTRLTQ-------------GDVILLGKTNMFRFNHP 109

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  125 LPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCTVNGREVTAS 204
Cdd:cd22705      1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907142925  205 CRLTqgrdyglnsgwcvTGAVITLGKAQKFRFNH 238
Cdd:cd22705     81 TRLK-------------TGSRVILGKNHVFRFNH 101

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  126 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCG-----VVILRPTQGARCTVNGRE 200
Cdd:cd22726      2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRsggeaVVTLEPCEGADTYVNGKK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907142925  201 VTASCRLTQGRDyglnsgwcvtgavITLGKAQKFRFNHPAEAavlRHQR 249
Cdd:cd22726     82 VTEPSILRSGNR-------------IIMGKSHVFRFNHPEQA---RQER 114

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  126 PHLMAL-EDDVLStGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRP-TQGARCTVNGREVTA 203
Cdd:cd22709      1 PHLLNLnEDPQLS-GVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPvSPGAKVIVNGVPVTG 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907142925  204 SCRLTQG-RdyglnsgwcvtgavITLGKAQKFRFNHP 239
Cdd:cd22709     80 ETELHHLdR--------------VILGSNHLYVFVGP 102

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  126 PHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITS---TCGVVI--LRPTQGARCTVNGRE 200
Cdd:cd22727      3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSernNNGEVIvtLEPCERSETYVNGKR 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907142925  201 VTASCRLTQGRDyglnsgwcvtgavITLGKAQKFRFNHPAE 241
Cdd:cd22727     83 VVQPVQLRSGNR-------------IIMGKNHVFRFNHPEQ 110

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  143 YHLKEgTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCTVNGREVTASCRLTQG-Rdyglnsgwcv 221
Cdd:cd22706     19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGdR---------- 87

                           90
                   ....*....|....*...
gi 1907142925  222 tgavITLGKAQKFRFNHP 239
Cdd:cd22706     88 ----ILWGNNHFFRLNCP 101

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.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNED 37
Cdd:cd01364    317 IIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  143 YHLKEGTTKIGRidsDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCT-VNGREVTASCRLTQgrdyglnsgwcv 221
Cdd:cd00060     14 FPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTfVNGKRITPPVPLQD------------ 78

                           90
                   ....*....|....*
gi 1907142925  222 tGAVITLGKAQkFRF 236
Cdd:cd00060     79 -GDVIRLGDTT-FRF 91

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  125 LPHLMALEDDVLSTG-VVLYHLKEGTTKIG--RIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQG-ARCTVNGRE 200
Cdd:cd22711      1 LPYLLELSPDGSDRDkPRRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYVNGQR 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907142925  201 VtasCRLTQgrdygLNSgwcvtGAVITLGKAQKFRFNHP 239
Cdd:cd22711     81 I---YETTM-----LQH-----GMVVQFGRSHTFRFCDP 106

Kinesin-associated;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925   34 VNEDANVKLIRELREEIERLKAVLL---------NFELRNFSSLNDDLDE----------------------------SL 76
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLYaqglgdiidTIAHPTKKRANTPAANasaataamagaspspslsalssraasvsSL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925   77 QELVFQSD--------LK-----IDTLTQHWTEK-------RNDRQALMEHYGVDINRKRARVVIDS--SLPHLMALEDD 134
Cdd:pfam16183   83 HERIMFTPgseeaierLKetekiIAELNETWEEKlrkteaiRMEREALLAEMGVAIREDGGTLGVFSpkKTPHLVNLNED 162

                          170
                   ....*....|....
gi 1907142925  135 VLSTGVVLYHLKEG 148
Cdd:pfam16183  163 PLMSECLLYYIKDG 176

Kinesin-like protein [Cytoskeleton];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNEDANVKL--------IRELREEIERLKA----VLLNFELRNFSSL 68
Cdd:COG5059    309 VICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFreqsQLSQSSLSGIFAY 388

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907142925   69 NDDLDESLQELVFQSDLKIDTLTQHWTEKRNDRQALMEHYGVDINRKR 116
Cdd:COG5059    389 MQSLKKETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLR 436

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  128 LMALEDDVLSTGVVLYHLKEGTtkigRIDSDQEQDIVLQGQWIERDHCTITSTC-GVVILRPTQGARCTVNGREVTASCR 206
Cdd:cd22729      4 LVNLNADPALNELLVYYLKDHT----RVGADTSQDIQLFGIGIQPEHCVIDIAAdGDVTLTPKENARTCVNGTLVCSVTQ 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907142925  207 LtqgrdyglnsgWcvTGAVITLGKAQKFRFNHPAEAavlRHQRLK 251
Cdd:cd22729     80 L-----------W--HGDRILWGNNHFFRINLPKRK---RRDWLK 108

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.

                           10        20
                   ....*....|....*....|....*...
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNI 28
Cdd:cd01370    318 MIANISPSSSSYEETHNTLKYANRAKNI 345

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142925  145 LKEGTTKIGRidsDQEQDIVLQGQWIERDHCTIT-STCGVVILRPTQGARCT-VNGREVTASCRLTQGrDyglnsgwcvt 222
Cdd:cd22673     18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENLSTTNPTlVNGKAIEKSAELKDG-D---------- 83

                           90
                   ....*....|....
gi 1907142925  223 gaVITLGKAqKFRF 236
Cdd:cd22673     84 --VITIGGR-SFRF 94

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.

                           10        20
                   ....*....|....*....|....*.
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAK 26
Cdd:cd00106    301 MIACISPSSENFEETLSTLRFASRAK 326

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.

                           10        20
                   ....*....|....*....|....*...
gi 1907142925    1 MVATVSPAHTSYSETMSTMRYASNAKNI 28
Cdd:cd01372    313 MIACVSPADSNFEETLNTLKYANRARNI 340

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142925  150 TKIGRidsDQEQDIVLQGQWIERDHCTITST-CGVVILRPTQGARCT-VNGREVT-ASCRLTQG 210
Cdd:pfam00498    1 VTIGR---SPDCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLGSTNGTfVNGQRLGpEPVRLKDG 61